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Database: UniProt
Entry: BIOA_DESVH
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Original site: BIOA_DESVH 
ID   BIOA_DESVH              Reviewed;         542 AA.
AC   Q728P4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE            EC=2.6.1.62 {ECO:0000255|HAMAP-Rule:MF_00834};
DE   AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE            Short=DAPA AT {ECO:0000255|HAMAP-Rule:MF_00834};
DE            Short=DAPA aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE   AltName: Full=7,8-diaminononanoate synthase {ECO:0000255|HAMAP-Rule:MF_00834};
DE            Short=DANS {ECO:0000255|HAMAP-Rule:MF_00834};
DE   AltName: Full=Diaminopelargonic acid synthase {ECO:0000255|HAMAP-Rule:MF_00834};
GN   Name=bioA {ECO:0000255|HAMAP-Rule:MF_00834}; OrderedLocusNames=DVU_2559;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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:0000255|HAMAP-
CC       Rule:MF_00834}.
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:0000255|HAMAP-Rule:MF_00834};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00834};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC       diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00834}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00834}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00834}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. BioA subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00834}.
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DR   EMBL; AE017285; AAS97031.1; -; Genomic_DNA.
DR   RefSeq; WP_010939829.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_011771.1; NC_002937.3.
DR   AlphaFoldDB; Q728P4; -.
DR   SMR; Q728P4; -.
DR   STRING; 882.DVU_2559; -.
DR   PaxDb; 882-DVU_2559; -.
DR   EnsemblBacteria; AAS97031; AAS97031; DVU_2559.
DR   KEGG; dvu:DVU_2559; -.
DR   PATRIC; fig|882.5.peg.2317; -.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_3_7; -.
DR   OrthoDB; 9801834at2; -.
DR   PhylomeDB; Q728P4; -.
DR   UniPathway; UPA00078; UER00160.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
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; Cytoplasm; Pyridoxal phosphate;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..542
FT                   /note="Adenosylmethionine-8-amino-7-oxononanoate
FT                   aminotransferase"
FT                   /id="PRO_0000411122"
FT   REGION          509..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         170..171
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         311
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         470
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   SITE            73
FT                   /note="Participates in the substrate recognition with KAPA
FT                   and in a stacking interaction with the adenine ring of SAM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   MOD_RES         340
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
SQ   SEQUENCE   542 AA;  58370 MW;  AFAA78F7239F9298 CRC64;
     MSTSPFNSRV APMPHDDATA PVLHYAHDAA GAHDAADAAG AHDAADAAGT PPCAASRTAR
     LRSLDAAHVW HPFTQMRDWM GSEPCIIDAA DGNHLIDTDG NRYLDGVSSL WTNVHGHRHP
     HIDEAIRRQL DRVAHSTLLG LGGTPSIELA ARLTAIAPAG LTRVFYSDSG STAVEAALKI
     AFQYHRQAPE GDARRTRVMA FSNAYHGDTI GSVSLGGMSL FHGIYGPLLF DPVRAPAPHC
     YRCPADLRPE TCGMACLGEV ERLMRHHGHE LCAVVVEPLV QGAAGMLVQP RGWLRGLRDL
     CDRHGVFMVA DEVAVGFGKT GTMFACEQEG VVPDMLCLAK GITGGYLPLA ATLVTEHIHD
     GFLGGYADFR TFFHGHTYTG NALACAAALA SLDVFEEERT LETLRPRIER LATLLAPLND
     LPHVGDIRRV GVMTGIELVA DRETRTPYRP EERIGHRVTL EARRRGVIVR PLGDVMVLMP
     PLSITETELE TLVHTVRGAI IAVTEHGADG GLWTKRPDGP DNPDKANTPD TPDGARTGET
     VV
//
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