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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)]

 F0JET8_DESDE            Unreviewed;       516 AA.
F0JET8;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
03-MAY-2011, sequence version 1.
05-DEC-2018, entry version 53.
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=DND132_0356 {ECO:0000313|EMBL:EGB13573.1};
Desulfovibrio desulfuricans ND132.
Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
Desulfovibrionaceae; Desulfovibrio.
NCBI_TaxID=641491 {ECO:0000313|EMBL:EGB13573.1, ECO:0000313|Proteomes:UP000007845};
[1] {ECO:0000313|EMBL:EGB13573.1, ECO:0000313|Proteomes:UP000007845}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ND132 {ECO:0000313|EMBL:EGB13573.1};
PubMed=21357488; DOI=10.1128/JB.00170-11;
Brown S.D., Gilmour C.C., Kucken A.M., Wall J.D., Elias D.A.,
Brandt C.C., Podar M., Chertkov O., Held B., Bruce D.C., Detter J.C.,
Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Woyke T.,
Mikhailova N., Ivanova N.N., Han J., Lucas S., Lapidus A.L.,
Land M.L., Hauser L.J., Palumbo A.V.;
"Genome sequence of the mercury-methylating strain Desulfovibrio
desulfuricans ND132.";
J. Bacteriol. 193:2078-2079(2011).
-!- 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: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}.
-----------------------------------------------------------------------
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EMBL; CP003220; EGB13573.1; -; Genomic_DNA.
RefSeq; WP_014321001.1; NC_016803.1.
STRING; 641491.DND132_0356; -.
EnsemblBacteria; EGB13573; EGB13573; DND132_0356.
KEGG; ddn:DND132_0356; -.
eggNOG; ENOG4108ENG; Bacteria.
eggNOG; COG0062; LUCA.
eggNOG; COG0063; LUCA.
KO; K17758; -.
KO; K17759; -.
OrthoDB; POG091H01XZ; -.
BioCyc; DDES641491:G1GRE-365-MONOMER; -.
Proteomes; UP000007845; Chromosome.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:UP000007845};
Isomerase {ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184}; Kinase {ECO:0000313|EMBL:EGB13573.1};
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:UP000007845};
Transferase {ECO:0000313|EMBL:EGB13573.1}.
DOMAIN 11 220 YjeF N-terminal.
{ECO:0000259|PROSITE:PS51385}.
NP_BIND 421 425 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
NP_BIND 440 449 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
REGION 61 65 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 132 138 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 384 390 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
METAL 62 62 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 128 128 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 166 166 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 163 163 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 333 333 NAD(P)HX; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01965}.
BINDING 450 450 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
SEQUENCE 516 AA; 53246 MW; 260D7DF330C606DB CRC64;
MLLPLPTPAE MAVWDRETIH TIGIPGVTLM ESASREAVNV LLEEYGDVGG AVIHCFAGSG
NNGGDAFAVA RHLNDLGAEV TVFHTRPKRG YRGETRTNLL WAQRLGIPLV HLAGVRLDTL
AQPDIIVDGL LGTGFAGALR EDFLQLVRTV NRLGERAFVL AVDIPSGLNG LTGRPQPEAV
RADATATFQA PKLGLVLPEA QPHTGALHVC PIGIPLMIQE KYQTRHRLIT GEVMAALPAP
APDMHKGSAG HVLVVGGSFG LTGAPHLAAL AALRSGAGLA TVACPAGLAD AVKAGSPDIM
TLPLGAGTAW TGDMAEAIKA ELHRFDAVVL GPGMGRTPEA RSLALELAAG CGLPMVLDAD
ALFALAASPE HLRSLPEQAV LTPHPGEMAR LLDTATAEVQ ADRLGAVDRF LAACDATLVL
KGAGTLVADR DMTCVSPFAE PNLSVGGAGD VLSGVVGALL AGGLSPMRAA CTGVFWHGLA
GRALNNEFPA RGNLASEIAN MLPHAAAAFT KEPEPC


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