ID F4PF10_BATDJ Unreviewed; 372 AA.
AC F4PF10;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Formaldehyde dehydrogenase, glutathione-independent {ECO:0008006|Google:ProtNLM};
GN ORFNames=BATDEDRAFT_15016 {ECO:0000313|EMBL:EGF76190.1};
OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF76190.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF76190.1, ECO:0000313|Proteomes:UP000007241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA Stajich J., Eisen M., Grigoriev I.V.;
RT "The draft genome of Batrachochytrium dendrobatidis.";
RL Submitted (DEC-2009) 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; GL882903; EGF76190.1; -; Genomic_DNA.
DR RefSeq; XP_006683196.1; XM_006683133.1.
DR AlphaFoldDB; F4PF10; -.
DR STRING; 684364.F4PF10; -.
DR GeneID; 18236998; -.
DR HOGENOM; CLU_026673_11_3_1; -.
DR InParanoid; F4PF10; -.
DR OMA; TIGTGQC; -.
DR OrthoDB; 948431at2759; -.
DR Proteomes; UP000007241; Unassembled WGS sequence.
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:UP000007241};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 1..109
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 161..229
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGF76190.1"
SQ SEQUENCE 372 AA; 39427 MW; 31475019EE880FCE CRC64;
VILKVISTNI CGSDQHMVRG RTTAPSGLVL GHEITGQVIE VGSDVEFIEK GDIVSVPFNI
ACGRCESCKK QDTHICTNVN PDRPGSAYGY VDMGGWVGGQ SEYVMVPYAD FQLLKFPDKD
QALEKILDLT MLSDIFPTGY HGAVSAGVKT GSTVYVAGAG PVGLAAAHSA QLLGASVVIV
GDLNEDRLAQ ARSFGCETVN LREHDDLGEQ IEQILGTPEV DCAVDAVGFE ASGHGRDAGE
APATVLNSIM GVTRAGGRLG IPGLYVTGDP GAADKDAKEG TLKIRFGLGF AKAHTFVTGQ
TPVMRYNRDL MKAILSGRAQ IAKAVNATVI SINEAPDGYK QFDGGVSRKF VIDPHNMIKQ
RNYLTTKQQV SN
//