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Protein

Alcohol dehydrogenase class-3

Gene
N/A
Organism
Sparus aurata (Gilthead sea bream)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.By similarity

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi47Zinc 1; catalyticBy similarity1
Metal bindingi69Zinc 1; catalyticBy similarity1
Metal bindingi99Zinc 2By similarity1
Metal bindingi102Zinc 2By similarity1
Metal bindingi105Zinc 2By similarity1
Metal bindingi113Zinc 2By similarity1
Sitei117Important for FDH activity and activation by fatty acidsBy similarity1
Metal bindingi176Zinc 1; catalyticBy similarity1

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)
OrganismiSparus aurata (Gilthead sea bream)
Taxonomic identifieri8175 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataEupercariaSpariformesSparidaeSparus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001607661 – 376Alcohol dehydrogenase class-3Add BLAST376

Expressioni

Tissue specificityi

Expressed in the skeletal muscle, heart, gill filaments and liver, with highest levels in the kidney.

Developmental stagei

Found in the eggs and in embryos 4, 8 and 12 hours after fertlization, as well as on all days post-hatching. Level of expression decreases during embryonal development but increases 4-fold from day 1 to day 21 after hatching.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP79896.
SMRiP79896.
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.

P79896-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METAGKVIKC KAAVAWEPGK PLSIEEVEVA PPNAHEVRIK LFATGVCHTD
60 70 80 90 100
AYTLSGSDPE GLFPVILGHE GAGTVESVGE GVTKFKPGDT VIPLYVPQCG
110 120 130 140 150
ECKFCKNPKT NLCQKIRITQ GQGLLPDKTS RFTCKGKQVF HFMGTSTFSE
160 170 180 190 200
YTVVADISLA KVNEKAPMDK VCLLGCGIST GYGAALNTAK VEPGSTCAVF
210 220 230 240 250
GLGAVGLAVI MGCKVAGATR IIGIDLNPAK FETAKEFGAT EFVNPKDHSK
260 270 280 290 300
PIQEVLVEMT DGGVDYSFEC IGNVQIMRAA LEACHKGWGE SVIIGVAGAG
310 320 330 340 350
QEISTRPFQL VTGRVWKGTA FGGWKSVESV PKLVEDYMSK KLKVDEFVTH
360 370
TLPFEKINEG FELMHAGKSI RTVLTF
Length:376
Mass (Da):40,215
Last modified:May 1, 1997 - v1
Checksum:i306F27117F3F2313
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84791 mRNA. Translation: AAB41888.1.
PIRiJC4967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84791 mRNA. Translation: AAB41888.1.
PIRiJC4967.

3D structure databases

ProteinModelPortaliP79896.
SMRiP79896.
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_SPAAU
AccessioniPrimary (citable) accession number: P79896
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1997
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

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.