ID   ASTC_SHIBS              Reviewed;         406 AA.
AC   Q321P0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=SBO_1342;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000036; ABB65968.1; -; Genomic_DNA.
DR   RefSeq; WP_000081975.1; NC_007613.1.
DR   AlphaFoldDB; Q321P0; -.
DR   SMR; Q321P0; -.
DR   EnsemblBacteria; ABB65968; ABB65968; SBO_1342.
DR   KEGG; sbo:SBO_1342; -.
DR   HOGENOM; CLU_016922_10_1_6; -.
DR   OMA; PFMVPTY; -.
DR   UniPathway; UPA00185; UER00281.
DR   Proteomes; UP000007067; 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_0000262443"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01173"
SQ   SEQUENCE   406 AA;  43727 MW;  33B6B4EB1F5512FE CRC64;
     MSQPITRENF DEWMIPVYAP APFIPVRGEG SRLWDQQGKE YIDFAGGIAV NALGHAHPEL
     REALNEQASK FWHTGNGYTN EPVLRLAKKL IDATFADRVF FCNSGAEANE AALKLARKFA
     HDRYGSHKSG IMAFKNAFHG RTLFTVSAGG QPAYSQDFAP LPPDIRHAAY NDINSASALI
     DDATCAVIVE PIQGEGGVVP ASNAFLQGLR ELCDRHNALL IFDEVQTGVG RTGELYAYMH
     YGVTPDLLTT AKALGGDFPV GALLTTEECA SVMTVGTHGT TYGGNPLASA VAGKVLELIN
     TPEMLNGVKQ RHDWFVERLN TINHRYGLFS EVRGLGLLIG CVLNADYAGQ AKQISQEAAK
     AGVMVLIAGG NVVRFAPALN VSEEEVTTGL DRFAAACEHF VSRGSS