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   03-AUG-2022, entry version 79.
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 coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
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; CP000970; ACB15928.1; -; Genomic_DNA.
DR   RefSeq; WP_000081988.1; NC_010498.1.
DR   AlphaFoldDB; B1LDY3; -.
DR   SMR; B1LDY3; -.
DR   EnsemblBacteria; ACB15928; ACB15928; EcSMS35_1443.
DR   KEGG; ecm:EcSMS35_1443; -.
DR   HOGENOM; CLU_016922_10_1_6; -.
DR   OMA; PFMVPTY; -.
DR   UniPathway; UPA00185; UER00281.
DR   Proteomes; UP000007011; 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_1000164387"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="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