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Protein

Acetaldehyde dehydrogenase

Gene

nbaJ

Organism
Geobacillus thermodenitrificans (strain NG80-2)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD+ and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds.UniRule annotation

Catalytic activityi

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei127 – 1271Acyl-thioester intermediateUniRule annotation
Binding sitei270 – 2701NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 144NADUniRule annotation
Nucleotide bindingi158 – 1669NADUniRule annotation

GO - Molecular functioni

  1. acetaldehyde dehydrogenase (acetylating) activity Source: UniProtKB-HAMAP
  2. NAD binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciGTHE420246:GIXT-3248-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetaldehyde dehydrogenaseUniRule annotation (EC:1.2.1.10UniRule annotation)
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating]UniRule annotation
Gene namesi
Name:nbaJ
Ordered Locus Names:GTNG_3152
OrganismiGeobacillus thermodenitrificans (strain NG80-2)
Taxonomic identifieri420246 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
ProteomesiUP000001578: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Acetaldehyde dehydrogenasePRO_0000387663Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi420246.GTNG_3152.

Structurei

3D structure databases

ProteinModelPortaliA4IT43.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acetaldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK04073.
OrthoDBiEOG6H1PXH.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01657. Ac_ald_DH_ac.
InterProiIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamiPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03215. ac_ald_DH_ac. 1 hit.

Sequencei

Sequence statusi: Complete.

A4IT43-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVKVAILG SGNIGTDLMI KLERSSHLEL TAMIGIDPES DGLKKAKTKG
60 70 80 90 100
YYVFDGGLKQ FLSEASELAD LVFDATSAKA HVRHAKALRE AGKMVIDLTP
110 120 130 140 150
AAVGPYVVPS VNLGDYLEES NLNLITCGGQ ATIPIVHAIN RVAQVHYSEI
160 170 180 190 200
VATIASKSAG PGTRANIDEF TQTTAHGLEA IGGAKKGKAI IILNPAEPPI
210 220 230 240 250
IMRNAVYALV ECEQMDEVAI ARSVQETVAY IQSYVPGYRL RTEPLFEGNK
260 270 280 290
VTVFVEVEGA GDYLPTYSGN LDIMTATAIK VAEEWVQHRV KAASV
Length:295
Mass (Da):31,582
Last modified:November 3, 2009 - v2
Checksum:iA139FCC99D8604EB
GO

Sequence cautioni

The sequence ABO68497.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA. Translation: ABO68497.1. Different initiation.
RefSeqiYP_001127242.2. NC_009328.1.

Genome annotation databases

EnsemblBacteriaiABO68497; ABO68497; GTNG_3152.
GeneIDi4968078.
KEGGigtn:GTNG_3152.
PATRICi21982947. VBIGeoThe136879_3316.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA. Translation: ABO68497.1. Different initiation.
RefSeqiYP_001127242.2. NC_009328.1.

3D structure databases

ProteinModelPortaliA4IT43.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi420246.GTNG_3152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO68497; ABO68497; GTNG_3152.
GeneIDi4968078.
KEGGigtn:GTNG_3152.
PATRICi21982947. VBIGeoThe136879_3316.

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK04073.
OrthoDBiEOG6H1PXH.

Enzyme and pathway databases

BioCyciGTHE420246:GIXT-3248-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01657. Ac_ald_DH_ac.
InterProiIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamiPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
    Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
    Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NG80-2.

Entry informationi

Entry nameiACDH_GEOTN
AccessioniPrimary (citable) accession number: A4IT43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: November 3, 2009
Last modified: January 7, 2015
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.