ID PYRF_TERTT Reviewed; 232 AA.
AC C5BSJ7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 01-MAY-2013, entry version 29.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23;
DE AltName: Full=OMP decarboxylase;
DE Short=OMPDCase;
DE Short=OMPdecase;
GN Name=pyrF; OrderedLocusNames=TERTU_1389;
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadales genera incertae sedis; Teredinibacter.
OX NCBI_TaxID=377629;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901;
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G.,
RA Elshahawi S., Hanora A., Schmidt E.W., Haygood M.G., Posfai J.,
RA Benner J., Madinger C., Nove J., Anton B., Chaudhary K., Foster J.,
RA Holman A., Kumar S., Lessard P.A., Luyten Y.A., Slatko B., Wood N.,
RA Wu B., Teplitski M., Mougous J.D., Ward N., Eisen J.A., Badger J.H.,
RA Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an
RT intracellular endosymbiont of marine wood-boring bivalves
RT (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-
CC monophosphate (OMP) to uridine 5'-monophosphate (UMP) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2).
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; UMP from orotate: step 2/2.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1
CC subfamily.
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DR EMBL; CP001614; ACR14352.1; -; Genomic_DNA.
DR RefSeq; YP_003072943.1; NC_012997.1.
DR ProteinModelPortal; C5BSJ7; -.
DR STRING; 377629.TERTU_1389; -.
DR EnsemblBacteria; ACR14352; ACR14352; TERTU_1389.
DR GeneID; 8211070; -.
DR KEGG; ttu:TERTU_1389; -.
DR PATRIC; 23869929; VBITerTur118718_1309.
DR eggNOG; COG0284; -.
DR HOGENOM; HOG000226071; -.
DR KO; K01591; -.
DR OMA; NFKIFLD; -.
DR ProtClustDB; PRK00230; -.
DR UniPathway; UPA00070; UER00120.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:HAMAP.
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_B; OMPdecase_type1_B; 1; -.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; RibP_bind_barrel; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT CHAIN 1 232 Orotidine 5'-phosphate decarboxylase.
FT /FTId=PRO_1000213827.
FT REGION 62 71 Substrate binding (By similarity).
FT ACT_SITE 64 64 Proton donor (By similarity).
FT BINDING 13 13 Substrate (By similarity).
FT BINDING 35 35 Substrate (By similarity).
FT BINDING 121 121 Substrate (By similarity).
FT BINDING 182 182 Substrate (By similarity).
FT BINDING 191 191 Substrate (By similarity).
FT BINDING 211 211 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 212 212 Substrate (By similarity).
SQ SEQUENCE 232 AA; 24322 MW; A5E2A30AC6B5475A CRC64;
MSVTGPQLLV AMDFNDINDC LALACQLDPQ SCRLKIGKEL FTTAGPAVVE SVQKLGFDVF
LDLKFHDIPN TVAGAVKAAA NMGVWMVNVH ASGGQRMMEA ARESLVLFSH KPLLIAVTVL
TSMDQSDLNG IGITESPEAM VARLASLAKL SGMDGVVCSA LEAGAMKVQQ GADFLTITPG
IRPASTEAGD QRRVVTPEQA IANGSDFIVV GRPITQAEDP AAACAQIVNS IQ
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