NNRD_PHANO
ID NNRD_PHANO Reviewed; 325 AA.
AC Q0UVK8;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
DE EC=4.2.1.93 {ECO:0000255|HAMAP-Rule:MF_03157};
DE AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
GN ORFNames=SNOG_04206;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_03157};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-NADPHX + ATP = ADP + H(+) + NADPH + phosphate;
CC Xref=Rhea:RHEA:32231, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:64076,
CC ChEBI:CHEBI:456216; EC=4.2.1.93;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03157};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03157}.
CC -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP-
CC Rule:MF_03157}.
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DR EMBL; CH445330; EAT87966.1; -; Genomic_DNA.
DR RefSeq; XP_001794629.1; XM_001794577.1.
DR AlphaFoldDB; Q0UVK8; -.
DR SMR; Q0UVK8; -.
DR STRING; 13684.SNOT_04206; -.
DR EnsemblFungi; SNOT_04206; SNOT_04206; SNOG_04206.
DR GeneID; 5971497; -.
DR KEGG; pno:SNOG_04206; -.
DR eggNOG; KOG3974; Eukaryota.
DR HOGENOM; CLU_030651_0_0_1; -.
DR InParanoid; Q0UVK8; -.
DR OMA; HIPHTNE; -.
DR OrthoDB; 1337331at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047453; F:ATP-dependent NAD(P)H-hydrate dehydratase activity; IBA:GO_Central.
DR GO; GO:0110051; P:metabolite repair; 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; PS01049; YJEF_C_1; 1.
DR PROSITE; PS01050; YJEF_C_2; 1.
DR PROSITE; PS51383; YJEF_C_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Lyase; NAD; NADP; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..325
FT /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /id="PRO_0000416188"
FT DOMAIN 9..315
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 119
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 172..178
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 211..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 230..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 240
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
SQ SEQUENCE 325 AA; 34911 MW; 842D263CA0BBA742 CRC64;
MASATRKDLL KKVYNMVPPM LESFHKGQLG RVAVIGGSED YTGAPYFSAM ASAKLGCDMS
HVICEPGAGA VIKTYSPNLM VHPYMRQSKN VGQNENIESI KSEVVAMLSR LHVVVIGPGL
GRDKLMQDTC AEVIQEARKQ GIPFVLDADG LYLAQTRPEL VDGCTECILT PNVVEFGRLA
KAKGVNVDEG DPSELCSKLA KAFGGVTIIQ KGAKDYISNG SQTLISEGEG GLKRSGGQGD
TLTGSLATLL AYRKAYHDKI WDHGTNMEPS ETLALAAYGG SCITRECSKL AYKEKGRSLQ
AADLTEHVHT AFLNVIGEKE ETPKL
