PYRB_PROMT
ID PYRB_PROMT Reviewed; 339 AA.
AC Q46HE0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=PMN2A_1600;
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000095; AAZ59088.1; -; Genomic_DNA.
DR RefSeq; WP_011294233.1; NC_007335.2.
DR AlphaFoldDB; Q46HE0; -.
DR SMR; Q46HE0; -.
DR STRING; 59920.PMN2A_1600; -.
DR EnsemblBacteria; AAZ59088; AAZ59088; PMN2A_1600.
DR KEGG; pmn:PMN2A_1600; -.
DR HOGENOM; CLU_043846_2_0_3; -.
DR OMA; FPTEREY; -.
DR OrthoDB; 1844275at2; -.
DR PhylomeDB; Q46HE0; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000002535; 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..339
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000301606"
SQ SEQUENCE 339 AA; 37944 MW; CBF6CE61FF2E49C1 CRC64;
MNNWKHNHVL DLSTFSLEDY KTVLELTTRF KDVHKSSSRK LPALHGRLIA NLFFEPSTRT
RTSFELAAKR LSADVQNFSV SSSSLNKGET PLDTILTYIS MGADILVIRH ESTNVPAELA
NYVDINNINT SILNAGDGFH SHPSQGLLDL FTLATFFNPN EPSTNSLLNK KITIVGDILH
SRVARSNLWA LTACGAEVTL CGPPSLLPEE FIDFVQNPPL GQNFDPINKR GSVFIKRSLK
DALKNSDAVM TLRLQKERMK QNMLTDLDSY YVQYGITHES LKWCEKKVPV LHPGPVNRGV
EISNRLVEDN SINLISKQVE NGIPTRMALL YLLGLNKKD
