PYRB_THEMA
ID PYRB_THEMA Reviewed; 527 AA.
AC P96111;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein PyrBI;
DE Includes:
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2;
DE AltName: Full=Aspartate transcarbamylase;
DE Short=ATCase;
DE Includes:
DE RecName: Full=Aspartate carbamoyltransferase regulatory region;
GN Name=pyrBI; OrderedLocusNames=TM_1642;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RA van de Casteele M.F.J., Chen P., van Vliet F., Legrain C., Cunin R.,
RA Glansdorff N.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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: In the N-terminal section; belongs to the
CC aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PyrI family.
CC {ECO:0000305}.
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DR EMBL; Y10300; CAA71345.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36709.1; -; Genomic_DNA.
DR PIR; B72231; B72231.
DR RefSeq; NP_229442.1; NC_000853.1.
DR RefSeq; WP_004082131.1; NZ_CP011107.1.
DR AlphaFoldDB; P96111; -.
DR SMR; P96111; -.
DR STRING; 243274.THEMA_06035; -.
DR PRIDE; P96111; -.
DR EnsemblBacteria; AAD36709; AAD36709; TM_1642.
DR KEGG; tma:TM1642; -.
DR eggNOG; COG0540; Bacteria.
DR eggNOG; COG1781; Bacteria.
DR InParanoid; P96111; -.
DR OMA; QAINGYW; -.
DR OrthoDB; 477078at2; -.
DR BioCyc; MetaCyc:MON-503; -.
DR BRENDA; 2.1.3.2; 6331.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.70.140; -; 1.
DR Gene3D; 3.40.50.1370; -; 2.
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 InterPro; IPR020545; Asp_carbamoyltransf_reg_N.
DR InterPro; IPR020542; Asp_carbamoyltrfase_reg_C.
DR InterPro; IPR036792; Asp_carbatrfase_reg_C_sf.
DR InterPro; IPR036793; Asp_carbatrfase_reg_N_sf.
DR PANTHER; PTHR11405:SF16; PTHR11405:SF16; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR Pfam; PF01948; PyrI; 1.
DR Pfam; PF02748; PyrI_C; 1.
DR SUPFAM; SSF53671; SSF53671; 1.
DR SUPFAM; SSF54893; SSF54893; 1.
DR SUPFAM; SSF57825; SSF57825; 1.
DR TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 3: Inferred from homology;
KW Metal-binding; Multifunctional enzyme; Pyrimidine biosynthesis;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..527
FT /note="Protein PyrBI"
FT /id="PRO_0000113240"
FT REGION 1..342
FT /note="Aspartate carbamoyltransferase"
FT REGION 343..357
FT /note="Linker"
FT REGION 368..527
FT /note="Aspartate carbamoyltransferase regulatory region"
FT BINDING 483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 525..527
FT /note="WSI -> T (in Ref. 1; CAA71345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 60772 MW; 24BBF883B3BFC03D CRC64;
MKRDFLGRTL AVIEDLSVEE QMFLYEKTRE LKQRWYSGED VSDFRIKKRN VGIYIVFVEP
STRTKESFIN AAKFHSGPNV KVNVFDSEHS SFNKQESYTD TFSMLTGYSD YSIFVVRTRL
EGVCRLLERR ISEFASRNGI EVPSFINAGD GKHEHPTQEL LDEYTFLEQN GFDNSFIHVA
LVGDLLHGRT VHSKVNGLKI FKNVKVDLVA PEELMMPEHY VEKMKKNGFE VRIFSSIREY
LDQKDVAKIW YFTRLQLERM GEDILEKVHV LREAVTFKKE YLDALPEGVK FYHPLPRHKV
YPTIPNFLDT LPLNGWETQA RNGYWVRIVL LSMFGGALEA PFDTSKKEEK PEEDFIIPAP
ITHGSKGVQK EGKRGIKPIE NGTVIDHIAK GKTPEEIYST ILKIRKILRL YDVDSADGIF
RSSDGSFKGY ISLPDRYLSK KEIKKLSAIS PNTTVNIIKN STVVEKYRIK LPPTIYGFEE
LRCKNENCIT NPAHGENASP SFVRNEKGQF ICEYCETPHS FEEIWSI
