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Protein

Alcohol dehydrogenase 1

Gene
N/A
Organism
Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi46Zinc 1; catalytic1
Metal bindingi68Zinc 1; catalytic1
Metal bindingi98Zinc 21
Metal bindingi101Zinc 21
Metal bindingi104Zinc 21
Metal bindingi112Zinc 21
Metal bindingi175Zinc 1; catalytic1
Binding sitei224NAD1
Binding sitei229NAD1
Binding sitei369NAD1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi200 – 205NAD6
Nucleotide bindingi293 – 295NAD3

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase 1 (EC:1.1.1.1)
OrganismiGadus morhua subsp. callarias (Baltic cod) (Gadus callarias)
Taxonomic identifieri8053 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataZeiogadariaGadariaeGadiformesGadoideiGadidaeGadus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001606791 – 375Alcohol dehydrogenase 1Add BLAST375

Amino acid modifications

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

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1375
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 14Combined sources8
Beta strandi22 – 28Combined sources7
Beta strandi35 – 44Combined sources10
Helixi47 – 54Combined sources8
Beta strandi63 – 65Combined sources3
Beta strandi70 – 77Combined sources8
Beta strandi89 – 92Combined sources4
Beta strandi99 – 101Combined sources3
Helixi102 – 105Combined sources4
Helixi116 – 118Combined sources3
Turni121 – 124Combined sources4
Beta strandi131 – 133Combined sources3
Beta strandi136 – 140Combined sources5
Helixi141 – 143Combined sources3
Beta strandi147 – 154Combined sources8
Helixi155 – 157Combined sources3
Beta strandi158 – 160Combined sources3
Helixi167 – 170Combined sources4
Helixi171 – 174Combined sources4
Helixi176 – 185Combined sources10
Turni186 – 188Combined sources3
Beta strandi195 – 199Combined sources5
Helixi203 – 214Combined sources12
Beta strandi218 – 223Combined sources6
Helixi227 – 229Combined sources3
Helixi230 – 235Combined sources6
Beta strandi240 – 242Combined sources3
Helixi244 – 246Combined sources3
Helixi251 – 259Combined sources9
Beta strandi263 – 268Combined sources6
Helixi273 – 281Combined sources9
Turni285 – 287Combined sources3
Beta strandi289 – 292Combined sources4
Beta strandi297 – 299Combined sources3
Beta strandi301 – 303Combined sources3
Helixi305 – 309Combined sources5
Beta strandi313 – 316Combined sources4
Helixi319 – 321Combined sources3
Helixi324 – 336Combined sources13
Helixi343 – 345Combined sources3
Beta strandi346 – 351Combined sources6
Helixi352 – 354Combined sources3
Helixi355 – 363Combined sources9
Beta strandi368 – 373Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CDOX-ray2.05A/B1-374[»]
ProteinModelPortaliP26325.
SMRiP26325.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26325.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG000195.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26325-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ATVGKVIKCK AAVAWEANKP LVIEEIEVDV PHANEIRIKI IATGVCHTDL
60 70 80 90 100
YHLFEGKHKD GFPVVLGHEG AGIVESVGPG VTEFQPGEKV IPLFISQCGE
110 120 130 140 150
CRFCQSPKTN QCVKGWANES PDVMSPKETR FTCKGRKVLQ FLGTSTFSQY
160 170 180 190 200
TVVNQIAVAK IDPSAPLDTV CLLGCGVSTG FGAAVNTAKV EPGSTCAVFG
210 220 230 240 250
LGAVGLAAVM GCHSAGAKRI IAVDLNPDKF EKAKVFGATD FVNPNDHSEP
260 270 280 290 300
ISQVLSKMTN GGVDFSLECV GNVGVMRNAL ESCLKGWGVS VLVGWTDLHD
310 320 330 340 350
VATRPIQLIA GRTWKGSMFG GFKGKDGVPK MVKAYLDKKV KLDEFITHRM
360 370
PLESVNDAID LMKHGKCIRT VLSLE
Length:375
Mass (Da):40,128
Last modified:May 1, 1992 - v1
Checksum:i0A8BDEAA0C9BCEAD
GO

Sequence databases

PIRiA42343.

Cross-referencesi

Sequence databases

PIRiA42343.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CDOX-ray2.05A/B1-374[»]
ProteinModelPortaliP26325.
SMRiP26325.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000195.

Miscellaneous databases

EvolutionaryTraceiP26325.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADH1_GADMC
AccessioniPrimary (citable) accession number: P26325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 2, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Functionally related to class-I mammalian enzymes, but structurally related to class-III.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.