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Protein

Alcohol dehydrogenase class-3

Gene

ADH5

Organism
Equus caballus (Horse)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Zinc 1; catalytic
Metal bindingi67 – 671Zinc 1; catalytic
Metal bindingi97 – 971Zinc 2
Metal bindingi100 – 1001Zinc 2
Metal bindingi103 – 1031Zinc 2
Metal bindingi111 – 1111Zinc 2
Sitei115 – 1151Important for FDH activity and activation by fatty acidsBy similarity
Metal bindingi174 – 1741Zinc 1; catalytic

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase class-3 (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase 5
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)
Gene namesi
Name:ADH5
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 374373Alcohol dehydrogenase class-3PRO_0000160758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei233 – 2331N6-succinyllysineBy similarity
Modified residuei247 – 2471PhosphoserineBy similarity
Modified residuei315 – 3151N6-succinyllysineBy similarity
Modified residuei324 – 3241PhosphoserineBy similarity
Modified residuei351 – 3511PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PeptideAtlasiP19854.
PRIDEiP19854.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP19854.
SMRiP19854. Positions 4-374.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG000195.
InParanoidiP19854.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19854-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAEVIKCKA AVAWEAGKPV SIEEVEVAPP KAHEVRIKII ATAVCHTDAY
60 70 80 90 100
TLSGADPEGS FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC
110 120 130 140 150
KFCLNPQTNL CQKIRTTQGK GLMPDGTSRF TCKGKTILHY MGTSTFSEYT
160 170 180 190 200
VVADISVAKI DPLAPLDKVC LLGCGVSTGY GAAVNTAKVE PGSTCAIFGL
210 220 230 240 250
GGVGLAVIMG CKVAGASRII GVDINKDKFA KAKEFGASEC INPQDFSKPI
260 270 280 290 300
QEVLIEMTDG GVDYSFECIG NVKVMRAALE ACHKGWGVSV VVGVAASGEE
310 320 330 340 350
IATRPFQLVT GRTWKGTAFG GWKSVESIPK LVSEYMSKKI KVDEFVTHSL
360 370
SFDQINEAFE LMHAGKSIRT VVKL
Length:374
Mass (Da):39,572
Last modified:April 3, 2007 - v2
Checksum:i190D38896ED9D094
GO

Sequence databases

PIRiA33419.
S02617.

Cross-referencesi

Sequence databases

PIRiA33419.
S02617.

3D structure databases

ProteinModelPortaliP19854.
SMRiP19854. Positions 4-374.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PeptideAtlasiP19854.
PRIDEiP19854.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000195.
InParanoidiP19854.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characteristics of mammalian class III alcohol dehydrogenases, an enzyme less variable than the traditional liver enzyme of class I."
    Kaiser R., Holmquist B., Vallee B.L., Joernvall H.
    Biochemistry 28:8432-8438(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-374, ACETYLATION AT SER-2.
  2. "Acetylated N-terminal structures of class III alcohol dehydrogenases. Differences among the three enzyme classes."
    Fairwell T., Julia P., Kaiser R., Holmquist B., Pares X., Vallee B.L., Joernvall H.
    FEBS Lett. 222:99-103(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-7, ACETYLATION AT SER-2.

Entry informationi

Entry nameiADHX_HORSE
AccessioniPrimary (citable) accession number: P19854
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: April 3, 2007
Last modified: July 6, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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.