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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)]

 A0A1W9NJ89_9GAMM        Unreviewed;       503 AA.
A0A1W9NJ89;
05-JUL-2017, integrated into UniProtKB/TrEMBL.
05-JUL-2017, sequence version 1.
18-JUL-2018, entry version 11.
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=B0D94_00895 {ECO:0000313|EMBL:OQX32425.1};
Gammaproteobacteria bacterium LUC14_002_19_P1.
Bacteria; Proteobacteria; Gammaproteobacteria;
sulfur-oxidizing symbionts.
NCBI_TaxID=1940819 {ECO:0000313|EMBL:OQX32425.1, ECO:0000313|Proteomes:UP000192543};
[1] {ECO:0000313|EMBL:OQX32425.1, ECO:0000313|Proteomes:UP000192543}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LUC14_002_19_P1 {ECO:0000313|EMBL:OQX32425.1};
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: (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:OQX32425.1}.
-----------------------------------------------------------------------
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EMBL; MUHZ01000068; OQX32425.1; -; Genomic_DNA.
Proteomes; UP000192543; 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:UP000192543};
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:UP000192543}.
DOMAIN 22 223 YjeF N-terminal.
{ECO:0000259|PROSITE:PS51385}.
NP_BIND 412 416 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
NP_BIND 431 440 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
REGION 70 74 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 137 143 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 375 381 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
METAL 71 71 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 133 133 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 169 169 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 166 166 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 329 329 NAD(P)HX; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01965}.
BINDING 441 441 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
SEQUENCE 503 AA; 51671 MW; 52318605CABBDB36 CRC64;
MSGSMVTETT ALPQALYRAA DVRELDRMAI EEQGIPGRVL MERAGAAAFA WMRRIWPAAR
SLLVVCGGGN NGGDGYVVAR LARQAGLDCR VMQVGDPSRL RGDALACAGA FAEAGGRAEP
FAGIPGRVEL IVDALFGTGL ERPVTGEWAV AVEAVNDHPA PVISLDLPSG LHSDSGRVLG
VAVRAAASIS FIGLKRGMFT GQGPAYCGRV LFDALEVPRA LHRGLPAPVR RIDWEALSGG
MRPRPRDAHK GVFGRLLLVG GDAGFAGAIA LAAEAAARTG AGLVRVATRQ MHCPALGAAC
PEVMWQGVER PGVLGALLGW ASAVVVGPGL GRSAWGQGLL ARVLESDLPL VVDADALNLL
AADPLWRDNW ILTPHPGEAA RLLGCSVAEV EADRFAALGE LRSRFGGTVL LKGAGTLIDD
EAGIALCSGG NPGMASGGMG DLLSGLIGGL LVQGFERPAV LGAALHAAAG DLAARGGERG
MLARDLLPGI RCLINPEVAD AAS


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