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Database: UniProt
Entry: Q0TYY1_PHANO
LinkDB: Q0TYY1_PHANO
Original site: Q0TYY1_PHANO 
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
//
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