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A7ZLN7 (ABDH_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Name:prr
Ordered Locus Names:EcE24377A_1624
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
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. HAMAP MF_01275

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. HAMAP MF_01275

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_1000067391

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
A7ZLN7 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 2F723041BFAB1A75

FASTA47450,846
        10         20         30         40         50         60 
MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VDAAVRAADA AFAEWGQTTP 

        70         80         90        100        110        120 
KVRAECLLKL ADVIEENGQV FAELESRNCG KPLHSAFNDE IPAIVDVFRF FAGAARCLNG 

       130        140        150        160        170        180 
LAAGEYLEGH TSMIRRDPLG VVASIAPWNY PLMMAAWKLA PALAAGNCVV LKPSEITPLT 

       190        200        210        220        230        240 
ALKLAELAKD IFPAGVINVL FGRGKTVGDP LTGHPKVRMV SLTGSIATGE HIISHTASSI 

       250        260        270        280        290        300 
KRTHMELGGK APVIVFDDAD IEAVVEGVRT FGYYNAGQDC TAACRIYAQK GIYDTLVEKL 

       310        320        330        340        350        360 
GAAVATLKSG APDDESTELG PLSSLAHLER VSKAVEEAKA TGHIKVITGG EKRKGNGYYY 

       370        380        390        400        410        420 
APTLLAGALQ DDAIVQKEVF GPVVSVTPFD NEEQVVNWAN DSQYGLASSV WTKDVGRAHR 

       430        440        450        460        470 
VSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV19711.1.
RefSeqYP_001462716.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZLN7.
SMRA7ZLN7. Positions 1-474.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZLN7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000022496; EBESCP00000021558; EBESCG00000021550.
GeneID5586995.
GenomeReviewsGene locus EcE24377A_1624 in contig CP000800_GR.
KEGGecw:EcE24377A_1624.
PATRIC18292503. VBIEscCol31211_1908.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
GeneTreeEBGT00050000009175.
HOGENOMHBG752218.
OMACRIYAQQ.
ProtClustDBPRK13473.

Enzyme and pathway databases

BioCycECOL331111:ECE24377A_1624-MONOMER.

Family and domain databases

HAMAPMF_01275. Aldedh_Prr.
[Tree]
InterProIPR017749. 1-pyrroline_dehydrogenase.
IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KOK00137.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR03374. ABALDH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. False negative.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameABDH_ECO24
AccessionPrimary (citable) accession number: A7ZLN7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families