ID   A0A2N8NSB6_STREU        Unreviewed;       482 AA.
AC   A0A2N8NSB6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   05-DEC-2018, entry version 6.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|HAMAP-Rule:MF_01966};
DE   Includes:
DE     RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|HAMAP-Rule:MF_01965};
DE              EC=4.2.1.136 {ECO:0000256|HAMAP-Rule:MF_01965};
DE     AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000256|HAMAP-Rule:MF_01965};
DE   Includes:
DE     RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|HAMAP-Rule:MF_01966};
DE              EC=5.1.99.6 {ECO:0000256|HAMAP-Rule:MF_01966};
DE     AltName: Full=NAD(P)HX epimerase {ECO:0000256|HAMAP-Rule:MF_01966};
GN   Name=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
GN   Synonyms=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
GN   ORFNames=AF335_22665 {ECO:0000313|EMBL:PNE31668.1};
OS   Streptomyces eurocidicus (Streptoverticillium eurocidicus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=66423 {ECO:0000313|EMBL:PNE31668.1, ECO:0000313|Proteomes:UP000235945};
RN   [1] {ECO:0000313|EMBL:PNE31668.1, ECO:0000313|Proteomes:UP000235945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27428 {ECO:0000313|EMBL:PNE31668.1,
RC   ECO:0000313|Proteomes:UP000235945};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of
CC       the S- and R-forms of NAD(P)HX and the dehydration of the S-form
CC       of NAD(P)HX at the expense of ADP, which is converted to AMP. This
CC       allows the repair of both epimers of NAD(P)HX, a damaged form of
CC       NAD(P)H that is a result of enzymatic or heat-dependent hydration.
CC       {ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at
CC       the expense of ADP, which is converted to AMP. Together with
CC       NAD(P)HX epimerase, which catalyzes the epimerization of the
CC       S- and R-forms, the enzyme allows the repair of both epimers of
CC       NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic
CC       or heat-dependent hydration. {ECO:0000256|HAMAP-Rule:MF_01965}.
CC   -!- FUNCTION: Catalyzes the epimerization of the S- and R-forms of
CC       NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic
CC       or heat-dependent hydration. This is a prerequisite for the S-
CC       specific NAD(P)H-hydrate dehydratase to allow the repair of both
CC       epimers of NAD(P)HX. {ECO:0000256|HAMAP-Rule:MF_01966}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215,
CC         ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01966,
CC         ECO:0000256|PIRNR:PIRNR017184};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227,
CC         ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01966,
CC         ECO:0000256|PIRNR:PIRNR017184};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate;
CC         Xref=Rhea:RHEA:32223, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:64074; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate;
CC         Xref=Rhea:RHEA:32235, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:64076; EC=4.2.1.136; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01965};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01965}.
CC   -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01965}.
CC   -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000256|HAMAP-
CC       Rule:MF_01966}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD
CC       family. {ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP
CC       family. {ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PNE31668.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LGUI01000008; PNE31668.1; -; Genomic_DNA.
DR   Proteomes; UP000235945; Unassembled WGS sequence.
DR   GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01171; YXKO-related; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 3.40.50.10260; -; 1.
DR   HAMAP; MF_01965; NADHX_dehydratase; 1.
DR   HAMAP; MF_01966; NADHX_epimerase; 1.
DR   InterPro; IPR000631; CARKD.
DR   InterPro; IPR030677; Nnr.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR004443; YjeF_N_dom.
DR   InterPro; IPR036652; YjeF_N_dom_sf.
DR   Pfam; PF01256; Carb_kinase; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   PIRSF; PIRSF017184; Nnr; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   SUPFAM; SSF64153; SSF64153; 1.
DR   TIGRFAMs; TIGR00196; yjeF_cterm; 1.
DR   TIGRFAMs; TIGR00197; yjeF_nterm; 1.
DR   PROSITE; PS51383; YJEF_C_3; 1.
DR   PROSITE; PS51385; YJEF_N; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01965,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Complete proteome {ECO:0000313|Proteomes:UP000235945};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01966,
KW   ECO:0000256|PIRNR:PIRNR017184}; Kinase {ECO:0000313|EMBL:PNE31668.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01965,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01966,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01965, ECO:0000256|PIRNR:PIRNR017184};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01965,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01966,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Transferase {ECO:0000313|EMBL:PNE31668.1}.
FT   DOMAIN       10    208       YjeF N-terminal. {ECO:0000259|PROSITE:
FT                                PS51385}.
FT   NP_BIND     390    394       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   NP_BIND     411    420       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   REGION       58     62       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   REGION      124    130       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   REGION      353    359       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01965}.
FT   METAL        59     59       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   METAL       120    120       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   METAL       154    154       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     151    151       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     305    305       NAD(P)HX; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   BINDING     421    421       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01965}.
SQ   SEQUENCE   482 AA;  47900 MW;  DC07F2EF1CEF701F CRC64;
     MRTAYSVETV RAAERALMAQ LPQGALMQRA AAGLAAACAD LLGRTYGARV ALLVGSGDNG
     GDALYAGARL ARRGAGVTAV LLAPERTHQG GLAALRAAGG RVASAEEGDR AVRRADLVVD
     GIVGIGGRGG LRPEAEALVA AAEGALVLAV DLPSGVDADS GEVRGATVRA DATVTFGAYK
     PGLLIDPARE RAGALRLIDI GLGPHLPRRP EAEALQHADV AALLPRPAAE SDKYRRGVVG
     VVAGSARYPG AAVLAVAGAL HGGAGAVRYA GPAAEAVVSR FPETLVSEGP PSKAGRVQAW
     VVGPGVGDDA AARRALDDVL ASDVPVLVDA DGLRLLPEAA VRARGAETVL TPHAGEAAAL
     LGVSRSRVES ARLSAARELA ARFGATALLK GSTTVVAAPG RTAVRVNPTG TPWLATAGSG
     DVLSGVTGSL LAAGLRGLDA ASVGAYLHGL AARSLGGAPL TASGVAEALA GAWGEVTGHS
     YE
//