Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P25405 (ADH1A_UROHA)

Last modified June 16, 2009. Version 58. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase 1A
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase I-A
      Short name=ADH IA
OrganismUromastyx hardwickii (Indian spiny-tailed lizard)
Taxonomic identifier40250 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Iguania › Acrodonta › Agamidae › Uromastycinae › Uromastyx

Hide | Top

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Multimeric (with different ratios of monomers).

Subcellular location

Cytoplasm.

Miscellaneous

In U.hardwickii there are two isozymes of alcohol dehydrogenase I.

Sequence similarities

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

Hide | Top

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 activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Alcohol dehydrogenase 1A
PRO_0000160677

Regions

Nucleotide binding199 – 2046NAD By similarity
Nucleotide binding293 – 2953NAD 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 site3701NAD By similarity

Amino acid modifications

Modified residue11N-acetylglycine Ref.1

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P25405-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: F315BB777996D906

FASTA37539,663
        10         20         30         40         50         60 
GTAGKVIKCK AAIAWEIKKP LSIEQIEVAP PKAHEVRIKI LATGICRSDD HVISGAFKMP 

        70         80         90        100        110        120 
LPMVLGHEAA GVVESVGEGV TCVKPGDKVI PLFVPQCGKC SSCRSTRGNL CTSNDLSAAT 

       130        140        150        160        170        180 
GLMPDGTSRF TCKGKSLHHF ISTSSFTEYT VVHENSVVKI DAAAPLEKVC LIGCGFSTGY 

       190        200        210        220        230        240 
GAAVETAKVE PGSTCAVFGL GGVGLSAVMG CKAAGASRII GVDINKDKFP KAKEMGATEC 

       250        260        270        280        290        300 
VNPLDYKKPI NEVLFDLTGG EGVDYSFEVI GRTDTMTAAL ASCHMDYGTS IIVGLPPSAS 

       310        320        330        340        350        360 
EITFSPGLIF TGRTWKGSVF GGWKSKDSVP RLVSDFMQKK FSLDPLITHT MPFDKINEGF 

       370 
ELLRAGKSIR SVLLF

« Hide

Hide | Top

References

[1]"Linking of isozyme and class variability patterns in the emergence of novel alcohol dehydrogenase functions. Characterization of isozymes in Uromastix hardwickii."
Hjelmqvist L., Shafqat J., Siddiqi A.R., Joernvall H.
Eur. J. Biochem. 236:563-570(1996) [PubMed: 8612630] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Reptilian alcohol dehydrogenase. Heterogeneity relevant to class multiplicity of the mammalian enzyme."
Hjelmqvist L., Ericsson M., Shafqat J., Carlquist M., Siddiqi A.R., Hoeoeg J.-O., Joernvall H.
FEBS Lett. 298:297-300(1992) [PubMed: 1544464] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-18.
Tissue: Liver.

Hide | Top

Cross-references

Sequence databases

PIRS62638.

3D structure databases

HSSPHSSP built from PDB template 1EE2 based on UniProtKB P00328.
SMRP25405. Positions 2-375.
ModBaseSearch...

Phylogenomic databases

HOVERGENP25405.

Enzyme and pathway databases

BRENDA1.1.1.1. 189323.

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...

Hide | Top

Entry information

Entry nameADH1A_UROHA
AccessionPrimary (citable) accession number: P25405
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Hide | Top

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