位置:首页 > 蛋白库 > PYRB_PROMA
PYRB_PROMA
ID   PYRB_PROMA              Reviewed;         338 AA.
AC   Q7VDV6;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Aspartate carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_00001};
DE            EC=2.1.3.2 {ECO:0000255|HAMAP-Rule:MF_00001};
DE   AltName: Full=Aspartate transcarbamylase {ECO:0000255|HAMAP-Rule:MF_00001};
DE            Short=ATCase {ECO:0000255|HAMAP-Rule:MF_00001};
GN   Name=pyrB {ECO:0000255|HAMAP-Rule:MF_00001}; OrderedLocusNames=Pro_0262;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00001};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000255|HAMAP-
CC       Rule:MF_00001}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017126; AAP99308.1; -; Genomic_DNA.
DR   RefSeq; NP_874656.1; NC_005042.1.
DR   RefSeq; WP_011124417.1; NC_005042.1.
DR   AlphaFoldDB; Q7VDV6; -.
DR   SMR; Q7VDV6; -.
DR   STRING; 167539.Pro_0262; -.
DR   EnsemblBacteria; AAP99308; AAP99308; Pro_0262.
DR   GeneID; 54199621; -.
DR   KEGG; pma:Pro_0262; -.
DR   PATRIC; fig|167539.5.peg.270; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_2_0_3; -.
DR   OMA; FPTEREY; -.
DR   OrthoDB; 1844275at2; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000001420; Chromosome.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-UniRule.
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   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   CHAIN           1..338
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000113173"
SQ   SEQUENCE   338 AA;  37154 MW;  49A832EF930A5C6C CRC64;
     MSNWSHKHIL DLSSFSIEDY QTVVELANRF KTIPRSGSRK LPALQGRLIA TLFFEPSTRT
     RSSFELAAKR LSADVQSFAP SNSSLIKGET PLDTVMTYVA MGAHVLVVRH GGTGVPEQLA
     KSLDQKKKNV SILNGGDGLH SHPSQGLLDL FTLTQFFNKE SPSPRNIAGK RIAIVGDILH
     SRVARSNLWS LTACGANVVL CGPPSLLPDD FAKFVEAPPS GQKKDPIKNR GKVTISRCLK
     EALTDTDAVI TLRLQKERMS ENLLSNLDKY HNEYGITHES LKWCGKHVPV LHPGPVNRGI
     EMSSELLEDN SISLIENQVS NGIPIRMALL YLLSADKN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024