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Database: UniProt
Entry: C5NUK0_9BACL
LinkDB: C5NUK0_9BACL
Original site: C5NUK0_9BACL 
ID   C5NUK0_9BACL            Unreviewed;       224 AA.
AC   C5NUK0;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
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   ECO:0000313|EMBL:EER69011.1};
GN   ORFNames=GEMHA0001_1224 {ECO:0000313|EMBL:EER69011.1};
OS   Gemella haemolysans ATCC 10379.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Gemellaceae; Gemella.
OX   NCBI_TaxID=546270 {ECO:0000313|EMBL:EER69011.1, ECO:0000313|Proteomes:UP000006004};
RN   [1] {ECO:0000313|EMBL:EER69011.1, ECO:0000313|Proteomes:UP000006004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER69011.1,
RC   ECO:0000313|Proteomes:UP000006004};
RA   Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA   Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA   Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EER69011.1, ECO:0000313|Proteomes:UP000006004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER69011.1,
RC   ECO:0000313|Proteomes:UP000006004};
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EER69011.1}.
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DR   EMBL; ACDZ02000005; EER69011.1; -; Genomic_DNA.
DR   RefSeq; WP_003144023.1; NZ_ACDZ02000005.1.
DR   AlphaFoldDB; C5NUK0; -.
DR   GeneID; 78009652; -.
DR   eggNOG; COG0120; Bacteria.
DR   OrthoDB; 5870696at2; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000006004; Unassembled WGS sequence.
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}.
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   224 AA;  24663 MW;  196FE9966949EE6E CRC64;
     MNLKEVVGKK AVDYVKDGMI VGLGTGSTVF YFVHALADRV KEGLNVEMVS TSIQTVELAK
     SLGLSIKELE EIDHIDLAVD GVDEIDKDFN AIKGGGAALF REKIVADIAR EVIWIYDESK
     DVEKLGNFNL PVEILPFGYS HTIRKMEEVG LKPVLRLKDG ATLITDNNNY IVDLHLGYGF
     DIKAVKEKLE SIVGVVEHGL FLNMCKLCIK GTEQGAVIIE NPNN
//
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