ID BIOA_YEAST Reviewed; 480 AA.
AC P50277; D6W1N3; E9P967; Q4R1J0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 192.
DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000305};
DE EC=2.6.1.62 {ECO:0000305|PubMed:10333520};
DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000303|PubMed:10333520};
DE Short=DAPA AT {ECO:0000303|PubMed:10333520};
DE Short=DAPA aminotransferase {ECO:0000303|PubMed:10333520};
DE AltName: Full=Diaminopelargonic acid synthase {ECO:0000305};
GN Name=BIO3 {ECO:0000303|PubMed:10333520}; OrderedLocusNames=YNR058W;
GN ORFNames=N3510;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=10333520; DOI=10.1016/s0378-1119(99)00117-1;
RA Phalip V., Kuhn I., Lemoine Y., Jeltsch J.-M.;
RT "Characterization of the biotin biosynthesis pathway in Saccharomyces
RT cerevisiae and evidence for a cluster containing BIO5, a novel gene
RT involved in vitamer uptake.";
RL Gene 232:43-51(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-229; ARG-295 AND
RP ASP-384.
RC STRAIN=ATCC 204626 / S288c / A364A;
RX PubMed=16269718; DOI=10.1128/aem.71.11.6845-6855.2005;
RA Wu H., Ito K., Shimoi H.;
RT "Identification and characterization of a novel biotin biosynthesis gene in
RT Saccharomyces cerevisiae.";
RL Appl. Environ. Microbiol. 71:6845-6855(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
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) (PubMed:10333520). It is the
CC only aminotransferase known to utilize SAM as an amino donor
CC (PubMed:10333520). {ECO:0000269|PubMed:10333520}.
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:0000305|PubMed:10333520};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P53555};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC {ECO:0000305|PubMed:10333520}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. BioA subfamily. {ECO:0000305}.
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DR EMBL; U47112; AAA88905.1; -; Genomic_DNA.
DR EMBL; U53467; AAB63970.1; -; Genomic_DNA.
DR EMBL; AB200248; BAE00005.1; -; Genomic_DNA.
DR EMBL; Z71673; CAA96340.1; -; Genomic_DNA.
DR EMBL; AY723862; AAU09779.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10599.1; -; Genomic_DNA.
DR PIR; S63390; S63390.
DR RefSeq; NP_014456.1; NM_001183235.1.
DR AlphaFoldDB; P50277; -.
DR SMR; P50277; -.
DR BioGRID; 35884; 25.
DR DIP; DIP-4822N; -.
DR IntAct; P50277; 5.
DR MINT; P50277; -.
DR STRING; 4932.YNR058W; -.
DR iPTMnet; P50277; -.
DR PaxDb; 4932-YNR058W; -.
DR PeptideAtlas; P50277; -.
DR EnsemblFungi; YNR058W_mRNA; YNR058W; YNR058W.
DR GeneID; 855795; -.
DR KEGG; sce:YNR058W; -.
DR AGR; SGD:S000005341; -.
DR SGD; S000005341; BIO3.
DR VEuPathDB; FungiDB:YNR058W; -.
DR eggNOG; KOG1401; Eukaryota.
DR GeneTree; ENSGT00940000176655; -.
DR HOGENOM; CLU_016922_4_3_1; -.
DR InParanoid; P50277; -.
DR OMA; LLGGFTH; -.
DR OrthoDB; 5487177at2759; -.
DR BioCyc; YEAST:YNR058W-MONOMER; -.
DR UniPathway; UPA00078; UER00160.
DR BioGRID-ORCS; 855795; 1 hit in 10 CRISPR screens.
DR PRO; PR:P50277; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P50277; Protein.
DR GO; GO:0005737; C:cytoplasm; ISS:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IDA:SGD.
DR GO; GO:0004141; F:dethiobiotin synthase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IDA:SGD.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00834; BioA; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR005815; BioA.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00508; bioA; 1.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Biotin biosynthesis; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..480
FT /note="Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000120378"
FT BINDING 126..127
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT BINDING 270
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT BINDING 351..352
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT MOD_RES 314
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT VARIANT 229
FT /note="K -> E (in strain: ATCC 28383 and ATCC 204626)"
FT /evidence="ECO:0000269|PubMed:16269718"
FT VARIANT 295
FT /note="H -> R (in strain: ATCC 28383 and ATCC 204626)"
FT /evidence="ECO:0000269|PubMed:16269718"
FT VARIANT 384
FT /note="N -> D (in strain: ATCC 28383 and ATCC 204626)"
FT /evidence="ECO:0000269|PubMed:16269718"
FT CONFLICT 140
FT /note="S -> P (in Ref. 5; AAU09779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 53709 MW; 00A8BC42DCBED19A CRC64;
MSQEISYTPD VAELLDFDKK HIWHPYTSLS SPLNVYPVKS AHGCKLVLDT DSPVDVEVID
AMSSWWCVIH GYNNPELNEA LTKQMLKFSH VLLGGFTHKG AVNLVQKLLK VIDEPSLQYC
FLADSGSVAV EVALKMALQS NMSGEATKNR TKFLTIKNGY HGDTFGAMSV CDPENSMHHI
YNDRLSENIF AQAPSIVDGL PTSQNGFEDH WNAEEVTDLK KQFELHSDKI CAVILEPILQ
GAGGLRPYHP QFLIEVQKLC NQYDVLFIMD EIATGFGRTG EIFAFKHCQK YQDQHGISPS
DQIKVVPDIL CVGKGLTSGY MTMSAVVVND KVASRISSPN SPTGGCFMHG PTFMGNALAC
SVAEKSMDIL LRGEWRKQVS AIENQIYREL YQYIKNPDNG LIGTVVKRVS VIGAVGIVEL
YKKTDPEWFQ KKFISKGVHI RPFNCLCYIM PPYVITTEEL TKVNQVLIEV LHEWKSHINQ
//
