Reviewed, UniProtKB/Swiss-Prot P42327 (ADH2_BACST)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase
      Short name=ADH
    EC=1.1.1.1

Gene names

Name:

adh

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Active with primary alcohols, including methanol.
Catalytic activity	An alcohol + NAD(+) = an aldehyde or ketone + NADH.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Enzyme regulation	The rate-limiting step is NADH release. Catabolite repression.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: InterPro
Molecular function	alcohol dehydrogenase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 339	339	Alcohol dehydrogenase		PRO_0000160737
Sites
	Metal binding	38	1	Zinc 1; catalytic By similarity
	Metal binding	61	1	Zinc 1; catalytic By similarity
	Metal binding	92	1	Zinc 2 By similarity
	Metal binding	95	1	Zinc 2 By similarity
	Metal binding	98	1	Zinc 2 By similarity
	Metal binding	106	1	Zinc 2 By similarity
	Metal binding	148	1	Zinc 1; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P42327-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 0EC33CE7287D7476	FASTA	339	36,205
	10 20 30 40 50 60 MKAAVVNEFK KALEIKEVER PKLEEGEVLV KIEACGVCHT DLHAAHGDWP IKPKLPLIPG 70 80 90 100 110 120 HEGVGIVVEV AKGVKSIKVG DRVGIPWLYS ACGECEYCLT GQETLCPHQL NGGYSVDGGY 130 140 150 160 170 180 AEYCKAPADY VAKIPDNLDP VEVAPILCAG VTTYKALKVS GARPGEWVAI YGIGGLGHIA 190 200 210 220 230 240 LQYAKAMGLN VVAVDISDEK SKLAKDLGAD IAINGLKEDP VKAIHDQVGG VHAAISVAVN 250 260 270 280 290 300 KKAFEQAYQS VKRGGTLVVV GLPNADLPIP IFDTVLNGVS VKGSIVGTRK DMQEALDFAA 310 320 330 RGKVRPIVET AELEEINEVF ERMEKGKING RIVLKLKED

References

[1]

"Gene structure and amino acid sequences of alcohol dehydrogenases of Bacillus stearothermophilus." Robinson G.A., Bailey C.J., Dowds B.C.A. Biochim. Biophys. Acta 1218:432-434(1994) [PubMed: 8049268] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-40. Strain: DSM 2334 / Var. Non-diastaticus.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z25544 Genomic DNA. Translation: CAA80989.1.
PIR	S47643.
3D structure databases
HSSP	HSSP built from PDB template 1JVB based on UniProtKB P39462.
SMR	P42327. Positions 1-338.
ModBase	Search...
Family and domain databases
InterPro	IPR013154. AlcDHase_GroES-like. IPR002085. AlcDHase_SF_Zn. IPR013149. AlcDHase_Zn-bd. IPR002328. AlcDHase_Zn_CS. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	P42327.

Entry information

Entry name

ADH2_BACST

Accession

Primary (citable) accession number: P42327

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 25, 2008
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)