ASTC_ECO55
ID ASTC_ECO55 Reviewed; 406 AA.
AC B7L6M2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=EC55989_1916;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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; CU928145; CAU97775.1; -; Genomic_DNA.
DR RefSeq; WP_000082039.1; NC_011748.1.
DR AlphaFoldDB; B7L6M2; -.
DR SMR; B7L6M2; -.
DR EnsemblBacteria; CAU97775; CAU97775; EC55989_1916.
DR KEGG; eck:EC55989_1916; -.
DR HOGENOM; CLU_016922_10_1_6; -.
DR OMA; PFMVPTY; -.
DR UniPathway; UPA00185; UER00281.
DR Proteomes; UP000000746; 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_1000164376"
FT MOD_RES 252
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01173"
SQ SEQUENCE 406 AA; 43733 MW; 5E35129CB711E686 CRC64;
MSQPITRENF NEWMIPVYAP APFIPVRGEG SRLWDQQGKE YIDFAGGIAV NALGHAHPEL
REALNEQASK FWHTGNGYTN EPVLRLAKKL IDATFADRVF FCNSGAEANE AALKLARKFA
HDRYGSHKSG IVAFKNAFHG RTLFTVSAGG QPAYSQDFAP LPPDIRHAAY NDINSASALI
DDATCAVIVE PIQGEGGVVP ASNAFLQDLR ELCDRHNALL IFDEVQTGVG RTGELYAYMH
YGVTPDLLTT AKALGGGFPV GALLATEECA RVMTVGTHGT TYGGNPLASA VAGKVLELIN
TPEMLNGVKQ RHDWFVERLN TLNHRYGLFS EVRGLGLLIG CVLNADYAGQ AKQISQEAAK
AGVMVLIAGG NVVRFAPALN VSEEEVTTGL DRFAAACEHF VSRGSS