ASTC_ECOLI
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 03-AUG-2022, entry version 170.
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; Proteobacteria; 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; P77581; -.
DR PRIDE; P77581; -.
DR EnsemblBacteria; AAC74818; AAC74818; b1748.
DR EnsemblBacteria; BAA15539; BAA15539; BAA15539.
DR GeneID; 66674357; -.
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; PFMVPTY; -.
DR PhylomeDB; P77581; -.
DR BioCyc; EcoCyc:SUCCORNTRANSAM-MON; -.
DR BioCyc; MetaCyc:SUCCORNTRANSAM-MON; -.
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:0006526; P:arginine biosynthetic process; IEA:UniProt.
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; 3.40.640.10; -; 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 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
