PYRB_MYCSK
ID PYRB_MYCSK Reviewed; 316 AA.
AC A1UFK0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Mkms_2410;
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=189918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000518; ABL91608.1; -; Genomic_DNA.
DR RefSeq; WP_011559761.1; NC_008705.1.
DR AlphaFoldDB; A1UFK0; -.
DR SMR; A1UFK0; -.
DR STRING; 189918.Mkms_2410; -.
DR EnsemblBacteria; ABL91608; ABL91608; Mkms_2410.
DR KEGG; mkm:Mkms_2410; -.
DR HOGENOM; CLU_043846_2_0_11; -.
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..316
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000321121"
SQ SEQUENCE 316 AA; 33677 MW; 972D9FD0386052FF CRC64;
MTRHLLTAAD LSRDEATAIL DDADRFSQAL IGREVKKLPT LRGRTVITMF YENSTRTRVS
FEVAGKWMSA DVINVSASGS SVAKGESLRD TALTLRAAGA DALIIRHPAS GAAQQLAEWT
AAEAGAPSVI NAGDGTHEHP TQALLDALTL RQRLGGIEGR RVVIVGDVLH SRVARSNVLL
LHTLGAEVVL VAPPTLLPVG VRQWPVTVSH DLDAELPAAD AVLMLRVQAE RMNGGFFPSA
REYSVRYGLS DKRQALLPDS AVVLHPGPML RGMEISSSVA DSSQSAVLQQ VSNGVHVRMA
VLFHLLVGAE QEAISA
