NNRD_PEDHC
ID NNRD_PEDHC Reviewed; 300 AA.
AC E0VSF4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
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=PHUM417680;
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA;
RX PubMed=20566863; DOI=10.1073/pnas.1003379107;
RA Kirkness E.F., Haas B.J., Sun W., Braig H.R., Perotti M.A., Clark J.M.,
RA Lee S.H., Robertson H.M., Kennedy R.C., Elhaik E., Gerlach D.,
RA Kriventseva E.V., Elsik C.G., Graur D., Hill C.A., Veenstra J.A.,
RA Walenz B., Tubio J.M., Ribeiro J.M., Rozas J., Johnston J.S., Reese J.T.,
RA Popadic A., Tojo M., Raoult D., Reed D.L., Tomoyasu Y., Krause E.,
RA Mittapalli O., Margam V.M., Li H.M., Meyer J.M., Johnson R.M.,
RA Romero-Severson J., Vanzee J.P., Alvarez-Ponce D., Vieira F.G., Aguade M.,
RA Guirao-Rico S., Anzola J.M., Yoon K.S., Strycharz J.P., Unger M.F.,
RA Christley S., Lobo N.F., Seufferheld M.J., Wang N., Dasch G.A.,
RA Struchiner C.J., Madey G., Hannick L.I., Bidwell S., Joardar V., Caler E.,
RA Shao R., Barker S.C., Cameron S., Bruggner R.V., Regier A., Johnson J.,
RA Viswanathan L., Utterback T.R., Sutton G.G., Lawson D., Waterhouse R.M.,
RA Venter J.C., Strausberg R.L., Berenbaum M.R., Collins F.H., Zdobnov E.M.,
RA Pittendrigh B.R.;
RT "Genome sequences of the human body louse and its primary endosymbiont
RT provide insights into the permanent parasitic lifestyle.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12168-12173(2010).
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 -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP-
CC Rule:MF_03157}.
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DR EMBL; DS235750; EEB16310.1; -; Genomic_DNA.
DR RefSeq; XP_002429048.1; XM_002429003.1.
DR AlphaFoldDB; E0VSF4; -.
DR SMR; E0VSF4; -.
DR STRING; 121225.PHUM417680-PA; -.
DR EnsemblMetazoa; PHUM417680-RA; PHUM417680-PA; PHUM417680.
DR GeneID; 8234427; -.
DR KEGG; phu:Phum_PHUM417680; -.
DR CTD; 8234427; -.
DR VEuPathDB; VectorBase:PHUM417680; -.
DR eggNOG; KOG3974; Eukaryota.
DR HOGENOM; CLU_030651_3_0_1; -.
DR InParanoid; E0VSF4; -.
DR OMA; HIPHTNE; -.
DR PhylomeDB; E0VSF4; -.
DR Proteomes; UP000009046; Unplaced.
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; IEA:UniProtKB-UniRule.
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; 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; PS51383; YJEF_C_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Lyase; NAD; NADP; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..300
FT /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /id="PRO_0000416168"
FT DOMAIN 6..297
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 106
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 158..164
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 188..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 218..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 228
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
SQ SEQUENCE 300 AA; 32508 MW; C0E48734BE8B49C7 CRC64;
MSNCKYAGKI KEFIPKLTPT LHKGQCGRIG IIGGSAEYTG APYFAAISAL KLGADLVYVF
CCKEAGPVIK SYSPELIVLP ILDSGNVTEK IENWLTRLHA LVIGPGLGTK PVNIIRLCNE
RSKLSVLPLI IDADGLRIVN DNLDLIKKYH GPVILTPNEV EFKRLSSKFS NTEAINVASS
LNSVLIQKGS TDVITNGINF DEFDFTFDDV TITCETFGSN RRCGGQGDIL SGCIATFVAW
FELFKSNNTF IIPLSSVSCY GACAVTKTCS KLAFQKFGRS MTASDMIGCI HQSFTSLFGS
