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PYRB_PROM3
ID   PYRB_PROM3              Reviewed;         348 AA.
AC   A2CCB6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=P9303_23931;
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303;
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; CP000554; ABM79126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2CCB6; -.
DR   SMR; A2CCB6; -.
DR   STRING; 59922.P9303_23931; -.
DR   PRIDE; A2CCB6; -.
DR   EnsemblBacteria; ABM79126; ABM79126; P9303_23931.
DR   KEGG; pmf:P9303_23931; -.
DR   HOGENOM; CLU_043846_2_0_3; -.
DR   OMA; FPTEREY; -.
DR   BioCyc; PMAR59922:G1G80-2105-MON; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000002274; 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; Transferase.
FT   CHAIN           1..348
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000301603"
SQ   SEQUENCE   348 AA;  37787 MW;  83DE27ECE40AEE8B CRC64;
     MSGWSHRHIL DLASFSLEDY SSVLELAHRF RSMPVTGARK LPALQGRLVA TLFFEPSTRT
     RSSFELAARR LSADVQSFTP ASSSLSKGET VLDTARTYVA MGADVLVVRH SSTSVPEQLA
     CALDRSGERT AVLNGGDGLH SHPSQGLLDL YTLAHYFDSQ NPLPEALQGK RIVIVGDVLH
     SRVARSNLWA LTACGADVVL CGPPSLVPQD FVAFVEAPPP GQSHDPVQHR GCVEVVRTLE
     EALPGADAVM TLRLQKERMH QHLLTDLNRF HRDYGLTHER LKLCGKPVPL LHPGPVNRGV
     ELGGSLLDDH SISLVEEQVR NGIPIRMALL YLMAAVESSS DPSLAAIG
 
 
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