PYRF_METJA
ID PYRF_METJA Reviewed; 213 AA.
AC Q57700;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200};
DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200};
DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200};
GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200}; OrderedLocusNames=MJ0252;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP-
CC Rule:MF_01200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01200};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB98239.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB98239.1; ALT_INIT; Genomic_DNA.
DR PIR; E64331; E64331.
DR RefSeq; WP_064496436.1; NC_000909.1.
DR PDB; 4LUI; X-ray; 1.60 A; A/B=1-213.
DR PDB; 4LUJ; X-ray; 1.60 A; A/B=1-213.
DR PDBsum; 4LUI; -.
DR PDBsum; 4LUJ; -.
DR AlphaFoldDB; Q57700; -.
DR SMR; Q57700; -.
DR STRING; 243232.MJ_0252; -.
DR EnsemblBacteria; AAB98239; AAB98239; MJ_0252.
DR GeneID; 1451106; -.
DR KEGG; mja:MJ_0252; -.
DR eggNOG; arCOG00081; Archaea.
DR HOGENOM; CLU_067069_2_0_2; -.
DR InParanoid; Q57700; -.
DR OMA; EMSHPGA; -.
DR OrthoDB; 54384at2157; -.
DR PhylomeDB; Q57700; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase 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 Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01200_A; OMPdecase_type1_A; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyrimidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..213
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134610"
FT ACT_SITE 61
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 59..68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 166..176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:4LUI"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:4LUI"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 34..38
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:4LUI"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:4LUI"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:4LUI"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:4LUI"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:4LUI"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:4LUI"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:4LUI"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4LUJ"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4LUI"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:4LUI"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:4LUI"
SQ SEQUENCE 213 AA; 23592 MW; 0B073BE37D50C556 CRC64;
MPKLMLALDV LDRDRALKIV EDVKDYVDAI KVGYPLVLST GTEIIKEIKK LCNKEVIADF
KVADIPATNE KIAKITLKYA DGIIVHGFVG EDSVKAVQDV AKKLNKKVIM VTEMSHPGAV
QFLQPIADKL SEMAKKLKVD AIVAPSTRPE RLKEIKEIAE LPVITPGVGA QGGKIEDILN
ILDENDYVIV GRAIYQSQNP KEEAKKYKEM LNK
