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Database: UniProt
Entry: Q12F36_POLSJ
LinkDB: Q12F36_POLSJ
Original site: Q12F36_POLSJ 
ID   Q12F36_POLSJ            Unreviewed;       442 AA.
AC   Q12F36;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE            EC=2.6.1.62 {ECO:0000256|HAMAP-Rule:MF_00834};
DE   AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE            Short=DAPA AT {ECO:0000256|HAMAP-Rule:MF_00834};
DE            Short=DAPA aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE   AltName: Full=7,8-diaminononanoate synthase {ECO:0000256|HAMAP-Rule:MF_00834};
DE            Short=DANS {ECO:0000256|HAMAP-Rule:MF_00834};
DE   AltName: Full=Diaminopelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00834};
GN   Name=bioA {ECO:0000256|HAMAP-Rule:MF_00834};
GN   OrderedLocusNames=Bpro_0900 {ECO:0000313|EMBL:ABE42856.1};
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE42856.1, ECO:0000313|Proteomes:UP000001983};
RN   [1] {ECO:0000313|Proteomes:UP000001983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX   PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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:0000256|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:0000256|HAMAP-Rule:MF_00834};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|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:0000256|HAMAP-Rule:MF_00834}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. BioA subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00834}.
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DR   EMBL; CP000316; ABE42856.1; -; Genomic_DNA.
DR   RefSeq; WP_011481858.1; NC_007948.1.
DR   AlphaFoldDB; Q12F36; -.
DR   STRING; 296591.Bpro_0900; -.
DR   KEGG; pol:Bpro_0900; -.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_3_4; -.
DR   OMA; VAVKMCL; -.
DR   OrthoDB; 3398487at2; -.
DR   UniPathway; UPA00078; UER00160.
DR   Proteomes; UP000001983; 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:SF17; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW   Rule:MF_00834}; Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00834}; Reference proteome {ECO:0000313|Proteomes:UP000001983};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_00834};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00834}.
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         113..114
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         252
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         316..317
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         401
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   SITE            18
FT                   /note="Participates in the substrate recognition with KAPA
FT                   and in a stacking interaction with the adenine ring of SAM"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   MOD_RES         281
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
SQ   SEQUENCE   442 AA;  47872 MW;  12F984EA01EEE31D CRC64;
     MDNTSMVQRS LRHVWHPCTQ MKLHESQPLI PVSRADGVWL HDFEGHRYLD GISSWWVNLF
     GHNHPHIRAA LIDQLGRLDH VMLAGFTHQS VVELSEKLAQ LTGLGHAFYG SDGASATEIA
     LKMSAHYWRN TGRPGKCRFV GLAGGYHGET VGALAVTDIA IFREAYAPLV RLAATVPSPD
     ARCARPGESA VDVAGRAAGA LQAWLEQHHA ETAALIVEPL VQCAAGMAMH DASYLRGVRA
     LCDRYEVHLV VDEIATGFGR TGTMFAHQQA GIRPDFICLS KGLTGGTLPL SAVLTTDTVY
     QAFYDDDVAR GFLHSHSYTG NPLACRAALA TLELFEQNDV LAGNVAVARS LTAAFAPLTA
     HPRVRNARQL GMIWAWDVAD ALPGFSRRYY QHALAQGVLL RPIGNTIYAM PPYVMDEESS
     GFLARGALAA LQATLAEEAA HG
//
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