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PYRB_MOOTA
ID   PYRB_MOOTA              Reviewed;         307 AA.
AC   Q2RK43;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Moth_0879;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC19196.1; -; Genomic_DNA.
DR   RefSeq; WP_011392398.1; NC_007644.1.
DR   RefSeq; YP_429739.1; NC_007644.1.
DR   AlphaFoldDB; Q2RK43; -.
DR   SMR; Q2RK43; -.
DR   STRING; 264732.Moth_0879; -.
DR   EnsemblBacteria; ABC19196; ABC19196; Moth_0879.
DR   KEGG; mta:Moth_0879; -.
DR   PATRIC; fig|264732.11.peg.943; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_2_0_9; -.
DR   OMA; FPTEREY; -.
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..307
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_1000000017"
SQ   SEQUENCE   307 AA;  33284 MW;  24971AEFA4F37868 CRC64;
     MRLQRKDLLG LKDLSAEEIE LILETAAPMK EILGRDIKKV PTLRGKLVVT MFYEPSTRTR
     TSFELAAKYM GADTMSIATA TSSVQKGESL RDTARTLAAM GTDAVIIRHS AAGSPALLAR
     TIEASVLNGG DGMHEHPTQA LLDMFTIKEK LGGFKGLKVA ILGDILHSRV ARSNIWGLTK
     MGAEVRVVGP ATLIPPEIEN LGVKVYYNAE EALKGVDVIN VLRIQRERQK KGLFPSLREY
     ARLYELTPER LKLARPGALV LHPGPMNRGI EIAPAVADGL QAAITEQVTN GVAVRMALLY
     LLIGGAN
 
 
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