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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)]

 A0A1Y1R7M0_9GAMM        Unreviewed;       504 AA.
A0A1Y1R7M0;
30-AUG-2017, integrated into UniProtKB/TrEMBL.
30-AUG-2017, sequence version 1.
05-DEC-2018, entry version 12.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|HAMAP-Rule:MF_01966};
Includes:
RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|HAMAP-Rule:MF_01965};
EC=4.2.1.136 {ECO:0000256|HAMAP-Rule:MF_01965};
AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|HAMAP-Rule:MF_01965};
Includes:
RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|HAMAP-Rule:MF_01966};
EC=5.1.99.6 {ECO:0000256|HAMAP-Rule:MF_01966};
AltName: Full=NAD(P)HX epimerase {ECO:0000256|HAMAP-Rule:MF_01966};
Name=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
Synonyms=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
ORFNames=B0D91_01890 {ECO:0000313|EMBL:OQX39294.1};
Oceanospirillales bacterium LUC14_002_19_P2.
Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
unclassified Oceanospirillales.
NCBI_TaxID=1940822 {ECO:0000313|EMBL:OQX39294.1, ECO:0000313|Proteomes:UP000192421};
[1] {ECO:0000313|EMBL:OQX39294.1, ECO:0000313|Proteomes:UP000192421}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LUC14_002_19_P2 {ECO:0000313|EMBL:OQX39294.1};
Lim S.J., Davis B.G., Gill D.E., Engel A.S., Anderson L.C.,
Campbell B.J.;
"Novel co-symbiosis in the unique lucinid bivalve Phacoides
pectinatus.";
Submitted (FEB-2017) 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:
Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215,
ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6;
Evidence={ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
-!- CATALYTIC ACTIVITY:
Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227,
ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6;
Evidence={ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184};
-!- CATALYTIC ACTIVITY:
Reaction=(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate;
Xref=Rhea:RHEA:32223, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456215,
ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP-
Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
-!- CATALYTIC ACTIVITY:
Reaction=(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate;
Xref=Rhea:RHEA:32235, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456215,
ChEBI:CHEBI:456216; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP-
Rule:MF_01965, 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: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OQX39294.1}.
-----------------------------------------------------------------------
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EMBL; MUIA01000082; OQX39294.1; -; Genomic_DNA.
Proteomes; UP000192421; 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; IPR017953; Carbohydrate_kinase_pred_CS.
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; PS01050; YJEF_C_2; 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:UP000192421};
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:UP000192421}.
DOMAIN 15 220 YjeF N-terminal.
{ECO:0000259|PROSITE:PS51385}.
NP_BIND 413 417 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
NP_BIND 432 441 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
REGION 66 70 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 134 140 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 376 382 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
METAL 67 67 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 130 130 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 166 166 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 145 145 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 163 163 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 326 326 NAD(P)HX; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01965}.
BINDING 442 442 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
SEQUENCE 504 AA; 53131 MW; 0A07742FF8A9C248 CRC64;
MDEWLPEALY TAEQVRHLDA VAINDYHING FELMKRAGQA AFDRMLERWP ALARGGTLQV
FCGAGNNGGD GYVIASLARQ RYLPVRVIAL KNPDELTGDA LRAWHWFRDL GGSTEVWSRN
VTITGTVLVD AMLGTGLSGE VRGDYRDAIQ MINHSQRPVL AVDIPSGLSA DTGAALGAAV
QAAMTVTFIG LKQGLLTGAG PRYCGTLNFA SLAVPDDIYS QELPASHLLR EQELAALVRP
RLADANKGTH GHLLVVGGDE GMGGAVVMAA EAALRTGAGL VTVATREEHV DAINARCPEI
MTRGVQDTDD LNRLITGKSA VVIGPGLGQS DWSKALLASI LQSDLPILAD ADALNLMAEE
GQLLDSTSRA LLMTPHPGEA SRLLQELIPD IQANRFAAVR QLQQQYGCVA VLKGAGSLVY
DGETVSLCGA GNPGMAVAGM GDVLSGVIGS LLAQGYDMVQ AAKIGVWLHA AAGDDCAAEA
GQIGMKASDL LPYIRRRVNQ LANA


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