ID A0A0G4MZ61_9PEZI Unreviewed; 236 AA.
AC A0A0G4MZ61;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|ARBA:ARBA00012228, ECO:0000256|HAMAP-Rule:MF_03159};
DE EC=5.1.99.6 {ECO:0000256|ARBA:ARBA00012228, ECO:0000256|HAMAP-Rule:MF_03159};
DE AltName: Full=NAD(P)HX epimerase {ECO:0000256|HAMAP-Rule:MF_03159};
GN ORFNames=BN1708_001626 {ECO:0000313|EMBL:CRK39409.1}, BN1723_007612
GN {ECO:0000313|EMBL:CRK47555.1}, HYQ45_005058
GN {ECO:0000313|EMBL:KAG7137652.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK39409.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|Proteomes:UP000044602, ECO:0000313|Proteomes:UP000045706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK39409.1}, and VL2
RC {ECO:0000313|EMBL:CRK47555.1};
RA Fogelqvist Johan;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAG7137652.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Vl32 {ECO:0000313|EMBL:KAG7137652.1};
RX PubMed=33955130;
RA Harting R., Starke J., Kusch H., Poggeler S., Maurus I., Schluter R.,
RA Landesfeind M., Bulla I., Nowrousian M., de Jonge R., Stahlhut G.,
RA Hoff K.J., Asshauer K.P., Thurmer A., Stanke M., Daniel R., Morgenstern B.,
RA Thomma B.P.H.J., Kronstad J.W., Braus-Stromeyer S.A., Braus G.H.;
RT "A 20-kb lineage-specific genomic region tames virulence in pathogenic
RT amphidiploid Verticillium longisporum.";
RL Mol. Plant Pathol. 0:0-0(2021).
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_03159}.
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_03159};
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_03159};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03159};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_03159};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03159}.
CC Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03159}.
CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000256|HAMAP-
CC Rule:MF_03159}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03159}.
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DR EMBL; CVQH01025860; CRK39409.1; -; Genomic_DNA.
DR EMBL; CVQI01036717; CRK47555.1; -; Genomic_DNA.
DR EMBL; JAEMWZ010000084; KAG7137652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4MZ61; -.
DR STRING; 100787.A0A0G4MZ61; -.
DR OrthoDB; 1493at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR Proteomes; UP000045706; Unassembled WGS sequence.
DR Proteomes; UP000689129; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR HAMAP; MF_01966; NADHX_epimerase; 1.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR InterPro; IPR032976; YJEFN_prot_NAXE-like.
DR NCBIfam; TIGR00197; yjeF_nterm; 1.
DR PANTHER; PTHR13232; NAD(P)H-HYDRATE EPIMERASE; 1.
DR PANTHER; PTHR13232:SF10; NAD(P)H-HYDRATE EPIMERASE; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03159};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_03159};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03159}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03159};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03159};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03159}; Potassium {ECO:0000256|HAMAP-Rule:MF_03159};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT DOMAIN 11..216
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT BINDING 61..65
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 62
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 123
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 127..133
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 156
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 159
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
SQ SEQUENCE 236 AA; 25588 MW; 04C66AC4C261514F CRC64;
MALKTLGAKA AAALDKDLMS AGAFSIDQLM ELAGLSVSQA VYKVHPPSKG RNILVACGPG
NNGGDGLVAA RHLHHYGYKP SIYYPKRSKK ELYQRLAKQL EDLEVSFVDD FPKALQTADH
IIDAIFGFSF SGEVREPFPA VIRALEETGL PVTSVDAPSS WDIEEGPPKT GLGSSFNPTV
LVSLTAPKPL VKHFQGRHFV GGRFVSDTVA KKYNLSLPEY QGIDQVVEVE NSVQKH
//
