(data stored in SCRATCH zone)

SWISSPROT: C5BDM6_EDWI9

ID   C5BDM6_EDWI9            Unreviewed;       497 AA.
AC   C5BDM6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 51.
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   OrderedLocusNames=NT01EI_0404 {ECO:0000313|EMBL:ACR67642.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67642.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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 S-
CC       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}.
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   -!- 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   -!- 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   -!- 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}.
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DR   EMBL; CP001600; ACR67642.1; -; Genomic_DNA.
DR   ProteinModelPortal; C5BDM6; -.
DR   STRING; 634503.NT01EI_0404; -.
DR   EnsemblBacteria; ACR67642; ACR67642; NT01EI_0404.
DR   KEGG; eic:NT01EI_0404; -.
DR   eggNOG; ENOG4105DR1; Bacteria.
DR   eggNOG; COG0062; LUCA.
DR   eggNOG; COG0063; LUCA.
DR   HOGENOM; HOG000228406; -.
DR   KO; K17758; -.
DR   KO; K17759; -.
DR   OMA; LVGPGHN; -.
DR   OrthoDB; POG091H01XZ; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-HAMAP.
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   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;
DR   PRODOM; C5BDM6.
DR   SWISS-2DPAGE; C5BDM6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01965,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN       22    223       YjeF N-terminal. {ECO:0000259|PROSITE:
FT                                PS51385}.
FT   NP_BIND     410    414       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   NP_BIND     429    438       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   REGION       70     74       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   REGION      137    143       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   REGION      373    379       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01965}.
FT   METAL        71     71       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   METAL       133    133       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   METAL       169    169       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     148    148       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     166    166       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     327    327       NAD(P)HX; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   BINDING     439    439       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01965}.
SQ   SEQUENCE   497 AA;  51392 MW;  39FE4B71EB6895A5 CRC64;
     MGHSCNRNID SLSHYVAPAD WVRDAETRAV AAQGIALATL MQRAGLAAFN RGRQCYPTSR
     RWLILCGRGN NGGDGYVIAR LARASGLQVT LMAVAGDSPL PPEAQQARAQ WLQCGGSEIA
     ASLPLPAAEV IVDALLGIGL SSAPRAPYDA LISAINAHSA PVLSIDLPSG LNADTGAAAG
     AVVRADHTQS FICLKPGLLT GLARAVVGQL HCDPLGLTVW LAQQDWPLQR LDGHCLPRWL
     APRSPLAHKG DNGRLLLIGG DSGMGGAIRL AGQAALRSGA GLVRVLTRGE HVAPLLAAAP
     ELMVKALSRD TLREALSWAE AVVVGPGLGQ GEWGQMVLAA LASVRKPMLW DADALNLLSG
     APSVCEWRVM TPHPGEAARL LGCGIADVEN DRPAAVRALQ RRYGGVALLK GAGTLIADDA
     RCAIADVGNP GMASGGMGDI LSGIIGGLLA QKLTLYDAAC AGAVLHGVAA DAAALRDGER
     GMLASDLLPE IRRWANP
//

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