ID A0A411E7X5_9FLAO Unreviewed; 321 AA.
AC A0A411E7X5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=KpsF/GutQ family sugar-phosphate isomerase {ECO:0000313|EMBL:QBA63707.1};
GN ORFNames=EQY75_03605 {ECO:0000313|EMBL:QBA63707.1};
OS Muriicola soli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Muriicola.
OX NCBI_TaxID=2507538 {ECO:0000313|EMBL:QBA63707.1, ECO:0000313|Proteomes:UP000290889};
RN [1] {ECO:0000313|EMBL:QBA63707.1, ECO:0000313|Proteomes:UP000290889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS17-SY002 {ECO:0000313|EMBL:QBA63707.1,
RC ECO:0000313|Proteomes:UP000290889};
RA Kang H.J., Kim S.B.;
RT "Muriicola soli sp. nov., isolated from soil.";
RL Submitted (JAN-2019) 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}.
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DR EMBL; CP035544; QBA63707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411E7X5; -.
DR KEGG; mur:EQY75_03605; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000290889; Chromosome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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 SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Isomerase {ECO:0000313|EMBL:QBA63707.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000290889};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 36..179
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 270..321
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 54
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 106
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 147
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 188
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 321 AA; 34339 MW; ED82ACB862254BC0 CRC64;
MNRRKGILEL AKKTMQTEGD AIKHLASFLD QQFVDAIDAI YTGDGRVVIT GIGKSALIAS
KIVATLNSTG TPAIFMHAAD AIHGDLGTIQ QKDIVICISK SGNTPEIKLL VPLIKSGSNK
LIAITGNPES FLAEQSDFVL NTYVEKEACP NNLAPTTSTT AQLVMGDALA ICLLELRGFS
SKDFAKFHPG GTLGKKLYLR VGDIAVKNMV PKVEADSAVK EVIVEISEKM LGVAAVLKNG
KLVGVVTDGD IRRMLNKYEN INGLKAKDIM TTHPKTIEPG VLAVKALNEM QSNGISQLLV
AEKGVYQGVV HLHNLINEGI L
//
