ID ASTC_YERPA Reviewed; 414 AA.
AC Q1C8B1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
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=YPA_1344;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG13311.1; -; Genomic_DNA.
DR RefSeq; WP_002216140.1; NZ_CP009906.1.
DR AlphaFoldDB; Q1C8B1; -.
DR SMR; Q1C8B1; -.
DR KEGG; ypa:YPA_1344; -.
DR UniPathway; UPA00185; UER00281.
DR Proteomes; UP000001971; 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; 3.90.1150.10; 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..414
FT /note="Succinylornithine transaminase"
FT /id="PRO_0000262445"
FT MOD_RES 260
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01173"
SQ SEQUENCE 414 AA; 44215 MW; 2266A414A65F2AEC CRC64;
MEQPSPVTRQ SFDEWIVPTY APADFIVVRG EGSTLWDQQG KSYIDFAGGI AVNALGHGHP
AVRAALIEQA DKVWHLGNGY TNEPVLRLAK QLIDATFAEK VFFCNSGAEA NEAALKLARK
YALDNFANKA GQQGEKNQIV AFRNAFHGRT LFTVSAGGQP KYSQDFAPLP GGIHHGIFND
LASAEHLITD QTCAVIVEPI QGEGGVLPAD KEFLHGLRAL CDRHNALLIF DEIQTGVGRT
GELYAYMHYG VSPDVLTSAK ALGGGFPIGA MLTTTKYASA LSVGSHGTTF GGNPLACAVA
GTVLSLINQP TLLAGVKARH QWFIDELAEI NARHNVFAEI RGRGLLIGCV LNAQYAGKSK
EIVQAAAQYG LIALIAGPDV VRFAPSLIIS PKEIKEGLAR LAMGIEQVCQ KVTS
//
