ID D9TTU8_THETC Unreviewed; 148 AA.
AC D9TTU8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Sugar-phosphate isomerase, RpiB/LacA/LacB family {ECO:0000313|EMBL:ADL69986.1};
DE EC=5.3.1.6 {ECO:0000313|EMBL:ADL69986.1};
GN OrderedLocusNames=Tthe_2530 {ECO:0000313|EMBL:ADL69986.1};
OS Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 /
OS NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium
OS thermosaccharolyticum).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacterium.
OX NCBI_TaxID=580327 {ECO:0000313|EMBL:ADL69986.1, ECO:0000313|Proteomes:UP000001626};
RN [1] {ECO:0000313|EMBL:ADL69986.1, ECO:0000313|Proteomes:UP000001626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM
RC 00135 / 2032 {ECO:0000313|Proteomes:UP000001626};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM
RT 571.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LacAB/RpiB family.
CC {ECO:0000256|ARBA:ARBA00008754}.
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DR EMBL; CP002171; ADL69986.1; -; Genomic_DNA.
DR RefSeq; WP_013298943.1; NC_014410.1.
DR AlphaFoldDB; D9TTU8; -.
DR STRING; 580327.Tthe_2530; -.
DR KEGG; ttm:Tthe_2530; -.
DR eggNOG; COG0698; Bacteria.
DR HOGENOM; CLU_091396_4_1_9; -.
DR OrthoDB; 1778624at2; -.
DR Proteomes; UP000001626; Chromosome.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; PTHR43732:SF1; RIBOSE 5-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR43732; RIBOSE 5-PHOSPHATE ISOMERASE-RELATED; 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:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ADL69986.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001626}.
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; 16017 MW; 98ABE00A9231E942 CRC64;
MIAIGSDHGG YELKEAIKKH LDEKGIEYKD FGTFSEESVD YPDFALKVAE AVASGQFEKG
ILLCGTGVGI SIAANKVPGI RAANVSDAFS ARYSKEHNNA NVLCMGGRVV GPGLAAILVD
EWLNAEFQGG RHQKRLDKIT EIEKKYSK
//
