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Database: UniProt
Entry: A9B2S5_HERA2
LinkDB: A9B2S5_HERA2
Original site: A9B2S5_HERA2 
ID   A9B2S5_HERA2            Unreviewed;       217 AA.
AC   A9B2S5;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Orotate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011971, ECO:0000256|HAMAP-Rule:MF_01208};
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|ARBA:ARBA00011971, ECO:0000256|HAMAP-Rule:MF_01208};
GN   Name=pyrE {ECO:0000256|HAMAP-Rule:MF_01208};
GN   OrderedLocusNames=Haur_2888 {ECO:0000313|EMBL:ABX05526.1};
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC   Herpetosiphonaceae; Herpetosiphon.
OX   NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX05526.1, ECO:0000313|Proteomes:UP000000787};
RN   [1] {ECO:0000313|Proteomes:UP000000787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95
RC   {ECO:0000313|Proteomes:UP000000787};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABX05526.1, ECO:0000313|Proteomes:UP000000787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95
RC   {ECO:0000313|Proteomes:UP000000787};
RX   PubMed=22675585; DOI=10.4056/sigs.2194987;
RA   Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A.,
RA   Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C.,
RA   Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA   Goker M., Woyke T., Klenk H.P., Bryant D.A.;
RT   "Complete genome sequence of the filamentous gliding predatory bacterium
RT   Herpetosiphon aurantiacus type strain (114-95(T)).";
RL   Stand. Genomic Sci. 5:356-370(2011).
CC   -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-
CC       phosphoribose 1-diphosphate to orotate, leading to the formation of
CC       orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208}.
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};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01208};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 1/2. {ECO:0000256|ARBA:ARBA00004889,
CC       ECO:0000256|HAMAP-Rule:MF_01208}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01208}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrE subfamily. {ECO:0000256|HAMAP-Rule:MF_01208}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01208}.
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DR   EMBL; CP000875; ABX05526.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9B2S5; -.
DR   STRING; 316274.Haur_2888; -.
DR   KEGG; hau:Haur_2888; -.
DR   eggNOG; COG0461; Bacteria.
DR   HOGENOM; CLU_074878_1_1_0; -.
DR   InParanoid; A9B2S5; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000000787; 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   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 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   NCBIfam; TIGR00336; pyrE; 1.
DR   PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000313|EMBL:ABX05526.1}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01208};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01208};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000313|EMBL:ABX05526.1}.
FT   DOMAIN          56..154
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   BINDING         97
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
FT   BINDING         101
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
FT   BINDING         123..131
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
FT   BINDING         127
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
SQ   SEQUENCE   217 AA;  23367 MW;  4CD32B7AB661A8B9 CRC64;
     MKHSSTAIAQ LLLEAGAVVL SPDRPFRFAS GILSPIYCDN RLLLAQVSAR RTITEAMCQQ
     ISDELLNTEV IAGTATAGVP WAAWVAHELS LPMAYVRSGA KKYGRGQQVE GGVQANQRVV
     VIEDLISTGG SSLDAVAGLR QINALVADCF AIFTYEMEES KQRFNAAGVR LMTLTNLSTL
     LDVAAQQNYI RAEHRSLISD WASDPAGWAD RAGISAE
//
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