NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29342 / M129;
DOI=10.1093/nar/24.22.4420; PubMed=8948633 [NCBI, ExPASy, EBI, Israel, Japan]
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae.";
Nucleic Acids Res. 24:4420-4449(1996).

Comments

CATALYTIC ACTIVITY: An alcohol + NADP⁺ = an aldehyde + NADPH.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
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

U00089; AAB95926.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S73604; S73604.

RefSeq

NP_110253.1; -.

3D structure databases

HSSP

P14941; 1YKF. [HSSP ENTRY / PDB]

ModBase

P75214.

Enzyme and pathway databases

BioCyc

MPNE272634:MPN564-MON; -.

Ontologies

GO:0008106;	Molecular function: alcohol dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.

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.

ProtoNet

P75214.

Genome annotation databases

GeneID

876853; -.

GenomeReviews

U00089_GR; MPN_564.

KEGG

mpn:MPN564; -.

Phylogenomic databases

HOGENOM

P75214; -.

Genome annotation databases

CMR

P75214; MPN_564.

Other

UniRef

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

Keywords

Complete proteome; Metal-binding; NADP; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 351`	`351`	`Probable NADP-dependent alcohol dehydrogenase.`	`PRO_0000160746`
`METAL`	`37 37`		`Zinc; catalytic (By similarity).`
`METAL`	`59 59`		`Zinc; catalytic (By similarity).`
`METAL`	`60 60`		`Zinc; catalytic (By similarity).`
`METAL`	`150 150`		`Zinc; catalytic (By similarity).`

Sequence information

Length: 351 AA [This is the length of the unprocessed precursor]

Molecular weight: 37812 Da [This is the MW of the unprocessed precursor]

CRC64: 3153B93BFFE64D2C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKAYAMLKIG ATGWIEKPRP VCGPNDAIIR PLAVAPCTSD VHTVWEGGIG ERHNMVLGHE 

        70         80         90        100        110        120 
GCGVVDEVGS EVKSFKVGDR VLVAAITPEW NSVNAQAGYP MHSGGMLGGW KFSNVKDGMF 

       130        140        150        160        170        180 
AEYFHVNDAE GNLALMPEGM DLADACMLSD MIPTGFHANE LADIQYGVAL SFFCAGPVGL 

       190        200        210        220        230        240 
MAIAGAALKG AGRIIVVDSR PDIVEIAKAY GATDYIDFKK VSVVDEILKW TNNEGVEKVL 

       250        260        270        280        290        300 
ISGGGSTILE TAIKVLRPGG KIGNVNYFGA GEFLTIPRVE WGVGMAHKAI HGGLMLGGRL 

       310        320        330        340        350 
RLEKLARLIM TKKLDPSKMI THRFKGFEHI EEALFLMKDK PKDLIKSVVI F

P75214 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