(data stored in SCRATCH zone)

SWISSPROT: C4KJI3_SULIK

ID   C4KJI3_SULIK            Unreviewed;       501 AA.
AC   C4KJI3;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 46.
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=M164_0067 {ECO:0000313|EMBL:ACR40703.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40703.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40703.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}.
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DR   EMBL; CP001402; ACR40703.1; -; Genomic_DNA.
DR   RefSeq; WP_012735361.1; NC_012726.1.
DR   ProteinModelPortal; C4KJI3; -.
DR   EnsemblBacteria; ACR40703; ACR40703; M164_0067.
DR   KEGG; sid:M164_0067; -.
DR   HOGENOM; HOG000228404; -.
DR   KO; K17758; -.
DR   KO; K17759; -.
DR   OMA; LVGPGHN; -.
DR   OrthoDB; POG093Z0AXM; -.
DR   BioCyc; SISL426118:GI01-67-MONOMER; -.
DR   Proteomes; UP000001479; 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: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-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; C4KJI3.
DR   SWISS-2DPAGE; C4KJI3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01965,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01966,
KW   ECO:0000256|PIRNR:PIRNR017184}; Kinase {ECO:0000313|EMBL:ACR40703.1};
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:ACR40703.1}.
FT   DOMAIN        7    208       YjeF N-terminal. {ECO:0000259|PROSITE:
FT                                PS51385}.
FT   NP_BIND     400    404       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   NP_BIND     419    428       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   REGION      126    132       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   REGION      363    369       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01965}.
FT   METAL       122    122       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   METAL       158    158       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     155    155       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01966}.
FT   BINDING     314    314       NAD(P)HX; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   BINDING     429    429       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01965}.
SQ   SEQUENCE   501 AA;  54418 MW;  0D677B23F536C73D CRC64;
     MISVKEMRAL EINSSALGVS TLILMENAGR SVKDEIVKRF NVKDKVAYVY VGHGGKGGDG
     LVAARHLADE GAKVTVILLG ENKHEDAILN LNVIEEMDYS ITLVEIKDMD ELKPISADIL
     IDAMLGTGFS GKPREPFRSA IKAFNNSKGF KVSIDVPSGI NADTGEAYED EYVKPDLVVT
     FHDIKPGLLK YNFNTVVTKI GIPVEAQIYV GPGDLIVNVH SRPYYSKKGD SGRVLVIGGS
     YTFSGAPTLA AMGALRAGAD LVYVASPEDT ARIIAGYSPD LITIKLRGKN ISPDNFEELK
     SWIDRADVVV IGPGMGLAEE TIEASKLIVN YVKEKNKLAV IDADALKAIS GFDLYENAVI
     TPHAGEFKIF FGEEPNKNIR DRIRQVIRYA KKCKCTVLLK GYVDIISDGK RFKLNKTGNP
     GMTVGGSGDT LTGITATLMA QKIEPFIAAY LGVFINSLAG TLAYNRLGAH LTPTDIINEI
     PNVINNPLDS FKRKLYKRVL S
//

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