(data stored in ACNUC7421 zone)

SWISSPROT: PYRB_RUEPO

ID   PYRB_RUEPO              Reviewed;         311 AA.
AC   Q5LX75;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 88.
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};
GN   OrderedLocusNames=SPO0287;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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
CC       pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00001}.
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00001}.
DR   EMBL; CP000031; AAV93605.1; -; Genomic_DNA.
DR   RefSeq; WP_011046048.1; NC_003911.12.
DR   SMR; Q5LX75; -.
DR   STRING; 246200.SPO0287; -.
DR   EnsemblBacteria; AAV93605; AAV93605; SPO0287.
DR   KEGG; sil:SPO0287; -.
DR   eggNOG; ENOG4105CXT; Bacteria.
DR   eggNOG; COG0540; LUCA.
DR   HOGENOM; HOG000022685; -.
DR   KO; K00609; -.
DR   OMA; WCDVANM; -.
DR   OrthoDB; 1844275at2; -.
DR   BioCyc; RPOM246200:G1G48-291-MONOMER; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000001023; 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;
DR   PRODOM; Q5LX75.
DR   SWISS-2DPAGE; Q5LX75.
KW   Complete proteome; Pyrimidine biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN         1    311       Aspartate carbamoyltransferase.
FT                                /FTId=PRO_0000113192.
SQ   SEQUENCE   311 AA;  34433 MW;  B42F0E282E57C576 CRC64;
     MSFAHRHLLG IEQLSPADIT AILDLAETYV ALNRQSAKHS DVLSGLTQIN MFFENSTRTQ
     ASFELAGKRL GADVMNMSMQ ASSIKKGETL IDTAMTLNAM HPDLLVVRHP HSGAVDLLAQ
     KVNCAVLNAG DGRHEHPTQA LLDALTIRRA KGRLHRLNIA ICGDIAHSRV ARSNLILLGK
     MENRIRLIGP PTLVPAQFAE FGAEVYDDMR EGLKDVDVVM MLRLQRERMD GGFIPSEREY
     YHRYGLDREK LGLAKPDAIV MHPGPMNRGV EIDGTLADDI NRSVIQEQVE MGVAVRMAAM
     ELLARNLREA T
//

If you have problems or comments...

PBIL Back to PBIL home page