PYRB_YERPE
ID PYRB_YERPE Reviewed; 311 AA.
AC Q8ZB39; Q0WB65;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 143.
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};
GN OrderedLocusNames=YPO3588, y0161, YP_3842;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(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; 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 -!- SUBUNIT: Heterododecamer (2C3:3R2) of six catalytic PyrB chains
CC organized as two trimers (C3), and six regulatory PyrI chains organized
CC as three dimers (R2). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001}.
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DR EMBL; AL590842; CAL22175.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM83755.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS63988.1; -; Genomic_DNA.
DR PIR; AD0436; AD0436.
DR RefSeq; WP_002210111.1; NZ_WUCM01000032.1.
DR RefSeq; YP_002348473.1; NC_003143.1.
DR PDB; 3LXM; X-ray; 2.00 A; A/B/C=1-311.
DR PDBsum; 3LXM; -.
DR AlphaFoldDB; Q8ZB39; -.
DR SMR; Q8ZB39; -.
DR IntAct; Q8ZB39; 2.
DR STRING; 214092.YPO3588; -.
DR PaxDb; Q8ZB39; -.
DR DNASU; 1145108; -.
DR EnsemblBacteria; AAM83755; AAM83755; y0161.
DR EnsemblBacteria; AAS63988; AAS63988; YP_3842.
DR GeneID; 57975128; -.
DR KEGG; ype:YPO3588; -.
DR KEGG; ypk:y0161; -.
DR KEGG; ypm:YP_3842; -.
DR PATRIC; fig|214092.21.peg.4081; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_1_2_6; -.
DR OMA; GDGPNEH; -.
DR UniPathway; UPA00070; UER00116.
DR EvolutionaryTrace; Q8ZB39; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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: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; 3.40.50.1370; -; 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 1: Evidence at protein level;
KW 3D-structure; Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..311
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000113237"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:3LXM"
FT TURN 37..42
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3LXM"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:3LXM"
FT HELIX 286..305
FT /evidence="ECO:0007829|PDB:3LXM"
SQ SEQUENCE 311 AA; 34559 MW; FE76627210B30444 CRC64;
MANPLYHKHI ISINDLSRDE LELVLRTAAS LKKTPQPELL KHKVIASCFF EASTRTRLSF
ETSIHRLGAS VVGFSDSSNT SLGKKGETLA DTMSVISTYV DAIVMRHPQE GASRLAAQFS
GNVPIVNAGD GANQHPTQTL LDLFTIQETQ GRLDNINIAM VGDLKYGRTV HSLTQALAKF
NGNHFFFIAP DALAMPAYIL QMLEEKEIEY SLHESLEEVV PELDILYMTR VQKERLDPSE
YANVKAQFIL RSSDLTGARD NLKVLHPLPR IDEITTDVDK TPYAYYFQQA GNGIFARQAL
LALVLNAELA L
