NNRD_FLAPJ
ID NNRD_FLAPJ Reviewed; 282 AA.
AC A6GXW4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_01965};
DE EC=4.2.1.136 {ECO:0000255|HAMAP-Rule:MF_01965};
DE AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_01965};
GN Name=nnrD {ECO:0000255|HAMAP-Rule:MF_01965}; OrderedLocusNames=FP0837;
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
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:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_01965};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01965};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01965}.
CC -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP-
CC Rule:MF_01965}.
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DR EMBL; AM398681; CAL42937.1; -; Genomic_DNA.
DR RefSeq; WP_011962993.1; NC_009613.3.
DR RefSeq; YP_001295753.1; NC_009613.3.
DR AlphaFoldDB; A6GXW4; -.
DR SMR; A6GXW4; -.
DR STRING; 402612.FP0837; -.
DR EnsemblBacteria; CAL42937; CAL42937; FP0837.
DR GeneID; 66552541; -.
DR KEGG; fps:FP0837; -.
DR PATRIC; fig|402612.5.peg.850; -.
DR eggNOG; COG0063; Bacteria.
DR HOGENOM; CLU_024853_2_2_10; -.
DR OMA; HIPHTNE; -.
DR Proteomes; UP000006394; 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 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; Reference proteome.
FT CHAIN 1..282
FT /note="ADP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /id="PRO_0000416142"
FT DOMAIN 8..280
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT BINDING 106
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT BINDING 157
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT BINDING 220
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT BINDING 221
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
SQ SEQUENCE 282 AA; 30918 MW; 21DB3A1D5AAAF34D CRC64;
MRDFCQIDTQ EIIKRYKPID KYTHKGLQGH ALIIGGSYGK MGSVVLASKA CIRSGAGLVT
AYIPKCGCDI VQISVPEVMV ITDDYLEHIA LINFDLNLKS IGIGVGMGQH PDTQHAFFNF
LKSNKLPLVI DADALNILSQ NIEWLSLLPK KAILTPHQKE LERLIGKWSS EEEKLEKVKR
LCLEYDLIFV LKGAPTMIVN NKSTYENTTG NQALATAGSG DVLAGIITSL LAQSYEPINA
AIIGVYLHGL TADIAYPKVG YQSFIASDII ETLGEAYLHI IK
