Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot A4WAR9 (ABDH_ENT38)

Last modified June 16, 2009. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Gamma-aminobutyraldehyde dehydrogenase
    EC=1.2.1.19
Alternative name(s):
    1-pyrroline dehydrogenase
    4-aminobutanal dehydrogenase
      Short name=ABALDH
Gene names
Ordered Locus Names: Ent638_2124
OrganismEnterobacter sp. (strain 638) [Complete proteome] [HAMAP]
Taxonomic identifier399742 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacter

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the oxidation of 1-pyrroline, which is spontaneously formed from 4-aminobutanal, leading to 4-aminobutanoate (GABA) By similarity.

Catalytic activity

4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH. HAMAP MF_01275

Pathway

Amine and polyamine degradation; putrescine degradation; 4-aminobutanoate from 4-aminobutanal: step 1/1. HAMAP MF_01275

Subunit structure

Homotetramer By similarity.

Miscellaneous

4-aminobutanal is also called gamma-aminobutyraldehyde. HAMAP MF_01275

Sequence similarities

Belongs to the aldehyde dehydrogenase family. Gamma-aminobutyraldehyde dehydrogenase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Gamma-aminobutyraldehyde dehydrogenase HAMAP MF_01275
PRO_1000067394

Regions

Nucleotide binding172 – 1754NAD By similarity
Nucleotide binding225 – 2317NAD By similarity

Sites

Active site2461 By similarity
Active site2801Nucleophile By similarity
Binding site1461NAD; via carbonyl oxygen By similarity
Binding site2091NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A4WAR9-1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 46C332B65B30D601

FASTA47450,905
        10         20         30         40         50         60 
MQNQLLINGE LVNGEGEKQP VYNPATGEVL LEIAEASAAQ VDAAVRAADR AFSEWGHTTP 

        70         80         90        100        110        120 
KARAECLLKL ADVIEEHAET FARLESQNCG KPLHCVISDE IPAVVDVFRF FAGAARCLNG 

       130        140        150        160        170        180 
LAAGEYLEGH TSMIRRDPVG VVASIAPWNY PLMMAAWKLA PALAAGNCVV IKPSEITPLT 

       190        200        210        220        230        240 
ALKLAELAKD IFPAGVLNVL FGRGKTVGDP LTGHEKVRMV SLTGSIATGE HIISHTASSI 

       250        260        270        280        290        300 
KRTHMELGGK APVIVFDDAD IDAVVEGVRT FGFYNAGQDC TAACRIYAQK GIYPQLVEKL 

       310        320        330        340        350        360 
GAAVATLKTG APEDESTELG PLSSAAHLER VCKAVDEAKA LGHVNVVTGG KKVEGGGYFF 

       370        380        390        400        410        420 
EPTLLAGAKQ EDAIVQREVF GPVVSMTEFD DEEQVLAWAN DSQYGLASSV WTQDVGRAHR 

       430        440        450        460        470 
MSARLQYGCT WVNTHFMLVS EMPHGGMKLS GYGKDMSVYG LEDYTVIRHV MIKH 

« Hide

References

[1]"Complete sequence of chromosome of Enterobacter sp. 638."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000653 Genomic DNA. Translation: ABP60799.1.
RefSeqYP_001176850.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5113705.
GenomeReviewsGene locus Ent638_2124 in contig CP000653_GR.
KEGGent:Ent638_2124.
NMPDRfig|399742.4.peg.2072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA4WAR9. QVLRWAN.

Family and domain databases

HAMAPMF_01275.
[Tree]
InterProIPR017749. 1-pyrroline_dehydrogenase.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03374. ABALDH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. False negative.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameABDH_ENT38
AccessionPrimary (citable) accession number: A4WAR9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: June 16, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents