ID A0A0S8FAT7_9BACT Unreviewed; 332 AA.
AC A0A0S8FAT7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=KpsF/GutQ family sugar-phosphate isomerase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMK73_09755 {ECO:0000313|EMBL:KPK57799.1};
OS Planctomycetes bacterium SM23_32.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1704029 {ECO:0000313|EMBL:KPK57799.1, ECO:0000313|Proteomes:UP000052164};
RN [1] {ECO:0000313|EMBL:KPK57799.1, ECO:0000313|Proteomes:UP000052164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_32 {ECO:0000313|EMBL:KPK57799.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK57799.1}.
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DR EMBL; LJUE01000218; KPK57799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8FAT7; -.
DR PATRIC; fig|1704029.3.peg.2059; -.
DR Proteomes; UP000052164; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; 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; cd04604; CBS_pair_SIS_assoc; 1.
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 SMART; SM00116; CBS; 2.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 32..174
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 199..265
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 271..330
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 50
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 101
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 142
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 183
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 332 AA; 36122 MW; 222625EE85585FB1 CRC64;
MDCIREAHQI IQLELDALQA MQEHLGAEFE RAVEMIFHCR GRVVVTGVGK AGIVGQKISA
TLASTGTPSH WIHAVDARHG DLGRVHPDDV VLALSNSGET EVVQLLPALK KLDVRIIAIT
GEARSTLARH ADVVLDIGEV EEACPLGLAP SSSTTAMIVM GDALALTLFR MRNWQPEDYA
FYHPGGELGR RLIKVGQVMR KGAQNPVARC DVSVRDALKV MTGTGRPVSP GAVSLVDDEG
KLVGFFTDGD FRRLMQDGEG NLLDRPVSDV MTHDPKTIST EGLLAEAYRM LREYRIDQVP
VVDVEGRPVG IVDVQDWLDV ERGAEPPEDA MP
//
