ID ASTC_ECO8A Reviewed; 406 AA.
AC B7M1G0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=ECIAI1_1809;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
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; CU928160; CAQ98665.1; -; Genomic_DNA.
DR RefSeq; WP_000081983.1; NC_011741.1.
DR AlphaFoldDB; B7M1G0; -.
DR SMR; B7M1G0; -.
DR GeneID; 75203054; -.
DR KEGG; ecr:ECIAI1_1809; -.
DR HOGENOM; CLU_016922_10_1_6; -.
DR UniPathway; UPA00185; UER00281.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; IPR049704; Aminotrans_3_PPA_site.
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 NCBIfam; TIGR03246; arg_catab_astC; 1.
DR NCBIfam; TIGR00707; argD; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF123; SUCCINYLORNITHINE TRANSAMINASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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_1000164380"
FT MOD_RES 252
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01173"
SQ SEQUENCE 406 AA; 43665 MW; B18ED13644C21176 CRC64;
MSQPITRENF DEWMIPVYAP APFIPVRGEG SRLWDQQGKE YIDFAGGIAV NALGHAHPEL
REALNEQASK FWHTGNGYTN EPVLRLAKKL IDATFADRVF FCNSGAEANE AALKLARKFA
HDRYGSHKSG IVAFKNAFHG RTLFTVSAGG QPAYSQDFAP LPADIRHAAY NDINSASALI
DDSTCAVIVE PIQGEGGVVP ASNAFLQGLR ELCNRHNALL IFDEVQTGVG RTGELYAYMH
YGVTPDLLTT AKALGGGFPV GALLATEECA RVMTVGTHGT TYGGNPLASA VAGKVLELIN
TPEMLNGVKQ RHDWFVERLN TINHRYGLFS EVRGLGLLIG CVLNADYAGQ AKQISQEAAK
AGVMVLIAGG NVVRFAPALN VSEEEVTTGL DRFAAACEHF VSRGSS
//
