PYRB_SYNSC
ID PYRB_SYNSC Reviewed; 349 AA.
AC Q3AMW4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=Syncc9605_0292;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000110; ABB34068.1; -; Genomic_DNA.
DR RefSeq; WP_011363320.1; NC_007516.1.
DR AlphaFoldDB; Q3AMW4; -.
DR SMR; Q3AMW4; -.
DR STRING; 110662.Syncc9605_0292; -.
DR EnsemblBacteria; ABB34068; ABB34068; Syncc9605_0292.
DR KEGG; syd:Syncc9605_0292; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_2_0_3; -.
DR OMA; FPTEREY; -.
DR OrthoDB; 1844275at2; -.
DR UniPathway; UPA00070; UER00116.
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..349
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000321169"
SQ SEQUENCE 349 AA; 37878 MW; D784420A7F9EDB60 CRC64;
MSGWPHRHVL DLASFSREDF AAVLELAQRF RSLPITGARK LPALQGRLVA TLFFEPSTRT
RSSFELAAKR LSADVMSFSP SSSSLSKGES VLDTARTYVA MGADVLVVRH RSTGVPQQLA
HDLQQMGERT VVLNGGDGLH SHPSQGLLDL LTLARFFSPR HPMPEALQGR RIVIVGDILH
SRVARSNLWA LSACGADVVL CGPPSLVPDD FAAFVDAPPP GLPEDPVPQR GKVSVVRRLE
HALPGADAVM TLRLQKERMG QQLLTSLERY HRDFGLSHER MQLCGQNVPV LHPGPVNRGV
ELSGSLLDDP RCSLVEEQVR NGVPTRMALL YLMAASESAA EASLVSSSS
