ID A0A437MDH3_9PROT Unreviewed; 325 AA.
AC A0A437MDH3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE SubName: Full=KpsF/GutQ family sugar-phosphate isomerase {ECO:0000313|EMBL:RVT95650.1};
GN ORFNames=EOD42_15740 {ECO:0000313|EMBL:RVT95650.1};
OS Rhodovarius crocodyli.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodovarius.
OX NCBI_TaxID=1979269 {ECO:0000313|EMBL:RVT95650.1, ECO:0000313|Proteomes:UP000282957};
RN [1] {ECO:0000313|EMBL:RVT95650.1, ECO:0000313|Proteomes:UP000282957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP-6 {ECO:0000313|EMBL:RVT95650.1,
RC ECO:0000313|Proteomes:UP000282957};
RA Chen W.-M.;
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}.
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:RVT95650.1}.
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DR EMBL; SACL01000005; RVT95650.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437MDH3; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000282957; 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:RVT95650.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000282957};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 41..184
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 209..264
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 273..325
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 59
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 111
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 152
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 193
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 325 AA; 33920 MW; 754B60AD53C27202 CRC64;
MRVDQSVPPS SYLAVARQVL QAEAEALQTL AAAIGVEFDQ AVETLAGCTG RVIVSGMGKS
GHVGRKIAAT MASTGTPAFF VHPGEASHGD LGMIQRGDVV LALSNSGETA ELSDLIAYSR
RFGIPLVGIT GRAGSSLARD ADVALVLPAV PEACPMGLAP TTSTTMQLAL GDALSVALLT
RRGFGAADFR VFHPGGKLGA QLMRVEQLMH AEMPLAAPET GMDTALVAMT AGRFGCLGIQ
QDGRLVGIIT DGDLRRAMKQ GGDLLARRAE EVMTRRPLSI APHTLAAEAL RIMNERSVTT
LFVVDGQGVP RGILHIHDLL RTGVA
//
