RPIA_BARHE
ID RPIA_BARHE Reviewed; 234 AA.
AC Q6G3V6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=BH06410;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of ribose-5-phosphate isomerase A from Bartonella
RT henselae.";
RL Submitted (MAY-2009) to the PDB data bank.
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 ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00170}.
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DR EMBL; BX897699; CAF27445.1; -; Genomic_DNA.
DR RefSeq; WP_011180565.1; NC_005956.1.
DR PDB; 3HHE; X-ray; 2.30 A; A/B=1-234.
DR PDBsum; 3HHE; -.
DR AlphaFoldDB; Q6G3V6; -.
DR SMR; Q6G3V6; -.
DR STRING; 283166.BH06410; -.
DR PaxDb; Q6G3V6; -.
DR PRIDE; Q6G3V6; -.
DR EnsemblBacteria; CAF27445; CAF27445; BH06410.
DR KEGG; bhe:BH06410; -.
DR eggNOG; COG0120; Bacteria.
DR OMA; FIDICDT; -.
DR UniPathway; UPA00115; UER00412.
DR EvolutionaryTrace; Q6G3V6; -.
DR Proteomes; UP000000421; 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 1: Evidence at protein level;
KW 3D-structure; Isomerase.
FT CHAIN 1..234
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_0000158388"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 28..31
FT /ligand="substrate"
FT BINDING 83..86
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 96..99
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170,
FT ECO:0000269|Ref.2"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:3HHE"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:3HHE"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:3HHE"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3HHE"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3HHE"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3HHE"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:3HHE"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:3HHE"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:3HHE"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3HHE"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:3HHE"
SQ SEQUENCE 234 AA; 25161 MW; D122B2390A42511E CRC64;
MNVQQLKKMA ALKALEFVED DMRLGIGSGS TVNEFIPLLG ERVANGLRVT CVATSQYSEQ
LCHKFGVPIS TLEKIPELDL DIDGADEIGP EMTLIKGGGG ALLHEKIVAS ASRAMFVIAD
ETKMVKTLGA FALPIEVNPF GIHATRIAIE KAADNLGLSG EITLRMNGDD PFKTDGGHFI
FDAFWGRILQ PKLLSEALLA IPGVVEHGLF LGLASRAIVA MADSQIKVLE PFDF
