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Database: UniProt
Entry: T5CWK6_HELPX
LinkDB: T5CWK6_HELPX
Original site: T5CWK6_HELPX 
ID   T5CWK6_HELPX            Unreviewed;       464 AA.
AC   T5CWK6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
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=nnrE {ECO:0000256|HAMAP-Rule:MF_01966};
GN   ORFNames=N405_03360 {ECO:0000313|EMBL:EQL60557.1};
OS   Helicobacter pylori FD568.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1191282 {ECO:0000313|EMBL:EQL60557.1, ECO:0000313|Proteomes:UP000015965};
RN   [1] {ECO:0000313|EMBL:EQL60557.1, ECO:0000313|Proteomes:UP000015965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD568 {ECO:0000313|EMBL:EQL60557.1,
RC   ECO:0000313|Proteomes:UP000015965};
RX   PubMed=23012278; DOI=10.1128/JB.01278-12;
RA   Gunaletchumy S.P., Teh X., Khosravi Y., Ramli N.S., Chua E.G., Kavitha T.,
RA   Mason J.N., Lee H.T., Alias H., Zaidan N.Z., Yassin N.B., Tay L.C.,
RA   Rudd S., Mitchell H.M., Kaakoush N.O., Loke M.F., Goh K.L., Vadivelu J.;
RT   "Draft genome sequences of Helicobacter pylori isolates from Malaysia,
RT   cultured from patients with functional dyspepsia and gastric cancer.";
RL   J. Bacteriol. 194:5695-5696(2012).
RN   [2] {ECO:0000313|EMBL:EQL60557.1, ECO:0000313|Proteomes:UP000015965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD568 {ECO:0000313|EMBL:EQL60557.1,
RC   ECO:0000313|Proteomes:UP000015965};
RX   PubMed=24051312;
RA   Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA   Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA   Loke M.F., Vadivelu J.;
RT   "Multiple genome sequences of Helicobacter pylori strains of diverse
RT   disease and antibiotic resistance backgrounds from malaysia.";
RL   Genome Announc. 1:E00687-E00713(2013).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of the
CC       S- and R-forms of NAD(P)HX and the dehydration of the S-form of
CC       NAD(P)HX at the expense of ADP, which is converted to AMP. This allows
CC       the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that
CC       is a result of enzymatic or heat-dependent hydration.
CC       {ECO:0000256|ARBA:ARBA00025153, ECO:0000256|PIRNR:PIRNR017184}.
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 or
CC       heat-dependent hydration. This is a prerequisite for the S-specific
CC       NAD(P)H-hydrate dehydratase to allow the repair of both epimers of
CC       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|ARBA:ARBA00000013, ECO:0000256|HAMAP-
CC         Rule:MF_01966, 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|ARBA:ARBA00000909, ECO:0000256|HAMAP-
CC         Rule:MF_01966, 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001026,
CC         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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001241,
CC         ECO:0000256|PIRNR:PIRNR017184};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01966,
CC         ECO:0000256|PIRNR:PIRNR017184};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184};
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|ARBA:ARBA00009524, ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP family.
CC       {ECO:0000256|ARBA:ARBA00006001, ECO:0000256|PIRNR:PIRNR017184}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01966}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQL60557.1}.
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DR   EMBL; AKHQ02000036; EQL60557.1; -; Genomic_DNA.
DR   RefSeq; WP_000954073.1; NZ_AKHQ02000036.1.
DR   AlphaFoldDB; T5CWK6; -.
DR   PATRIC; fig|1191282.4.peg.1154; -.
DR   Proteomes; UP000015965; 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
DR   CDD; cd01171; YXKO-related; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 3.40.50.10260; YjeF N-terminal domain; 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   NCBIfam; TIGR00196; yjeF_cterm; 1.
DR   NCBIfam; TIGR00197; yjeF_nterm; 1.
DR   PANTHER; PTHR12592:SF0; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE; 1.
DR   PANTHER; PTHR12592; ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER; 1.
DR   Pfam; PF01256; Carb_kinase; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   PIRSF; PIRSF017184; Nnr; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   SUPFAM; SSF64153; YjeF N-terminal domain-like; 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|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR017184};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01966};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR017184};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01966}; Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01966};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01966};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01966};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01966, ECO:0000256|PIRNR:PIRNR017184}.
FT   DOMAIN          8..205
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51385"
FT   DOMAIN          213..464
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51383"
FT   BINDING         56..60
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         57
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         118
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         149
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
FT   BINDING         152
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01966"
SQ   SEQUENCE   464 AA;  50584 MW;  2202BA02096E1677 CRC64;
     MLSVYEKVNA LDKRALEKFN LSEDILMENA AMALERAVLQ NASLGAKVII LCGSGDNGGD
     GYALARRLVG RFKTLVFEMK PAKSPMCQLQ KERAKKVGVV IKAWEEKNKD LECDVLIDCV
     VGSHFKGELE PFLNFESLSQ KARFKIACDI PSGIDSKGRV DKGAFKADMT ISMGAIKSCL
     LSDRAKDYIG ELKVGHLGVF NQTYEIPTDT FLLEKSDLKL PLRDKKNAHK GDYGHAHILL
     GKHSGAGLLS ALSALSFGSG VVSVQALECE ITSSNKPLEL VFCENFPNPL SAFALGMGLE
     GFPKDFNKWL ELAPCVLDAG IFYHKEVLQA LEKEVVLTPH PKEFLSLLKL VGINISMLEL
     LDNKLEIARD FSQKYPKVVL LLKGANTLIA HQGQVFINIL GSVALAKAGS GDVLAGLILS
     LLSQNYTPLD AAINASLAHA IASLEFKNNY ALTPLDLIEK IKRL
//
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