ID A0A173E083_9CHLA Unreviewed; 216 AA.
AC A0A173E083;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=M787_004500 {ECO:0000313|EMBL:ANG66566.1};
OS Chlamydia gallinacea 08-1274/3.
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=1143323 {ECO:0000313|EMBL:ANG66566.1, ECO:0000313|Proteomes:UP000019147};
RN [1] {ECO:0000313|EMBL:ANG66566.1, ECO:0000313|Proteomes:UP000019147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=08-1274/3 {ECO:0000313|EMBL:ANG66566.1,
RC ECO:0000313|Proteomes:UP000019147};
RX PubMed=24461712; DOI=10.1016/j.syapm.2013.12.004;
RA Sachse K., Laroucau K., Riege K., Wehner S., Dilcher M., Creasy H.H.,
RA Weidmann M., Myers G., Vorimore F., Vicari N., Magnino S.,
RA Liebler-Tenorio E., Ruettger A., Bavoil P.M., Hufert F.T.,
RA Rossello-Mora R., Marz M.;
RT "Evidence for the existence of two new members of the family Chlamydiaceae
RT and proposal of Chlamydia avium sp. nov. and Chlamydia gallinacea sp.
RT nov.";
RL Syst. Appl. Microbiol. 37:79-88(2014).
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};
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 Note=Binds 1 divalent metal cation per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_02227};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02227}.
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DR EMBL; CP015840; ANG66566.1; -; Genomic_DNA.
DR RefSeq; WP_051273843.1; NZ_CP015840.1.
DR AlphaFoldDB; A0A173E083; -.
DR STRING; 1143323.M787_004500; -.
DR GeneID; 81478565; -.
DR KEGG; cgz:M787_004500; -.
DR eggNOG; COG0036; Bacteria.
DR OrthoDB; 1645589at2; -.
DR Proteomes; UP000019147; Chromosome.
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; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 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 Isomerase {ECO:0000256|HAMAP-Rule:MF_02227};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02227}.
FT ACT_SITE 26
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT ACT_SITE 168
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT BINDING 24
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT BINDING 26
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT BINDING 57
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT BINDING 133..136
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT BINDING 168..170
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT BINDING 168
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT BINDING 190..191
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
SQ SEQUENCE 216 AA; 23541 MW; 620312653A5ECF35 CRC64;
MGGDLASLGS EARRIAQSGA DFIHIDIMDG HFVPNFTFGP GIIAAINRST DIFLEVHAMI
YSPFDFIEAF VKAGADRIIV HFEASENLKE LLTYIKKCGI QAGLAFSPET SIEFIPSFLP
LCDVILLMSV HPGFCGQSFL PEVSEKIRFT KKAIQLAALE GKCFIEVDGG ITENSAKICR
EAGADILVAA SYIFQHDGLT MEEKVSLLRG ENHGIK
//
