ID A0A2D2B138_9CAUL Unreviewed; 317 AA.
AC A0A2D2B138;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=KpsF/GutQ family sugar-phosphate isomerase {ECO:0000313|EMBL:ATQ43958.1};
GN ORFNames=CSW64_16955 {ECO:0000313|EMBL:ATQ43958.1};
OS Caulobacter mirabilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=69666 {ECO:0000313|EMBL:ATQ43958.1, ECO:0000313|Proteomes:UP000228945};
RN [1] {ECO:0000313|EMBL:ATQ43958.1, ECO:0000313|Proteomes:UP000228945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FWC 38 {ECO:0000313|EMBL:ATQ43958.1,
RC ECO:0000313|Proteomes:UP000228945};
RA Fiebig A., Crosson S.;
RT "Genome sequence of Caulobacter mirabilis FWC38.";
RL Submitted (OCT-2017) 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; CP024201; ATQ43958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D2B138; -.
DR KEGG; cmb:CSW64_16955; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000228945; 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 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 Isomerase {ECO:0000313|EMBL:ATQ43958.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000228945};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 34..177
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 202..262
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 266..317
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 52
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 104
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 145
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 186
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 317 AA; 32979 MW; B3A21A3CF235E433 CRC64;
MSFDAVSVGR RVLATEADAL RLMADGLGQP FVTAVETLFN CKGRIVCTGM GKSGHVARKI
AATMASTGAP AMFVHPAEAS HGDLGMIGSD DVILGLSKSG EVRELADVLA YSGRFGIPLI
GITANPESAL GKASTIVLQL PDAPEATGEV SAPTTSTTLQ IALGDALAVA LLERRGFTAR
DFHVFHPGGK LGAMLRTVGD LMHRLEEAPL VGEATPMPDT VSVMSERRLG IVGVVSDDGR
LIGVVTDGDL RRHFNDLAGK TVGEIMTRNP KAVTAETLAG DAARLMNDSR ITALFVVKDG
KPIGVLHVHD VLSAGVV
//
