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
//