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Database: UniProt
Entry: D9TNT3_THETC
LinkDB: D9TNT3_THETC
Original site: D9TNT3_THETC 
ID   D9TNT3_THETC            Unreviewed;       306 AA.
AC   D9TNT3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=Tthe_1542 {ECO:0000313|EMBL:ADL69052.1};
OS   Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 /
OS   NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium
OS   thermosaccharolyticum).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=580327 {ECO:0000313|EMBL:ADL69052.1, ECO:0000313|Proteomes:UP000001626};
RN   [1] {ECO:0000313|EMBL:ADL69052.1, ECO:0000313|Proteomes:UP000001626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM
RC   00135 / 2032 {ECO:0000313|Proteomes:UP000001626};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM
RT   571.";
RL   Submitted (AUG-2010) 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; CP002171; ADL69052.1; -; Genomic_DNA.
DR   RefSeq; WP_013298019.1; NC_014410.1.
DR   AlphaFoldDB; D9TNT3; -.
DR   STRING; 580327.Tthe_1542; -.
DR   KEGG; ttm:Tthe_1542; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_1_1_9; -.
DR   OMA; QSAFFER; -.
DR   OrthoDB; 9808470at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000001626; 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:UP000001626}.
FT   DOMAIN          16..273
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   306 AA;  34238 MW;  D24EAA3FE121902C CRC64;
     MFSDKLINAI KSKNNPTVVG LDPRIESIPE FIKEITFKKY GNNVKGISEA IYYFNKGIID
     SIFDVVPAVK IQVAFYEVYG PDGFDIFFKT AEYAKEKGLM VIADVKRGDI ADVAEMYSKA
     YLQNEYIDAI TVNPYMGEDT ITPYIHDVIE HEKGLFILVK TSNKGSYTIQ NLETENGTVY
     ENVANMVNKI SNLVKGKLGY SSIGAVVGAT HKEEAKILRE KMPSAIFLVP GYGAQGATAE
     DVTNCFDENN LGAIVNSSRK VIFAYKSQYW KDVYSEYEYA QAARSEVVLM RGMINNALLK
     RKYIAC
//
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