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Reviewed, UniProtKB/Swiss-Prot P80222 (ADH1_ALLMI)

Last modified September 22, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase 1
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase, major
OrganismAlligator mississippiensis (American alligator)
Taxonomic identifier8496 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Crocodylidae › Alligatorinae › Alligator

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Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalcohol dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 374374Alcohol dehydrogenase 1
PRO_0000160675

Regions

Nucleotide binding199 – 2046NAD By similarity
Nucleotide binding292 – 2943NAD By similarity

Sites

Metal binding461Zinc 1; catalytic By similarity
Metal binding671Zinc 1; catalytic By similarity
Metal binding971Zinc 2 By similarity
Metal binding1001Zinc 2 By similarity
Metal binding1031Zinc 2 By similarity
Metal binding1111Zinc 2 By similarity
Metal binding1741Zinc 1; catalytic By similarity
Binding site2231NAD By similarity
Binding site2281NAD By similarity
Binding site3691NAD By similarity

Amino acid modifications

Modified residue11N-acetylserine

Natural variations

Natural variant1861D → T
Natural variant3171S → T

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Sequences

Sequence LengthMass (Da)Tools
P80222-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 384BCB2D36E2FA32

FASTA37439,670
        10         20         30         40         50         60 
STAGKVIKCK AAITWEIKKP FSIEEIEVAP PKAHEVRIKI LATGICRSDD HVTAGLLTMP 

        70         80         90        100        110        120 
LPMILGHEAA GVVESTGEGV TSLKPGDKVI PLFVPQCGEC MPCLKSNGNL CIRNDLGSPS 

       130        140        150        160        170        180 
GLMADGTSRF TCKGKDIHHF IGTSTFTEYT VVHETAVARI DAAAPLEKVC LIGCGFSTGY 

       190        200        210        220        230        240 
GAAVKDAKVE PGSTCAVFGL GGVGLSTIMG CKAAGASRII GIDINKDKFA KAKELGATEC 

       250        260        270        280        290        300 
INPLDCKKPI QEVLSEMTGG GVDYSFEVIG RIDTMTAALA CCQDNYGTSV IVGVPPASEK 

       310        320        330        340        350        360 
ITFNPMMLFT GRTWKGSVFG GWKSKESVPK LVADYMEKKI NLDGLITHTL PFDKINEGFE 

       370 
LLRTGKSIRS VLTF

« Hide

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References

[1]"Basic features of class-I alcohol dehydrogenase: variable and constant segments coordinated by inter-class and intra-class variability. Conclusions from characterization of the alligator enzyme."
Persson B., Bergman T., Keung W.M., Waldenstroem U., Holmquist B., Vallee B.L., Joernvall H.
Eur. J. Biochem. 216:49-56(1993) [PubMed: 8365416] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.

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Cross-references

Sequence databases

PIRS35669.

3D structure databases

HSSPHSSP built from PDB template 1HEU based on UniProtKB P00327.
SMRP80222. Positions 1-374.
ModBaseSearch...

Phylogenomic databases

HOVERGENP80222.

Enzyme and pathway databases

BRENDA1.1.1.1. 189351.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameADH1_ALLMI
AccessionPrimary (citable) accession number: P80222
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 22, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents