(data stored in ACNUC7421 zone)

SWISSPROT: A1AY33_PARDP

ID   A1AY33_PARDP            Unreviewed;       234 AA.
AC   A1AY33;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 98.
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   OrderedLocusNames=Pden_0060 {ECO:0000313|EMBL:ABL68177.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68177.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-
CC       monophosphate (OMP) to uridine 5'-monophosphate (UMP).
CC       {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|SAAS:SAAS01083804}.
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|HAMAP-Rule:MF_01200,
CC         ECO:0000256|RuleBase:RU000512};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from orotate: step 2/2. {ECO:0000256|HAMAP-
CC       Rule:MF_01200, ECO:0000256|RuleBase:RU000512}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01200,
CC       ECO:0000256|SAAS:SAAS01083803}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01200,
CC       ECO:0000256|SAAS:SAAS01083813}.
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DR   EMBL; CP000489; ABL68177.1; -; Genomic_DNA.
DR   RefSeq; WP_011746410.1; NC_008686.1.
DR   STRING; 318586.Pden_0060; -.
DR   PRIDE; A1AY33; -.
DR   EnsemblBacteria; ABL68177; ABL68177; Pden_0060.
DR   KEGG; pde:Pden_0060; -.
DR   eggNOG; ENOG4106EG9; Bacteria.
DR   eggNOG; COG0284; LUCA.
DR   HOGENOM; HOG000226070; -.
DR   KO; K01591; -.
DR   OMA; NFKIFLD; -.
DR   BioCyc; PDEN318586:G1GW1-61-MONOMER; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000000361; Chromosome 1.
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   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   PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR01740; pyrF; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AY33.
DR   SWISS-2DPAGE; A1AY33.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200,
KW   ECO:0000256|RuleBase:RU000512};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|RuleBase:RU000512,
KW   ECO:0000313|EMBL:ABL68177.1};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01200,
KW   ECO:0000256|RuleBase:RU000512};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT   DOMAIN        8    227       OMPdecase. {ECO:0000259|SMART:SM00934}.
FT   REGION       64     73       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01200}.
FT   ACT_SITE     66     66       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING      14     14       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING      36     36       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING     119    119       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING     182    182       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING     191    191       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
FT   BINDING     211    211       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01200}.
FT   BINDING     212    212       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01200}.
SQ   SEQUENCE   234 AA;  23992 MW;  6CC50CEA7F07ACEB CRC64;
     MTQTPDERLI VALDVPNALA GLELAEKIGD AAGFYKIGLG MLTGGGLALA NELKQEHGKR
     IFLDMKFFDI GATVEAAVRG IAQYDLDFLT VHGDPHVVRA AKQGASGSGL KILAVTILTS
     LDRADLDAGL IVPGDVAEIV ATRAARAFEA GADGIIASPR EAAAIRALPE AAGRLIVTPG
     VRPAGSDAGD QKRIETPATA IANGADHIVV GRPIWQAADP RAAAQAIAAE LAGL
//

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