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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)]

 Q0C0G6_HYPNA            Unreviewed;       480 AA.
Q0C0G6;
17-OCT-2006, integrated into UniProtKB/TrEMBL.
17-OCT-2006, sequence version 1.
27-SEP-2017, entry version 74.
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};
OrderedLocusNames=HNE_2080 {ECO:0000313|EMBL:ABI77498.1};
Hyphomonas neptunium (strain ATCC 15444).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Hyphomonadaceae; Hyphomonas.
NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI77498.1, ECO:0000313|Proteomes:UP000001959};
[1] {ECO:0000313|EMBL:ABI77498.1, ECO:0000313|Proteomes:UP000001959}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI77498.1,
ECO:0000313|Proteomes:UP000001959};
PubMed=16980487; DOI=10.1128/JB.00111-06;
Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T.,
Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E.,
Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A.,
Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C.,
Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D.,
Davidsen T.M., Yang Q., Zafar N., Ward N.L.;
"Comparative genomic evidence for a close relationship between the
dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
crescentus.";
J. Bacteriol. 188:6841-6850(2006).
-!- 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|HAMAP-Rule:MF_01966}.
-!- 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|HAMAP-Rule:MF_01966}.
-!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate +
NADH. {ECO:0000256|HAMAP-Rule:MF_01965}.
-!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
tetrahydronicotinamide adenine-dinucleotide phosphate = AMP +
phosphate + NADPH. {ECO:0000256|HAMAP-Rule:MF_01965}.
-!- 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; CP000158; ABI77498.1; -; Genomic_DNA.
RefSeq; WP_011647076.1; NC_008358.1.
ProteinModelPortal; Q0C0G6; -.
STRING; 228405.HNE_2080; -.
EnsemblBacteria; ABI77498; ABI77498; HNE_2080.
KEGG; hne:HNE_2080; -.
eggNOG; ENOG4105DR1; Bacteria.
eggNOG; COG0062; LUCA.
eggNOG; COG0063; LUCA.
HOGENOM; HOG000228404; -.
OMA; LVGPGHN; -.
OrthoDB; POG091H01XZ; -.
Proteomes; UP000001959; 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.
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:UP000001959};
Isomerase {ECO:0000256|HAMAP-Rule:MF_01966,
ECO:0000256|PIRNR:PIRNR017184}; Kinase {ECO:0000313|EMBL:ABI77498.1};
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_01966, ECO:0000256|PIRNR:PIRNR017184};
NADP {ECO:0000256|HAMAP-Rule:MF_01966, 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:UP000001959};
Transferase {ECO:0000313|EMBL:ABI77498.1}.
DOMAIN 11 204 YjeF N-terminal.
{ECO:0000259|PROSITE:PS51385}.
NP_BIND 391 395 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
NP_BIND 411 420 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
REGION 57 61 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 122 128 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 355 361 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
METAL 58 58 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 118 118 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 150 150 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 147 147 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 304 304 NAD(P)HX; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01965}.
BINDING 421 421 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
SEQUENCE 480 AA; 49401 MW; D56A55DA2F0448EE CRC64;
MGRPILTPQE MLAAEQAVFN TGTDRFTLMQ RAGEAVAEFV HAHWPDGQIQ VLCGPGGNGG
DGFIAAAALA KLWRKVEVYS VLPVSELTGD TAKAASAWEG PVHKLEDALK SQPELIVDAL
YGAGLTRPLE GAAAELAQRG GRVISVDVPS GIDGYTGKPL GPAFQAEATL TFAALRPAHV
LLPGSAFSGV VMVADIGVPV KTALAENSPA LWHSQMPQPG FGVHKYQRGH LKVVSGGPWN
TGAARLTAKA GLRAGAGLVT MLSPPDAAGV HAAHLTAIML APFVTPDDLA AYAARSTAMV
IGPAAGVTDA TRANVEAILK GPARVVLDAD ALTAFGEDPE VLFKQLRPTD ILTPHEGEFS
RLFGDLLATS DNKVQATRAA AAKAGCVILL KGADTVIAQP DGNALVNTHA TRWLATAGSG
DVLAGIIAGF MAQGVDTFVA AAIGCWLHGE AGRRVGAGLI AEDIEMQLPV ILSALHGELG


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