(data stored in SCRATCH zone)

SWISSPROT: Q6BM33_DEBHA

ID   Q6BM33_DEBHA            Unreviewed;       188 AA.
AC   Q6BM33;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 97.
DE   RecName: Full=Gluconokinase {ECO:0000256|RuleBase:RU363066};
DE            EC=2.7.1.12 {ECO:0000256|RuleBase:RU363066};
GN   OrderedLocusNames=DEHA2F08646g {ECO:0000313|EMBL:CAG89078.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89078.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89078.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+);
CC         Xref=Rhea:RHEA:19433, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58759, ChEBI:CHEBI:456216;
CC         EC=2.7.1.12; Evidence={ECO:0000256|RuleBase:RU363066};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation.
CC       {ECO:0000256|RuleBase:RU363066}.
CC   -!- SIMILARITY: Belongs to the gluconokinase GntK/GntV family.
CC       {ECO:0000256|RuleBase:RU363066}.
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DR   EMBL; CR382138; CAG89078.2; -; Genomic_DNA.
DR   RefSeq; XP_460738.2; XM_460738.1.
DR   STRING; 4959.XP_460738.2; -.
DR   EnsemblFungi; CAG89078; CAG89078; DEHA2F08646g.
DR   GeneID; 2903753; -.
DR   KEGG; dha:DEHA2F08646g; -.
DR   HOGENOM; HOG000032567; -.
DR   InParanoid; Q6BM33; -.
DR   KO; K00851; -.
DR   OMA; ARKGHFM; -.
DR   OrthoDB; 1275465at2759; -.
DR   UniPathway; UPA00792; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004340; F:glucokinase activity; IEA:EnsemblFungi.
DR   GO; GO:0046316; F:gluconokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0061688; P:glycolytic process via Entner-Doudoroff Pathway; IEA:EnsemblFungi.
DR   CDD; cd02021; GntK; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR006001; Therm_gnt_kin.
DR   Pfam; PF01202; SKI; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01313; therm_gnt_kin; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BM33.
DR   SWISS-2DPAGE; Q6BM33.
KW   ATP-binding {ECO:0000256|RuleBase:RU363066};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Kinase {ECO:0000256|RuleBase:RU363066};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transferase {ECO:0000256|RuleBase:RU363066}.
SQ   SEQUENCE   188 AA;  20882 MW;  8B76E7C2BB9C5439 CRC64;
     MTTTPNTVIV VGGPAGTGKT TIAELLATHF QCPFIEGDAL HPPQNISKMS EGIPLTDEDR
     WDWLKELTRA SVGQCIDSTN KSNIAIVSCS ILKKIYREYI KQCSGESSAG EIQFKFVFLH
     TTLEHLFERV QNRPGHFMKS DMVSSQYSIM EIPCDDELLE NGGEALPVDT TNKSPQEIYK
     EVVSSLKL
//

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