ID   A0A2V5BL89_9GAMM        Unreviewed;       483 AA.
AC   A0A2V5BL89;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   07-NOV-2018, entry version 3.
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=DEU53_105268 {ECO:0000313|EMBL:PYG48848.1};
OS   Pantoea sp. AG1095.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=2184004 {ECO:0000313|EMBL:PYG48848.1, ECO:0000313|Proteomes:UP000247871};
RN   [1] {ECO:0000313|EMBL:PYG48848.1, ECO:0000313|Proteomes:UP000247871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG1095 {ECO:0000313|EMBL:PYG48848.1,
RC   ECO:0000313|Proteomes:UP000247871};
RA   Venturi V.;
RT   "Genome sequencing of rice bacterial endophytes.";
RL   Submitted (JUN-2018) 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: (6R)-6-beta-hydroxy-1,4,5,6-
CC       tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy-
CC       1,4,5,6-tetrahydronicotinamide-adenine dinucleotide.
CC       {ECO:0000256|HAMAP-Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6-
CC       tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6-
CC       beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_01966,
CC       ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
CC       tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate +
CC       NADH. {ECO:0000256|HAMAP-Rule:MF_01965,
CC       ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6-
CC       tetrahydronicotinamide adenine-dinucleotide phosphate = AMP +
CC       phosphate + NADPH. {ECO:0000256|HAMAP-Rule:MF_01965,
CC       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: 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:PYG48848.1}.
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; QKMJ01000005; PYG48848.1; -; Genomic_DNA.
DR   Proteomes; UP000247871; Unassembled WGS sequence.
DR   GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR017953; Carbohydrate_kinase_pred_CS.
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; PS01050; YJEF_C_2; 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:UP000247871};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01966,
KW   ECO:0000256|PIRNR:PIRNR017184};
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}.
FT   DOMAIN        1    203       YjeF N-terminal. {ECO:0000259|PROSITE:
FT                                PS51385}.
FT   NP_BIND     390    394       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   NP_BIND     410    419       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   REGION       49     53       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   REGION      117    123       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        50     50       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   METAL       113    113       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   METAL       149    149       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     128    128       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     146    146       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     307    307       NAD(P)HX; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   BINDING     420    420       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01965}.
SQ   SEQUENCE   483 AA;  50469 MW;  0788CE753E99D228 CRC64;
     MAQLERDAAD SLGLTLFELM QRAGQASYEL GCQLWPQAQH WLILCGHGNN GGDGYVVARL
     AQAAGLNVTL LACAGSKALP EEAQQAQDAW LAAGGVIHAA DAPWPEQVEV IVDALLGTGL
     NRAPADPYDR LITLINAHAA PVLAIDIPSG LLAANGTAPG KTVIADHTLS MITLKPGQLT
     GKARDYVGVL HNHELGLSAY LAAEQAPISR YDAGDLTCWL KPRRATSHKG DQGRLLVVGG
     DSGTAGAIRM TGEAALRTGA GLVRVLTHED NIGPILTARP ELMVDALSDE RLDQALEWAD
     VIAVGPGLGQ RDWAQKALKK IAASEKPMLW DADALNLLAI KQDNRQNRII TPHPGEAARL
     LGVKTSEIES DRLHAARALA KRYGGVVVLK GAGTVIASAA GDIAIADVGN AGMASGGMGD
     VLSGIIAALL GQKLTLLDAA CAGCVAHGAT ADAVARQRGT RGMLATDLFE LLWQFVNPEM
     IQQ
//