ID ADH2_GEOSE Reviewed; 339 AA.
AC P42327;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 05-OCT-2016, entry version 85.
DE RecName: Full=Alcohol dehydrogenase;
DE Short=ADH;
DE EC=1.1.1.1;
GN Name=adh;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-40.
RC STRAIN=DSM 2334 / Var. Non-diastaticus;
RX PubMed=8049268; DOI=10.1016/0167-4781(94)90199-6;
RA Robinson G.A., Bailey C.J., Dowds B.C.A.;
RT "Gene structure and amino acid sequences of alcohol dehydrogenases of
RT Bacillus stearothermophilus.";
RL Biochim. Biophys. Acta 1218:432-434(1994).
CC -!- FUNCTION: Active with primary alcohols, including methanol.
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 -!- ENZYME REGULATION: The rate-limiting step is NADH release.
CC Catabolite repression.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
DR EMBL; Z25544; CAA80989.1; -; Genomic_DNA.
DR PIR; S47643; S47643.
DR ProteinModelPortal; P42327; -.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; -; 1.
DR Gene3D; 3.90.180.10; -; 1.
DR InterPro; IPR013149; ADH_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002085; ADH_SF_Zn-type.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR11695; PTHR11695; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1 339 Alcohol dehydrogenase.
FT /FTId=PRO_0000160737.
FT NP_BIND 172 177 NAD. {ECO:0000250}.
FT NP_BIND 260 262 NAD. {ECO:0000250}.
FT METAL 38 38 Zinc 1; catalytic. {ECO:0000250}.
FT METAL 61 61 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 148 148 Zinc 1; catalytic. {ECO:0000250}.
FT BINDING 195 195 NAD. {ECO:0000250}.
FT BINDING 200 200 NAD. {ECO:0000250}.
FT BINDING 331 331 NAD. {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 26 134 ipfam:ADH_N [T]
FT MYHIT 175 300 ipfam:ADH_zinc_N [T]
FT MYHIT 60 74 ipat:ADH_ZINC [T]
FT MYHIT 11 334 ismart:PKS_ER [T]
SQ SEQUENCE 339 AA; 36205 MW; 0EC33CE7287D7476 CRC64;
MKAAVVNEFK KALEIKEVER PKLEEGEVLV KIEACGVCHT DLHAAHGDWP IKPKLPLIPG
HEGVGIVVEV AKGVKSIKVG DRVGIPWLYS ACGECEYCLT GQETLCPHQL NGGYSVDGGY
AEYCKAPADY VAKIPDNLDP VEVAPILCAG VTTYKALKVS GARPGEWVAI YGIGGLGHIA
LQYAKAMGLN VVAVDISDEK SKLAKDLGAD IAINGLKEDP VKAIHDQVGG VHAAISVAVN
KKAFEQAYQS VKRGGTLVVV GLPNADLPIP IFDTVLNGVS VKGSIVGTRK DMQEALDFAA
RGKVRPIVET AELEEINEVF ERMEKGKING RIVLKLKED
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