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Database: UniProt
Entry: A0A151RNT7_CAJCA
LinkDB: A0A151RNT7_CAJCA
Original site: A0A151RNT7_CAJCA 
ID   A0A151RNT7_CAJCA        Unreviewed;       227 AA.
AC   A0A151RNT7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|PIRNR:PIRNR001461};
DE            EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|PIRNR:PIRNR001461};
GN   ORFNames=KK1_034311 {ECO:0000313|EMBL:KYP44199.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP44199.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP44199.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
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   -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00009541, ECO:0000256|PIRNR:PIRNR001461}.
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DR   EMBL; KQ483636; KYP44199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151RNT7; -.
DR   STRING; 3821.A0A151RNT7; -.
DR   OMA; STIDMAW; -.
DR   Proteomes; UP000075243; Unassembled WGS sequence.
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:InterPro.
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; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001461};
KW   Cobalt {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   Reference proteome {ECO:0000313|Proteomes:UP000075243};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   ACT_SITE        37
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-1"
FT   ACT_SITE        177
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-1"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         35
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         37
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         148..151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         177
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         199..200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
SQ   SEQUENCE   227 AA;  24679 MW;  9B96F2ABA920E16B CRC64;
     MEVAPKIAPS MLSSDFANLA SEAHRMLNLG ADWLHMDIMV THFVPNLTIG APVIESLRKH
     TMGYLDCHLM VTNPLDYVEP LAKAGASGFT FHVETSKNNW KELIQKIKSH GMRPGVALKP
     RTPIGDVYPL VEAENPVEMV LVMTVEPGFG GQKFMPEMMD KVRILRKKYP SLDIEVDGGL
     GPSTIDMAAS AGANCIVAGS SVFGAPEPAQ VISLLRNSVE KAQHTMI
//
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