ID A0A363RRC7_9BURK Unreviewed; 332 AA.
AC A0A363RRC7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=KpsF/GutQ family sugar-phosphate isomerase {ECO:0000313|EMBL:PWB19277.1};
GN ORFNames=DCO45_08775 {ECO:0000313|EMBL:PWB19277.1};
OS Comamonas sp. JNW.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=2170731 {ECO:0000313|EMBL:PWB19277.1, ECO:0000313|Proteomes:UP000251772};
RN [1] {ECO:0000313|EMBL:PWB19277.1, ECO:0000313|Proteomes:UP000251772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JNW {ECO:0000313|EMBL:PWB19277.1,
RC ECO:0000313|Proteomes:UP000251772};
RA Go L.Y., Mitchell J.A.;
RL Submitted (APR-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:PWB19277.1}.
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DR EMBL; QETI01000004; PWB19277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A363RRC7; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000251772; 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: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:PWB19277.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000251772};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 44..187
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 213..271
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 280..332
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 62
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 114
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 155
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 196
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 332 AA; 34670 MW; 90FF2FF38B5C4010 CRC64;
MSTLQPKRPV EAAQILRLAA STFAIEAEAI AALTQRLDDN FVQVVQRMLD IPGRVVVTGM
GKSGHVGRKI AATLASTGTP AFFVHPGEAS HGDLGMVTGQ DLVLAISNSG ESGEISVLLP
VLKRLGVPVV AMTGNLQSSM ARHADWVLNT QVDKEACPLN LAPTASTTAQ MAMGDALAVA
LLDARGFKAE DFARSHPGGA LGRRLLTHVS DVMRSGDALP TVLPSASFSD LMREMSAKGM
GAAAIVDAHG LLQGVFTDGD LRRRIEAGAD LRGLTAAEVM HATPRQISAD ALAADAAALM
EAHRITSVLV TDADQRLVGI VHVGDLMRAK VI
//