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BIOA_STRCO
ID   BIOA_STRCO              Reviewed;         428 AA.
AC   Q9FCC2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=SCO1245;
GN   ORFNames=2SCG1.20;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939108; CAC01469.1; -; Genomic_DNA.
DR   RefSeq; NP_625533.1; NC_003888.3.
DR   RefSeq; WP_011027665.1; NZ_VNID01000006.1.
DR   AlphaFoldDB; Q9FCC2; -.
DR   SMR; Q9FCC2; -.
DR   STRING; 100226.SCO1245; -.
DR   GeneID; 1096668; -.
DR   KEGG; sco:SCO1245; -.
DR   PATRIC; fig|100226.15.peg.1245; -.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_3_11; -.
DR   InParanoid; Q9FCC2; -.
DR   OMA; VAVKMCL; -.
DR   PhylomeDB; Q9FCC2; -.
DR   UniPathway; UPA00078; UER00160.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00508; bioA; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Biotin biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..428
FT                   /note="Adenosylmethionine-8-amino-7-oxononanoate
FT                   aminotransferase"
FT                   /id="PRO_0000411125"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         119..120
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         249
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         312..313
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   BINDING         395
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT   SITE            23
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         278
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
SQ   SEQUENCE   428 AA;  45915 MW;  C2C46DE731FF7922 CRC64;
     MPDPALNVAE LLDLDRRHVW HPYGPMPGRQ DPLVVESASG VRLRPADGSG ELVDGMSSWW
     SAIHGYNHPV LNAAAREQLE RMSHVMFGGL THEPAVRLAK LLVDMSPEGL EHVFLADSGS
     VSVEVAVKMC LQYWRSLGRP GKHRLLTWRG GYHGDTWQPM SVCDPEGGMH ELWSGVLPRQ
     VFADAPPAEY EETYADHLRS MVERHAGELA AVIVEPVVQG AGGMRFHSPA YLRVLREACD
     AHDVLLVFDE IATGFGRTGA LFAAEHAAVT PDVMCVGKAL TGGYLTMAAT LCTSRVAEGI
     SRGEVPVLAH GPTFMGNPLA AAVACASIGL LLGQDWLAEV KRIETGLGEG LAPAAGLPGV
     RDVRVLGAIG VVQLDHAVDM RAATKAAVRE GVWLRPFRDL VYTMPPYVTG DADVARIARA
     VCAAAREG
 
 
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