ID Q2GSC3_CHAGB Unreviewed; 614 AA.
AC Q2GSC3;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=CHGG_09131 {ECO:0000313|EMBL:EAQ85117.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ85117.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH408034; EAQ85117.1; -; Genomic_DNA.
DR RefSeq; XP_001227058.1; XM_001227057.1.
DR AlphaFoldDB; Q2GSC3; -.
DR GeneID; 4395094; -.
DR VEuPathDB; FungiDB:CHGG_09131; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_444801_0_0_1; -.
DR InParanoid; Q2GSC3; -.
DR OrthoDB; 2688376at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR CDD; cd08249; enoyl_reductase_like; 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; IPR016477; Fructo-/Ketosamine-3-kinase.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR047122; Trans-enoyl_RdTase-like.
DR PANTHER; PTHR45348; HYPOTHETICAL OXIDOREDUCTASE (EUROFUNG); 1.
DR PANTHER; PTHR45348:SF2; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C2E1P3.01; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF03881; Fructosamin_kin; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT DOMAIN 15..342
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 370..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..614
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 65794 MW; 4FF22975485B17D9 CRC64;
MASNLNRAAW LHKAGTPLEV GEAPMPTAGP NELVIRNAAV AINPLDCHMQ SAGVFVQQWP
SVFGCDVAGV VHEVGSDVHE RFKVGDRVIG HAINLTSGRP QDGAFALYTT IPASKAAILP
SSIPFTSGVV VPFALEAAVC ALSVKQPGTA LPNVPTPALG LPYPSLTDPP TTITTTTTTN
PQKTLIIYGG SSSVGSMATQ LATAAGIRVL AIASARNFSL CRACGAAAVF DYHDTSFVDD
VVSAATAEGG EFVGIFDAVS TPETYANGLA MLQRLGSGHL ACVHPPPEVP EGVQAGMIFA
VDEIATPVWR DYVTAALEAG RLKCLPPPLV VGKGLEFVQE ALEKCAQGGF EGELHVDSKR
RRTSMWVLDA GSRKTPHQRR ADDSSRNNTS THRTEGPSQV TTMSMTRAKA TPLAELVLPN
TQSQTERAAV DIIHHPHFQS SFEVGGNITK ACRYQVVFNL GAVGKHMCNG EFESLKAIHA
VSPGFVPEPY AWGEVTDGQG DYFLLVEFCH LRCQPAVPEK LSSRLADMHM RSVSPTGKFG
FHVPTCHAKI IQAVDAWDDS CVYQDMTTLC KMFCSKDLEQ AMVHLEERKT LEGTLTVASS
EDEDEEEEEE EEEE
//