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Reviewed, UniProtKB/Swiss-Prot P25406 (ADH1B_UROHA)

Last modified June 16, 2009. Version 56. 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 1B
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase I-B
      Short name=ADH IB
OrganismUromastyx hardwickii (Indian spiny-tailed lizard)
Taxonomic identifier40250 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Iguania › Acrodonta › Agamidae › Uromastycinae › Uromastyx

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Protein attributes

Sequence length375 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.

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.

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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 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 – 375375Alcohol dehydrogenase 1B
PRO_0000160678

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-acetylserine Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P25406-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 392071E594C32E0D

FASTA37540,060
        10         20         30         40         50         60 
STAGKVIKCK AAVVWEPKKP FSIVEIEVAP PKAHEVRIKI LASGICRSDD HVLSGALKVN 

        70         80         90        100        110        120 
FPIILGHEAA GVVESVGEGV TSMKPGDKVI PIFLPQCGEC NSCRHPRGNV CKKSELGPFT 

       130        140        150        160        170        180 
GLLYDGTSRF TYQGKPVYHF VRTGTFTEYT VAPEDSVVKI DASAPLEKVC LIGCGFSTGY 

       190        200        210        220        230        240 
GAAINSAKVQ PGSTCAVFGL GGVGLSAVMG CKAAGASRII GIDINKEKFP KAKELGATEC 

       250        260        270        280        290        300 
VNPLDYKKPI NEVLFDMTDG EGVEYSFEVI GRTDTMTAAL ASCHNNYGTS VIVGVPPSAS 

       310        320        330        340        350        360 
QIAFDPLLLF TGRTWKGSVF GGWKSKDAVP RLVSDFMGKK FILDPLITHT MPFEKINEGF 

       370 
ELLRSGKSIR TVLTF

« Hide

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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.

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Cross-references

Sequence databases

PIRS62639.

3D structure databases

HSSPHSSP built from PDB template 1HT0 based on UniProtKB P00326.
SMRP25406. Positions 1-375.
ModBaseSearch...

Phylogenomic databases

HOVERGENP25406.

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...

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Entry information

Entry nameADH1B_UROHA
AccessionPrimary (citable) accession number: P25406
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 56 of the entry and version 2 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