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Database: UniProt
Entry: F2NID7_DESAR
LinkDB: F2NID7_DESAR
Original site: F2NID7_DESAR 
ID   F2NID7_DESAR            Unreviewed;       334 AA.
AC   F2NID7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=KpsF/GutQ family protein {ECO:0000313|EMBL:AEB10339.1};
DE            EC=5.3.1.13 {ECO:0000313|EMBL:AEB10339.1};
GN   OrderedLocusNames=Desac_2521 {ECO:0000313|EMBL:AEB10339.1};
OS   Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobaccia; Desulfobaccales;
OC   Desulfobaccaceae; Desulfobacca.
OX   NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB10339.1, ECO:0000313|Proteomes:UP000000483};
RN   [1] {ECO:0000313|EMBL:AEB10339.1, ECO:0000313|Proteomes:UP000000483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC   {ECO:0000313|Proteomes:UP000000483};
RX   PubMed=21886866;
RA   Goker M., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA   Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of the acetate-degrading sulfate reducer
RT   Desulfobacca acetoxidans type strain (ASRB2).";
RL   Stand. Genomic Sci. 4:393-401(2011).
RN   [2] {ECO:0000313|Proteomes:UP000000483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC   {ECO:0000313|Proteomes:UP000000483};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Desulfobacca acetoxidans DSM 11109.";
RL   Submitted (MAR-2011) 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; CP002629; AEB10339.1; -; Genomic_DNA.
DR   RefSeq; WP_013707448.1; NC_015388.1.
DR   AlphaFoldDB; F2NID7; -.
DR   STRING; 880072.Desac_2521; -.
DR   KEGG; dao:Desac_2521; -.
DR   eggNOG; COG0517; Bacteria.
DR   eggNOG; COG0794; Bacteria.
DR   HOGENOM; CLU_040681_13_1_7; -.
DR   OrthoDB; 9762536at2; -.
DR   Proteomes; UP000000483; 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; 2.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Isomerase {ECO:0000313|EMBL:AEB10339.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000483};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT   DOMAIN          42..185
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          211..272
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          278..334
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT   SITE            60
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            112
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            153
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            194
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ   SEQUENCE   334 AA;  35506 MW;  F0E0DB6BF7F4CA7F CRC64;
     MTAQKRPLSH PKILQLAREV LAIESEGIAN LIPKLDHNFV RAVQMIFQAK GRLIVTGVGK
     SGIVARKIVA TLNSTGAPSL FLHPVEAMHG DLGMISPQDV VLALSNSGET SELTILLPSI
     KRLGVPLIAL TGRVESTLAS HSDVVIDVGV PREACPLGLA PTASTTAALA MGDALAVALL
     TQRGFKASDF RRFHPGGSLG ARLSLAIGEV MLTGNRVPRV HPEDPLISAL REMDEKGFGA
     TLVVDGAGVL LGIFTDGDLR RCLRKFQHLQ DKTVAQVMTP SPHAIGPESL ASQALEHMEH
     KAITVLPVVD AKRVVLGIVH LHDLLGRGEF QFKA
//
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