(data stored in ACNUC7421 zone)

SWISSPROT: A4ATB0_MARSH

ID   A4ATB0_MARSH            Unreviewed;       213 AA.
AC   A4ATB0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=Orotate phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS00615437};
DE            Short=OPRT {ECO:0000256|HAMAP-Rule:MF_01208};
DE            Short=OPRTase {ECO:0000256|HAMAP-Rule:MF_01208};
DE            EC=2.4.2.10 {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS00345661};
GN   Name=pyrE {ECO:0000256|HAMAP-Rule:MF_01208};
GN   OrderedLocusNames=FB2170_16386 {ECO:0000313|EMBL:EAR00680.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00680.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00680.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from
CC       5-phosphoribose 1-diphosphate to orotate, leading to the formation
CC       of orotidine monophosphate (OMP). {ECO:0000256|HAMAP-
CC       Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
CC         ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
CC         ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
CC         ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01208};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from orotate: step 1/2. {ECO:0000256|HAMAP-
CC       Rule:MF_01208, ECO:0000256|SAAS:SAAS00015801}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01208,
CC       ECO:0000256|SAAS:SAAS00216311}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. PyrE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS00541116}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01208}.
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DR   EMBL; CP002157; EAR00680.1; -; Genomic_DNA.
DR   RefSeq; WP_013304483.1; NC_014472.1.
DR   STRING; 313603.FB2170_16386; -.
DR   EnsemblBacteria; EAR00680; EAR00680; FB2170_16386.
DR   KEGG; fbc:FB2170_16386; -.
DR   eggNOG; ENOG4107RIV; Bacteria.
DR   eggNOG; COG0461; LUCA.
DR   HOGENOM; HOG000037975; -.
DR   KO; K00762; -.
DR   OMA; HAAWVSE; -.
DR   OrthoDB; 1280396at2; -.
DR   BioCyc; MSP313603:G1GNS-56-MONOMER; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   HAMAP; MF_01208; PyrE; 1.
DR   InterPro; IPR023031; OPRT.
DR   InterPro; IPR004467; Or_phspho_trans_dom.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR00336; pyrE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4ATB0.
DR   SWISS-2DPAGE; A4ATB0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00423761, ECO:0000313|EMBL:EAR00680.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01208};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00423725};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00423769, ECO:0000313|EMBL:EAR00680.1}.
FT   DOMAIN       55    148       Pribosyltran. {ECO:0000259|Pfam:PF00156}.
FT   REGION      126    134       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01208}.
FT   BINDING     100    100       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     104    104       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     106    106       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     130    130       Orotate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01208}.
SQ   SEQUENCE   213 AA;  23941 MW;  062114C8333C1ADC CRC64;
     MVLDKNTAKK TAELLLQINA IKLNPENPFT WASGWKSPIY CDNRIILSYT MIRNFVREEM
     AKQVENLYGK PDVIAGVATG AIGIGALVAD YMGLPFIYVR PEPKSHGRQN QIEGYLEPNQ
     TVVVIEDLIS TGKSSLNAVD ALEASQANIK GMLAIFTYGF DVADANFAEK KLELHTLSDY
     NHLIEQASET GYIKEEQLKT LMEWRKKPSE WQQ
//

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