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Database: UniProt
Entry: E4RMI9_HALHG
LinkDB: E4RMI9_HALHG
Original site: E4RMI9_HALHG 
ID   E4RMI9_HALHG            Unreviewed;       222 AA.
AC   E4RMI9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000256|HAMAP-Rule:MF_00170};
DE            EC=5.3.1.6 {ECO:0000256|HAMAP-Rule:MF_00170};
DE   AltName: Full=Phosphoriboisomerase A {ECO:0000256|HAMAP-Rule:MF_00170};
DE            Short=PRI {ECO:0000256|HAMAP-Rule:MF_00170};
GN   Name=rpiA {ECO:0000256|HAMAP-Rule:MF_00170};
GN   OrderedLocusNames=Halsa_1086 {ECO:0000313|EMBL:ADQ14520.1};
OS   Halanaerobium hydrogeniformans (Halanaerobium sp. (strain sapolanicus)).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=656519 {ECO:0000313|EMBL:ADQ14520.1, ECO:0000313|Proteomes:UP000007434};
RN   [1] {ECO:0000313|EMBL:ADQ14520.1, ECO:0000313|Proteomes:UP000007434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Begemann M.B., Mormile M.R., Wall J.D., Elias D.A., Woyke T.;
RT   "Complete sequence of Halanaerobium sp. sapolanicus.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ14520.1, ECO:0000313|Proteomes:UP000007434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RX   PubMed=21602336; DOI=10.1128/JB.05209-11;
RA   Brown S.D., Begemann M.B., Mormile M.R., Wall J.D., Han C.S., Goodwin L.A.,
RA   Pitluck S., Land M.L., Hauser L.J., Elias D.A.;
RT   "Complete Genome Sequence of the Haloalkaliphilic, Hydrogen Producing
RT   Halanaerobium hydrogenoformans.";
RL   J. Bacteriol. 193:3682-3683(2011).
CC   -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC       ribulose 5-phosphate. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00170}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00170}.
CC   -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00170}.
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DR   EMBL; CP002304; ADQ14520.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4RMI9; -.
DR   STRING; 656519.Halsa_1086; -.
DR   KEGG; has:Halsa_1086; -.
DR   eggNOG; COG0120; Bacteria.
DR   HOGENOM; CLU_056590_1_0_9; -.
DR   OrthoDB; 5870696at2; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000007434; 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   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.1360; -; 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   NCBIfam; TIGR00021; rpiA; 1.
DR   PANTHER; PTHR11934; RIBOSE-5-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR11934:SF0; RIBOSE-5-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF06026; Rib_5-P_isom_A; 1.
DR   SUPFAM; SSF75445; D-ribose-5-phosphate isomerase (RpiA), lid domain; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007434}.
FT   ACT_SITE        102
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         25..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         80..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         93..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   222 AA;  24207 MW;  7E201E0D8D47EDA4 CRC64;
     MNPKKLTGEK AAEFISDGMI IGLGTGSTAY YAIKKVGEMV RDGLNVKAVP TSKETAELAL
     EEGIELIELS QVEKLDLTID GADEVDPDFN LIKGGGGALL REKIVAAATE KLIIIVDESK
     LVDKLGDFLL PVEVTPFSWQ YTQKMINKMG GSSEIRKKDG EIFVTDNDNY ILDCDFGKIE
     KPEKLTIDLN TIPGVVENGI FAKMAEVVVV GHNDGKIEVL YR
//
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