ID   ASTC_ECOLI              Reviewed;         406 AA.
AC   P77581;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Succinylornithine transaminase;
DE            Short=SOAT;
DE            EC=2.6.1.81 {ECO:0000305|PubMed:9696779};
DE   AltName: Full=Carbon starvation protein C;
DE   AltName: Full=Succinylornithine aminotransferase;
GN   Name=astC {ECO:0000303|PubMed:9696779}; Synonyms=argM, cstC, ydjW;
GN   OrderedLocusNames=b1748, JW1737;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9696780; DOI=10.1128/jb.180.16.4287-4290.1998;
RA   Fraley C.D., Kim J.H., McCann M.P., Matin A.;
RT   "The Escherichia coli starvation gene cstC is involved in amino acid
RT   catabolism.";
RL   J. Bacteriol. 180:4287-4290(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 3-21 AND 295-309, FUNCTION, CATALYTIC ACTIVITY,
RP   DISRUPTION PHENOTYPE, PATHWAY, AND INDUCTION.
RX   PubMed=9696779; DOI=10.1128/jb.180.16.4278-4286.1998;
RA   Schneider B.L., Kiupakis A.K., Reitzer L.J.;
RT   "Arginine catabolism and the arginine succinyltransferase pathway in
RT   Escherichia coli.";
RL   J. Bacteriol. 180:4278-4286(1998).
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. Is
CC       involved in the utilization of arginine as a nitrogen source, via the
CC       AST pathway, and seems also to play a role in ornithine catabolism
CC       (PubMed:9696779). {ECO:0000269|PubMed:9696779}.
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;
CC         Evidence={ECO:0000305|PubMed:9696779};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16954;
CC         Evidence={ECO:0000269|PubMed:9696779};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 3/5.
CC       {ECO:0000269|PubMed:9696779}.
CC   -!- INDUCTION: Its expression is under nitrogen control; a nitrogen-limited
CC       medium highly increases succinylornithine transaminase activity.
CC       {ECO:0000269|PubMed:9696779}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to grow
CC       on arginine as the nitrogen source. The disruption of this gene also
CC       impairs ornithine catabolism. {ECO:0000269|PubMed:9696779}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. AstC subfamily. {ECO:0000305}.
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DR   EMBL; U90416; AAB51148.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74818.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15539.1; -; Genomic_DNA.
DR   PIR; D64934; D64934.
DR   RefSeq; NP_416262.1; NC_000913.3.
DR   RefSeq; WP_000081983.1; NZ_STEB01000009.1.
DR   PDB; 4ADB; X-ray; 2.20 A; A/B/C/D=1-406.
DR   PDB; 4ADC; X-ray; 2.30 A; A/B/C/D=1-406.
DR   PDB; 4ADD; X-ray; 2.45 A; A/B/C/D=1-406.
DR   PDB; 4ADE; X-ray; 2.75 A; A/B=1-406.
DR   PDBsum; 4ADB; -.
DR   PDBsum; 4ADC; -.
DR   PDBsum; 4ADD; -.
DR   PDBsum; 4ADE; -.
DR   AlphaFoldDB; P77581; -.
DR   SMR; P77581; -.
DR   BioGRID; 4263005; 22.
DR   BioGRID; 850615; 1.
DR   DIP; DIP-9145N; -.
DR   IntAct; P77581; 2.
DR   STRING; 511145.b1748; -.
DR   jPOST; P77581; -.
DR   PaxDb; 511145-b1748; -.
DR   EnsemblBacteria; AAC74818; AAC74818; b1748.
DR   GeneID; 75203054; -.
DR   GeneID; 946255; -.
DR   KEGG; ecj:JW1737; -.
DR   KEGG; eco:b1748; -.
DR   PATRIC; fig|1411691.4.peg.508; -.
DR   EchoBASE; EB3755; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_1_6; -.
DR   InParanoid; P77581; -.
DR   OMA; MVPGFKY; -.
DR   OrthoDB; 9801052at2; -.
DR   PhylomeDB; P77581; -.
DR   BioCyc; EcoCyc:SUCCORNTRANSAM-MONOMER; -.
DR   BioCyc; MetaCyc:SUCCORNTRANSAM-MONOMER; -.
DR   UniPathway; UPA00185; UER00281.
DR   PRO; PR:P77581; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IDA:EcoCyc.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0043825; F:succinylornithine transaminase activity; IDA:EcoliWiki.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IGI:EcoCyc.
DR   GO; GO:0006527; P:arginine catabolic process; IMP:EcoliWiki.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR   GO; GO:0019545; P:arginine catabolic process to succinate; IMP:EcoCyc.
DR   GO; GO:0006593; P:ornithine catabolic process; IMP:EcoliWiki.
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   1: Evidence at protein level;
KW   3D-structure; Aminotransferase; Arginine metabolism;
KW   Direct protein sequencing; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..406
FT                   /note="Succinylornithine transaminase"
FT                   /id="PRO_0000120352"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        361
FT                   /note="A -> R (in Ref. 1; AAB51148)"
FT                   /evidence="ECO:0000305"
FT   HELIX           7..13
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          40..45
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           46..49
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           58..68
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           81..93
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          97..104
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           105..123
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          130..134
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           143..148
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           152..154
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           156..158
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          163..168
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           173..177
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          184..189
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   TURN            194..197
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           203..215
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          219..223
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   TURN            225..232
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          233..236
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           237..241
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          246..250
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          261..265
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           267..271
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           286..299
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           302..326
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          329..335
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          338..343
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   TURN            345..349
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           351..360
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          366..369
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   STRAND          372..375
FT                   /evidence="ECO:0007829|PDB:4ADB"
FT   HELIX           383..401
FT                   /evidence="ECO:0007829|PDB:4ADB"
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
//