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Database: UniProt
Entry: D5U5J7_BRAM5
LinkDB: D5U5J7_BRAM5
Original site: D5U5J7_BRAM5 
ID   D5U5J7_BRAM5            Unreviewed;       451 AA.
AC   D5U5J7;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01200, ECO:0000256|HAMAP-Rule:MF_01208};
DE   Includes:
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};
DE   Includes:
DE     RecName: Full=Orotate phosphoribosyltransferase {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|HAMAP-Rule:MF_01208};
GN   Name=pyrF {ECO:0000256|HAMAP-Rule:MF_01200};
GN   Synonyms=pyrE {ECO:0000256|HAMAP-Rule:MF_01208};
GN   OrderedLocusNames=Bmur_2403 {ECO:0000313|EMBL:ADG72474.1};
OS   Brachyspira murdochii (strain ATCC 51284 / DSM 12563 / 56-150) (Serpulina
OS   murdochii).
OC   Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC   Brachyspira.
OX   NCBI_TaxID=526224 {ECO:0000313|EMBL:ADG72474.1, ECO:0000313|Proteomes:UP000001915};
RN   [1] {ECO:0000313|EMBL:ADG72474.1, ECO:0000313|Proteomes:UP000001915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51284 / DSM 12563 / 56-150
RC   {ECO:0000313|Proteomes:UP000001915};
RX   PubMed=21304710; DOI=10.4056/sigs.831993;
RA   Pati A., Sikorski J., Gronow S., Munk C., Lapidus A., Copeland A.,
RA   Glavina Del Tio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA   Han C., Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Brachyspira murdochii type strain (56-150).";
RL   Stand. Genomic Sci. 2:260-269(2010).
CC   -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC       (OMP) to uridine 5'-monophosphate (UMP).
CC       {ECO:0000256|ARBA:ARBA00002356, ECO:0000256|HAMAP-Rule:MF_01200}.
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=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|ARBA:ARBA00001419, ECO:0000256|HAMAP-
CC         Rule:MF_01200};
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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861,
CC       ECO:0000256|HAMAP-Rule:MF_01200}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01200}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01200}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrE subfamily. {ECO:0000256|HAMAP-Rule:MF_01208}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the OMP decarboxylase
CC       family. {ECO:0000256|ARBA:ARBA00009769}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00006221}.
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; CP001959; ADG72474.1; -; Genomic_DNA.
DR   RefSeq; WP_013114812.1; NC_014150.1.
DR   AlphaFoldDB; D5U5J7; -.
DR   STRING; 526224.Bmur_2403; -.
DR   KEGG; brm:Bmur_2403; -.
DR   eggNOG; COG0284; Bacteria.
DR   eggNOG; COG0461; Bacteria.
DR   HOGENOM; CLU_048996_0_0_12; -.
DR   OMA; ASFIAYE; -.
DR   OrthoDB; 9806203at2; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000001915; 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: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   CDD; cd04725; OMP_decarboxylase_like; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01200_B; OMPdecase_type1_B; 1.
DR   HAMAP; MF_01208; PyrE; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR047596; OMPdecase_bac.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR023031; OPRT.
DR   InterPro; IPR004467; Or_phspho_trans_dom.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR00336; pyrE; 1.
DR   NCBIfam; TIGR01740; pyrF; 1.
DR   PANTHER; PTHR32119; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR32119:SF2; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_01200};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000313|EMBL:ADG72474.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01200};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01208};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01200};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000313|EMBL:ADG72474.1}.
FT   DOMAIN          11..232
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        68
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         66..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         338
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         342
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         344
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         364..372
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         368
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
SQ   SEQUENCE   451 AA;  50430 MW;  6E0367CAE6F8B7BF CRC64;
     MIKLTDNPKE RLIIALDFNS MGEAAKLIDE LGDEAVFYKV GLELFLYTKG EIIEYLASKN
     KKVFLDLKFH DIPNTTAMAS LFAAKQNIFM FNVHTSGGKK MMERTVEEIK KLNKDNLIIG
     VTILTSLSEN DVKNMFSSNL PLTDLAVNWA KLGKEAGLDG VVCSPKEASI IKKECGENFR
     TVCPGVRPKW ASTDDQERIM TPKEAIENGC DYLVVGRPIT RSEDRVKACK MVVEEIAEGI
     EHNKKLKARL IASALLETKA VKLNVKEPFT FVSGIKSPIY CDNRYVIGFP KHRQVIVDAF
     VSLLKDKDFD VIAGTATAGI PWASFIAYEL NKPLCYIRAE KKEHGRGKQI EGAECDGKKL
     ILIEDLISTG GSSIKAFEAT KNEGAIGLEI ISIFSYEFEK AYKNFEEAGI KFSSLSNFTS
     LMEIAKDENY ITEDELNKAL EWNKNPDEWG K
//
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