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Database: UniProt
Entry: A0A1P8WBI0_9PLAN
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ID   A0A1P8WBI0_9PLAN        Unreviewed;       293 AA.
AC   A0A1P8WBI0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|HAMAP-Rule:MF_01965};
DE            EC=4.2.1.136 {ECO:0000256|HAMAP-Rule:MF_01965};
DE   AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|HAMAP-Rule:MF_01965};
GN   Name=nnr_2 {ECO:0000313|EMBL:APZ91418.1};
GN   Synonyms=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
GN   ORFNames=Fuma_01006 {ECO:0000313|EMBL:APZ91418.1};
OS   Fuerstiella marisgermanici.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Fuerstiella.
OX   NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ91418.1, ECO:0000313|Proteomes:UP000187735};
RN   [1] {ECO:0000313|EMBL:APZ91418.1, ECO:0000313|Proteomes:UP000187735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NH11 {ECO:0000313|EMBL:APZ91418.1,
RC   ECO:0000313|Proteomes:UP000187735};
RX   PubMed=28066393; DOI=10.3389/fmicb.2016.02079;
RA   Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., Rast P.,
RA   Borchert D., Glockner I., Freese H.M., Klenk H.P., Overmann J.,
RA   Kaster A.K., Rohde M., Wiegand S., Jogler C.;
RT   "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of the
RT   Phylum Planctomycetes from the German Wadden Sea.";
RL   Front. Microbiol. 7:2079-2079(2016).
CC   -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the
CC       expense of ADP, which is converted to AMP. 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_01965}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate;
CC         Xref=Rhea:RHEA:32223, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456215,
CC         ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01965};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate;
CC         Xref=Rhea:RHEA:32235, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456215,
CC         ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01965};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01965};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01965}.
CC   -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01965}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01965}.
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DR   EMBL; CP017641; APZ91418.1; -; Genomic_DNA.
DR   RefSeq; WP_077023184.1; NZ_CP017641.1.
DR   AlphaFoldDB; A0A1P8WBI0; -.
DR   STRING; 1891926.Fuma_01006; -.
DR   KEGG; fmr:Fuma_01006; -.
DR   OrthoDB; 9806925at2; -.
DR   Proteomes; UP000187735; Chromosome.
DR   GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   NCBIfam; TIGR00196; yjeF_cterm; 1.
DR   PANTHER; PTHR12592:SF0; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE; 1.
DR   PANTHER; PTHR12592; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER; 1.
DR   Pfam; PF01256; Carb_kinase; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS01049; YJEF_C_1; 1.
DR   PROSITE; PS51383; YJEF_C_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01965};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01965};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01965};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01965};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01965}; Reference proteome {ECO:0000313|Proteomes:UP000187735}.
FT   DOMAIN          4..287
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51383"
FT   BINDING         110
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         162
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         199..203
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         227
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT   BINDING         228
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
SQ   SEQUENCE   293 AA;  30104 MW;  815E6606AAA69E6C CRC64;
     MSTKIQIDDL EFANRPVDGH KGTFGKVAVI GGSLGMSGSI TLSATAALRG GAGLVTAAVP
     QSIQAIVAGY EPSYMTVALP TDVHGQLAAV DADIVTELLD GKSAVAIGPG LGQTKLAADL
     VLAVLKQADC PVVLDADALN LAAEFELLHG IPRRSRWVIT PHPGEFARLT GESISHVSAN
     RESLAERFAA EHELTVVLKG ANTVVTDGSR TYVNQTGNSG MATGGSGDIL TGLTAAVLGQ
     HADALEGAIL AVYVHGIAGD LAAEALSQRG MIASDLLRFL SAAWRNLSHE PSD
//
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