ID   FRMA_ECOSM              Reviewed;         369 AA.
AC   B1LIP1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   16-JUN-2009, entry version 10.
DE   RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase;
DE            EC=1.1.1.284;
DE   AltName: Full=Glutathione-dependent formaldehyde dehydrogenase;
DE            Short=GSH-FDH;
DE            Short=FALDH;
DE            Short=FDH;
DE            EC=1.1.1.-;
DE   AltName: Full=Alcohol dehydrogenase class-3;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase class-III;
GN   Name=frmA; OrderedLocusNames=EcSMS35_0387;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18708504; DOI=10.1128/JB.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia
RT   coli SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
CC   -!- FUNCTION: Has high formaldehyde dehydrogenase activity in the
CC       presence of glutathione and catalyzes the oxidation of normal
CC       alcohols in a reaction that is not GSH-dependent (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-(hydroxymethyl)glutathione + NAD(P)(+) = S-
CC       formylglutathione + NAD(P)H.
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily.
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DR   EMBL; CP000970; ACB18273.1; -; Genomic_DNA.
DR   RefSeq; YP_001742490.1; -.
DR   GeneID; 6143543; -.
DR   GenomeReviews; CP000970_GR; EcSMS35_0387.
DR   KEGG; ecm:EcSMS35_0387; -.
DR   OMA; B1LIP1; AKFELAR.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004022; F:alcohol dehydrogenase activity; IEA:EC.
DR   GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase ...; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR014183; ADH_3.
DR   InterPro; IPR013154; ADH_GroES-like.
DR   InterPro; IPR002085; ADH_SF_Zn.
DR   InterPro; IPR013149; ADH_Zn-bd.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   PANTHER; PTHR11695; ADH_Sf_Zn; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   TIGRFAMs; TIGR02818; adh_III_F_hyde; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW   Zinc.
FT   CHAIN         1    369       S-(hydroxymethyl)glutathione
FT                                dehydrogenase.
FT                                /FTId=PRO_0000341284.
FT   METAL        40     40       Zinc 1; catalytic (By similarity).
FT   METAL        62     62       Zinc 1; catalytic (By similarity).
FT   METAL        92     92       Zinc 2 (By similarity).
FT   METAL        95     95       Zinc 2 (By similarity).
FT   METAL        98     98       Zinc 2 (By similarity).
FT   METAL       106    106       Zinc 2 (By similarity).
FT   METAL       169    169       Zinc 1; catalytic (By similarity).
SQ   SEQUENCE   369 AA;  39391 MW;  6614D0578802EDB0 CRC64;
     MKSRAAVAFA PGKPLEIVEI DVAPPKKGEV LIKVTHTGVC HTDAFTLSGD DPEGVFPVVL
     GHEGAGVVVE VGEGVTSVKP GDHVIPLYTA ECGECEFCRS GKTNLCVAVR ETQGKGLMPD
     GTTRFSYNGQ PLYHYMGCST FSEYTVVAEV SLAKINPEAN HEHVCLLGCG VTTGIGAVHN
     TAKVQPDDSV AVFGLGAIGL AVVQGARQAK AGRIIAIDTN PKKFDLARRF GATDCINPND
     YDKPIKDVLL DINKWGIDHT FECIGNVNVM RAALESAHRG WGQSVIIGVA GSGQEISTRP
     FQLVTGRVWK GSAFGGVKGR SQLPGMVEDA MKGDIDLEPF VTHTMSLDEI NDAFDLMHEG
     KSIRTVIRY
//