ID A0A268U277_9HELI Unreviewed; 489 AA.
AC A0A268U277;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=BKH43_02360 {ECO:0000313|EMBL:PAF51073.1};
OS Helicobacter sp. 13S00401-1.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1905758 {ECO:0000313|EMBL:PAF51073.1, ECO:0000313|Proteomes:UP000216091};
RN [1] {ECO:0000313|EMBL:PAF51073.1, ECO:0000313|Proteomes:UP000216091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13S00401-1 {ECO:0000313|EMBL:PAF51073.1,
RC ECO:0000313|Proteomes:UP000216091};
RX PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT independent niche adaptation followed by diversification in a
RT poikilothermic host.";
RL Sci. Rep. 7:8387-8387(2017).
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 dehydration of the S-form of NAD(P)HX at the
CC expense of ADP, which is converted to AMP. Together with NAD(P)HX
CC epimerase, which catalyzes the epimerization of the S- and R-forms, the
CC enzyme 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|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|ARBA:ARBA00000013,
CC 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,
CC 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, 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001241, 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;
CC Evidence={ECO:0000256|HAMAP-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|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: 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:PAF51073.1}.
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DR EMBL; MLAR01000003; PAF51073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268U277; -.
DR OrthoDB; 9806925at2; -.
DR Proteomes; UP000216091; 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-EC.
DR GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
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; YjeF N-terminal domain; 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 NCBIfam; TIGR00196; yjeF_cterm; 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|HAMAP-
KW Rule:MF_01965};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR017184};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01965};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR017184};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01965};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01965};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01965}; Potassium {ECO:0000256|PIRNR:PIRNR017184};
KW Reference proteome {ECO:0000313|Proteomes:UP000216091}.
FT DOMAIN 8..221
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT DOMAIN 229..487
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51383"
FT BINDING 262
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT BINDING 310
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT BINDING 362
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT BINDING 403..407
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT BINDING 431
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
FT BINDING 432
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01965"
SQ SEQUENCE 489 AA; 52620 MW; DB05A319975FEFDC CRC64;
MKPLFESKTI LDANAVNSYG IDNQVLMENA SLSLAKAIKK QALKRGLKSV LFCIGSGDNG
ADGLASARIL DSISSLDIYI YNLLAPKSKL CILQNERTKK LGLKHVDSFI EADILVDCIF
GTGFKPRNLN EAKDSKLDIK TALTLEESQT TISNFALEFN KKVAYKIACD CPSMLGSEQA
LKVNLTIAMG ALSLNLYESK SKDYVGKIKV APLGLKREKY ESKSPYFVLE KSDLKLPSRK
IQNVNKGSFG HVCVVSGEFK GASLLSAKAA LTMGAALVST LGYDASGSFP TLMYSQTLPP
HANVLVLGPG LGRSNTLKHE ALLKGALDKG LKVVLDADML YLPSLWKILD TYKDASIVLT
PHPKELFSML KSPFSSLEKL LENMHKVASS LTKEYPHVGF ILKGTNSIIA NEGMLYINPL
GHASLAKGGS GDVLSGLVGG LLAQGYSIKD ASLTASLAHA LASKTKNAYS FNPLKLIKNI
GKLESKLRA
//
