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PYRB_SALTY
ID   PYRB_SALTY              Reviewed;         311 AA.
AC   P0A1Z4; P08420;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Aspartate carbamoyltransferase catalytic subunit;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB; OrderedLocusNames=STM4460;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=3036524; DOI=10.1111/j.1432-1033.1987.tb13483.x;
RA   Michaels G., Kelln R.A., Nargang F.E.;
RT   "Cloning, nucleotide sequence and expression of the pyrBI operon of
RT   Salmonella typhimurium LT2.";
RL   Eur. J. Biochem. 166:55-61(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC   -!- SUBUNIT: Heterododecamer (2C3:3R2) of six catalytic PyrB chains
CC       organized as two trimers (C3), and six regulatory PyrI chains organized
CC       as three dimers (R2).
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000305}.
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DR   EMBL; X05641; CAA29129.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL23279.1; -; Genomic_DNA.
DR   PIR; S00049; OWEBAC.
DR   RefSeq; NP_463320.1; NC_003197.2.
DR   RefSeq; WP_000013055.1; NC_003197.2.
DR   AlphaFoldDB; P0A1Z4; -.
DR   SMR; P0A1Z4; -.
DR   STRING; 99287.STM4460; -.
DR   PaxDb; P0A1Z4; -.
DR   EnsemblBacteria; AAL23279; AAL23279; STM4460.
DR   GeneID; 1255986; -.
DR   KEGG; stm:STM4460; -.
DR   PATRIC; fig|99287.12.peg.4693; -.
DR   HOGENOM; CLU_043846_1_2_6; -.
DR   OMA; FPTEREY; -.
DR   PhylomeDB; P0A1Z4; -.
DR   BioCyc; SENT99287:STM4460-MON; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   HAMAP; MF_00001; Asp_carb_tr; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   PANTHER; PTHR11405:SF16; PTHR11405:SF16; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..311
FT                   /note="Aspartate carbamoyltransferase catalytic subunit"
FT                   /id="PRO_0000113189"
FT   CONFLICT        172..176
FT                   /note="SLTQA -> FAKPRT (in Ref. 1; CAA29129)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        252..253
FT                   /note="AS -> P (in Ref. 1; CAA29129)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="R -> A (in Ref. 1; CAA29129)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   311 AA;  34384 MW;  8F512750433ADBB7 CRC64;
     MANPLYQKHI ISINDLSRDD LNLVLATAAK LKANPQPELL KHKVIASCFF EASTRTRLSF
     ETSMHRLGAS VVGFSDSANT SLGKKGETLA DTISVISTYV DAIVMRHPQE GAARLATEFS
     GQVPVLNAGD GSNQHPTQTL LDLFTIQETQ GRLDNLHIAM VGDLKYGRTV HSLTQALAKF
     SGNRFYFIAP DALAMPQYIL DMLDEKGMAW SLHGSIEEVM ADVDILYMTR VQKERLDPSE
     YANVKAQFVL RASDLNGARE NMKVLHPLPR IDEITTDVDK TPHAWYFQQA GNGIFARQAL
     LALVLNSELS L
 
 
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