NNRD_POLPP
ID NNRD_POLPP Reviewed; 413 AA.
AC D3BMU4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 48.
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=PPL_12517;
OS Polysphondylium pallidum (strain ATCC 26659 / Pp 5 / PN500) (Heterostelium
OS pallidum).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Acytosteliales;
OC Acytosteliaceae; Heterostelium.
OX NCBI_TaxID=670386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26659 / Pp 5 / PN500;
RX PubMed=21757610; DOI=10.1101/gr.121137.111;
RA Heidel A.J., Lawal H.M., Felder M., Schilde C., Helps N.R., Tunggal B.,
RA Rivero F., John U., Schleicher M., Eichinger L., Platzer M., Noegel A.A.,
RA Schaap P., Gloeckner G.;
RT "Phylogeny-wide analysis of social amoeba genomes highlights ancient
RT origins for complex intercellular communication.";
RL Genome Res. 21:1882-1891(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADBJ01000043; EFA77306.1; -; Genomic_DNA.
DR AlphaFoldDB; D3BMU4; -.
DR SMR; D3BMU4; -.
DR STRING; 670386.D3BMU4; -.
DR InParanoid; D3BMU4; -.
DR OMA; DHRRETE; -.
DR OrthoDB; 1337331at2759; -.
DR Proteomes; UP000001396; Unassembled WGS sequence.
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; 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;
KW ATP-binding; Lyase; NAD; NADP; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..413
FT /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /id="PRO_0000416171"
FT DOMAIN 98..402
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 199
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 252..258
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 292..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 311..320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 321
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
SQ SEQUENCE 413 AA; 45077 MW; 03404403724C06FF CRC64;
MFCIIHFGNP KNDKFLGSST LYSQKLKTNN IKILCLQVFY YNIYESTNNN NNNKNKNKTL
LLNNIRTYST LSKGALSTTT TATTKKMSMD DSFELPTNLN HFLSYVPSLE YHMHKGQCGR
IGVFGGSAEY TGAPFFAGIT SLRLGADIVH IFAPSEGGTA TAIKTLSPEL IVHPLDQQMD
PSTIIPWLLS IHVLIIGPGL GRSSIAWKSA KEVIKAARNI NLPMVLDGDA LRLICEDLEL
VKGYDKVILT PNFVEYRALS DAAKKLNNDN SNNILSPSDL AKALGNVVIV QKGQEDIITD
GTISYSCDKA GMPRRCGGQG DVLAGVIGTF YAWTQNALKG KTSEELEHLK ESIGENQSAA
ASAAYAGCVL VRYAAKLAFK NNRRSTITDD IIKSVPNALV WGFLTDDRGR PTI