ID   ASTC_ECO27              Reviewed;         406 AA.
AC   B7USC9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=E2348C_1876;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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}.
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DR   EMBL; FM180568; CAS09424.1; -; Genomic_DNA.
DR   RefSeq; WP_000082028.1; NC_011601.1.
DR   AlphaFoldDB; B7USC9; -.
DR   SMR; B7USC9; -.
DR   EnsemblBacteria; CAS09424; CAS09424; E2348C_1876.
DR   KEGG; ecg:E2348C_1876; -.
DR   HOGENOM; CLU_016922_10_1_6; -.
DR   OMA; PFMVPTY; -.
DR   UniPathway; UPA00185; UER00281.
DR   Proteomes; UP000008205; 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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR026330; SOAT.
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; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..406
FT                   /note="Succinylornithine transaminase"
FT                   /id="PRO_1000164374"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01173"
SQ   SEQUENCE   406 AA;  43649 MW;  BC82C9D9F0A42E57 CRC64;
     MSQPITRENF DEWMIPVYAP APFIPVRGEG SRLWDQQGKE YIDFSGGIAV NALGHAHPEL
     REALNEQASK FWHTGNGYTN EPVLRLAKKL IDATFADRVF FCNSGAEANE AALKLARKFA
     HDRYGSHKSG IVAFKNAFHG RTLFTVSAGG QPAYSQDFAP LPPDIRHAAY NDINSASALI
     DDATCAVIVE PIQGEGGVVP ASNAFLQGLR ELCDRHNALL IFDEVQTGVG RTGELYAYMH
     YGVTPDLLTT AKALGGGFPV GALLATKECA SVMTVGTHGT TYGGNPLASA VAGKVLDLIN
     TPEMLNGVKQ RHDWFVERLN SINHHYSLFS EVRGLGLLIG CVLNADYAGQ AKQISQEAVK
     AGVMVLIAGG NVVRFAPALN VSEEEVTTGL DRFSAACEHF VSRGSS