ID X0C7P0_FUSOX Unreviewed; 289 AA.
AC X0C7P0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Dehydrogenases with different specificities (Related to short-chain alcohol dehydrogenases) {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOQG_07230 {ECO:0000313|EMBL:EXK90445.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK90445.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK90445.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK90445.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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DR EMBL; JH658375; EXK90445.1; -; Genomic_DNA.
DR AlphaFoldDB; X0C7P0; -.
DR eggNOG; KOG1205; Eukaryota.
DR HOGENOM; CLU_010194_2_9_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
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; PTHR43976:SF16; NAD(P)-BINDING PROTEIN; 1.
DR PANTHER; PTHR43976; SHORT CHAIN DEHYDROGENASE; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..289
FT /note="Dehydrogenases with different specificities (Related
FT to short-chain alcohol dehydrogenases)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004937419"
SQ SEQUENCE 289 AA; 30949 MW; 21E0F02FDA14D232 CRC64;
MTTPVWFITG SSNGLGLLLS LRVLKAGHRV IATVRDTTRS ADAVRQIEEA GGKIVTIDLT
ESKASITKKV QDAEKAYGRI DFLVNNAGYS VLGGIELFTE AEAEHQIQTN LFGPLYTIQA
ALPGMRSRGS GTIINISSIA GQDAQPSCGL YSASKFALEG LSESLSKEVK EFGINVLLVE
PGAFRTNFLE ASIKSNISGE TAYQGTLLEA TLQKFEKAAG KQPGDPNKAV DIIFEVATGE
GAAGDLKGKV LRLPLGKDCF ARLKTKLEFL QHDIEATREI GITTDLDEK
//