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Protein

Alcohol dehydrogenase class-3

Gene
N/A
Organism
Saara hardwickii (Indian spiny-tailed lizard) (Uromastyx hardwickii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.

Catalytic activityi

An alcohol + NAD+ = an aldehyde or ketone + NADH.
S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi44Zinc 1; catalytic1
Metal bindingi66Zinc 1; catalytic1
Metal bindingi96Zinc 21
Metal bindingi99Zinc 21
Metal bindingi102Zinc 21
Metal bindingi110Zinc 21
Sitei114Important for FDH activity and activation by fatty acidsBy similarity1
Metal bindingi173Zinc 1; catalytic1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandMetal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase class-3 (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase class-III
Glutathione-dependent formaldehyde dehydrogenase (EC:1.1.1.-)
Short name:
FALDH
Short name:
FDH
Short name:
GSH-FDH
S-(hydroxymethyl)glutathione dehydrogenase (EC:1.1.1.284)
OrganismiSaara hardwickii (Indian spiny-tailed lizard) (Uromastyx hardwickii)
Taxonomic identifieri40250 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaIguaniaAcrodontaAgamidaeUromastycinaeSaara

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001607671 – 373Alcohol dehydrogenase class-3Add BLAST373

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP80467.
SMRiP80467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG000195.

Family and domain databases

CDDicd08300. alcohol_DH_class_III. 1 hit.
Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiView protein in InterPro
IPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
PfamiView protein in Pfam
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiView protein in PROSITE
PS00059. ADH_ZINC. 1 hit.

Sequencei

Sequence statusi: Complete.

P80467-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ASGVIKCKAA VAWEAGKPLS IEEIEVAPPK AHEVRVKIIA TAVCHTDAYT
60 70 80 90 100
LSGADPEGSF PVILGHEGAG IVESVGEGVT KFKPGDTVIP LYIPQCGECK
110 120 130 140 150
FCLNPKTNLC QKIRVTQGKG VMPDGTSRFT CKGKQVLHFM GTSTFSEYTV
160 170 180 190 200
VADISLTKIN ASAPLDKVCL LGCGVSTGYG AALNTAKVEP GSTCAVFGLG
210 220 230 240 250
GVGLAVIMGC KVAGASRIIG IDLNKDKFAK AKEFGATECI SPADFKKPIQ
260 270 280 290 300
EVLIEMTDGG VDYSFECIGN VGVMRAALEA CHKGWGVSVI VGVAAAGQEI
310 320 330 340 350
ATRPFQLVTG RTWKGTAFGG WKSVESVPKL VDEYMSKKMK VDEFVTHTLP
360 370
FEQINEAFEL MHAGKSIRSV LKF
Length:373
Mass (Da):39,430
Last modified:February 1, 1996 - v1
Checksum:i2BB3B44A0A9FCF06
GO

Sequence databases

PIRiS68061.

Cross-referencesi

Sequence databases

PIRiS68061.

3D structure databases

ProteinModelPortaliP80467.
SMRiP80467.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000195.

Family and domain databases

CDDicd08300. alcohol_DH_class_III. 1 hit.
Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiView protein in InterPro
IPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
PfamiView protein in Pfam
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiView protein in PROSITE
PS00059. ADH_ZINC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiADHX_SAAHA
AccessioniPrimary (citable) accession number: P80467
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: March 15, 2017
This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.