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Database: UniProt
Entry: E6VU27_PSEA9
LinkDB: E6VU27_PSEA9
Original site: E6VU27_PSEA9 
ID   E6VU27_PSEA9            Unreviewed;       343 AA.
AC   E6VU27;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=KpsF/GutQ family protein {ECO:0000313|EMBL:ADU62220.1};
DE            EC=5.3.1.13 {ECO:0000313|EMBL:ADU62220.1};
GN   OrderedLocusNames=Daes_1206 {ECO:0000313|EMBL:ADU62220.1};
OS   Pseudodesulfovibrio aespoeensis (strain ATCC 700646 / DSM 10631 / Aspo-2)
OS   (Desulfovibrio aespoeensis).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae.
OX   NCBI_TaxID=643562 {ECO:0000313|EMBL:ADU62220.1, ECO:0000313|Proteomes:UP000002191};
RN   [1] {ECO:0000313|Proteomes:UP000002191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC   {ECO:0000313|Proteomes:UP000002191};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pedersen K., Jagevall S.,
RA   Hazen T., Woyke T.;
RT   "Complete sequence of Desulfovibrio aespoeensis Aspo-2.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU62220.1, ECO:0000313|Proteomes:UP000002191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC   {ECO:0000313|Proteomes:UP000002191};
RX   PubMed=24874683;
RA   Pedersen K., Bengtsson A., Edlund J., Rabe L., Hazen T., Chakraborty R.,
RA   Goodwin L., Shapiro N.;
RT   "Complete Genome Sequence of the Subsurface, Mesophilic Sulfate-Reducing
RT   Bacterium Desulfovibrio aespoeensis Aspo-2.";
RL   Genome Announc. 2:e00509-14(2014).
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; CP002431; ADU62220.1; -; Genomic_DNA.
DR   RefSeq; WP_013514151.1; NC_014844.1.
DR   AlphaFoldDB; E6VU27; -.
DR   STRING; 643562.Daes_1206; -.
DR   KEGG; das:Daes_1206; -.
DR   eggNOG; COG0517; Bacteria.
DR   eggNOG; COG0794; Bacteria.
DR   HOGENOM; CLU_040681_13_1_7; -.
DR   OrthoDB; 9762536at2; -.
DR   Proteomes; UP000002191; Chromosome.
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; 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:ADU62220.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT   DOMAIN          39..182
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          266..332
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT   SITE            57
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            109
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            150
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            191
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ   SEQUENCE   343 AA;  35731 MW;  9DA761C69BCEC951 CRC64;
     MACTSDRTDW LELAREVLDI EIEGLRTVSG QLGDGFVRAL TLMAECRGRV VITGIGKSGL
     VGRKIAATLS STGTPAFFLH PVEGAHGDMG MIRSEDVVLA LSNSGGSDEV NAIIPTLRSL
     GATVIAMTGN TASAMAELAD ITIEVRVPRE ACPMGLAPTS STTAHLAVGD ALAVCLMEWK
     SFGQDDFRKF HPGGSLGQRL AMCVDQLMHT ADLPVVTDTV TVREAITALN SGGLGLVAII
     DAGTMLRGVF TDGDVRRLVC SDAMDMDRPV AGVMTVSPRR AVVGESSAHV LDVMEQNEIT
     VLPVVLEDGR LAGMVHLHDL LGKGALRFSG SSGFGSAGSG SAE
//
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