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Multifunctional fusion 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) (NAD(P)HX epimerase)]

 A0A0A8WSP1_9DELT        Unreviewed;       528 AA.
A0A0A8WSP1;
04-MAR-2015, integrated into UniProtKB/TrEMBL.
04-MAR-2015, sequence version 1.
16-JAN-2019, entry version 31.
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=nnr {ECO:0000313|EMBL:GAM10670.1};
Synonyms=nnrD {ECO:0000256|HAMAP-Rule:MF_01965},
nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
ORFNames=OR1_02963 {ECO:0000313|EMBL:GAM10670.1};
Geobacter sp. OR-1.
Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
Geobacteraceae; Geobacter.
NCBI_TaxID=1266765 {ECO:0000313|EMBL:GAM10670.1, ECO:0000313|Proteomes:UP000030972};
[1] {ECO:0000313|EMBL:GAM10670.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM10670.1,
ECO:0000313|Proteomes:UP000030972};
PubMed=23668621; DOI=10.1021/es400231x;
Ohtsuka T., Yamaguchi N., Makino T., Sakurai K., Kimura K., Kudo K.,
Homma E., Dong DT., Amachi S.;
"Arsenic dissolution from Japanese paddy soil by a dissimilatory
arsenate-reducing bacterium Geobacter sp. OR-1.";
Environ. Sci. Technol. 47:6263-6271(2013).
[2] {ECO:0000313|EMBL:GAM10670.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM10670.1,
ECO:0000313|Proteomes:UP000030972};
Ehara A., Suzuki H., Amachi S.;
"Draft Genome Sequence of Geobacter sp. Strain OR-1, an Arsenate-
Respiring Bacterium Isolated from Japanese Paddy Soil.";
Genome Announc. 3:e01478-14(2015).
-!- 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:GAM10670.1}.
-----------------------------------------------------------------------
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EMBL; BAZF01000014; GAM10670.1; -; Genomic_DNA.
RefSeq; WP_041972598.1; NZ_BAZF01000014.1.
EnsemblBacteria; GAM10670; GAM10670; OR1_02963.
OrthoDB; 1748633at2; -.
Proteomes; UP000030972; 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:UP000030972};
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:UP000030972}.
DOMAIN 9 220 YjeF N-terminal.
{ECO:0000259|PROSITE:PS51385}.
NP_BIND 424 428 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
NP_BIND 444 453 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
REGION 59 63 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 134 140 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 387 393 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
METAL 60 60 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 335 335 NAD(P)HX; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01965}.
BINDING 454 454 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
SEQUENCE 528 AA; 54576 MW; 8C5A5ED8E5DFD5EC CRC64;
MKIVTAEQMQ LIDQETIKNY GIPGLHLMER AGSACAEVMI SSVSPTAGVS AIIFAGKGNN
GGDGYVIARK LFQAGWDVSV VVLAQQRDIT GDAADNLAGL PEGVGLSFCS DMDSLVNSLA
EIGKYALVVD AIFGTGLKSQ VSGIYRHAID AINAMGQQVI AVDIPSGIHG STGEVLGAAV
KADLTVTFAS AKLGHVLYPG ASFTGDLKVV DIGIPSEIIQ KAKSYDFIDS EAAAALLRPR
SPVAHKGSFG HGVIIAGSTG HTGAAVLAGN SAVRSGAGLV SLAIPSSLNQ VIEIKTTEAM
TIPVDDSGRG YLGDESLPDI HVGLDGKDVV AIGPGLSRKP ETTLLVQKLI GSVPLPLVVD
ADGLNAISEN IALLCHRTSP VVILTPHPGE MARLAGLSVP EIECDRIGVS VAFAVKYKVF
LILKGARTVI VSPEGDVAIN GSGNPGMASG GMGDVLTGIV TSLLCQGYPP FDACRLSVFI
HGFSGDLLAR EKGEMGITAT DVSENLPYAF NKLKEHSPVK SGFKRYSN


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