ID BIODA_ARATH Reviewed; 833 AA.
AC B0F481; B0F482; Q681L5; Q6NQL9; Q9FKL4; Q9FKL5;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Bifunctional dethiobiotin synthetase/7,8-diamino-pelargonic acid aminotransferase, mitochondrial;
DE AltName: Full=Bifunctional BIO3-BIO1 protein {ECO:0000303|PubMed:17993549};
DE Includes:
DE RecName: Full=Dethiobiotin synthetase;
DE EC=6.3.3.3 {ECO:0000269|PubMed:22547782};
DE AltName: Full=DTB synthetase;
DE Short=DTBS;
DE AltName: Full=Protein BIOTIN AUXOTROPH 3 {ECO:0000303|PubMed:17993549};
DE Includes:
DE RecName: Full=7,8-diamino-pelargonic acid aminotransferase;
DE Short=DAPA AT;
DE Short=DAPA aminotransferase;
DE AltName: Full=7,8-diaminononanoate synthase;
DE Short=DANS;
DE AltName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase;
DE EC=2.6.1.62 {ECO:0000269|PubMed:22547782};
DE AltName: Full=Diaminopelargonic acid synthase;
DE AltName: Full=Protein BIOTIN AUXOTROPH 1 {ECO:0000303|PubMed:17993549};
DE Flags: Precursor;
GN Name=BIO3-BIO1 {ECO:0000303|PubMed:17993549};
GN Synonyms=BIO1 {ECO:0000303|PubMed:17993549},
GN BIO3 {ECO:0000303|PubMed:17993549};
GN OrderedLocusNames=At5g57590 {ECO:0000312|Araport:AT5G57590};
GN ORFNames=MUA2.17/MUA2.18 {ECO:0000312|EMBL:BAB08794.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING,
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17993549; DOI=10.1104/pp.107.107409;
RA Muralla R., Chen E., Sweeney C., Gray J.A., Dickerman A., Nikolau B.J.,
RA Meinke D.;
RT "A bifunctional locus (BIO3-BIO1) required for biotin biosynthesis in
RT Arabidopsis.";
RL Plant Physiol. 146:60-73(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RA Alban C., Pinon V.;
RT "Arabidopsis thaliana 7,8-diaminopelargonic acid aminotransferase (AtbioA)
RT mRNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Alban C., Pautre V.;
RT "cDNA sequences for BIO3-BIO1 from Arabidopsis.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND MUTAGENESIS OF 777-TYR--THR-833.
RX PubMed=2909401; DOI=10.1016/s0012-1606(89)80047-8;
RA Schneider T., Dinkins R., Robinson K., Shellhammer J., Meinke D.W.;
RT "An embryo-lethal mutant of Arabidopsis thaliana is a biotin auxotroph.";
RL Dev. Biol. 131:161-167(1989).
RN [9]
RP FUNCTION.
RX PubMed=16667573; DOI=10.1104/pp.93.3.1162;
RA Shellhammer J., Meinke D.;
RT "Arrested embryos from the bio1 auxotroph of Arabidopsis thaliana contain
RT reduced levels of biotin.";
RL Plant Physiol. 93:1162-1167(1990).
RN [10]
RP FUNCTION.
RX PubMed=8676868; DOI=10.1007/bf02172516;
RA Patton D.A., Volrath S., Ward E.R.;
RT "Complementation of an Arabidopsis thaliana biotin auxotroph with an
RT Escherichia coli biotin biosynthetic gene.";
RL Mol. Gen. Genet. 251:261-266(1996).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=11779812; DOI=10.1093/genetics/159.4.1751;
RA McElver J., Tzafrir I., Aux G., Rogers R., Ashby C., Smith K., Thomas C.,
RA Schetter A., Zhou Q., Cushman M.A., Tossberg J., Nickle T., Levin J.Z.,
RA Law M., Meinke D., Patton D.;
RT "Insertional mutagenesis of genes required for seed development in
RT Arabidopsis thaliana.";
RL Genetics 159:1751-1763(2001).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12644697; DOI=10.1104/pp.013243;
RA Che P., Weaver L.M., Wurtele E.S., Nikolau B.J.;
RT "The role of biotin in regulating 3-methylcrotonyl-coenzyme a carboxylase
RT expression in Arabidopsis.";
RL Plant Physiol. 131:1479-1486(2003).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23031218; DOI=10.1111/tpj.12037;
RA Pommerrenig B., Popko J., Heilmann M., Schulmeister S., Dietel K.,
RA Schmitt B., Stadler R., Feussner I., Sauer N.;
RT "SUCROSE TRANSPORTER 5 supplies Arabidopsis embryos with biotin and affects
RT triacylglycerol accumulation.";
RL Plant J. 73:392-404(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 23-833 IN COMPLEX WITH
RP (4R,5S)-DETHIOBIOTIN; 7-KETO-8-AMINOPELARGONIC ACID; L-TARTARIC ACID AND
RP PYRIDOXAL PHOSPHATE, FUNCTION, MUTAGENESIS OF PHE-348; SER-382 AND ILE-815,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PATHWAY, COFACTOR, ALTERNATIVE
RP SPLICING, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=22547782; DOI=10.1105/tpc.112.097675;
RA Cobessi D., Dumas R., Pautre V., Meinguet C., Ferrer J.-L., Alban C.;
RT "Biochemical and structural characterization of the Arabidopsis
RT bifunctional enzyme dethiobiotin synthetase-diaminopelargonic acid
RT aminotransferase: evidence for substrate channeling in biotin synthesis.";
RL Plant Cell 24:1608-1625(2012).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes two different reactions
CC involved in the biotin biosynthesis. {ECO:0000269|PubMed:12644697,
CC ECO:0000269|PubMed:17993549, ECO:0000269|PubMed:22547782,
CC ECO:0000269|PubMed:23031218}.
