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Database: UniProt
Entry: A0A1W6E5H9_9BACT
LinkDB: A0A1W6E5H9_9BACT
Original site: A0A1W6E5H9_9BACT 
ID   A0A1W6E5H9_9BACT        Unreviewed;       397 AA.
AC   A0A1W6E5H9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Formaldehyde dehydrogenase, glutathione-independent {ECO:0000313|EMBL:ARK10674.1};
GN   ORFNames=A6C57_10225 {ECO:0000313|EMBL:ARK10674.1};
OS   Fibrella sp. ES10-3-2-2.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Fibrella.
OX   NCBI_TaxID=1834519 {ECO:0000313|EMBL:ARK10674.1, ECO:0000313|Proteomes:UP000193660};
RN   [1] {ECO:0000313|Proteomes:UP000193660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES10-3-2-2 {ECO:0000313|Proteomes:UP000193660};
RA   Kim M.K., Srinivasan S., Kim E.B., Kim K.S.;
RL   Submitted (APR-2016) 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; CP015317; ARK10674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6E5H9; -.
DR   STRING; 1834519.A6C57_10225; -.
DR   KEGG; fib:A6C57_10225; -.
DR   OrthoDB; 9787435at2; -.
DR   Proteomes; UP000193660; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08282; PFDH_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; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR014184; HCHO_DH_non_GSH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR02819; fdhA_non_GSH; 1.
DR   PANTHER; PTHR42813:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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:UP000193660};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          35..144
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          197..264
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   397 AA;  41733 MW;  6F35878E458A2C8F CRC64;
     MASNRGVVYT GPGNVEVQNI DFPELANPKG KKIGHGVILK VISTNICGSD QHMVRGRTTA
     EPGLILGHEI TGEVIEKGAD VEFLDIGDIV SVPFNVACGR CRTCKEQQTG ICLNVNDSRA
     GGAYGYVDMG GWIGGQAEYV MVPYADFNLL RFPDREQAMA KIRDLTMLSD IFPTGFHGAV
     KAGVGPGTTV YIAGAGPVGM AAAASAQLLG AAVVIVGDMN KARLAHARSI GCETVDLNED
     ASLADQIAQI LGVPEVDCAV DCVGFEARGH GGQVQKEVPA AVLNSLMEIA RAGGAIGIPG
     LYVTEDPGAE ESTAKTGNLS IRFGLGWAKS HSFFTGQTPV IKYNRQLMMS ILYDKVQIAK
     AVNVEVITLD QAPEGYAEFD SGVAKKFVLD PHGLVPA
//
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