ID   A0A1W6YYQ1_9BORD        Unreviewed;       402 AA.
AC   A0A1W6YYQ1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:ARP86009.1};
GN   ORFNames=CAL13_07170 {ECO:0000313|EMBL:ARP86009.1};
OS   Bordetella genomosp. 9.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1416803 {ECO:0000313|EMBL:ARP86009.1, ECO:0000313|Proteomes:UP000194139};
RN   [1] {ECO:0000313|EMBL:ARP86009.1, ECO:0000313|Proteomes:UP000194139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17164 {ECO:0000313|EMBL:ARP86009.1,
RC   ECO:0000313|Proteomes:UP000194139};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP021109; ARP86009.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6YYQ1; -.
DR   Proteomes; UP000194139; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08283; FDH_like_1; 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; IPR020843; PKS_ER.
DR   PANTHER; PTHR42813:SF7; ALCOHOL DEHYDROGENASE (ZN-DEPENDENT)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 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|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194139};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          7..391
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          261..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  42563 MW;  515A8B0EF6DB9508 CRC64;
     MKAVVFHAIG DIRLEDVPDP QLQEDTDAIV RLQVSAICGT DLHFIRGTME GVAPGTILGH
     EGVGVVEQVG AGVRNLQVGD RVVIPSTVAC GYCSYCRAGY YAQCDNANPH GKSAGTAFYG
     GPQQAGGFHG LQAEKARIPY AHVNLVKLPP EINDDQAIML SDIFPTGYFG ADLADIAPGR
     TVAVFGCGPV GQFAIASAKL MHAGRIFAVD AVPDRLAMAR AQGAETVDFN AEDPVETIKH
     LTGGIGVDRA IDAVGVDAVH PHHGPAADPQ QNAAMEAQSR ELAPHAHPDG ANWVPGDAPS
     QALNWAVQAL AKAGTLSIIG VYPPTDNAFP IGLAMNKNLT VRMGNCNHRK YIPMLIELVQ
     SGRIDPARIL TKREPLTSVL EAYKAFDTRQ PGWMKVELAP VA
//