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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //