Reviewed, UniProtKB/Swiss-Prot Q9P6C8 (ADH1_NEUCR)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase 1
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase I

Gene names

Name:	adh-1
ORF Names:	B17C10.210, NCU01754

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alcohol dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 353	353	Alcohol dehydrogenase 1		PRO_0000160726
Regions
	Nucleotide binding	181 – 187	7	NAD By similarity
	Nucleotide binding	274 – 276	3	NAD By similarity
Sites
	Metal binding	47	1	Zinc 1; catalytic By similarity
	Metal binding	70	1	Zinc 1; catalytic By similarity
	Metal binding	101	1	Zinc 2 By similarity
	Metal binding	104	1	Zinc 2 By similarity
	Metal binding	107	1	Zinc 2 By similarity
	Metal binding	115	1	Zinc 2 By similarity
	Metal binding	157	1	Zinc 1; catalytic By similarity
	Binding site	205	1	NAD By similarity
	Binding site	210	1	NAD By similarity
	Binding site	346	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9P6C8-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 66B71D891324C854	FASTA	353	37,443
	10 20 30 40 50 60 MPQFEIPEQQ WAQVVEKKGG PVVFKQIPVQ KPGPDEVLIN VKYSGVCHTD LHAMKGDWPL 70 80 90 100 110 120 ATKMPLVGGH EGAGVVVAKG ELVTEVEVGD HAGIKWLNGS CLACSFCMQA DEPLCPHALL 130 140 150 160 170 180 SGYTVDGSFQ QYAIAKAAHV AKIPKGCDLE TTAPVLCAGI TVYKGLKESG VRPGQCVAIV 190 200 210 220 230 240 GAGGGLGSMA IQYANAMGLH AIAIDGGEEK GKNCRELGAQ AYVDFTTTKD LVADVKAATP 250 260 270 280 290 300 DGLGPHAVIL LAVSEKPFHQ AVDYVRSRGT IICIGLPAGA KFQAPVFDTV IRMITIKGSY 310 320 330 340 350 VGNRQDTQEA LDFFARGLIK VPIKTVGLSK LQEVYDLMEE GKIVGRYVVD TSK

References

[1]

"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence." Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U. Nucleic Acids Res. 31:1944-1954(2003) [PubMed: 12655011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

[2]

"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL355926 Genomic DNA. Translation: CAB91241.1. AABX02000005 Genomic DNA. Translation: EAA27941.1.
PIR	T49440.
RefSeq	XP_957177.1.
3D structure databases
SMR	Q9P6C8. Positions 5-353.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9P6C8.
Genome annotation databases
GeneID	3873329.
KEGG	ncr:NCU01754.
NMPDR	fig|5141.1.peg.6126.
Phylogenomic databases
eggNOG	fuNOG04605.
OrthoDB	EOG95HTDV.
PhylomeDB	Q9P6C8.
Enzyme and pathway databases
BioCyc	NCRA-XX3-01:NCRA-XX3-01-005464-MONOMER.
BRENDA	1.1.1.1. 266.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [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...

Entry information

Entry name

ADH1_NEUCR

Accession

Primary (citable) accession number: Q9P6C8
Secondary accession number(s): Q7RV68

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	October 1, 2000
Last modified:	January 19, 2010
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)