ID ASTC_ECOL5 Reviewed; 406 AA.
AC Q0TH82;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Succinylornithine transaminase {ECO:0000255|HAMAP-Rule:MF_01173};
DE Short=SOAT;
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=ECP_1694;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
CC -!- FUNCTION: Catalyzes the transamination of N(2)-succinylornithine and
CC alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and
CC glutamate. Can also act as an acetylornithine aminotransferase.
CC {ECO:0000255|HAMAP-Rule:MF_01173}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-
CC succinyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:16953,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58514,
CC ChEBI:CHEBI:58520; EC=2.6.1.81; Evidence={ECO:0000255|HAMAP-
CC 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; CP000247; ABG69697.1; -; Genomic_DNA.
DR RefSeq; WP_000081990.1; NC_008253.1.
DR AlphaFoldDB; Q0TH82; -.
DR SMR; Q0TH82; -.
DR KEGG; ecp:ECP_1694; -.
DR HOGENOM; CLU_016922_10_1_6; -.
DR UniPathway; UPA00185; UER00281.
DR Proteomes; UP000009182; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043825; F:succinylornithine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProt.
DR GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-UniRule.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_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; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR026330; SOAT.
DR NCBIfam; TIGR03246; arg_catab_astC; 1.
DR NCBIfam; TIGR00707; argD; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF123; SUCCINYLORNITHINE TRANSAMINASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Arginine metabolism; Pyridoxal phosphate; Transferase.
FT CHAIN 1..406
FT /note="Succinylornithine transaminase"
FT /id="PRO_0000262440"
FT MOD_RES 252
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01173"
SQ SEQUENCE 406 AA; 43558 MW; 94E35D9E8A20B655 CRC64;
MSQPITRENF DEWMIPVYAP APFIPVRGEG SRLWDQQGKE YIDFAGGIAV NALGHAHPEL
REALNEQASK FWHTGNGYTN EPVLRLAKKL IDATFADRVF FCNSGAEANE AALKLARKFA
HDRYGSHKSG IVAFKNAFHG RTLFTVSAGG QPAYSQDFAP LPPDIRHAAY NDINSASALI
DDATCAVIVE PIQGEGGVVP ASNAFLQGLR ELCDRHNALL IFDEVQTGVG RTGELYACMH
YGVTPDLLTT AKALGGGFPV GALLATEECA SVMTVGTHGT TYGGNPLASA VAGKVLDLIN
TPEMLNGVKQ RHDWFVERLN SINHHYSLFS EVRGLGLLIG CVLNADYAGQ AKQISQEAVK
AGVMVLIAGG NVVRFAPALN VSEEEVTTGL DRFAAACEHF VSRGSS
//
