ID A0A1V6QN03_9EURO Unreviewed; 409 AA.
AC A0A1V6QN03;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENSOL_c058G07141 {ECO:0000313|EMBL:OQD90357.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD90357.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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:OQD90357.1}.
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DR EMBL; MDYO01000058; OQD90357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QN03; -.
DR STRING; 60172.A0A1V6QN03; -.
DR OrthoDB; 3017546at2759; -.
DR Proteomes; UP000191612; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05285; sorbitol_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR045306; SDH-like.
DR PANTHER; PTHR43161:SF25; ALCOHOL DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14390)-RELATED; 1.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 30..142
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 197..355
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 409 AA; 42818 MW; CCBECCBF35266E8B CRC64;
MADTTTNALV LHGAKDLRLE QRTITPPSTT EVQVAIRATG ICGSDLHYYS HGRNGDFVVR
APMCLGHESA GTVTAIGNGV TTLKVGDRVA LEVGLPCRTC ALCKQGRYNI CKAMQFRSSA
KAFPHLDGTL MERTNHPADM CHLLPDSVSD AGGALVEPLA VTLHAVRRSH PPSKEEVSQN
REAGEETAAL VFGAGAIGLL LAGALAASEN FSAIVVADID ARRLKIAEDM GLGLKTALIP
RAETPPPAKD APHAEQTAYA LENAQKVAAK LIEAVGAKDG LVVHGFTRVY DCTGVPACVQ
AGIYASAPGG VLVQIGMGNP IQTLPVGAAA LREVDIIGVF RYDGFAYPAA IALLASGKVK
SVEEKVVTHR LKLEEGERAF TLAGKGVDEE GNPVVKVIIE NRRGASGSL
//