CC -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
CC dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-
CC diaminopelargonic acid (DAPA) to form an ureido ring. {ECO:0000250,
CC ECO:0000269|PubMed:16667573, ECO:0000269|PubMed:17993549,
CC ECO:0000269|PubMed:22547782, ECO:0000269|PubMed:2909401,
CC ECO:0000269|PubMed:8676868}.
CC -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
CC adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to
CC form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase
CC known to utilize SAM as an amino donor. {ECO:0000269|PubMed:22547782}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-
CC dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473,
CC ChEBI:CHEBI:456216; EC=6.3.3.3;
CC Evidence={ECO:0000269|PubMed:22547782};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine =
CC (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-
CC oxobutanoate; Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:149468, ChEBI:CHEBI:149469;
CC EC=2.6.1.62; Evidence={ECO:0000269|PubMed:22547782};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22547782};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:22547782};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=415 nm {ECO:0000269|PubMed:22547782};
CC Note=Shoulder at 335 nm (at pH 7.5 and 30 degrees Celsius).
CC {ECO:0000269|PubMed:22547782};
CC Kinetic parameters:
CC Note=kcat is 0.072 min(-1) for 7,8-diamino-pelargonic acid
CC aminotransferase + dethiobiotin synthetase activities, and 1.85 min(-
CC 1) for 7,8-diamino-pelargonic acid aminotransferase activity only (at
CC pH 7.5 and 30 degrees Celsius). {ECO:0000269|PubMed:22547782};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 1/2. {ECO:0000269|PubMed:22547782}.
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC {ECO:0000269|PubMed:22547782}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22547782}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:22547782}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Only the isoform BIO3-BIO1 is detected at protein level in
CC mitochondria. {ECO:0000269|PubMed:22547782};
CC Name=1; Synonyms=BIO3-BIO1;
CC IsoId=B0F481-1; Sequence=Displayed;
CC Name=2; Synonyms=BIO3 long;
CC IsoId=B0F481-2; Sequence=VSP_043888, VSP_043889;
CC Name=3; Synonyms=BIO1 short;
CC IsoId=B0F481-3; Sequence=VSP_043884, VSP_043887;
CC Name=4; Synonyms=BIO3 short;
CC IsoId=B0F481-4; Sequence=VSP_043886;
CC Name=5; Synonyms=BIO1 long;
CC IsoId=B0F481-5; Sequence=VSP_043885;
CC -!- DISRUPTION PHENOTYPE: Arrested embryos at the transition to cotyledon
CC stages of development (PubMed:11779812, PubMed:17993549). Biotin
CC depletion leading to lethality; this phenotype is rescued by exogenous
CC supply of biotin (PubMed:12644697, PubMed:23031218).
CC {ECO:0000269|PubMed:11779812, ECO:0000269|PubMed:12644697,
CC ECO:0000269|PubMed:17993549, ECO:0000269|PubMed:23031218}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the dethiobiotin
CC synthetase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-III
CC pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08794.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g57590 and At5g57600.; Evidence={ECO:0000305};
CC Sequence=BAB08795.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g57590 and At5g57600.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Seed defective Arabidopsis mutants;
CC URL="http://seedgenes.org/MutantList";
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DR EMBL; EU089963; ABW80569.1; -; mRNA.
DR EMBL; EU090805; ABU50828.1; -; mRNA.
DR EMBL; EU090805; ABU50829.1; -; mRNA.
DR EMBL; EF081156; ABN80998.1; -; mRNA.
DR EMBL; HQ857557; AEW48251.1; -; mRNA.
