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Q5R6B5 (AL1B1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde dehydrogenase X, mitochondrial

EC=1.2.1.3
Alternative name(s):
Aldehyde dehydrogenase family 1 member B1
Gene names
Name:ALDH1B1
Synonyms:ALDHX
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation By similarity.

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Pathway

Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processethanol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaldehyde dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1717Mitochondrion Potential
Chain18 – 517500Aldehyde dehydrogenase X, mitochondrial
PRO_0000271412

Regions

Nucleotide binding262 – 2676NAD By similarity

Sites

Active site2851Proton acceptor By similarity
Active site3191Nucleophile By similarity
Site1861Transition state stabilizer By similarity

Amino acid modifications

Modified residue511N6-acetyllysine By similarity
Modified residue521N6-acetyllysine; alternate By similarity
Modified residue521N6-succinyllysine; alternate By similarity
Modified residue811N6-succinyllysine By similarity
Modified residue3641N6-acetyllysine; alternate By similarity
Modified residue3641N6-succinyllysine; alternate By similarity
Modified residue3831N6-acetyllysine; alternate By similarity
Modified residue3831N6-succinyllysine; alternate By similarity
Modified residue3991N6-acetyllysine; alternate By similarity
Modified residue3991N6-succinyllysine; alternate By similarity
Modified residue4141N6-acetyllysine; alternate By similarity
Modified residue4141N6-succinyllysine; alternate By similarity
Modified residue4261N6-acetyllysine; alternate By similarity
Modified residue4261N6-succinyllysine; alternate By similarity
Modified residue4291N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R6B5 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 105F47E5840D4229

FASTA51757,261
        10         20         30         40         50         60 
MLRFLAPRLL SLQGRTARYS SAAALPSPIL NPDIPYNQLF INNEWQDAVS KKTFPTVNPT 

        70         80         90        100        110        120 
TGEVIGHVAE GDRADVDRAV KAAREAFRLG SPWRRMDASE RGRLLNCLAD LVERDRVYLA 

       130        140        150        160        170        180 
SLETLDNGKP FQESYALDLD EVIKVYRYFA GWADKWHGKT IPMDGQHFCF TRHEPIGVCG 

       190        200        210        220        230        240 
QIIPWNFPLV MQGWKLAPAL ATGNTVVMKV AEQTPLSALY LASLIKEAGF PPGVVNIITG 

       250        260        270        280        290        300 
YGPTAGAAIA QHMDVDKVAF TGSTEVGHLI QKAAGDSNLK RVTLELGGKS PSIVLADADM 

       310        320        330        340        350        360 
EHAVEQCHEA LFFNMGQCCC AGSRTFVEES IYNEFLERTV EKAKQRKVGN PFELDTQQGP 

       370        380        390        400        410        420 
QVDKEQFERV LGYIQLGQKE GAKLLCGGER FGERGFFIKP TVFGGVQDDM RIAKEEIFGP 

       430        440        450        460        470        480 
VQPLFKFKKM EEVIERANTT RYGLAAAVFT RDLDKAMYFT QALQAGTVWV NTYNIVTCHT 

       490        500        510 
PFGGFKESGN GRELGEDGLK AYTEVKTVTI KVPQKNS 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860576 mRNA. Translation: CAH92701.1.
RefSeqNP_001127576.1. NM_001134104.1.

3D structure databases

ProteinModelPortalQ5R6B5.
SMRQ5R6B5. Positions 25-517.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R6B5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174654.
KEGGpon:100174654.

Organism-specific databases

CTD219.

Phylogenomic databases

HOVERGENHBG000097.
InParanoidQ5R6B5.
KOK00128.

Enzyme and pathway databases

UniPathwayUPA00780; UER00768.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAL1B1_PONAB
AccessionPrimary (citable) accession number: Q5R6B5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: December 21, 2004
Last modified: March 19, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways