PYRF_ARCFU
ID PYRF_ARCFU Reviewed; 209 AA.
AC O29333;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 120.
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=AF_0929;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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=AAB90309.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000782; AAB90309.1; ALT_INIT; Genomic_DNA.
DR PIR; A69366; A69366.
DR RefSeq; WP_048064309.1; NC_000917.1.
DR PDB; 4MUZ; X-ray; 1.39 A; A/B=1-209.
DR PDB; 4N2Y; X-ray; 1.55 A; A/B/C/D=1-209.
DR PDBsum; 4MUZ; -.
DR PDBsum; 4N2Y; -.
DR AlphaFoldDB; O29333; -.
DR SMR; O29333; -.
DR STRING; 224325.AF_0929; -.
DR EnsemblBacteria; AAB90309; AAB90309; AF_0929.
DR GeneID; 1484152; -.
DR KEGG; afu:AF_0929; -.
DR eggNOG; arCOG00081; Archaea.
DR HOGENOM; CLU_067069_2_0_2; -.
DR OMA; EMSHPGA; -.
DR OrthoDB; 54384at2157; -.
DR PhylomeDB; O29333; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-UniRule.
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 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyrimidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..209
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134608"
FT ACT_SITE 59
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 57..66
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 114
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 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:4MUZ"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:4MUZ"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:4MUZ"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:4MUZ"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:4MUZ"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:4MUZ"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:4MUZ"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:4N2Y"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:4MUZ"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:4MUZ"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:4MUZ"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:4MUZ"
SQ SEQUENCE 209 AA; 22538 MW; C6CBB39E9C105B66 CRC64;
MKQLILALDV MDGEKAMEIA KKVAEHVDRI KVNYPLVLSA GVGIMKRLSE IKPVIADFKI
ADVPYTSSLI ARIAFENSAE SVIVHGFVGS DTLREVCRVA EEFGGKVYAV TELSSPGGEE
FMSAVSLKIV EKAKEAGCHG LIAPSTRIER LREIRKAAGD MEILCPGIGA QKGSIEAVKY
ADGIIVGRGI YASGNPAEEA RKLRRVLKI
