ID   ASTC_SALDC              Reviewed;         408 AA.
AC   B5FJD8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=SeD_A2043;
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001144; ACH74964.1; -; Genomic_DNA.
DR   RefSeq; WP_000059504.1; NC_011205.1.
DR   AlphaFoldDB; B5FJD8; -.
DR   SMR; B5FJD8; -.
DR   KEGG; sed:SeD_A2043; -.
DR   HOGENOM; CLU_016922_10_1_6; -.
DR   OMA; PFMVPTY; -.
DR   UniPathway; UPA00185; UER00281.
DR   Proteomes; UP000008322; 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; IPR001763; Rhodanese-like_dom.
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..408
FT                   /note="Succinylornithine transaminase"
FT                   /id="PRO_1000164390"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01173"
SQ   SEQUENCE   408 AA;  43752 MW;  1E25B25CDED31C0C CRC64;
     MSLSVTRENF DEWMVPVYVP APFIPVRGEG SRLWDQQGKE YIDFAGGIAV NALGHAHPAL
     REALNEQANR FWHTGNGYTN EPALRLAKKL IDATFAERVF FCNSGAEANE AALKLARKYA
     HDRVGNHKSG IVAFKNAFHG RTLFTVSAGG QPTYSQDFAP LPPDIRHAAY NDLNSASALI
     DDNTCAVIVE PVQGEGGVIP ATKAFLQGLR ELCDRHQALL IFDEVQTGVG RTGELYAYMH
     YGVTPDILTT AKALGGGFPI GAMLTTQDYA SVMTPGTHGT TYGGNPLATA VAGKVLDIIN
     TPEMQNGVRQ RHDAFIERLN TINVRFGMFS EIRGLGLLLG CVLQTEFAGK AKLIAQEAAK
     AGVMVLIAGG DVVRFAPALN VSDEEIATGL DRFALACERL QAGGASCG