(data stored in ACNUC7421 zone)

SWISSPROT: D4YYS0_SPHJU

ID   D4YYS0_SPHJU            Unreviewed;       193 AA.
AC   D4YYS0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   RecName: Full=Orotate phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS00727964};
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:SAAS00805816};
GN   Name=pyrE {ECO:0000256|HAMAP-Rule:MF_01208,
GN   ECO:0000313|EMBL:BAI95502.1};
GN   OrderedLocusNames=SJA_C1-06680 {ECO:0000313|EMBL:BAI95502.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95502.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95502.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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:SAAS00763393}.
CC   -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate
CC       + 5-phospho-alpha-D-ribose 1-diphosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01208, ECO:0000256|SAAS:SAAS00805810}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01208, ECO:0000256|SAAS:SAAS00763397};
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:SAAS00805820}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01208,
CC       ECO:0000256|SAAS:SAAS00805815}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. PyrE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS00805822}.
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; AP010803; BAI95502.1; -; Genomic_DNA.
DR   RefSeq; WP_013039196.1; NC_014006.1.
DR   ProteinModelPortal; D4YYS0; -.
DR   STRING; 452662.SJA_C1-06680; -.
DR   EnsemblBacteria; BAI95502; BAI95502; SJA_C1-06680.
DR   GeneID; 29272341; -.
DR   KEGG; sjp:SJA_C1-06680; -.
DR   eggNOG; ENOG4107VCP; Bacteria.
DR   eggNOG; COG0461; LUCA.
DR   HOGENOM; HOG000059806; -.
DR   KO; K00762; -.
DR   OMA; YFQCAKV; -.
DR   OrthoDB; POG091H034Q; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   HAMAP; MF_01208; PyrE; 1.
DR   InterPro; IPR023031; OPRT.
DR   InterPro; IPR006273; Orotate_PRibTrfase_bac.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01367; pyrE_Therm; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYS0.
DR   SWISS-2DPAGE; D4YYS0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00805817, ECO:0000313|EMBL:BAI95502.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00763396};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00805821};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00805823, ECO:0000313|EMBL:BAI95502.1}.
FT   DOMAIN       48    172       Pribosyltran. {ECO:0000259|Pfam:PF00156}.
FT   REGION      117    125       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01208}.
FT   BINDING      94     94       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     121    121       Orotate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01208}.
FT   BINDING     149    149       Orotate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01208}.
SQ   SEQUENCE   193 AA;  20831 MW;  C6E9FF2E1526F909 CRC64;
     MTDEEVLAEF RAAGALLEGH FILSSGRRSA NYLQCARVLM NAERAGRLAR ATVQKLPREL
     RQEIDLVVSP AMGGLIIGHE IGRALDKDAV FLERPEGRFE LRRGFSIAPG QKVLMVEDVV
     TTGLSSRQAI EAVAAEGGIV IAEATLVDRS AGEVELGVPF YPLVSINFPV YDADQIPPEL
     AAIPAIKPGS RKQ
//

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