ID A0A1V6RNR9_9EURO Unreviewed; 694 AA.
AC A0A1V6RNR9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|HAMAP-Rule:MF_03159};
DE EC=5.1.99.6 {ECO:0000256|HAMAP-Rule:MF_03159};
DE AltName: Full=NAD(P)HX epimerase {ECO:0000256|HAMAP-Rule:MF_03159};
GN ORFNames=PENSOL_c001G07045 {ECO:0000313|EMBL:OQE03266.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQE03266.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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|HAMAP-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|HAMAP-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, P-body
CC {ECO:0000256|ARBA:ARBA00004201}. Cytoplasm {ECO:0000256|HAMAP-
CC Rule:MF_03159}. Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03159}.
CC -!- SIMILARITY: Belongs to the EDC3 family.
CC {ECO:0000256|ARBA:ARBA00006610}.
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}.
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:OQE03266.1}.
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DR EMBL; MDYO01000001; OQE03266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RNR9; -.
DR STRING; 60172.A0A1V6RNR9; -.
DR OrthoDB; 1409462at2759; -.
DR Proteomes; UP000191612; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; 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; IPR025762; DFDF.
DR InterPro; IPR019050; FDF_dom.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR PANTHER; PTHR13612:SF0; ENHANCER OF MRNA-DECAPPING PROTEIN 3; 1.
DR PANTHER; PTHR13612; UNCHARACTERIZED; 1.
DR Pfam; PF09532; FDF; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SMART; SM01199; FDF; 1.
DR SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR PROSITE; PS51512; DFDF; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03159};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_03159};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03159};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03159};
KW NAD {ECO:0000256|HAMAP-Rule:MF_03159};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03159};
KW Potassium {ECO:0000256|HAMAP-Rule:MF_03159};
KW Reference proteome {ECO:0000313|Proteomes:UP000191612}.
FT DOMAIN 265..301
FT /note="DFDF"
FT /evidence="ECO:0000259|PROSITE:PS51512"
FT DOMAIN 442..667
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT REGION 69..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 565
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 603
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
FT BINDING 606
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03159"
SQ SEQUENCE 694 AA; 75584 MW; DAA0984A5A8F8EF6 CRC64;
MASEFIGYNV LVTLREPQGG RLVGQVANVF GQRLLLQDVT FLWNGQRLPQ YSIDASAIID
LSLETNTQAP PQRQQLPQHQ PLQPYGTMPL PSAPSQSTPT QQQFTDPAIL SFSKAPLISK
PFVENASTAV PANQIPGAVS ASLSEPFSSL ELNADSDKTG IQGTSHKKLL QSPQELSPSK
QTPKRNRRGN QENVREERGY VAKHVPKHGA AASTNPKSKG WRQTAFVEPA APAFQDSPEA
MSRSGTKLRK KKSRRYAEDP SGWATEDATD IQELGEFDFE SNLSKFDKRT VFEQIRNDDT
TADEERLVSF NRKVKPGTNG GKNLHWTENV LDSPQNSDTG DDIEGISEIK LGSDTLSGRE
RSRAPTHAQP PRKDSAIQAP PMVPQLSALG RSQLHVNISR TTSPRPSRSS VSPMITPNVS
GAGSLRLTTT NRSCPTVSPL QTLEIEQISV AEFGLADEII TENAGRGIAE AAVALLSNDA
AAPTMLILTG NHRTGARAIA AARHLRNRGH RVTVCLLGLE HEAELLENCR KQLDIFRKVG
GRVLKWEELS ARLATSDLGP DLIIDALFGM HLSFDDLRTD DQGVAFEMIS WMNRSNVDVL
SVDVPSGLNA STGEVTLAEG GRLCVNATSV VCLGAPKTGV LNALLSGERL SWNLAVADIG
IPQIVWRKYG TRRRHGIDFG NKWVVPLKYQ PLLS
//
