ID A0A1Q5TJQ9_9EURO Unreviewed; 286 AA.
AC A0A1Q5TJQ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=D-arabinitol 2-dehydrogenase [ribulose-forming] {ECO:0000313|EMBL:OKP00459.1};
GN ORFNames=PENSUB_7916 {ECO:0000313|EMBL:OKP00459.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP00459.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKP00459.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP00459.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:OKP00459.1}.
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DR EMBL; MNBE01000647; OKP00459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5TJQ9; -.
DR STRING; 1316194.A0A1Q5TJQ9; -.
DR OrthoDB; 1701404at2759; -.
DR Proteomes; UP000186955; 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 GO; GO:0044550; P:secondary metabolite 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; PTHR43008; BENZIL REDUCTASE; 1.
DR PANTHER; PTHR43008:SF4; CHAIN DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G08710)-RELATED; 1.
DR Pfam; PF13561; adh_short_C2; 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:UP000186955}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 286 AA; 30994 MW; FA1183013EA13C02 CRC64;
MSVAIETTEA PTAPNTAQPV MMGHKSRMPE FSLAGKIVCV SGAGRGLGLT QSEALLEAGA
KVYALDRLEE PAPEFAQIQQ KAKELGTELH YRRIDVRDTE LLNSVIEAIA NTEGRMDGLV
AAAGIQQETP ALEYSAKDSN TMFEVNVTGV FMTAQAVAKQ MIRFGNGGSI AMIASMSGTI
ANRGLICPAY NASKAAVIQL ARNLAAEWGQ YNIRVNTISP GYIVTQMVEK LFVEFPERRE
QWPKENMLGR LSRPEEYRGA AVFLLSDASS FMTGSDLRMD GGHAAW
//
