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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)]

 A0A1Q8KW26_9PSEU        Unreviewed;       501 AA.
A0A1Q8KW26;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
25-OCT-2017, entry version 7.
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=Ae707Ps1_4940c {ECO:0000313|EMBL:OLM20681.1};
Pseudonocardia sp. Ae707_Ps1.
Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
Pseudonocardia.
NCBI_TaxID=1885572 {ECO:0000313|EMBL:OLM20681.1, ECO:0000313|Proteomes:UP000186124};
[1] {ECO:0000313|EMBL:OLM20681.1, ECO:0000313|Proteomes:UP000186124}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ae707_Ps1 {ECO:0000313|EMBL:OLM20681.1,
ECO:0000313|Proteomes:UP000186124};
Holmes N.A., Innocent T.M., Heine D., Al Bassam M., Worsley S.F.,
Trottmann F., Patrick E.H., Yu D.W., Murrell J.C., Schioett M.,
Wilkinson B., Boomsma J., Hutchings M.I.;
"Genome Analysis of Two Pseudonocardia Phylotypes Associated with
Acromyrmex Leafcutter Ants Reveals Their Biosynthetic Potential.";
Front. Microbiol. 7:1-16(2016).
-!- 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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OLM20681.1}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; MCIR01000001; OLM20681.1; -; Genomic_DNA.
RefSeq; WP_075314717.1; NZ_MCIR01000001.1.
Proteomes; UP000186124; 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.
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:UP000186124};
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}.
DOMAIN 10 223 YjeF N-terminal.
{ECO:0000259|PROSITE:PS51385}.
NP_BIND 403 407 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
NP_BIND 423 432 ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
REGION 58 62 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 139 145 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
REGION 370 376 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
METAL 59 59 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 135 135 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
METAL 171 171 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 168 168 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01966}.
BINDING 319 319 NAD(P)HX; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01965}.
BINDING 433 433 NAD(P)HX. {ECO:0000256|HAMAP-
Rule:MF_01965}.
SEQUENCE 501 AA; 49722 MW; F3F49D93169382B8 CRC64;
MHGVYTAEQI RAAESAMMRT VADGVLMRRA AGGLAAHLRG FLGSTYGRRV VLLVGAGDNG
GDALWAGAEL RRRGARVTAV LLAPDRAHPG GLAALRAARG RVLPLGPGAG LGGVADPGAL
DAARAAVAGA DVVVDGIVGI SGRGALRDPA PALVEAADDA GVPIVACDLP SGVDTDTGTT
DGPHVRAALT VTFGARKPVH ALAAPLCGPV RLVDFGLGPF LPADPHARLL TDADAGLFWP
VPGPDDDKYS QGVVGIAAGS ATYPGAAVLA AGAAALATSG MVRFAGSAAD EVRRHWPEIV
ATGDITDAGR TQAWAVGPGI GTGAQGLAVL ESVLDREVPL CIDADGITLL AQHAHLRDRI
LGEPVVLTPH AGEFARIAGD VGPDRVAAAR RAAADLGVTV LLKGNATVVA APDGRALVDP
AGDSWAATAG SGDVLTGMIG ALLAAGLDPW WAAGCATLVH ARAATAAARE HGLPPVPAPA
SAMQAAIPVA LRAVRAAAGS G


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