ID A0A0H2YX35_ECOK1 Unreviewed; 429 AA. AC A0A0H2YX35; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 02-OCT-2024, entry version 44. 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 ECO:0000313|EMBL:ABJ00156.1}; GN ORFNames=APECO1_1315 {ECO:0000313|EMBL:ABJ00156.1}; OS Escherichia coli O1:K1 / APEC. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; 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., Johnson S.J., RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.; RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 RT shares strong similarities with human extraintestinal pathogenic E. coli RT 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 (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}. 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 RefSeq; WP_001362906.1; NZ_CADILS010000026.1. DR AlphaFoldDB; A0A0H2YX35; -. DR KEGG; ecv:APECO1_1315; -. DR HOGENOM; CLU_016922_4_3_6; -. 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-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; IPR049704; Aminotrans_3_PPA_site. 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. 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:UP000008216}; 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 52 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 112..113 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 245 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 274 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 307 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 308..309 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 391 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT SITE 17 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 274 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="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 //