ID Q74CR6_GEOSL Unreviewed; 148 AA.
AC Q74CR6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Ribose-5-phosphate isomerase B {ECO:0000313|EMBL:AAR34980.1};
GN Name=rpiB {ECO:0000313|EMBL:AAR34980.1};
GN OrderedLocusNames=GSU1606 {ECO:0000313|EMBL:AAR34980.1};
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR34980.1, ECO:0000313|Proteomes:UP000000577};
RN [1] {ECO:0000313|EMBL:AAR34980.1, ECO:0000313|Proteomes:UP000000577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA
RC {ECO:0000313|Proteomes:UP000000577};
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
CC -!- SIMILARITY: Belongs to the LacAB/RpiB family.
CC {ECO:0000256|ARBA:ARBA00008754}.
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DR EMBL; AE017180; AAR34980.1; -; Genomic_DNA.
DR RefSeq; NP_952657.1; NC_002939.5.
DR RefSeq; WP_010942251.1; NC_002939.5.
DR AlphaFoldDB; Q74CR6; -.
DR SMR; Q74CR6; -.
DR STRING; 243231.GSU1606; -.
DR EnsemblBacteria; AAR34980; AAR34980; GSU1606.
DR KEGG; gsu:GSU1606; -.
DR PATRIC; fig|243231.5.peg.1648; -.
DR eggNOG; COG0698; Bacteria.
DR HOGENOM; CLU_091396_4_1_7; -.
DR InParanoid; Q74CR6; -.
DR OrthoDB; 1778624at2; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0019316; P:D-allose catabolic process; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR Gene3D; 3.40.1400.10; Sugar-phosphate isomerase, RpiB/LacA/LacB; 1.
DR InterPro; IPR004785; RpiB.
DR InterPro; IPR003500; RpiB_LacA_LacB.
DR InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR NCBIfam; TIGR01120; rpiB; 1.
DR NCBIfam; TIGR00689; rpiB_lacA_lacB; 1.
DR PANTHER; PTHR30345:SF0; DNA DAMAGE-REPAIR_TOLERATION PROTEIN DRT102; 1.
DR PANTHER; PTHR30345; RIBOSE-5-PHOSPHATE ISOMERASE B; 1.
DR Pfam; PF02502; LacAB_rpiB; 1.
DR PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR SUPFAM; SSF89623; Ribose/Galactose isomerase RpiB/AlsB; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:AAR34980.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000577}.
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT ACT_SITE 97
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT BINDING 7..8
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 65..69
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 98
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 108
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 131
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 135
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
SQ SEQUENCE 148 AA; 15967 MW; C377FD12407ACF93 CRC64;
MIVVGSDHGG LELKEAVKRL LAERGETFED CGTDNGNSVD YPDFGIKVAR RVSNGEAGKG
ILLCGTGIGM SIVANKFPRV RAALATDAFM ARMAKEHNNA NILVLGGRVL EEAVAREMVI
AWLDGVYEGG RHQGRLDKIA ALERELMK
//