GenomeNet

Database: UniProt
Entry: C0C457_9FIRM
LinkDB: C0C457_9FIRM
Original site: C0C457_9FIRM 
ID   C0C457_9FIRM            Unreviewed;       308 AA.
AC   C0C457;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
DE            EC=4.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01215};
DE   AltName: Full=OMP decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
DE            Short=OMPDCase {ECO:0000256|HAMAP-Rule:MF_01215};
DE            Short=OMPdecase {ECO:0000256|HAMAP-Rule:MF_01215};
GN   Name=pyrF {ECO:0000256|HAMAP-Rule:MF_01215,
GN   ECO:0000313|EMBL:EEG72850.1};
GN   ORFNames=CLOHYLEM_06872 {ECO:0000313|EMBL:EEG72850.1};
OS   [Clostridium] hylemonae DSM 15053.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=553973 {ECO:0000313|EMBL:EEG72850.1, ECO:0000313|Proteomes:UP000004893};
RN   [1] {ECO:0000313|EMBL:EEG72850.1, ECO:0000313|Proteomes:UP000004893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG72850.1,
RC   ECO:0000313|Proteomes:UP000004893};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium hylemonae (DSM 15053).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG72850.1, ECO:0000313|Proteomes:UP000004893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG72850.1,
RC   ECO:0000313|Proteomes:UP000004893};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001419, ECO:0000256|HAMAP-
CC         Rule:MF_01215};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861,
CC       ECO:0000256|HAMAP-Rule:MF_01215}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008847, ECO:0000256|HAMAP-Rule:MF_01215}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEG72850.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABYI02000034; EEG72850.1; -; Genomic_DNA.
DR   RefSeq; WP_006444229.1; NZ_GG657760.1.
DR   AlphaFoldDB; C0C457; -.
DR   STRING; 553973.CLOHYLEM_06872; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_1_1_9; -.
DR   OrthoDB; 9808470at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000004893; Unassembled WGS sequence.
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   CDD; cd04725; OMP_decarboxylase_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01215; OMPdecase_type2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011995; OMPdecase_type-2.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR02127; pyrF_sub2; 1.
DR   PANTHER; PTHR43375; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43375:SF1; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01215};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01215}.
FT   DOMAIN          15..281
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        105
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   308 AA;  33318 MW;  62A9EAAE955EB85A CRC64;
     MINQLVSNIK KTGAPVVVGL DPMLSYIPEH VQKKAFAEYG ETLEGAAEAI WQFNKAIVDS
     TCDLIPAVKP QIAMYEQFGI PGLAAFRRTT EYCKEKGLVV IGDIKRGDIG STSKAYAVGH
     LGKVQVGNNT CVPFDEDFVT VNPYLGSDGV DPFLEVCREE KKGVFVLVKT SNPSSGEFQD
     QLVGGRPLYE LVGEKVAAWG EELMGDDYSY VGAVVGATYP EMGKALRAVM PKAYILVPGY
     GAQGGRGKDL VHFFNEDGLG AIVNSSRGII AAYRQEQYAR FGEANFADAS RAAVEDMIKD
     IKGALEHE
//
DBGET integrated database retrieval system