RPIA2_YERPE
ID RPIA2_YERPE Reviewed; 236 AA.
AC Q8ZGJ9; Q0WHC0; Q8D025;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ribose-5-phosphate isomerase A 2 {ECO:0000255|HAMAP-Rule:MF_00170};
DE EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170};
DE AltName: Full=Phosphoriboisomerase A 2 {ECO:0000255|HAMAP-Rule:MF_00170};
DE Short=PRI 2 {ECO:0000255|HAMAP-Rule:MF_00170};
GN Name=rpiA2 {ECO:0000255|HAMAP-Rule:MF_00170};
GN OrderedLocusNames=YPO1292, y2892, YP_1299;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273;
CC EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM86443.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS61542.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL19946.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86443.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS61542.1; ALT_INIT; Genomic_DNA.
DR PIR; AH0157; AH0157.
DR RefSeq; WP_002208805.1; NZ_WUCM01000013.1.
DR RefSeq; YP_002346318.1; NC_003143.1.
DR AlphaFoldDB; Q8ZGJ9; -.
DR SMR; Q8ZGJ9; -.
DR IntAct; Q8ZGJ9; 2.
DR STRING; 214092.YPO1292; -.
DR PaxDb; Q8ZGJ9; -.
DR DNASU; 1147839; -.
DR EnsemblBacteria; AAM86443; AAM86443; y2892.
DR EnsemblBacteria; AAS61542; AAS61542; YP_1299.
DR GeneID; 66842242; -.
DR KEGG; ype:YPO1292; -.
DR KEGG; ypk:y2892; -.
DR KEGG; ypm:YP_1299; -.
DR PATRIC; fig|214092.21.peg.1601; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_0_6; -.
DR OMA; FIDICDT; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0006014; P:D-ribose metabolic process; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR CDD; cd01398; RPI_A; 1.
DR HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR PANTHER; PTHR11934; PTHR11934; 1.
DR Pfam; PF06026; Rib_5-P_isom_A; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00021; rpiA; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome.
FT CHAIN 1..236
FT /note="Ribose-5-phosphate isomerase A 2"
FT /id="PRO_0000158502"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 31..34
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 99..102
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ SEQUENCE 236 AA; 26034 MW; 2E1D870A15A044FA CRC64;
MSNQQNDAKR AAARRVIQDF VFDGMTLGLG SGTTSHFFVR ELGQHVAKGL QLTCTTTSRA
TSEVARDVGI ELSDPNEMNE IDLTIDGPDE IDRRFNMIKG GGACLLWEKI IAHASKRMIC
ICDETKIVNC LGQFPLPVEI VPFAWKQTER RVERVLAEQG LHHVPIIRRM GGGHPVITDS
GNFILDCHCG AIITAPEPLE IELNRIPGVV ENGLFTREAT GMVVGYFDGS SYVQLR
