ID A0A3R7KUZ5_9STRA Unreviewed; 250 AA.
AC A0A3R7KUZ5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000256|HAMAP-Rule:MF_03157};
DE EC=4.2.1.93 {ECO:0000256|HAMAP-Rule:MF_03157};
DE AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000256|HAMAP-Rule:MF_03157};
GN ORFNames=BBI17_000759 {ECO:0000313|EMBL:RLN10919.1}, BBO99_00004329
GN {ECO:0000313|EMBL:RLN80658.1}, JM16_002502
GN {ECO:0000313|EMBL:KAG2526025.1}, JM18_002310
GN {ECO:0000313|EMBL:KAG2527707.1};
OS Phytophthora kernoviae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN80658.1, ECO:0000313|Proteomes:UP000285624};
RN [1] {ECO:0000313|EMBL:KAG2526025.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2526025.1}, and NZFS 3630
RC {ECO:0000313|EMBL:KAG2527707.1};
RX PubMed=26981359;
RA Studholme D.J., McDougal R.L., Sambles C., Hansen E., Hardy G., Grant M.,
RA Ganley R.J., Williams N.M.;
RT "Genome sequences of six Phytophthora species associated with forests in
RT New Zealand.";
RL Genom Data 7:54-56(2015).
RN [2] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chile2 {ECO:0000313|EMBL:RLN10919.1}, and Chile4
RC {ECO:0000313|EMBL:RLN80658.1};
RA Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA Williams N.M., Mcdougal R.L.;
RT "Genome sequencing of oomycete isolates from Chile give support for New
RT Zealand origin for Phytophthora kernoviae and make available the first
RT Nothophytophthora sp. genome.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2526025.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2526025.1}, and NZFS 3630
RC {ECO:0000313|EMBL:KAG2527707.1};
RA Studholme D.J.;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the
CC expense of ATP, which is converted to ADP. 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_03157}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate;
CC Xref=Rhea:RHEA:19017, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57945, ChEBI:CHEBI:64074,
CC ChEBI:CHEBI:456216; EC=4.2.1.93; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03157};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-NADPHX + ATP = ADP + H(+) + NADPH + phosphate;
CC Xref=Rhea:RHEA:32231, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:64076,
CC ChEBI:CHEBI:456216; EC=4.2.1.93; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03157};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03157};
CC -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000256|HAMAP-
CC Rule:MF_03157}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03157}.
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:RLN80658.1}.
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DR EMBL; JPWV03000081; KAG2526025.1; -; Genomic_DNA.
DR EMBL; JPWU03000073; KAG2527707.1; -; Genomic_DNA.
DR EMBL; MAYM02001761; RLN10919.1; -; Genomic_DNA.
DR EMBL; MBDN02000102; RLN80658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7KUZ5; -.
DR STRING; 325452.A0A3R7KUZ5; -.
DR Proteomes; UP000285624; Unassembled WGS sequence.
DR Proteomes; UP000285883; Unassembled WGS sequence.
DR Proteomes; UP000785171; Unassembled WGS sequence.
DR Proteomes; UP000792063; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047453; F:ATP-dependent NAD(P)H-hydrate dehydratase activity; 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 HAMAP; MF_01965; NADHX_dehydratase; 1.
DR InterPro; IPR000631; CARKD.
DR InterPro; IPR029056; Ribokinase-like.
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 SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS51383; YJEF_C_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03157};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03157};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03157};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03157}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03157};
KW Reference proteome {ECO:0000313|Proteomes:UP000285624}.
FT DOMAIN 4..174
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51383"
FT BINDING 120
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03157"
SQ SEQUENCE 250 AA; 26521 MW; 361655A272F6569C CRC64;
MPSTRSLVSR LIPPLASHWH KGQQGRVGVV GGSFEYTGAP YYAGISSLKT GADLCHLFCV
EEAAVPIKSY SPELIVHPLL RSDASLESLE EPKRVEVLNE AVEKISQILP RLDVLVVGPG
LGRDVSVQEI TRQVIARAKA ANLPLVLDGD ALYLVSLEPE VVKGYTNAIL TPNAVLSGAI
GTFAAWTKHA DISNTGFKGN PLLLAAYGGS LVTRASSSLA FDKHLRSMTA PDVLHSVGNG
FIKAFPSASI
//
