ID   A0A0H2YX35_ECOK1        Unreviewed;       429 AA.
AC   A0A0H2YX35;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-SEP-2016, entry version 9.
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   AltName: Full=7,8-diaminononanoate synthase {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   ECO:0000313|EMBL:ABJ00156.1};
GN   ORFNames=APECO1_1315 {ECO:0000313|EMBL:ABJ00156.1};
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955 {ECO:0000313|EMBL:ABJ00156.1, ECO:0000313|Proteomes:UP000008216};
RN   [1] {ECO:0000313|EMBL:ABJ00156.1, ECO:0000313|Proteomes:UP000008216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APEC O1 {ECO:0000313|EMBL:ABJ00156.1};
RX   PubMed=17293413; DOI=10.1128/JB.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA   Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA   Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain
RT   O1:K1:H7 shares strong similarities with human extraintestinal
RT   pathogenic E. coli genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
CC   -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
CC       adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid
CC       (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only
CC       animotransferase known to utilize SAM as an amino donor.
CC       {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
CC       oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
CC       diaminononanoate. {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00834};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC       diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
CC       1/1. {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; CP000468; ABJ00156.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0A0H2YX35; -.
DR   EnsemblBacteria; ABJ00156; ABJ00156; APECO1_1315.
DR   KEGG; ecv:APECO1_1315; -.
DR   KO; K00833; -.
DR   OMA; ANPRINQ; -.
DR   UniPathway; UPA00078; UER00160.
DR   Proteomes; UP000008216; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   PANTHER; PTHR11986; PTHR11986; 1.
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 {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:ABJ00156.1};
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008216};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000256|RuleBase:RU003560};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:ABJ00156.1}.
FT   REGION      112    113       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   REGION      308    309       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING      52     52       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     144    144       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     245    245       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00834}.
FT   BINDING     274    274       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     307    307       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING     391    391       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   SITE         17     17       Participates in the substrate recognition
FT                                with KAPA and in a stacking interaction
FT                                with the adenine ring of SAM.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
SQ   SEQUENCE   429 AA;  47229 MW;  0E6C7784C13AC22E CRC64;
     MTTDDLAFDQ RHIWHPYTSM TSPLPVYPVA SAEGCELILS DGRRLVDGMS SWWAAIHGYN
     HPQLNAAMKS QIDAMSHVMF GGITHAPAIE LCRKLVAMTP QPLECVFLAD SGSVAVEVAM
     KMALQYWQAK GEARQRFLTF RNGYHGDTFG AMSVCDPDNS MHSLWKGYLP ENLFAPAPQS
     RMDGEWDERD MVGFARLMAA HRHEIAAVII EPIVQGAGGM RMYHPEWLKR IRKMCDREGI
     LLIADEIATG FGRTGKLFAC EHAEIAPDIL CLGKALTGGT MTLSATLTTR EVAETISNGE
     AGCFMHGPTF MGNPLACAAA NASLAILESG DWQHQVAAIE AQLREQLAPA CDAEMVADVR
     VLGAIGVVET TRPVNMAALQ KFFVEQGVWI RPFGKLIYLM PPYIILPQQL QRLTAAVNRA
     VQDETFFCQ
//