PYRB_VIBPA
ID PYRB_VIBPA Reviewed; 309 AA.
AC Q87LF8;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=VP2654;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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}.
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DR EMBL; BA000031; BAC60917.1; -; Genomic_DNA.
DR RefSeq; NP_799033.1; NC_004603.1.
DR RefSeq; WP_005478824.1; NC_004603.1.
DR AlphaFoldDB; Q87LF8; -.
DR SMR; Q87LF8; -.
DR STRING; 223926.28807664; -.
DR EnsemblBacteria; BAC60917; BAC60917; BAC60917.
DR GeneID; 1190199; -.
DR KEGG; vpa:VP2654; -.
DR PATRIC; fig|223926.6.peg.2549; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_1_2_6; -.
DR OMA; GDGPNEH; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000002493; Chromosome 1.
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..309
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000113225"
SQ SEQUENCE 309 AA; 34495 MW; 4D1A0D9B4582E0BA CRC64;
MANSLYQKHI ISIPELSREE LELIVETAGN LKKEPRPELI KNKVVASCFF EPSTRTRLSF
ETAIQRIGGD VIGFDNDGNT SLAKKGETLS DSVQVISSYV DAFVMRHPQE GAARLASEFS
NGVPVINAGD GANQHPTQTL LDLYTIAETQ GRLDNLNVAF VGDLKYGRTV HSLTQALAKF
NNIRFYFVAP DALAMPEYIC EELDEAGIEY SLHTEMEAVI PELDILYMTR VQKERFDESE
YAHIKSAYIL TAALLKGARE NLKVLHPLPR VDEITTDVDK TPHAYYFQQA QNGVYARQAL
LALVLNETL