DR EMBL; HQ857558; AEW48252.1; -; mRNA.
DR EMBL; AB011482; BAB08794.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB011482; BAB08795.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96924.1; -; Genomic_DNA.
DR EMBL; BT010433; AAQ62434.1; -; mRNA.
DR EMBL; AK175602; BAD43365.1; -; mRNA.
DR RefSeq; NP_200567.2; NM_125140.4. [B0F481-1]
DR PDB; 4A0F; X-ray; 2.71 A; A/B=23-833.
DR PDB; 4A0G; X-ray; 2.50 A; A/B/C/D=23-833.
DR PDB; 4A0H; X-ray; 2.81 A; A/B=23-833.
DR PDB; 4A0R; X-ray; 2.68 A; A/B=23-833.
DR PDBsum; 4A0F; -.
DR PDBsum; 4A0G; -.
DR PDBsum; 4A0H; -.
DR PDBsum; 4A0R; -.
DR AlphaFoldDB; B0F481; -.
DR SMR; B0F481; -.
DR STRING; 3702.B0F481; -.
DR PaxDb; 3702-AT5G57590-1; -.
DR ProteomicsDB; 240795; -. [B0F481-1]
DR EnsemblPlants; AT5G57590.1; AT5G57590.1; AT5G57590. [B0F481-1]
DR GeneID; 835863; -.
DR Gramene; AT5G57590.1; AT5G57590.1; AT5G57590. [B0F481-1]
DR KEGG; ath:AT5G57590; -.
DR Araport; AT5G57590; -.
DR TAIR; AT5G57590; BIO1.
DR eggNOG; KOG1401; Eukaryota.
DR HOGENOM; CLU_010794_0_0_1; -.
DR InParanoid; B0F481; -.
DR OMA; KGWASRA; -.
DR OrthoDB; 5487177at2759; -.
DR PhylomeDB; B0F481; -.
DR BioCyc; MetaCyc:MONOMER-8566; -.
DR BRENDA; 2.6.1.62; 399.
DR BRENDA; 6.3.3.3; 399.
DR UniPathway; UPA00078; UER00160.
DR UniPathway; UPA00078; UER00161.
DR PRO; PR:B0F481; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B0F481; baseline and differential.
DR Genevisible; B0F481; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004141; F:dethiobiotin synthase activity; IDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IDA:TAIR.
DR CDD; cd03109; DTBS; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00336; BioD; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR004472; DTB_synth_BioD.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR Pfam; PF13500; AAA_26; 1.
DR Pfam; PF00202; Aminotran_3; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Aminotransferase; ATP-binding;
KW Biotin biosynthesis; Ligase; Magnesium; Metal-binding; Mitochondrion;
KW Multifunctional enzyme; Nucleotide-binding; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..833
FT /note="Bifunctional dethiobiotin synthetase/7,8-diamino-
FT pelargonic acid aminotransferase, mitochondrial"
FT /id="PRO_0000417696"
FT REGION 36..299
FT /note="Dethiobiotin synthetase"
FT /evidence="ECO:0000305"
FT REGION 332..830
FT /note="7,8-diamino-pelargonic acid aminotransferase"
FT /evidence="ECO:0000305"
FT BINDING 47..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0G"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0R"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0G"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 210..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0G"
FT BINDING 270..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 391..392
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0H"
FT BINDING 453..454
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0G, ECO:0007744|PDB:4A0H,
FT ECO:0007744|PDB:4A0R"
FT BINDING 495
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0H"
FT BINDING 518..520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 637
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0G, ECO:0007744|PDB:4A0H,
FT ECO:0007744|PDB:4A0R"
FT BINDING 666
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0H"
FT BINDING 700
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0H"
FT BINDING 701..702
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0G, ECO:0007744|PDB:4A0H,
FT ECO:0007744|PDB:4A0R"
FT BINDING 797
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0H"
FT SITE 348
FT /note="Participates in the substrate recognition with KAPA
FT and in a stacking interaction with the adenine ring of SAM"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT MOD_RES 666
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:22547782,
FT ECO:0007744|PDB:4A0F, ECO:0007744|PDB:4A0G,
FT ECO:0007744|PDB:4A0H, ECO:0007744|PDB:4A0R"
FT VAR_SEQ 1..382
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17993549, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.7"
FT /id="VSP_043884"
FT VAR_SEQ 1..321
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_043885"
FT VAR_SEQ 288..833
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_043886"
FT VAR_SEQ 383..399
FT /note="QQFDACASWWTQGPDPT -> MLVQAGGHRGQILLSRL (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:17993549, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.7"
FT /id="VSP_043887"
FT VAR_SEQ 403..405
FT /note="ELA -> VSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17993549, ECO:0000303|Ref.3"
FT /id="VSP_043888"
FT VAR_SEQ 406..833
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17993549, ECO:0000303|Ref.3"
FT /id="VSP_043889"
FT MUTAGEN 348
FT /note="F->Y: No important impact on the enzyme kinetic
FT parameters."
