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Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]

 A0A0Q9I714_9BRAD        Unreviewed;       505 AA.
A0A0Q9I714;
20-JAN-2016, integrated into UniProtKB/TrEMBL.
20-JAN-2016, sequence version 1.
18-JUL-2018, entry version 25.
RecName: Full=Bifunctional NAD(P)H-hydrate repair enzyme {ECO:0000256|PIRNR:PIRNR017184};
AltName: Full=Nicotinamide nucleotide repair protein {ECO:0000256|PIRNR:PIRNR017184};
Includes:
RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|PIRNR:PIRNR017184};
EC=4.2.1.136 {ECO:0000256|PIRNR:PIRNR017184};
AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|PIRNR:PIRNR017184};
Includes:
RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|PIRNR:PIRNR017184};
EC=5.1.99.6 {ECO:0000256|PIRNR:PIRNR017184};
Name=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
Synonyms=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
ORFNames=ASE66_20755 {ECO:0000313|EMBL:KRE12913.1};
Bosea sp. Root483D1.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Bradyrhizobiaceae; Bosea.
NCBI_TaxID=1736544 {ECO:0000313|EMBL:KRE12913.1, ECO:0000313|Proteomes:UP000051771};
[1] {ECO:0000313|EMBL:KRE12913.1, ECO:0000313|Proteomes:UP000051771}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Root483D1 {ECO:0000313|EMBL:KRE12913.1,
ECO:0000313|Proteomes:UP000051771};
Millard Andrew;
Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:KRE12913.1, ECO:0000313|Proteomes:UP000051771}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Root483D1 {ECO:0000313|EMBL:KRE12913.1,
ECO:0000313|Proteomes:UP000051771};
Vorholt J.;
"Functional overlap of the Arabidopsis leaf and root microbiotas.";
Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of
the S- and R-forms of NAD(P)HX and the dehydration of the S-form
of NAD(P)HX at the expense of ADP, which is converted to AMP. This
allows the repair of both epimers of NAD(P)HX, a damaged form of
NAD(P)H that is a result of enzymatic or heat-dependent hydration.
{ECO:0000256|PIRNR:PIRNR017184}.
-!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at
the expense of ADP, which is converted to AMP. Together with
NAD(P)HX epimerase, which catalyzes the epimerization of the
S- and R-forms, the enzyme allows the repair of both epimers of
NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic
or heat-dependent hydration. {ECO:0000256|HAMAP-Rule:MF_01965}.
-!- FUNCTION: Catalyzes the epimerization of the S- and R-forms of
NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic
or heat-dependent hydration. This is a prerequisite for the S-
specific NAD(P)H-hydrate dehydratase to allow the repair of both
epimers of NAD(P)HX. {ECO:0000256|HAMAP-Rule:MF_01966}.
-!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6-
tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy-
1,4,5,6-tetrahydronicotinamide-adenine dinucleotide.
{ECO:0000256|PIRNR:PIRNR017184}.
-!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6-
tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6-
beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
phosphate. {ECO:0000256|PIRNR:PIRNR017184}.
-!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate +
NADH. {ECO:0000256|PIRNR:PIRNR017184}.
-!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
tetrahydronicotinamide adenine-dinucleotide phosphate = AMP +
phosphate + NADPH. {ECO:0000256|PIRNR:PIRNR017184}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01965};
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01965}.
-!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000256|HAMAP-
Rule:MF_01965}.
-!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000256|HAMAP-
Rule:MF_01966}.
-!- SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD
family. {ECO:0000256|PIRNR:PIRNR017184}.
-!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP
family. {ECO:0000256|PIRNR:PIRNR017184}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KRE12913.1}.
-----------------------------------------------------------------------
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EMBL; LMJW01000022; KRE12913.1; -; Genomic_DNA.
EnsemblBacteria; KRE12913; KRE12913; ASE66_20755.
Proteomes; UP000051771; Unassembled WGS sequence.
GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-UniRule.
GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-UniRule.
CDD; cd01171; YXKO-related; 1.
Gene3D; 3.40.1190.20; -; 1.
Gene3D; 3.40.50.10260; -; 1.
HAMAP; MF_01965; NADHX_dehydratase; 1.
HAMAP; MF_01966; NADHX_epimerase; 1.
InterPro; IPR000631; CARKD.
InterPro; IPR030677; Nnr.
InterPro; IPR029056; Ribokinase-like.
InterPro; IPR004443; YjeF_N_dom.
InterPro; IPR036652; YjeF_N_dom_sf.
Pfam; PF01256; Carb_kinase; 1.
Pfam; PF03853; YjeF_N; 1.
PIRSF; PIRSF017184; Nnr; 1.
SUPFAM; SSF53613; SSF53613; 1.
SUPFAM; SSF64153; SSF64153; 1.
TIGRFAMs; TIGR00196; yjeF_cterm; 1.
TIGRFAMs; TIGR00197; yjeF_nterm; 1.
PROSITE; PS51383; YJEF_C_3; 1.
PROSITE; PS51385; YJEF_N; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01965,
ECO:0000256|PIRNR:PIRNR017184};
Complete proteome {ECO:0000313|Proteomes:UP000051771};
Isomerase {ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
Lyase {ECO:0000256|HAMAP-Rule:MF_01965,
ECO:0000256|PIRNR:PIRNR017184};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
NAD {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
NADP {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01965,
ECO:0000256|PIRNR:PIRNR017184};
Potassium {ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
Reference proteome {ECO:0000313|Proteomes:UP000051771};
Signal {ECO:0000256|SAM:SignalP}.
SIGNAL 1 18 {ECO:0000256|SAM:SignalP}.
CHAIN 19 505 Bifunctional NAD(P)H-hydrate repair
enzyme. {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5006374645.
DOMAIN 17 215 YjeF N-terminal.
{ECO:0000259|PROSITE:PS51385}.
NP_BIND 419 423 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
NP_BIND 439 448 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
REGION 64 68 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 129 135 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 381 387 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
METAL 65 65 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 125 125 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 161 161 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 158 158 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 327 327 NAD(P)HX; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01965}.
BINDING 449 449 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
SEQUENCE 505 AA; 51238 MW; E29AF7EEC86816D4 CRC64;
MTAAPPAALA LLSVAEMAAA DAMTIAAGTP GIVLMEKAGR AVADAVTRRV RPGQRVLALC
GPGNNGGDGF VAARLLAERG CRVTLALAGE RVALRGDAAL AAESWTGAID AIGGIDPARH
DIVIDALFGA GLGRPISGEV ATLVERVNAA RRAVIAVDVP SGVHGDTGLT EGPAIRADET
VTFFRLKPGH LLHPGRALCG VVTLADIGIR PEIVFAPDKI VPSAFRNSPA LWRTRLPDHA
AGVHKYTRGA VAVAAGGLSG VGAPRLGARA ALRIGAGLAT IICRPEALAA HAGRGPDALM
QAAAADAPAF ETALSARKLD ALLIGPALGL DAEARSWVAV ALHSAAPCVL DADALSHIGA
QRPGFTDLLR QRTGPAVLTP HEGEFKRLFA EAAGFEPGRG KLERARQAAR QTGAVVVLKG
PDTVIAAPDG RAAINDTGSP AMATAGSGDV LGGIVAGLLA QKMPAFEAAC AAVWFHGRAG
EEIGMGLIAD DLPEALPRLL ADLDD


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