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Protein

Alcohol dehydrogenase 2

Gene

adhB

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
LigandIron, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase 2 (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase II
Short name:
ADH II
Gene namesi
Name:adhB
Ordered Locus Names:ZMO1596
OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Taxonomic identifieri264203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
Proteomesi
  • UP000001173 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000878152 – 383Alcohol dehydrogenase 2Add BLAST382

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1383
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi10 – 15Combined sources6
Helixi18 – 24Combined sources7
Turni25 – 28Combined sources4
Beta strandi33 – 39Combined sources7
Helixi40 – 44Combined sources5
Helixi47 – 56Combined sources10
Turni57 – 59Combined sources3
Beta strandi61 – 68Combined sources8
Helixi74 – 86Combined sources13
Beta strandi90 – 97Combined sources8
Helixi98 – 112Combined sources15
Helixi117 – 120Combined sources4
Beta strandi122 – 124Combined sources3
Beta strandi133 – 137Combined sources5
Beta strandi139 – 141Combined sources3
Turni144 – 146Combined sources3
Beta strandi148 – 154Combined sources7
Turni155 – 158Combined sources4
Beta strandi159 – 164Combined sources6
Helixi166 – 168Combined sources3
Beta strandi171 – 175Combined sources5
Helixi177 – 179Combined sources3
Turni180 – 182Combined sources3
Helixi185 – 204Combined sources20
Helixi210 – 232Combined sources23
Helixi237 – 257Combined sources21
Helixi261 – 272Combined sources12
Helixi277 – 306Combined sources30
Helixi316 – 333Combined sources18
Beta strandi338 – 340Combined sources3
Turni341 – 344Combined sources4
Helixi347 – 349Combined sources3
Helixi350 – 357Combined sources8
Helixi361 – 365Combined sources5
Helixi372 – 381Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OWOX-ray2.07A/B/C/D1-383[»]
3OX4X-ray2.00A/B/C/D1-383[»]
ProteinModelPortaliP0DJA2.
SMRiP0DJA2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0DJA2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK13954.
OMAiIPTVNLM.

Family and domain databases

InterProiView protein in InterPro
IPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
PfamiView protein in Pfam
PF00465. Fe-ADH. 1 hit.
PROSITEiView protein in PROSITE
PS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0DJA2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSTFYIPF VNEMGEGSLE KAIKDLNGSG FKNALIVSDA FMNKSGVVKQ
60 70 80 90 100
VADLLKAQGI NSAVYDGVMP NPTVTAVLEG LKILKDNNSD FVISLGGGSP
110 120 130 140 150
HDCAKAIALV ATNGGEVKDY EGIDKSKKPA LPLMSINTTA GTASEMTRFC
160 170 180 190 200
IITDEVRHVK MAIVDRHVTP MVSVNDPLLM VGMPKGLTAA TGMDALTHAF
210 220 230 240 250
EAYSSTAATP ITDACALKAA SMIAKNLKTA CDNGKDMPAR EAMAYAQFLA
260 270 280 290 300
GMAFNNASLG YVHAMAHQLG GYYNLPHGVC NAVLLPHVLA YNASVVAGRL
310 320 330 340 350
KDVGVAMGLD IANLGDKEGA EATIQAVRDL AASIGIPANL TELGAKKEDV
360 370 380
PLLADHALKD ACALTNPRQG DQKEVEELFL SAF
Length:383
Mass (Da):40,145
Last modified:December 14, 2011 - v1
Checksum:iE1C3A159B1652342
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38S → G AA sequence (PubMed:2935393).Curated1
Sequence conflicti45 – 48SGVV → GVS AA sequence (PubMed:2935393).Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15394 Genomic DNA. Translation: AAA27683.1.
AE008692 Genomic DNA. Translation: AAV90220.1.
PIRiA25978.
RefSeqiWP_000168720.1. NC_006526.2.

Genome annotation databases

EnsemblBacteriaiAAV90220; AAV90220; ZMO1596.
KEGGizmo:ZMO1596.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15394 Genomic DNA. Translation: AAA27683.1.
AE008692 Genomic DNA. Translation: AAV90220.1.
PIRiA25978.
RefSeqiWP_000168720.1. NC_006526.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OWOX-ray2.07A/B/C/D1-383[»]
3OX4X-ray2.00A/B/C/D1-383[»]
ProteinModelPortaliP0DJA2.
SMRiP0DJA2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV90220; AAV90220; ZMO1596.
KEGGizmo:ZMO1596.

Phylogenomic databases

KOiK13954.
OMAiIPTVNLM.

Miscellaneous databases

EvolutionaryTraceiP0DJA2.

Family and domain databases

InterProiView protein in InterPro
IPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
PfamiView protein in Pfam
PF00465. Fe-ADH. 1 hit.
PROSITEiView protein in PROSITE
PS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiADH2_ZYMMO
AccessioniPrimary (citable) accession number: P0DJA2
Secondary accession number(s): P06758, Q5NM40
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 14, 2011
Last sequence update: December 14, 2011
Last modified: March 15, 2017
This is version 26 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In Z.mobilis there are two isozymes of alcohol dehydrogenase.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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.