PYRB_MYCLE
ID PYRB_MYCLE Reviewed; 321 AA.
AC Q9CCR5;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2;
DE AltName: Full=Aspartate transcarbamylase;
DE Short=ATCase;
GN Name=pyrB; OrderedLocusNames=ML0532;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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;
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000305}.
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DR EMBL; AL583918; CAC30040.1; -; Genomic_DNA.
DR PIR; D86975; D86975.
DR RefSeq; NP_301452.1; NC_002677.1.
DR RefSeq; WP_010907776.1; NC_002677.1.
DR AlphaFoldDB; Q9CCR5; -.
DR SMR; Q9CCR5; -.
DR STRING; 272631.ML0532; -.
DR EnsemblBacteria; CAC30040; CAC30040; CAC30040.
DR KEGG; mle:ML0532; -.
DR PATRIC; fig|272631.5.peg.932; -.
DR Leproma; ML0532; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_2_0_11; -.
DR OMA; FPTEREY; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000000806; 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..321
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000113160"
SQ SEQUENCE 321 AA; 34257 MW; DDC76151F3EAEE86 CRC64;
MMRRHLLNAG DLSRDDAIAI FDDADRFAHA LVGREIKKLP TLRGRTVITM FYENSTRTRV
SFEVAGKWMS ANVINVSPAG SSVGKGESLR DTALTLRAAG ADALIIRHPA SGAAHLLADW
TAAETGEDGP AVINAGDGTH EHPTQALLDA LTIRQRLGSI EGRRILIVGD ILHSRVARSN
VVLLDTLGAE VVLVAPRTLL PIGVDGWPAT VSCDFDAELP AADAVLMLRV QAERMNGGFF
PSVREYSCLY GLTERRQALL PGHAVVLHPG PMLRGMEIAS SVADSSQSAV LQQVSNGVHV
RMAVLFHVLV GTQSAEEEGA A