FT /evidence="ECO:0000269|PubMed:22547782"
FT MUTAGEN 382
FT /note="S->Y: Reduced substrate channeling leading to slower
FT 7,8-diamino-pelargonic acid aminotransferase + dethiobiotin
FT synthetase activities."
FT /evidence="ECO:0000269|PubMed:22547782"
FT MUTAGEN 777..833
FT /note="Missing: In bio1-1: Arrested embryo."
FT /evidence="ECO:0000269|PubMed:2909401"
FT MUTAGEN 815
FT /note="I->W: Reduced substrate channeling leading to slower
FT 7,8-diamino-pelargonic acid aminotransferase + dethiobiotin
FT synthetase activities."
FT /evidence="ECO:0000269|PubMed:22547782"
FT CONFLICT 236
FT /note="G -> E (in Ref. 6; AAQ62434)"
FT /evidence="ECO:0000305"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:4A0G"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 88..103
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 179..193
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4A0F"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:4A0F"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:4A0G"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:4A0G"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 312..343
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 398..415
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 426..437
FT /evidence="ECO:0007829|PDB:4A0G"
FT TURN 438..443
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 453..470
FT /evidence="ECO:0007829|PDB:4A0G"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 500..504
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:4A0G"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 560..564
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 566..570
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 572..584
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 596..602
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:4A0G"
FT TURN 608..611
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 612..615
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 617..629
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 634..637
FT /evidence="ECO:0007829|PDB:4A0G"
FT TURN 639..646
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 647..650
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 652..655
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 660..664
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 666..669
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 676..680
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 682..686
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 690..692
FT /evidence="ECO:0007829|PDB:4A0R"
FT HELIX 693..695
FT /evidence="ECO:0007829|PDB:4A0G"
FT TURN 702..705
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 707..721
FT /evidence="ECO:0007829|PDB:4A0G"
FT TURN 723..725
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 733..736
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 742..750
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:4A0F"
FT STRAND 754..760
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 763..768
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 780..791
FT /evidence="ECO:0007829|PDB:4A0G"
FT STRAND 802..806
FT /evidence="ECO:0007829|PDB:4A0G"
FT HELIX 813..827
FT /evidence="ECO:0007829|PDB:4A0G"
FT TURN 828..830
FT /evidence="ECO:0007829|PDB:4A0G"
SQ SEQUENCE 833 AA; 91935 MW; 87A5D5C624E19649 CRC64;
MIPVTATLIR HRLRHLRHRI RFKSTSVSPF HLPLNHPTYL IWSANTSLGK TLVSTGIAAS
FLLQQPSSSA TKLLYLKPIQ TGFPSDSDSR FVFSKLDSLS LRRQIPISIS NSVLHSSLPA
AKSLGLNVEV SESGMCSLNF RDEKTVTGAP ELLCKTLYAW EAAISPHLAA ERENATVEDS
VVLQMIEKCL KEEMECGVKS EKSDLLCLVE TAGGVASPGP SGTLQCDLYR PFRLPGILVG
DGRLGGISGT IAAYESLKLR GYDIAAVVFE DHGLVNEVPL TSYLRNKVPV LVLPPVPKDP
SDDLIEWFVE SDGVFKALKE TMVLANLERL ERLNGMAKLA GEVFWWPFTQ HKLVHQETVT
VIDSRCGENF SIYKASDNSS LSQQFDACAS WWTQGPDPTF QAELAREMGY TAARFGHVMF
PENVYEPALK CAELLLDGVG KGWASRVYFS DNGSTAIEIA LKMAFRKFCV DHNFCEATEE
EKHIVVKVIA LRGSYHGDTL GAMEAQAPSP YTGFLQQPWY TGRGLFLDPP TVFLSNGSWN
ISLPESFSEI APEYGTFTSR DEIFDKSRDA STLARIYSAY LSKHLQEHSG VRQSAHVGAL
IIEPVIHGAG GMHMVDPLFQ RVLVNECRNR KIPVIFDEVF TGFWRLGVET TTELLGCKPD
IACFAKLLTG GMVPLAVTLA TDAVFDSFSG DSKLKALLHG HSYSAHAMGC ATAAKAIQWF
KDPETNHNIT SQGKTLRELW DEELVQQISS HSAVQRVVVI GTLFALELKA DASNSGYASL
YAKSLLIMLR EDGIFTRPLG NVIYLMCGPC TSPEICRRLL TKLYKRLGEF NRT
//
