RPIA_CHLTA
ID RPIA_CHLTA Reviewed; 242 AA.
AC Q3KME9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170};
DE AltName: Full=Phosphoriboisomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE Short=PRI {ECO:0000255|HAMAP-Rule:MF_00170};
GN Name=rpiA {ECO:0000255|HAMAP-Rule:MF_00170}; OrderedLocusNames=CTA_0233;
OS Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=315277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT genitotropic strains.";
RL Infect. Immun. 73:6407-6418(2005).
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}.
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DR EMBL; CP000051; AAX50473.1; -; Genomic_DNA.
DR RefSeq; WP_011324643.1; NC_007429.1.
DR AlphaFoldDB; Q3KME9; -.
DR SMR; Q3KME9; -.
DR EnsemblBacteria; AAX50473; AAX50473; CTA_0233.
DR KEGG; cta:CTA_0233; -.
DR HOGENOM; CLU_056590_1_0_0; -.
DR OMA; YDWDEVN; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000002532; Chromosome.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:UniProtKB-UniRule.
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 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.
FT CHAIN 1..242
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_1000016920"
FT ACT_SITE 117
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 39..42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 95..98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 108..111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ SEQUENCE 242 AA; 26672 MW; FD9FB2937E923A0A CRC64;
MSKQPENSFS SDKFFPIKQK LALEAVALVE PGMCVGLGSG STAREFILAL GDRVRTERLV
ITAVASSRIS QLLAEAVGIP LLDHSLLQDV DLVVDGADEV DPCLRMIKGG GGALFREKIL
LQSGKRNVIL VDERKLVPTL GKFSLPIEIA PFGCSSVQRI LNKQGYFGEW RETSAGERFI
TDNGNYIYDV RTPDSYANPE EDMIRLLQIR GIIDVGFVIA KAEVWVGYAD GSIVRKKKHN
EY
