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Database: UniProt
Entry: A3VB12_9RHOB
LinkDB: A3VB12_9RHOB
Original site: A3VB12_9RHOB 
ID   A3VB12_9RHOB            Unreviewed;       235 AA.
AC   A3VB12;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   13-SEP-2023, entry version 88.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200};
DE            EC=4.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01200};
DE   AltName: Full=OMP decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200};
DE            Short=OMPDCase {ECO:0000256|HAMAP-Rule:MF_01200};
DE            Short=OMPdecase {ECO:0000256|HAMAP-Rule:MF_01200};
GN   Name=pyrF {ECO:0000256|HAMAP-Rule:MF_01200};
GN   ORFNames=RB2654_15711 {ECO:0000313|EMBL:EAQ14130.1};
OS   Maritimibacter alkaliphilus HTCC2654.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Maritimibacter.
OX   NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ14130.1, ECO:0000313|Proteomes:UP000002931};
RN   [1] {ECO:0000313|EMBL:EAQ14130.1, ECO:0000313|Proteomes:UP000002931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ14130.1,
RC   ECO:0000313|Proteomes:UP000002931};
RX   PubMed=20729358; DOI=10.1128/JB.00873-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT   alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT   genera.";
RL   J. Bacteriol. 192:5552-5553(2010).
CC   -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC       (OMP) to uridine 5'-monophosphate (UMP).
CC       {ECO:0000256|ARBA:ARBA00002356, ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00001419, ECO:0000256|HAMAP-
CC         Rule:MF_01200, ECO:0000256|RuleBase:RU000512};
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_01200, ECO:0000256|RuleBase:RU000512}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01200}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01200}.
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:EAQ14130.1}.
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DR   EMBL; AAMT01000002; EAQ14130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3VB12; -.
DR   STRING; 314271.RB2654_15711; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_067069_1_0_5; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000002931; 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_01200_B; OMPdecase_type1_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR047596; OMPdecase_bac.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR01740; pyrF; 1.
DR   PANTHER; PTHR32119; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR32119:SF2; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_01200};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01200};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01200}; Reference proteome {ECO:0000313|Proteomes:UP000002931}.
FT   DOMAIN          11..230
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        69
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         67..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
SQ   SEQUENCE   235 AA;  24614 MW;  883386108BD9B7BC CRC64;
     MAENMTKTDD RLIVALDVPN ALAGLELAQR LGDPVGFYKI GLGMLTGGGL ALARELIDGM
     DKRIFLDMKL FDIGNTVEAA VRGLANYGLD FLTVHGDPHV VRAAQEGKGA SDLKILAVTI
     LTSLDRADLD DMLMSQGDVQ DIVVERARRA MAAGADGVIA SPHEAALIRA LPEASGKLIV
     TPGVRPQGAE TGDQKRIATP EKAISDGADH IVVGRPIKSA PDPRAAAEAI LASLP
//
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