(data stored in ACNUC7421 zone)

SWISSPROT: FRMA_ECO57

ID   FRMA_ECO57              Reviewed;         369 AA.
AC   Q8X5J4; Q7AH45;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 111.
DE   RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase;
DE            EC=1.1.1.284;
DE   AltName: Full=Alcohol dehydrogenase class-3;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase class-III;
DE   AltName: Full=Glutathione-dependent formaldehyde dehydrogenase;
DE            Short=FALDH;
DE            Short=FDH;
DE            Short=GSH-FDH;
DE            EC=1.1.1.-;
GN   Name=frmA; OrderedLocusNames=Z0456, ECs0411;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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. {ECO:0000250}.
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:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000305}.
DR   EMBL; AE005174; AAG54707.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33834.1; -; Genomic_DNA.
DR   PIR; C90680; C90680.
DR   PIR; G85530; G85530.
DR   RefSeq; NP_308438.1; NC_002695.1.
DR   RefSeq; WP_000842102.1; NZ_MWVM01000022.1.
DR   ProteinModelPortal; Q8X5J4; -.
DR   SMR; Q8X5J4; -.
DR   STRING; 155864.Z0456; -.
DR   EnsemblBacteria; AAG54707; AAG54707; Z0456.
DR   EnsemblBacteria; BAB33834; BAB33834; BAB33834.
DR   GeneID; 914513; -.
DR   KEGG; ece:Z0456; -.
DR   KEGG; ecs:ECs0411; -.
DR   PATRIC; fig|386585.9.peg.506; -.
DR   eggNOG; ENOG4107QPD; Bacteria.
DR   eggNOG; COG1062; LUCA.
DR   HOGENOM; HOG000294674; -.
DR   KO; K00121; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR   CDD; cd08300; alcohol_DH_class_III; 1.
DR   InterPro; IPR014183; ADH_3.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR02818; adh_III_F_hyde; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X5J4.
DR   SWISS-2DPAGE; Q8X5J4.
KW   Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW   Zinc.
FT   CHAIN         1    369       S-(hydroxymethyl)glutathione
FT                                dehydrogenase.
FT                                /FTId=PRO_0000341287.
FT   METAL        40     40       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL        62     62       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL        92     92       Zinc 2. {ECO:0000250}.
FT   METAL        95     95       Zinc 2. {ECO:0000250}.
FT   METAL        98     98       Zinc 2. {ECO:0000250}.
FT   METAL       106    106       Zinc 2. {ECO:0000250}.
FT   METAL       169    169       Zinc 1; catalytic. {ECO:0000250}.
SQ   SEQUENCE   369 AA;  39333 MW;  37C601848801ECFB CRC64;
     MKSRAAVAFA PGKPLEIVEI DVAPPKKGEV LIKVTHTGVC HTDAFTLSGD DPEGVFPVVL
     GHEGAGVVVE VGEGVTSVKP GDHVIPLYTA ECGECEFCRS GKTNLCVAVR ETQGKGLMPD
     GTTRFSYNGQ PLYHYMGCST FSEYTVVAEV SLAKINPEAN HEHVCLLGCG VTTGIGAVHN
     TAKVQPGDSV AVFGLGAIGL AVVQGARQAK AGRIIAIDTN PKKFDLARRF GATDCINPND
     YDKPIKDVLL DINKWGIDHT FECIGNVNVM RAALESAHRG WGQSVIIGVA GSGQEISTRP
     FQLVTGRVWK GSAFGGVKGR SQLPGMVEDA MKGDIDLEPF VTHTMSLDEI NDAFDLMHEG
     KSIRTVIRY
//

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