ID Q0TYY1_PHANO Unreviewed; 755 AA.
AC Q0TYY1;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=SNOG_15408 {ECO:0000313|EMBL:EAT77341.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT77341.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024149};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CH445361; EAT77341.2; -; Genomic_DNA.
DR RefSeq; XP_001805556.1; XM_001805504.1.
DR AlphaFoldDB; Q0TYY1; -.
DR STRING; 321614.Q0TYY1; -.
DR GeneID; 5982485; -.
DR KEGG; pno:SNOG_15408; -.
DR VEuPathDB; FungiDB:JI435_098670; -.
DR VEuPathDB; FungiDB:JI435_309290; -.
DR InParanoid; Q0TYY1; -.
DR OrthoDB; 5295198at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08297; CAD3; 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; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR11699:SF204; ALDEDH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 25..335
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT ACT_SITE 565
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 755 AA; 80223 MW; 1B36532BC5866252 CRC64;
MVSTVTRAGP TIPRTHKAII YTNPQSLDTA VVDVDTPQPR AGECLIRLTH SGVCHSDLAF
ITNGYAHMPE PTPSGQIGGH EGIGIVVSLG PYVDAVAVGD RVGVKWIASA CLTCSACTQG
FDGRCAKRKV AGFKDPGTFQ QYIISDPRYV TPIPDSIDSA DAAPLLCGGL TVYSALLKAD
CSPGDWIALS GAAGGLGHLA IQYCNAYGLR VLAIDHGSKR DFCLGLGAHV FLDFTQFDDA
GLAAEAKRLT HGGCHAVLVC NASSRVYDTA LDLLRYAGTL VCVGVPELDP HPIANALPWK
LIVNQYSIKG AVTGSRKDSI DCLRPAAQGQ VKAAVRLEPM NKLTEIFHQL PRVYEADASD
VDLAVDAAEA AFPAWSDLGG FERARFFYRL ADALELANSD LAALEAISMG RPVGQYREAI
NGAALLRYYA GKCTDVQGDS SLQTSGFVNV VLRQPFGVCA GITPWNAPIT MMLFKIAGAC
VCGNTIICKS SEKAPLTALY LAKLIKQAGF PPGVINILSG KGTPCGDALA RHPRIRKISL
TGSINAGRAV KKAAAESNLK NVSLELGGKS PLIIFEDADL DKAIPAAARS IISNTGQVCI
ASSRLLVQSS ILKTFSTRLV AEIEATGYNP ESSQGNPLSP ETLRGPQADL KQYDSIIGFL
QESKAAGHEV LTGGGRDTRH GKKGFFVQPT LILNPGDQSR ISREEIFGPV QVLATFQTEE
DAIRRSIDSE YGLYASVYTR YGPSFRGPDT LVILQ
//