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Database: UniProt
Entry: A0A179G6T5_METCM
LinkDB: A0A179G6T5_METCM
Original site: A0A179G6T5_METCM 
ID   A0A179G6T5_METCM        Unreviewed;       303 AA.
AC   A0A179G6T5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=NAD(P)-binding Rossmann-fold containing protein {ECO:0000313|EMBL:OAQ72889.1};
GN   ORFNames=VFPPC_00737 {ECO:0000313|EMBL:OAQ72889.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ72889.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ72889.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ72889.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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:OAQ72889.1}.
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DR   EMBL; LSBJ02000001; OAQ72889.1; -; Genomic_DNA.
DR   RefSeq; XP_018148972.1; XM_018280699.1.
DR   AlphaFoldDB; A0A179G6T5; -.
DR   STRING; 1380566.A0A179G6T5; -.
DR   GeneID; 28844693; -.
DR   KEGG; pchm:VFPPC_00737; -.
DR   OrthoDB; 2654086at2759; -.
DR   Proteomes; UP000078397; Chromosome 1.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR44229; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1.
DR   PANTHER; PTHR44229:SF4; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078397}.
SQ   SEQUENCE   303 AA;  33004 MW;  C0A1FBD1DDECF7BE CRC64;
     MALNVSGKTA IVTGAGSGIN LAFAQLLLRS NCNVVFADLA LRPEAEEVVK THIDGSNGPR
     AIFQRTDVTD WVQLEAMFDV AEQTFGAVDI VCPGAGVYEP PFSNFWIPPG TGVTKDDPRG
     SRYAAMDINV THPIRCTQIA IAHFIKHSRP GAVVHISSIA AQRPFLQCPL YVASKAAISG
     FVRSLALLET PKSTELPSIR VNCVAPGLIK TPLWTENPEK LRWIDVEQDE WVTAEDVAQV
     MLDLVQKEEY VGGTVLEVGQ NQVRRVEVLN DPGPKGAGHT VSAADVGEKE VWDRLTRPSW
     GQW
//
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