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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)]

 A0A1L7RAG5_9ACTO        Unreviewed;       599 AA.
A0A1L7RAG5;
15-MAR-2017, integrated into UniProtKB/TrEMBL.
15-MAR-2017, sequence version 1.
23-MAY-2018, entry version 13.
SubName: Full=Sugar kinase {ECO:0000313|EMBL:CED90837.1};
EC=4.2.1.136 {ECO:0000313|EMBL:CED90837.1};
Name=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
Synonyms=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
ORFNames=AAM4_1005 {ECO:0000313|EMBL:CED90837.1};
Actinomyces succiniciruminis.
Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
Actinomyces.
NCBI_TaxID=1522002 {ECO:0000313|EMBL:CED90837.1};
[1] {ECO:0000313|EMBL:CED90837.1}
NUCLEOTIDE SEQUENCE.
STRAIN=AM4 {ECO:0000313|EMBL:CED90837.1};
Zhang J.E., Yang H., Guo J., Deng Z., Luo H., Luo M., Zhao B.;
Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
-!- 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};
Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01966};
-!- 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}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}.
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EMBL; LK995485; CED90837.1; -; Genomic_DNA.
GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR029056; Ribokinase-like.
InterPro; IPR004443; YjeF_N_dom.
InterPro; IPR036652; YjeF_N_dom_sf.
Pfam; PF01256; Carb_kinase; 1.
Pfam; PF03853; YjeF_N; 1.
SUPFAM; SSF53613; SSF53613; 1.
SUPFAM; SSF64153; SSF64153; 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};
Isomerase {ECO:0000256|HAMAP-Rule:MF_01966};
Kinase {ECO:0000313|EMBL:CED90837.1};
Lyase {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000313|EMBL:CED90837.1};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01966};
NAD {ECO:0000256|HAMAP-Rule:MF_01965};
NADP {ECO:0000256|HAMAP-Rule:MF_01965};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01965};
Potassium {ECO:0000256|HAMAP-Rule:MF_01966};
Transferase {ECO:0000313|EMBL:CED90837.1}.
DOMAIN 57 279 YjeF N-terminal.
{ECO:0000259|PROSITE:PS51385}.
NP_BIND 471 475 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
NP_BIND 491 500 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
REGION 115 119 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 187 193 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 429 435 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
METAL 116 116 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 183 183 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 225 225 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 222 222 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 371 371 NAD(P)HX; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01965}.
BINDING 501 501 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
SEQUENCE 599 AA; 58570 MW; E33CE8A73FFA6CA6 CRC64;
MNARAVPGAL GPTVQPHRPT TDLARGAGRG GSRRGDDGAV STATASPSAS GSTLAAAAAY
PARAVADAEA PLTAGTDRYM HAAAHALARA AVEELRGARG AVPGARVLLL VGGGHNGGDA
LLAGALLARH GCAVTAAPAT DPARLHAGAL DAARAAGVRL AADPMAAARA AAGGAAGVDL
VVDGLTGIAA TGPLRPAAAE IIAPLCAAGD PGERPFRVLA VDLPSGVGVD DGTLPGPVLA
ADRTVTFTCF KAAHLAPPAA PRCGRVDVVD LGLPVPNGAP LAVRPTDTEL GGLLRVPGDR
DHKYTRGVVG LWAGSQTYPG AAVLAASAAV RTGAGMVRLA APARVVDLVL ARRPEVVPVD
GRCQALVIGP GTDPADAPRA AELDAALGRV LGEAGEPVDA VIDAGALPLL AARVVSGGRC
MPRQVLTPHA GEAAALLGAL GEQTSRESVE AAPAAAARRL AELTGATVLL KTTPTLIASP
GGTLLSVDSG PGWLATAGSG DVLAGIIGAL LAASRADAEN GKAVGGEDVQ AEAPARCAAL
GVRLHALAAA RAAGLVDASP AVTAGAGRLF ACSGHPLAAL DLTEAIPAAW EQLWCAGRG


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