[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[3]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-387 IN COMPLEX WITH ZINC IONS AND NADP, FUNCTION, AND SUBUNIT. DOI=10.1016/j.jmb.2004.07.034; PubMed=15327949 [NCBI, ExPASy, EBI, Israel, Japan] Sulzenbacher G., Alvarez K., Van Den Heuvel R.H., Versluis C., Spinelli S., Campanacci V., Valencia C., Cambillau C., Eklund H., Tegoni M.; "Crystal structure of E.coli alcohol dehydrogenase YqhD: evidence of a covalently modified NADP coenzyme."; J. Mol. Biol. 342:489-502(2004).

Comments

FUNCTION: NADP-dependent ADH activity.
CATALYTIC ACTIVITY: An alcohol + NADP⁺ = an aldehyde + NADPH.
COFACTOR: Binds 1 zinc ion per subunit.
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the iron-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

U28377; AAA69178.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76047.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77068.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A65088; A65088.

RefSeq

AP_003562.1; -.
NP_417484.1; -.

3D structure databases

PDB

1OJ7; X-ray; 2.00 A; A/B/C/D=2-387.

[ExPASy / RCSB / EBI]

PDBsum

1OJ7; -.

ModBase

Q46856.

Protein-protein interaction databases

IntAct

Q46856; -.

Enzyme and pathway databases

BioCyc

EcoCyc:G7564-MON; -.

Organism-specific databases

EchoBASE

EB2834; -.

EcoGene

EG13014; yqhD.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001670; Fe_AlcDHase.
Graphical view of domain structure.

Pfam

PF00465; Fe-ADH; 1.
Pfam graphical view of domain structure.

PROSITE

PS00913; ADH_IRON_1; 1.
PS00060; ADH_IRON_2; 1.

BLOCKS

Q46856.

Genome annotation databases

GeneID

947493; -.

GenomeReviews

U00096_GR; b3011.
AP009048_GR; JW2978.

KEGG

ecj:JW2978; -.
eco:b3011; -.

Phylogenomic databases

HOGENOM

Q46856; -.

Genome annotation databases

CMR

Q46856; b3011.

Other

ProtoNet

Q46856.

UniRef

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

Keywords

3D-structure; Complete proteome; Metal-binding; NADP; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 387`	`387`	`Alcohol dehydrogenase yqhD.`	`PRO_0000087832`
`NP_BIND`	`38 40`	`3`	`NADP.`
`NP_BIND`	`93 99`	`7`	`NADP.`
`NP_BIND`	`179 182`	`4`	`NADP.`
`METAL`	`194 194`		`Zinc (catalytic).`
`METAL`	`198 198`		`Zinc (catalytic).`
`METAL`	`267 267`		`Zinc (catalytic).`
`METAL`	`281 281`		`Zinc (catalytic).`
`BINDING`	`138 138`		`NADP.`
`BINDING`	`147 147`		`NADP.`
`BINDING`	`160 160`		`NADP.`
`STRAND`	`4 15`	`12`
`HELIX`	`18 21`	`4`
`HELIX`	`22 25`	`4`
`STRAND`	`31 36`	`6`
`HELIX`	`40 44`	`5`
`HELIX`	`46 53`	`8`
`TURN`	`54 56`	`3`
`STRAND`	`57 62`	`6`
`HELIX`	`71 84`	`14`
`STRAND`	`88 94`	`7`
`HELIX`	`95 107`	`13`
`HELIX`	`118 121`	`4`
`TURN`	`122 126`	`5`
`STRAND`	`133 139`	`7`
`HELIX`	`144 146`	`3`
`STRAND`	`147 154`	`8`
`TURN`	`155 158`	`4`
`STRAND`	`159 164`	`6`
`HELIX`	`166 168`	`3`
`STRAND`	`171 175`	`5`
`HELIX`	`177 180`	`4`
`HELIX`	`185 203`	`19`
`STRAND`	`204 206`	`3`
`HELIX`	`211 233`	`23`
`HELIX`	`238 251`	`14`
`STRAND`	`252 254`	`3`
`TURN`	`255 259`	`5`
`HELIX`	`265 277`	`13`
`HELIX`	`281 295`	`15`
`TURN`	`296 300`	`5`
`HELIX`	`301 312`	`12`
`HELIX`	`319 336`	`18`
`HELIX`	`343 346`	`4`
`HELIX`	`353 362`	`10`
`STRAND`	`366 368`	`3`
`TURN`	`369 372`	`4`
`HELIX`	`376 385`	`10`

Sequence information

Length: 387 AA [This is the length of the unprocessed precursor]

Molecular weight: 42097 Da [This is the MW of the unprocessed precursor]

CRC64: 448A7610787D2146 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNNFNLHTPT RILFGKGAIA GLREQIPHDA RVLITYGGGS VKKTGVLDQV LDALKGMDVL 

        70         80         90        100        110        120 
EFGGIEPNPA YETLMNAVKL VREQKVTFLL AVGGGSVLDG TKFIAAAANY PENIDPWHIL 

       130        140        150        160        170        180 
QTGGKEIKSA IPMGCVLTLP ATGSESNAGA VISRKTTGDK QAFHSAHVQP VFAVLDPVYT 

       190        200        210        220        230        240 
YTLPPRQVAN GVVDAFVHTV EQYVTKPVDA KIQDRFAEGI LLTLIEDGPK ALKEPENYDV 

       250        260        270        280        290        300 
RANVMWAATQ ALNGLIGAGV PQDWATHMLG HELTAMHGLD HAQTLAIVLP ALWNEKRDTK 

       310        320        330        340        350        360 
RAKLLQYAER VWNITEGSDD ERIDAAIAAT RNFFEQLGVP THLSDYGLDG SSIPALLKKL 

       370        380 
EEHGMTQLGE NHDITLDVSR RIYEAAR

Q46856 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