ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P33744


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ADHE_CLOAB
Primary accession number P33744
Secondary accession numbers Q45808 Q45809
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on August 29, 2001 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 60)
Name and origin of the protein
Protein name Aldehyde-alcohol dehydrogenase
Synonyms None
Includes Alcohol dehydrogenase
     (ADH)
     (EC 1.1.1.1)
Acetaldehyde dehydrogenase [acetylating]
     (ACDH)
     (EC 1.2.1.10)
Gene name
Name: adhE
Synonyms: aad
OrderedLocusNames: CA_P0162
From
Clostridium acetobutylicum [TaxID: 1488] [HAMAP proteome]
Encoded on Plasmid pSOL1.
Taxonomy Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; Clostridium.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=8226639 [NCBI, ExPASy, EBI, Israel, Japan]
Fischer R.J., Helms J., Duerre P.;
"Cloning, sequencing, and molecular analysis of the sol operon of Clostridium acetobutylicum, a chromosomal locus involved in solventogenesis.";
J. Bacteriol. 175:6959-6969(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=8300540 [NCBI, ExPASy, EBI, Israel, Japan]
Nair R.V., Bennett G.N., Papoutsakis E.T.;
"Molecular characterization of an aldehyde/alcohol dehydrogenase gene from Clostridium acetobutylicum ATCC 824.";
J. Bacteriol. 176:871-885(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
DOI=10.1128/JB.183.16.4823-4838.2001; PubMed=11466286 [NCBI, ExPASy, EBI, Israel, Japan]
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.;
"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum.";
J. Bacteriol. 183:4823-4838(2001).
Comments
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
X72831; CAA51344.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L14817; AAD04638.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE001438; AAK76907.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A49346; A49346.
RefSeq NP_149325.1; -.
3D structure databases
ModBase P33744.
Enzyme and pathway databases
BioCyc CACE272562:CAP0162-MON; -.
Ontologies
GO
GO:0008774; Molecular function: acetaldehyde dehydrogenase (acetylating) activity (inferred from electronic annotation from InterPro).
GO:0004022; Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0046872; Molecular function: metal ion binding (inferred from electronic annotation from InterPro).
GO:0015976; Biological process: carbon utilization (inferred from electronic annotation from InterPro).
GO:0006066; Biological process: cellular alcohol metabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016162; Ald_DHase_N.
IPR012079; Bifunc_Ald/AlcDHase.
IPR001670; Fe_AlcDHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
Pfam PF00465; Fe-ADH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000111; ALDH_ADH; 1.
PROSITE PS00913; ADH_IRON_1; 1.
PS00060; ADH_IRON_2; FALSE_NEG.
ProtoNet P33744.
Genome annotation databases
GeneID 1116167; -.
GenomeReviews AE001438_GR; CA_P0162.
KEGG cac:CA_P0162; -.
NMPDR fig|272562.1.peg.160; -.
Phylogenomic databases
HOGENOM P33744; -.
Genome annotation databases
CMR P33744; CA_P0162.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Multifunctional enzyme; NAD; Oxidoreductase; Plasmid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   862  862     Aldehyde-alcohol dehydrogenase. PRO_0000087839
NP_BIND   420   425  6     NAD (Potential). 
ACT_SITE   244   244        By similarity. 
Sequence information
Length: 862 AA [This is the length of the unprocessed precursor] Molecular weight: 95321 Da [This is the MW of the unprocessed precursor] CRC64: BE09E32B28DD08B0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKVTTVKELD EKLKVIKEAQ KKFSCYSQEM VDEIFRNAAM AAIDARIELA KAAVLETGMG 

        70         80         90        100        110        120 
LVEDKVIKNH FAGEYIYNKY KDEKTCGIIE RNEPYGITKI AEPIGVVAAI IPVTNPTSTT 

       130        140        150        160        170        180 
IFKSLISLKT RNGIFFSPHP RAKKSTILAA KTILDAAVKS GAPENIIGWI DEPSIELTQY 

       190        200        210        220        230        240 
LMQKADITLA TGGPSLVKSA YSSGKPAIGV GPGNTPVIID ESAHIKMAVS SIILSKTYDN 

       250        260        270        280        290        300 
GVICASEQSV IVLKSIYNKV KDEFQERGAY IIKKNELDKV REVIFKDGSV NPKIVGQSAY 

       310        320        330        340        350        360 
TIAAMAGIKV PKTTRILIGE VTSLGEEEPF AHEKLSPVLA MYEADNFDDA LKKAVTLINL 

       370        380        390        400        410        420 
GGLGHTSGIY ADEIKARDKI DRFSSAMKTV RTFVNIPTSQ GASGDLYNFR IPPSFTLGCG 

       430        440        450        460        470        480 
FWGGNSVSEN VGPKHLLNIK TVAERRENML WFRVPHKVYF KFGCLQFALK DLKDLKKKRA 

       490        500        510        520        530        540 
FIVTDSDPYN LNYVDSIIKI LEHLDIDFKV FNKVGREADL KTIKKATEEM SSFMPDTIIA 

       550        560        570        580        590        600 
LGGTPEMSSA KLMWVLYEHP EVKFEDLAIK FMDIRKRIYT FPKLGKKAML VAITTSAGSG 

       610        620        630        640        650        660 
SEVTPFALVT DNNTGNKYML ADYEMTPNMA IVDAELMMKM PKGLTAYSGI DALVNSIEAY 

       670        680        690        700        710        720 
TSVYASEYTN GLALEAIRLI FKYLPEAYKN GRTNEKAREK MAHASTMAGM ASANAFLGLC 

       730        740        750        760        770        780 
HSMAIKLSSE HNIPSGIANA LLIEEVIKFN AVDNPVKQAP CPQYKYPNTI FRYARIADYI 

       790        800        810        820        830        840 
KLGGNTDEEK VDLLINKIHE LKKALNIPTS IKDAGVLEEN FYSSLDRISE LALDDQCTGA 

       850        860 
NPRFPLTSEI KEMYINCFKK QP 

P33744 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!