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Database: UniProt
Entry: A0A2V1AWL7_9ASCO
LinkDB: A0A2V1AWL7_9ASCO
Original site: A0A2V1AWL7_9ASCO 
ID   A0A2V1AWL7_9ASCO        Unreviewed;       342 AA.
AC   A0A2V1AWL7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=NAD-dependent epimerase/dehydratase domain-containing protein {ECO:0000259|Pfam:PF01370};
GN   ORFNames=CXQ85_005059 {ECO:0000313|EMBL:PVH22490.1};
OS   [Candida] haemuloni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH22490.1, ECO:0000313|Proteomes:UP000244309};
RN   [1] {ECO:0000313|EMBL:PVH22490.1, ECO:0000313|Proteomes:UP000244309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B11899 {ECO:0000313|EMBL:PVH22490.1,
RC   ECO:0000313|Proteomes:UP000244309};
RA   Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA   Litvintseva A.P.;
RT   "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT   Patient with Chronic Leg Ulcers in Israel.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Dihydroflavonol-4-reductase subfamily.
CC       {ECO:0000256|ARBA:ARBA00023445}.
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:PVH22490.1}.
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DR   EMBL; PKFO01000008; PVH22490.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1AWL7; -.
DR   STRING; 45357.A0A2V1AWL7; -.
DR   EnsemblFungi; CXQ85_005059-t46_1; CXQ85_005059-t46_1-p1; CXQ85_005059.
DR   VEuPathDB; FungiDB:CXQ85_005059; -.
DR   OrthoDB; 1200131at2759; -.
DR   Proteomes; UP000244309; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd05227; AR_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR   PANTHER; PTHR10366:SF853; NADPH-DEPENDENT ALDEHYDE REDUCTASE ARI1-RELATED; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244309}.
FT   DOMAIN          6..259
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
FT   REGION          288..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   342 AA;  37584 MW;  B3905E80D20C4A1D CRC64;
     MSSTKVLISG ASGFIAVHTV QQLIRNGYTV VGSVRSSEKG EYVKKASGKP DKFSYEIVED
     IAKEGAFDEF VKKHSDATVF LHTASPFHYK VTDVETDLLK PAIHGTKNAL SSIAKYGTNI
     KRVVVTSSNA AIASRDQDSD PKNVFDETSW NNITWEKALE SPAFGYSGSK AFAERAAWDF
     VKEQNPGFVL STVNPVLVFG PQPTNDFNTD KLNTSSEVIN VILKSSSPDD KVAPYNSSAV
     DVRDVAKAHL VAFEKDEAKN QRLFLTSDAF TQQTILDVLH EKFPKQTEKV PVGTPGTDKD
     EFDQKATKNN DKTRKILGFE LISVRQSIAD SAQQLLQVEG KL
//
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