ID A0A3P1T127_9BACT Unreviewed; 324 AA.
AC A0A3P1T127;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=KpsF/GutQ family sugar-phosphate isomerase {ECO:0000313|EMBL:RRD03044.1};
GN ORFNames=EII32_00905 {ECO:0000313|EMBL:RRD03044.1};
OS Prevotella sp. OH937_COT-195.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2491051 {ECO:0000313|EMBL:RRD03044.1, ECO:0000313|Proteomes:UP000267043};
RN [1] {ECO:0000313|EMBL:RRD03044.1, ECO:0000313|Proteomes:UP000267043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH937_COT-195 {ECO:0000313|EMBL:RRD03044.1,
RC ECO:0000313|Proteomes:UP000267043};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000256|ARBA:ARBA00008165, ECO:0000256|PIRNR:PIRNR004692}.
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:RRD03044.1}.
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DR EMBL; RQZH01000001; RRD03044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1T127; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000267043; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05014; SIS_Kpsf; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR004800; KdsD/KpsF-type.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035474; SIS_Kpsf.
DR NCBIfam; TIGR00393; kpsF; 1.
DR PANTHER; PTHR42745; -; 1.
DR PANTHER; PTHR42745:SF1; ARABINOSE 5-PHOSPHATE ISOMERASE KDSD; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01380; SIS; 1.
DR PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Isomerase {ECO:0000313|EMBL:RRD03044.1}.
FT DOMAIN 40..183
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 209..266
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 276..324
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT SITE 58
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 110
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 151
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 192
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 324 AA; 35614 MW; E9C7ECED8D546597 CRC64;
MVKHNERLAM VRRYAIQCIK DESNAVLDLI NQIDEEFDRA VEFMLNCKGK IIVTGVGKSG
HIGAKIAATL SSTGTPSFFI NPLDVFHGDL GVMTRDDVVM AISNSGNTDE LLRFIPMVLH
MQIPIIGISG NENSLLAKYS TTHIKVKVDK EACPLNLAPT SSTTATLVMG DALAIALMEV
RDFKPTDFAH FHPGGELGKR LLTTAKDVMR SNDLPVIPKE MQLGEAIILV SKGKLGLGVS
IDGEGRIEGL ITDGDIRRAM EKWQAEFVRH KVEEIMTRTP KCVLADTKIT EIQKIMHANF
VHTVLVTDKE GHLLGVVDHY SCMI
//
