(data stored in ACNUC7421 zone)

SWISSPROT: Q75C61_ASHGO

ID   Q75C61_ASHGO            Unreviewed;       358 AA.
AC   Q75C61;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 94.
DE   RecName: Full=ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|HAMAP-Rule:MF_03157};
DE            EC=4.2.1.93 {ECO:0000256|HAMAP-Rule:MF_03157};
DE   AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000256|HAMAP-Rule:MF_03157};
GN   ORFNames=AGOS_ACR055W {ECO:0000313|EMBL:AAS51282.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51282.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51282.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the
CC       expense of ATP, which is converted to ADP. Together with NAD(P)HX
CC       epimerase, which catalyzes the epimerization of the S-and R-forms, the
CC       enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of
CC       NAD(P)H that is a result of enzymatic or heat-dependent hydration.
CC       {ECO:0000256|HAMAP-Rule:MF_03157}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate;
CC         Xref=Rhea:RHEA:19017, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57945, ChEBI:CHEBI:64074,
CC         ChEBI:CHEBI:456216; EC=4.2.1.93; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03157};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03157};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03157}.
CC   -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000256|HAMAP-
CC       Rule:MF_03157}.
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DR   EMBL; AE016816; AAS51282.2; -; Genomic_DNA.
DR   RefSeq; NP_983458.2; NM_208811.2.
DR   STRING; 33169.AAS51282; -.
DR   EnsemblFungi; AAS51282; AAS51282; AGOS_ACR055W.
DR   GeneID; 4619583; -.
DR   KEGG; ago:AGOS_ACR055W; -.
DR   HOGENOM; HOG000163126; -.
DR   InParanoid; Q75C61; -.
DR   KO; K17757; -.
DR   OMA; NLMVHPL; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047453; F:ATP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0052856; F:NADHX epimerase activity; IBA:GO_Central.
DR   GO; GO:0052857; F:NADPHX epimerase activity; IBA:GO_Central.
DR   GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01171; YXKO-related; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_01965; NADHX_dehydratase; 1.
DR   InterPro; IPR017953; Carbohydrate_kinase_pred_CS.
DR   InterPro; IPR000631; CARKD.
DR   InterPro; IPR029056; Ribokinase-like.
DR   Pfam; PF01256; Carb_kinase; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00196; yjeF_cterm; 1.
DR   PROSITE; PS01050; YJEF_C_2; 1.
DR   PROSITE; PS51383; YJEF_C_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75C61.
DR   SWISS-2DPAGE; Q75C61.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03157};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03157};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_03157};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_03157};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03157};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   NP_BIND         240..244
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT   NP_BIND         261..270
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT   REGION          210..216
FT                   /note="NAD(P)HX"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT   BINDING         146
FT                   /note="NAD(P)HX; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
FT   BINDING         271
FT                   /note="NAD(P)HX"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
SQ   SEQUENCE   358 AA;  37921 MW;  D2BB447F4A419A84 CRC64;
     MAWPRRAAEV ARSTMASRLD KLPEAVSRLQ SLSHRQLLRL AQGVCIPALS PSLHKGQSGR
     VCVVGGSLEY TGAPYFSAHA AALMGSDLVH VLCEWNAATP IKAYSPDLMV HPHLRDSSSL
     ARGLEPATEA VRALVDRVHV LVLGPGLGRD PAMLRSVAGI LEYVADKHEG GIPVVLDADA
     LLLLSEQATA AAARAALRRF PPDRVILTPN AVEAKRLAGA FELDDPARLA EHLNCTVVLK
     GGPDRIYAPG GSSPLSCSHE GSLKRVGGQG DTLTGCLAAM LAYNRAIHDF GIAEPDYTGL
     EGGTLSASER TALCCYVACA VARGASHRAY EAQGRAMQTS DLNGHVGAIF RDFFPERQ
//

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