ID   A0A084QJ72_STAC4        Unreviewed;       897 AA.
AC   A0A084QJ72;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=S40285_05484 {ECO:0000313|EMBL:KFA64007.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA64007.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA64007.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA64007.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
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|ARBA:ARBA00009986, 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; KL660705; KFA64007.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084QJ72; -.
DR   STRING; 1283841.A0A084QJ72; -.
DR   HOGENOM; CLU_014154_0_0_1; -.
DR   InParanoid; A0A084QJ72; -.
DR   OrthoDB; 1818863at2759; -.
DR   Proteomes; UP000028524; Unassembled WGS sequence.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08278; benzyl_alcohol_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; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
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; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR11699:SF198; DEHYDROGENASE FAMILY PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G03250)-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; PS00070; ALDEHYDE_DEHYDR_CYS; 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:UP000028524};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          534..895
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   897 AA;  94777 MW;  B308CD80919983C2 CRC64;
     MPDTYKLWLA GKEQPGGADL IPVEDPATGE IIAHCHAASE ADVHTAVAAA HDAYKSGVWS
     RASRHTRADV LERCAALLTP ALPQLIALEV RQTGRAVREL QAQVPSLVRW FKYYASLLRV
     EERAVLPTTG KLHNFLDRVP LGVVAHVTPF NHPLLIAVKK LAPALAAGNS VVVKPSELTP
     LTTLLLGDVL RRAGVPDGVF TVLPGYGATT GKQLVEHPLV RKVDVTGGTA AGRAIGAIVG
     GNLAKYTAEL GGKAPLVVFE DADVDVAVNG IAFGSFIASG QTCIASTRII VENSILDEVL
     AKLKAKVESI ARRVGSPANP DCMMGPLISA KQLQQVERLV DEAVQGEFAK ALTGGRRMQG
     ASALDGTDLS RGYFYEPTVL VSTAGNNSIT QTAIWRAEAF GPVVVVAGFD TEPQAVALAN
     DSEFGLGASI WTRDLSRGFR VAEQVEAGIV WVNTHHRNDP SSPWGGAKAA SGVGSENGVD
     AYHAYTTTKS TIINYATAEE SLAADDWFRE GGFYTESIRT PSMGFESEAL VARGPLSEGK
     WAVEPVTLRE LREDEVLVEM VASGICHTDL HCGDTPADAG VPGVFYPRVL GHEGSGYVVQ
     AGSAVTKVKP GDAVLLSFSY CGSCYMCGRG LRSHCVDFFA INFLGERDVF AGGIGGRFFG
     QSSLARHSVV CAKSVVNVEG LGLTRDDLRL LAPLGCGLQT GSGTVAKVAD AGADDCLAVV
     GMGGVGLAAV MAARNRGCRA VIGVDRVEAR LELARSLGAT HTVNTAGLSM DEVAARIRDA
     AEGLGPTISI DTSAHPPLVM ALIAASRYGG RIIQVGTGLP ESHVSIHMQS FMVSAKQYFG
     AVQGHALTEE SIPQLVRWWR EGVFPVEKLV EFFPYKDFEK AMSVMGSGSV VKPVIVW
//