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Database: UniProt
Entry: L1NN99_9NEIS
LinkDB: L1NN99_9NEIS
Original site: L1NN99_9NEIS 
ID   L1NN99_9NEIS            Unreviewed;       266 AA.
AC   L1NN99;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|HAMAP-Rule:MF_02227};
DE            EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|HAMAP-Rule:MF_02227};
GN   Name=rpe {ECO:0000256|HAMAP-Rule:MF_02227};
GN   ORFNames=HMPREF9120_02068 {ECO:0000313|EMBL:EKY04806.1};
OS   Neisseria sp. oral taxon 020 str. F0370.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=1127694 {ECO:0000313|EMBL:EKY04806.1, ECO:0000313|Proteomes:UP000010457};
RN   [1] {ECO:0000313|EMBL:EKY04806.1, ECO:0000313|Proteomes:UP000010457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0370 {ECO:0000313|EMBL:EKY04806.1,
RC   ECO:0000313|Proteomes:UP000010457};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC       phosphate to D-xylulose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_02227}.
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|HAMAP-Rule:MF_02227, 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|HAMAP-Rule:MF_02227,
CC         ECO:0000256|PIRSR:PIRSR001461-2};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_02227, ECO:0000256|PIRSR:PIRSR001461-2};
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|HAMAP-Rule:MF_02227}.
CC   -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00009541, ECO:0000256|HAMAP-Rule:MF_02227,
CC       ECO:0000256|PIRNR:PIRNR001461}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKY04806.1}.
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DR   EMBL; AMER01000165; EKY04806.1; -; Genomic_DNA.
DR   AlphaFoldDB; L1NN99; -.
DR   STRING; 1127694.HMPREF9120_02068; -.
DR   PATRIC; fig|1127694.3.peg.1903; -.
DR   HOGENOM; CLU_054856_2_1_4; -.
DR   Proteomes; UP000010457; Unassembled WGS sequence.
DR   GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019323; P:pentose catabolic process; IEA:UniProtKB-UniRule.
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-RELATED; 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|HAMAP-Rule:MF_02227,
KW   ECO:0000256|PIRNR:PIRNR001461}; Cobalt {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02227};
KW   Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_02227}; Reference proteome {ECO:0000313|Proteomes:UP000010457};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   ACT_SITE        76
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-1"
FT   ACT_SITE        220
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-1"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         74
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         76
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         107
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         183..186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         220..222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT   BINDING         220
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         242..243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-3"
SQ   SEQUENCE   266 AA;  29090 MW;  089F6E38B521DEE6 CRC64;
     MAIVPAKCRV AEFYVAKMQS HRFLCRLKIL NGLCPKTEEP MYKFRIAPSI LSADFARLGE
     EVSRVIEAGA DLIHFDVMDN HYVPNLTFGP MVCAAIKPYA SVPVDIHLMV EPVDDLIHAF
     AKAGAGIITF HPEASRHVDR SLSLIREHGC QAGLVLNPAT SVSVLENVLD RLDMVLLMSV
     NPGFGGQSFI PHTLEKIRQT RALLDRYRER SGRHIAIEVD GGVKTANIAE IAAAGADTFV
     AGSAIFGQPD YRAVIDDMRA ELAKAV
//
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