ASTC_SALTY
ID ASTC_SALTY Reviewed; 408 AA.
AC Q8ZPV2;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
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}; OrderedLocusNames=STM1303;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP INDUCTION.
RX PubMed=10074092; DOI=10.1128/jb.181.6.1934-1938.1999;
RA Lu C.-D., Abdelal A.T.;
RT "Role of ArgR in activation of the ast operon, encoding enzymes of the
RT arginine succinyltransferase pathway in Salmonella typhimurium.";
RL J. Bacteriol. 181:1934-1938(1999).
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 -!- INDUCTION: By nitrogen and carbon starvation, and arginine, via the
CC ArgR and Crp transcriptional regulators. {ECO:0000269|PubMed:10074092}.
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; AE006468; AAL20228.1; -; Genomic_DNA.
DR RefSeq; NP_460269.1; NC_003197.2.
DR RefSeq; WP_000059493.1; NC_003197.2.
DR AlphaFoldDB; Q8ZPV2; -.
DR SMR; Q8ZPV2; -.
DR STRING; 99287.STM1303; -.
DR PaxDb; Q8ZPV2; -.
DR EnsemblBacteria; AAL20228; AAL20228; STM1303.
DR GeneID; 1252821; -.
DR KEGG; stm:STM1303; -.
DR PATRIC; fig|99287.12.peg.1385; -.
DR HOGENOM; CLU_016922_10_1_6; -.
DR OMA; PFMVPTY; -.
DR PhylomeDB; Q8ZPV2; -.
DR BioCyc; SENT99287:STM1303-MON; -.
DR UniPathway; UPA00185; UER00281.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0043825; F:succinylornithine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProt.
DR GO; GO:0006527; P:arginine catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Aminotransferase; Arginine metabolism; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..408
FT /note="Succinylornithine transaminase"
FT /id="PRO_0000120357"
FT MOD_RES 252
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01173"
SQ SEQUENCE 408 AA; 43832 MW; A24E2D9EA3D702C4 CRC64;
MSLSVTRENF DEWMVPVYVP APFIPVRGEG SRLWDQQGKE YIDFAGGIAV NALGHAHPAL
REALNEQANR FWHIGNGYTN EPALRLAKKL IDATFAERVF FCNSGAEANE AALKLARKYA
HDRVGNHKSG IVAFKNAFHG RTLFTVSAGG QPTYSQDFAP LPPDIRHAAY NDLNSASALI
DDNTCAVIVE PVQGEGGVIP ATKAFLQGLR ELCDRHQALL IFDEVQTGVG RTGELYAYMH
YGVTPDILTT AKALGGGFPI GAMLTTQDYA SVMTPGTHGT TYGGNPLATA VAGKVLDIIN
TPEMQNGVRQ RHDAFIERLN TLNVRFGMFS EIRGLGLLLG CVLQTEFAGK AKLIAQEAAK
AGVMVLIAGG DVVRFAPALN VSDEEIATGL DRFALACERL QTGGVPCG
