ID ASTC_ECOSM Reviewed; 406 AA. AC B1LDY3; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=Succinylornithine transaminase {ECO:0000255|HAMAP-Rule:MF_01173}; DE EC=2.6.1.81 {ECO:0000255|HAMAP-Rule:MF_01173}; DE AltName: Full=Succinylornithine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01173}; GN Name=astC {ECO:0000255|HAMAP-Rule:MF_01173}; GN Synonyms=argM {ECO:0000255|HAMAP-Rule:MF_01173}; GN OrderedLocusNames=EcSMS35_1443; OS Escherichia coli (strain SMS-3-5 / SECEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=439855; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SMS-3-5 / SECEC; RX PubMed=18708504; DOI=10.1128/JB.00661-08; RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., RA Ravel J., Stepanauskas R.; RT "Insights into the environmental resistance gene pool from the genome RT sequence of the multidrug-resistant environmental isolate Escherichia RT coli SMS-3-5."; RL J. Bacteriol. 190:6779-6794(2008). CC -!- FUNCTION: Catalyzes the transamination of N(2)-succinylornithine CC and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde CC and glutamate. Can also act as an acetylornithine CC aminotransferase. {ECO:0000255|HAMAP-Rule:MF_01173}. CC -!- CATALYTIC ACTIVITY: N(2)-succinyl-L-ornithine + 2-oxoglutarate = CC N-succinyl-L-glutamate 5-semialdehyde + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_01173}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01173}; CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST CC pathway; L-glutamate and succinate from L-arginine: step 3/5. CC {ECO:0000255|HAMAP-Rule:MF_01173}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. AstC subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01173}. 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; CP000970; ACB15928.1; -; Genomic_DNA. DR RefSeq; WP_000081988.1; NC_010498.1. DR ProteinModelPortal; B1LDY3; -. DR SMR; B1LDY3; -. DR EnsemblBacteria; ACB15928; ACB15928; EcSMS35_1443. DR KEGG; ecm:EcSMS35_1443; -. DR HOGENOM; HOG000020206; -. DR KO; K00840; -. DR OMA; GIATCTL; -. DR UniPathway; UPA00185; UER00281. DR Proteomes; UP000007011; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0043825; F:succinylornithine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway. DR GO; GO:0006593; P:ornithine catabolic process; IEA:InterPro. DR CDD; cd00610; OAT_like; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR HAMAP; MF_01107; ArgD_aminotrans_3; 1. DR HAMAP; MF_01173; AstC_aminotrans_3; 1. DR InterPro; IPR017652; Ac/SucOrn_transaminase_bac. DR InterPro; IPR004636; AcOrn/SuccOrn_fam. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2. DR InterPro; IPR026330; SOAT. DR PANTHER; PTHR11986:SF101; PTHR11986:SF101; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR03246; arg_catab_astC; 1. DR TIGRFAMs; TIGR00707; argD; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Aminotransferase; Arginine metabolism; Complete proteome; KW Pyridoxal phosphate; Transferase. FT CHAIN 1 406 Succinylornithine transaminase. FT /FTId=PRO_1000164387. FT MOD_RES 252 252 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_01173}. SQ SEQUENCE 406 AA; 43541 MW; 3AFE0CEDCFE9C6DD CRC64; MSQPITRENF DEWMIPVYAP APFIPVRGEG SRLWDQQGKE YIDFAGGIAV NALGHAHPEL REALNEQASK FWHTGNGYTN EPVLRLAKKL IDATFADRVF FCNSGAEANE AALKLARKFA HDRYGSHKSG IVAFKNAFHG RTLFTVSAGG QPAYSQDFAP LPPDIHHAAY NDINSASALI DDATCAVIVE PIQGEGGVVP ASNAFLQGLR ELCDRHNALL IFDEVQTGVG RTGELYAYMH YGVTPDLLTT AKALGGGFPV GALLATEECA SVMTVGTHGT TYGGNPLASA VAGKVLDLIN TPEMLNGVKQ RHDWFVERLN SINHHYGLFS EVRGLGLLIG CVLNADYAGQ AKQISQEAAK AGVMVLIAGG NVVRFAPALN VSEEEVTTGL DRFAAACEHF VSRGSS //