(data stored in SCRATCH zone)

SWISSPROT: A8FQ69_SHESH

ID   A8FQ69_SHESH            Unreviewed;       213 AA.
AC   A8FQ69;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 77.
DE   RecName: Full=Orotate phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS00634338};
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   OrderedLocusNames=Ssed_0379 {ECO:0000313|EMBL:ABV34992.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34992.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34992.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34992.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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:SAAS00682396}.
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};
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}.
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DR   EMBL; CP000821; ABV34992.1; -; Genomic_DNA.
DR   RefSeq; WP_012140730.1; NC_009831.1.
DR   ProteinModelPortal; A8FQ69; -.
DR   STRING; 425104.Ssed_0379; -.
DR   EnsemblBacteria; ABV34992; ABV34992; Ssed_0379.
DR   KEGG; sse:Ssed_0379; -.
DR   eggNOG; ENOG4107QP2; Bacteria.
DR   eggNOG; COG0461; LUCA.
DR   HOGENOM; HOG000037974; -.
DR   KO; K00762; -.
DR   OMA; MKAYQRQ; -.
DR   OrthoDB; POG091H034Q; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000002015; Chromosome.
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   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; A8FQ69.
DR   SWISS-2DPAGE; A8FQ69.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00805817, ECO:0000313|EMBL:ABV34992.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01208};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00805821};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00805823, ECO:0000313|EMBL:ABV34992.1}.
FT   DOMAIN       43    160       Pribosyltran. {ECO:0000259|Pfam:PF00156}.
FT   REGION       34     35       Orotate binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01208}.
FT   REGION       72     73       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01208}.
FT   REGION      124    132       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01208}.
FT   BINDING      26     26       5-phosphoribose 1-diphosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01208}.
FT   BINDING      99     99       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     100    100       5-phosphoribose 1-diphosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01208}.
FT   BINDING     103    103       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     105    105       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     128    128       Orotate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01208}.
FT   BINDING     156    156       Orotate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01208}.
SQ   SEQUENCE   213 AA;  23600 MW;  7D0A0B60F9D5213B CRC64;
     MKAYQREFIE FALERQVLRF GEFTLKSGRT SPYFFNAGLF NTGRDLARLG RFYAAALVDS
     GIKHDLLFGP AYKGIPIATT TAVALCEHHD IDIPYCFNRK EKKDHGEGGS LVGSELKGRV
     MLVDDVITAG TAIRESMEII EAHKAELAGV LIALDRQEKG KGELSAIQEV ERDFGCEIVS
     IIKLGDLINY LSEKSGMEAQ LESVSAYRDQ YGI
//

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