ID E6QYD7_CRYGW Unreviewed; 224 AA.
AC E6QYD7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013920, ECO:0000256|PIRNR:PIRNR001461};
DE EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|PIRNR:PIRNR001461};
GN OrderedLocusNames=CGB_A7430C {ECO:0000313|EMBL:ADV19870.1};
OS Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus gattii species complex.
OX NCBI_TaxID=367775 {ECO:0000313|EMBL:ADV19870.1, ECO:0000313|Proteomes:UP000007805};
RN [1] {ECO:0000313|EMBL:ADV19870.1, ECO:0000313|Proteomes:UP000007805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM276 / ATCC MYA-4071 {ECO:0000313|Proteomes:UP000007805};
RX PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 2:E342-E342(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WM276;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwong-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 0:0-0(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:13677, ChEBI:CHEBI:57737, ChEBI:CHEBI:58121;
CC EC=5.1.3.1; Evidence={ECO:0000256|ARBA:ARBA00001782,
CC ECO:0000256|PIRNR:PIRNR001461};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001461-2};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000256|PIRSR:PIRSR001461-2};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC xylulose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage):
CC step 1/1. {ECO:0000256|ARBA:ARBA00005016}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000256|ARBA:ARBA00009541, ECO:0000256|PIRNR:PIRNR001461}.
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DR EMBL; CP000286; ADV19870.1; -; Genomic_DNA.
DR RefSeq; XP_003191657.1; XM_003191609.1.
DR AlphaFoldDB; E6QYD7; -.
DR GeneID; 10188088; -.
DR KEGG; cgi:CGB_A7430C; -.
DR VEuPathDB; FungiDB:CGB_A7430C; -.
DR eggNOG; KOG3111; Eukaryota.
DR HOGENOM; CLU_054856_0_1_1; -.
DR OrthoDB; 101513at2759; -.
DR UniPathway; UPA00115; UER00411.
DR Proteomes; UP000007805; Chromosome A.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_02227; RPE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR01163; rpe; 1.
DR PANTHER; PTHR11749; RIBULOSE-5-PHOSPHATE-3-EPIMERASE; 1.
DR PANTHER; PTHR11749:SF3; RIBULOSE-PHOSPHATE 3-EPIMERASE; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR PIRSF; PIRSF001461; RPE; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001461};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|PIRSR:PIRSR001461-2};
KW Isomerase {ECO:0000256|PIRNR:PIRNR001461};
KW Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2};
KW Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-1"
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-1"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 36
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 68
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 145..148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 196..197
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
SQ SEQUENCE 224 AA; 24253 MW; 56BF682000325C73 CRC64;
MSKAIISPSV LASDLSDLSN ECRRMMANGC DWLHMDVMDG HFVPNITMGA PILEHVYKNV
PNIFMDCHMM VSNPAQWVPE VSKAGGKLYT FHYEATEEPE KVIELVHSHK MLAGLAISPE
TPASAVTDSL GKAADLLLVM TVRPGRGGQK FMPECLEKVK ELRERFPGKN IQVDGGVGSG
NACQCAQAGS NVLVAGTAIF GAKDPKQTIQ EMRTAVDDAI AQRK
//
