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Database: UniProt
Entry: I3Z4G8_BELBD
LinkDB: I3Z4G8_BELBD
Original site: I3Z4G8_BELBD 
ID   I3Z4G8_BELBD            Unreviewed;       279 AA.
AC   I3Z4G8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
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   OrderedLocusNames=Belba_1524 {ECO:0000313|EMBL:AFL84136.1};
OS   Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Belliella.
OX   NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL84136.1, ECO:0000313|Proteomes:UP000006050};
RN   [1] {ECO:0000313|Proteomes:UP000006050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC   {ECO:0000313|Proteomes:UP000006050};
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA   Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA   Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Belliella baltica DSM 15883.";
RL   Submitted (JUN-2012) 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}.
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DR   EMBL; CP003281; AFL84136.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3Z4G8; -.
DR   STRING; 866536.Belba_1524; -.
DR   KEGG; bbd:Belba_1524; -.
DR   PATRIC; fig|866536.3.peg.1580; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_1_0_10; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000006050; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006050}.
FT   DOMAIN          23..259
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        100
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   279 AA;  30948 MW;  F339DC3242B65682 CRC64;
     MPKSNRGMNK AELFDQIKQK SSFLCVGLDT DLTKIPQHLR KNSDPLFEFN KQIIDATADL
     AIAYKPNIAF YEALGPKGWE SLQKTLEYIP NDIFTIADAK RGDIGNTSSL YAKAFFETMD
     FDSITVAPYM GVDSVKPFLT FEGKWVILLA LTSNEGSLDF QLIASKSGKP LFQEVLEKSQ
     LWGNTDNMMY VVGATRGEKI AEVRQIVPEH FFLVPGVGAQ GGSLEEVAKF GMNATCGLLV
     NSSRGIIYAS QEKDFAAAAK VEAMKLQQEM SELLDKYCY
//
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