ID   ASTC_YERPE              Reviewed;         414 AA.
AC   Q8D0D7; Q0WFI7; Q9ZC66;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 139.
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}, cstC;
GN   OrderedLocusNames=YPO1962, y2349, YP_1707;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=6/69;
RX   PubMed=10456941; DOI=10.1128/iai.67.9.4851-4861.1999;
RA   Buchrieser C., Rusniok C., Frangeul L., Couve E., Billault A., Kunst F.,
RA   Carniel E., Glaser P.;
RT   "The 102-kilobase pgm locus of Yersinia pestis: sequence analysis and
RT   comparison of selected regions among different Yersinia pestis and Yersinia
RT   pseudotuberculosis strains.";
RL   Infect. Immun. 67:4851-4861(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM85907.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAS61936.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL031866; CAA21341.1; -; Genomic_DNA.
DR   EMBL; AL590842; CAL20600.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM85907.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE017042; AAS61936.1; ALT_INIT; Genomic_DNA.
DR   PIR; AE0239; AE0239.
DR   PIR; T46998; T46998.
DR   RefSeq; WP_002216140.1; NZ_WUCM01000003.1.
DR   RefSeq; YP_002346951.1; NC_003143.1.
DR   AlphaFoldDB; Q8D0D7; -.
DR   SMR; Q8D0D7; -.
DR   STRING; 214092.YPO1962; -.
DR   PaxDb; Q8D0D7; -.
DR   EnsemblBacteria; AAM85907; AAM85907; y2349.
DR   EnsemblBacteria; AAS61936; AAS61936; YP_1707.
DR   KEGG; ype:YPO1962; -.
DR   KEGG; ypk:y2349; -.
DR   KEGG; ypm:YP_1707; -.
DR   PATRIC; fig|214092.21.peg.2339; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_1_6; -.
DR   OMA; PFMVPTY; -.
DR   UniPathway; UPA00185; UER00281.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; 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; 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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..414
FT                   /note="Succinylornithine transaminase"
FT                   /id="PRO_0000120358"
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