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Database: UniProt
Entry: A0A178E8U4_9PLEO
LinkDB: A0A178E8U4_9PLEO
Original site: A0A178E8U4_9PLEO 
ID   A0A178E8U4_9PLEO        Unreviewed;       218 AA.
AC   A0A178E8U4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000256|ARBA:ARBA00012228};
DE            EC=5.1.99.6 {ECO:0000256|ARBA:ARBA00012228};
GN   ORFNames=IQ07DRAFT_586090 {ECO:0000313|EMBL:OAL51729.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL51729.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL51729.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL51729.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- 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};
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DR   EMBL; KV441642; OAL51729.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178E8U4; -.
DR   STRING; 765867.A0A178E8U4; -.
DR   InParanoid; A0A178E8U4; -.
DR   OrthoDB; 1493at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10260; YjeF N-terminal domain; 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   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT   DOMAIN          1..199
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51385"
SQ   SEQUENCE   218 AA;  23814 MW;  507F93ED10589BB2 CRC64;
     MSTGAFSIDQ LMELAGLSVS QAVFKLQPLS KGKRILIACG PGNNGGDGLV AARHLFHYGY
     QPTVYYPKQS KNELYQRLKK QLEDLKVPFT EDFSGALKQT DHIVDAIFGF SFSGEVREPF
     PKVIEALAST SIPVLAVDAP SSWDIEDGPR DSGPGKGFMP PALISLTAPK PLVKQFKGRH
     FLGGRFLSPE IAQKYHLDIP KYEGLDQVVE VPVEAGKL
//
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