(data stored in ACNUC7421 zone)

SWISSPROT: D6ZB80_SEGRD

ID   D6ZB80_SEGRD            Unreviewed;       512 AA.
AC   D6ZB80;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 55.
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};
GN   Name=nnrD {ECO:0000256|HAMAP-Rule:MF_01965};
GN   OrderedLocusNames=Srot_0352 {ECO:0000313|EMBL:ADG96839.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96839.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96839.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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-and
CC       R-forms, the enzyme allows the repair of both epimers of NAD(P)HX,
CC       a damaged form of NAD(P)H that is a result of enzymatic or heat-
CC       dependent hydration. {ECO:0000256|HAMAP-Rule:MF_01965}.
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|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|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:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456215,
CC         ChEBI:CHEBI:456216; 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:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456215,
CC         ChEBI:CHEBI:456216; 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;
CC         Evidence={ECO:0000256|PIRNR:PIRNR017184};
CC       Note=Binds 1 potassium ion per subunit.
CC       {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: 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; CP001958; ADG96839.1; -; Genomic_DNA.
DR   STRING; 640132.Srot_0352; -.
DR   EnsemblBacteria; ADG96839; ADG96839; Srot_0352.
DR   KEGG; srt:Srot_0352; -.
DR   eggNOG; ENOG4107QTJ; Bacteria.
DR   eggNOG; COG0062; LUCA.
DR   eggNOG; COG0063; LUCA.
DR   HOGENOM; HOG000228405; -.
DR   KO; K17758; -.
DR   KO; K17759; -.
DR   OMA; LVGPGHN; -.
DR   BioCyc; SROT640132:G1GLH-353-MONOMER; -.
DR   Proteomes; UP000002247; Chromosome.
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:0016853; F:isomerase activity; 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: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   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   PROSITE; PS01050; YJEF_C_2; 1.
DR   PROSITE; PS51383; YJEF_C_3; 1.
DR   PROSITE; PS51385; YJEF_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZB80.
DR   SWISS-2DPAGE; D6ZB80.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01965,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR017184};
KW   Kinase {ECO:0000313|EMBL:ADG96839.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01965,
KW   ECO:0000256|PIRNR:PIRNR017184};
KW   Metal-binding {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|PIRNR:PIRNR017184};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Transferase {ECO:0000313|EMBL:ADG96839.1}.
FT   DOMAIN       10    214       YjeF N-terminal. {ECO:0000259|PROSITE:
FT                                PS51385}.
FT   NP_BIND     396    400       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   NP_BIND     416    425       ADP. {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   REGION      362    368       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01965}.
FT   BINDING     317    317       NAD(P)HX; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01965}.
FT   BINDING     426    426       NAD(P)HX. {ECO:0000256|HAMAP-Rule:
FT                                MF_01965}.
SQ   SEQUENCE   512 AA;  51036 MW;  D51AF573D84B5021 CRC64;
     MPSYYPAALV KRADESLIRA LAPGVPMRRA AFGLAQVVLR ELRDHAGGAV GQKVWLVVGV
     GDNGADALWA GAFLKRRGVD VRALLLNPRR AHPAGLAAFR RAGGKFVDDV PDAPAPFGGG
     PGRGVVVDGV VGLSGKGPLR GHAAEIFSRP SGHRVVAVDL PSGVDPDTGA VAGPAVTADV
     TVAMGVFKQA HALNPGRCGR LELVDIGYPE AGFGPLGVLD GARGLTALGQ ERLAALLPAP
     GPGDDKYTQG VLGVVAGSPT YPGAGALCAS GALATTSGMV RAVGPGAKAL VAVHPELVVS
     EDVESTGRVN AWVLGPGADE STRALLLRAL ATDLPVVADA SALRLVPDAI KRRSAPTVVT
     PHEREFEAFA GRPVGADRAA AAAALATECG ATVLLKGHVT IIAEPGGQVL VNIAGNSWAA
     TAGSGDVLSG MIGALLASAA AEHAAPVAAA IHSRAAALAA GAEPGAPITA SALAARIPDA
     IRSARASGLA RRTPSVRAAG RTGDGNAIGS YP
//

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