[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 31821 / ZM4 / CP4; PubMed=2185223 [NCBI, ExPASy, EBI, Israel, Japan] Keshav K.F., Yomano L.P., An H., Ingram L.O.; "Cloning of the Zymomonas mobilis structural gene encoding alcohol dehydrogenase I (adhA): sequence comparison and expression in Escherichia coli."; J. Bacteriol. 172:2491-2497(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 31821 / ZM4 / CP4; O'Mullan P.J., Stein D., Chase T. Jr., Eveleigh D.E.; "Mannitol dehydrogenase from Zymomonas mobilis."; Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 31821 / ZM4 / CP4; DOI=10.1038/nbt1045; PubMed=15592456 [NCBI, ExPASy, EBI, Israel, Japan] Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J., Kang H.S.; "The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."; Nat. Biotechnol. 23:63-68(2005).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40. STRAIN=ATCC 31821 / ZM4 / CP4; PubMed=8320209 [NCBI, ExPASy, EBI, Israel, Japan] Yomano L.P., Scopes R.K., Ingram L.O.; "Cloning, sequencing, and expression of the Zymomonas mobilis phosphoglycerate mutase gene (pgm) in Escherichia coli."; J. Bacteriol. 175:3926-3933(1993).
[5]	PROTEIN SEQUENCE OF 1-31. PubMed=2935393 [NCBI, ExPASy, EBI, Israel, Japan] Neale A.D., Scopes R.K., Kelly J.M., Wettenhall R.E.H.; "The two alcohol dehydrogenases of Zymomonas mobilis. Purification by differential dye ligand chromatography, molecular characterisation and physiological roles."; Eur. J. Biochem. 154:119-124(1986).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
ENZYME REGULATION: Inhibited by ethanol.
PATHWAY: Alcohol metabolism; ethanol biosynthesis via fermentation pathway .
SUBUNIT: Multimeric (with different ratios of monomers).
MISCELLANEOUS: In Z.mobilis there are two isozymes of alcohol dehydrogenase.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M32100; AAA27682.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY170008; AAO38758.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008692; AAV89860.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L09650; AAA71935.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35260; A35260.

RefSeq

YP_162971.1; -.

3D structure databases

HSSP

P39462; 1JVB. [HSSP ENTRY / PDB]

ModBase

P20368.

Enzyme and pathway databases

BioCyc

ZMOB264203:ZMO1236-MON; -.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00059; ADH_ZINC; 1.

BLOCKS

P20368.

Genome annotation databases

GeneID

3188393; -.

GenomeReviews

AE008692_GR; ZMO1236.

KEGG

zmo:ZMO1236; -.

NMPDR

fig|264203.3.peg.428; -.

Phylogenomic databases

HOGENOM

P20368; -.

Genome annotation databases

CMR

P20368; ZMO1236.

Other

ProtoNet

P20368.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 337`	`337`	`Alcohol dehydrogenase 1.`	`PRO_0000160750`
`METAL`	`37 37`		`Zinc 1; catalytic (By similarity).`
`METAL`	`58 58`		`Zinc 1; catalytic (By similarity).`
`METAL`	`89 89`		`Zinc 2 (By similarity).`
`METAL`	`92 92`		`Zinc 2 (By similarity).`
`METAL`	`95 95`		`Zinc 2 (By similarity).`
`METAL`	`103 103`		`Zinc 2 (By similarity).`
`METAL`	`145 145`		`Zinc 1; catalytic (By similarity).`
`CONFLICT`	`17 17`		`T -> I (in Ref. 5; AA sequence).`
`CONFLICT`	`26 26`		`E -> F (in Ref. 5; AA sequence).`
`CONFLICT`	`28 28`		`L -> H (in Ref. 5; AA sequence).`
`CONFLICT`	`30 30`		`E -> P (in Ref. 5; AA sequence).`
`CONFLICT`	`76 76`		`V -> A (in Ref. 1; AAA27682).`

Sequence information

Length: 337 AA [This is the length of the unprocessed precursor]

Molecular weight: 36122 Da [This is the MW of the unprocessed precursor]

CRC64: 98D75C912CE1EBE5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKAAVITKDH TIEVKDTKLR PLKYGEALLE MEYCGVCHTD LHVKNGDFGD ETGRITGHEG 

        70         80         90        100        110        120 
IGIVKQVGEG VTSLKVGDRA SVAWFFKGCG HCEYCVSGNE TLCRNVENAG YTVDGAMAEE 

       130        140        150        160        170        180 
CIVVADYSVK VPDGLDPAVA SSITCAGVTT YKAVKVSQIQ PGQWLAIYGL GGLGNLALQY 

       190        200        210        220        230        240 
AKNVFNAKVI AIDVNDEQLA FAKELGADMV INPKNEDAAK IIQEKVGGAH ATVVTAVAKS 

       250        260        270        280        290        300 
AFNSAVEAIR AGGRVVAVGL PPEKMDLSIP RLVLDGIEVL GSLVGTREDL KEAFQFAAEG 

       310        320        330 
KVKPKVTKRK VEEINQIFDE MEHGKFTGRM VVDFTHH

P20368 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools