PYRB_TREDE
ID PYRB_TREDE Reviewed; 535 AA.
AC Q04595;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 142.
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; Synonyms=pyrB; OrderedLocusNames=TDE_0129;
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33520 / W / CIP 103917;
RX PubMed=1444372; DOI=10.1128/aem.58.10.3399-3403.1992;
RA Ishihara K., Ishihara M., Takazoe I., Okuda K.;
RT "Cloning and expression of the aspartate carbamoyltransferase gene from
RT Treponema denticola.";
RL Appl. Environ. Microbiol. 58:3399-3403(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00941.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D10052; BAA00941.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE017226; AAS10627.1; -; Genomic_DNA.
DR PIR; A48948; A48948.
DR RefSeq; NP_970746.1; NC_002967.9.
DR RefSeq; WP_002666669.1; NC_002967.9.
DR AlphaFoldDB; Q04595; -.
DR SMR; Q04595; -.
DR STRING; 243275.TDE_0129; -.
DR EnsemblBacteria; AAS10627; AAS10627; TDE_0129.
DR GeneID; 2739612; -.
DR KEGG; tde:TDE_0129; -.
DR PATRIC; fig|243275.7.peg.129; -.
DR eggNOG; COG0540; Bacteria.
DR eggNOG; COG1781; Bacteria.
DR HOGENOM; CLU_039403_0_0_12; -.
DR OMA; QAINGYW; -.
DR OrthoDB; 477078at2; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000008212; Chromosome.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
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 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 PRINTS; PR00100; AOTCASE.
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..535
FT /note="Protein PyrBI"
FT /id="PRO_0000113241"
FT REGION 1..341
FT /note="Aspartate carbamoyltransferase"
FT REGION 342..370
FT /note="Linker"
FT REGION 371..535
FT /note="Aspartate carbamoyltransferase regulatory region"
FT BINDING 488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 117
FT /note="K -> E (in Ref. 1; BAA00941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 61944 MW; 15BDF8A8F5D57A81 CRC64;
MENKFMGRSL TVIDDLSIDE RKYLFDKTKR LKKAIQEDDQ KVMDEFRIND KDFGIYEVFL
EPSTRTKESF RNAAKFHQVK LSDLAAESSS FNKGESYADT FNTLAGYQNS IFIVRSKVEG
VCRWLEDEAQ AFYQRNNLKR KPAFINAGDG KHEHPTQELL DEFTFIEDNN WSFDKIHIAL
VGDLYHGRTV HSKADGLKIF KSVKVDLIAP AELAMPEYYK VRMQENGFTV REFSSIEEYL
RQADVALIWY FTRPQLERMG EQVLKKQDEL RRSITFRKEF IEKLPENTRF YHPLPRHRVH
PTIPTFLDAT PLNGWERQSI NGMYVRMVLL SMIAGKIGDD YKGPEPKSCE RVEDEDYIVE
VPINNSKESK VETFSEGVRP IQNGIVIDHI CRGDKPSVIR HHMSKIINVM GLEEGKGGEW
VSTSTKDKGT FKGIIFRPGE YKFSRADLKR LSAVASSCTL NLIKDGKIQS KYRTHLPPRI
YNFEDLICKN EACISHPAQS EGVPAIFYRT IDNRYACQYC GTIHTFKEIW GEKKN
