ID A0A2R8BJP1_9RHOB Unreviewed; 332 AA.
AC A0A2R8BJP1;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Arabinose 5-phosphate isomerase KdsD {ECO:0000313|EMBL:SPH23616.1};
DE EC=5.3.1.13 {ECO:0000313|EMBL:SPH23616.1};
GN Name=kdsD {ECO:0000313|EMBL:SPH23616.1};
GN ORFNames=DEA8626_02681 {ECO:0000313|EMBL:SPH23616.1};
OS Defluviimonas aquaemixtae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Defluviimonas.
OX NCBI_TaxID=1542388 {ECO:0000313|EMBL:SPH23616.1, ECO:0000313|Proteomes:UP000244924};
RN [1] {ECO:0000313|EMBL:SPH23616.1, ECO:0000313|Proteomes:UP000244924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8626 {ECO:0000313|EMBL:SPH23616.1,
RC ECO:0000313|Proteomes:UP000244924};
RA Keele B.F.;
RL Submitted (MAR-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}.
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DR EMBL; OMOQ01000002; SPH23616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8BJP1; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000244924; Unassembled WGS sequence.
DR GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0097367; F:carbohydrate derivative binding; 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; SSF54631; CBS-domain pair; 1.
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:SPH23616.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000244924};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 46..189
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 214..276
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 278..332
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 64
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 116
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 157
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 198
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 332 AA; 34381 MW; FBD7E90AFB910011 CRC64;
MTATSSSTEP NVGGETFLAT ARRVIGIEAA GLAALSDALG DSFAEAIDLI LKAKGRVIVS
GMGKSGHVGR KIAATLASTG TPAQYVHPAE ASHGDLGMVT EGDVALVLSN SGETPELKDI
IAHTRRFSIP LIGIASRPGS TLLRQSDVAI VLPDAEEACG TGVVPTTSTT MTLALGDALA
VVLMEHRRFT PEHFRTFHPG GKLGAMLMKV EDLMHGGDAV PLVPAGTQMS DALLTMSQKG
FGVVGVTDAK GRLMGIVTDG DLRRHMAGLL DHTADEVMTE GPLTIGPGEV AQKAVALMRD
RKITCLFVVD PEGDGLASGL IHIHDCLRAG VV
//
