NNRD_RHOBA
ID NNRD_RHOBA Reviewed; 304 AA.
AC Q7UFW7;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=RB8287;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294147; CAD78562.1; -; Genomic_DNA.
DR RefSeq; NP_868284.1; NC_005027.1.
DR RefSeq; WP_011121794.1; NC_005027.1.
DR AlphaFoldDB; Q7UFW7; -.
DR SMR; Q7UFW7; -.
DR STRING; 243090.RB8287; -.
DR EnsemblBacteria; CAD78562; CAD78562; RB8287.
DR KEGG; rba:RB8287; -.
DR PATRIC; fig|243090.15.peg.3994; -.
DR eggNOG; COG0063; Bacteria.
DR HOGENOM; CLU_024853_2_2_0; -.
DR InParanoid; Q7UFW7; -.
DR OMA; HIPHTNE; -.
DR OrthoDB; 1748633at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052856; F:NADHX epimerase activity; IBA:GO_Central.
DR GO; GO:0052857; F:NADPHX epimerase 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; 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..304
FT /note="ADP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /id="PRO_0000416148"
FT DOMAIN 8..299
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT BINDING 170
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT BINDING 239
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
FT BINDING 240
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01965"
SQ SEQUENCE 304 AA; 30876 MW; D96F2888E65B6288 CRC64;
MPSIETQSTS PPPLRIPHRE ASAHKGNFGR VLLIGGSRGM AGSIALSSIA ALHTGSGLVA
AAVPDCILDC VAGFHPALMT IGLGDDGEKF ADPAWQSLKD RLSAQAAIGC GPGMTTGSGG
ATIVEGLLAK KDLPLVLDAD ALNIIAQNDW LSDGRFERSK ADAACVLTPH PGELQRLTGA
SAKDVDAQVE AAAELACRLG LTIVVKGGPS HVAYQNGDGG KQVWQNTTGN PGMATAGCGD
VLTGIVTSLL GQGLSGPDAA KLGVWIHGRC GDEAAARWSH AGMTSLHALD ALALVADEMT
QPAD
