PYRE_VIBCH
ID PYRE_VIBCH Reviewed; 213 AA.
AC Q9KVD5;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01208};
DE Short=OPRT {ECO:0000255|HAMAP-Rule:MF_01208};
DE Short=OPRTase {ECO:0000255|HAMAP-Rule:MF_01208};
DE EC=2.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01208};
GN Name=pyrE {ECO:0000255|HAMAP-Rule:MF_01208}; OrderedLocusNames=VC_0211;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-
CC phosphoribose 1-diphosphate to orotate, leading to the formation of
CC orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
CC ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
CC ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
CC ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01208};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01208};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {ECO:0000255|HAMAP-Rule:MF_01208}.
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DR EMBL; AE003852; AAF93387.1; -; Genomic_DNA.
DR PIR; E82350; E82350.
DR RefSeq; NP_229868.2; NC_002505.1.
DR RefSeq; WP_001884129.1; NZ_LT906614.1.
DR PDB; 3N2L; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-213.
DR PDBsum; 3N2L; -.
DR AlphaFoldDB; Q9KVD5; -.
DR SMR; Q9KVD5; -.
DR STRING; 243277.VC_0211; -.
DR DNASU; 2614710; -.
DR EnsemblBacteria; AAF93387; AAF93387; VC_0211.
DR GeneID; 57738948; -.
DR KEGG; vch:VC_0211; -.
DR PATRIC; fig|243277.26.peg.192; -.
DR eggNOG; COG0461; Bacteria.
DR HOGENOM; CLU_074878_0_1_6; -.
DR OMA; MKAYQRQ; -.
DR UniPathway; UPA00070; UER00119.
DR EvolutionaryTrace; Q9KVD5; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0046132; P:pyrimidine ribonucleoside biosynthetic process; IBA:GO_Central.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01208; PyrE; 1.
DR InterPro; IPR023031; OPRT.
DR InterPro; IPR004467; Or_phspho_trans_dom.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00336; pyrE; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Magnesium; Pyrimidine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..213
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_0000110765"
FT BINDING 26
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 34..35
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 72..73
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 99
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 100
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 103
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 105
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 124..132
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 128
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 156
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:3N2L"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:3N2L"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3N2L"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3N2L"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3N2L"
FT HELIX 43..60
FT /evidence="ECO:0007829|PDB:3N2L"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3N2L"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:3N2L"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:3N2L"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3N2L"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:3N2L"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3N2L"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3N2L"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:3N2L"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:3N2L"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:3N2L"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:3N2L"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:3N2L"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:3N2L"
FT HELIX 197..211
FT /evidence="ECO:0007829|PDB:3N2L"
SQ SEQUENCE 213 AA; 23402 MW; 71A3E2A3451BEE82 CRC64;
MKAYQREFIE FALEKQVLKF GEFTLKSGRK SPYFFNAGLF NTGRDLARLG RFYAAALVDS
GIEFDVLFGP AYKGIPIATT TAVALADHHD VDTPYCFNRK EAKNHGEGGN LVGSKLEGRV
MLVDDVITAG TAIRESMELI QANKADLAGV LVAIDRQEKG KGELSAIQEV ERDFGCAVIS
IVSLTDLITY LEQQGNNTEH LEAVKAYRAQ YGI
