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Q8X9W5 (ABDH_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. 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:Z2275, ECs2048
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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_0000269692

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
Q8X9W5 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 3C5A470E8869FA11

FASTA47450,900
        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 HIISHTAPSI 

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

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

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

       430        440        450        460        470 
VSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG56331.1.
BA000007 Genomic DNA. Translation: BAB35471.1.
PIRG85733.
H90884.
RefSeqNP_287717.1. NC_002655.2.
NP_310075.1. NC_002695.1.

3D structure databases

HSSPHSSP built from PDB template 1WND based on UniProtKB P77674.
ProteinModelPortalQ8X9W5.
SMRQ8X9W5. Positions 1-474.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000024471; EBESCP00000023364; EBESCG00000023525.
EBESCT00000057793; EBESCP00000055621; EBESCG00000056841.
GeneID917246.
960824.
GenomeReviewsGene locus Z2275 in contig AE005174_GR.
Gene locus ECs2048 in contig BA000007_GR.
KEGGece:Z2275.
ecs:ECs2048.
PATRIC18353264. VBIEscCol44059_1851.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009175.
HOGENOMHBG752218.
OMACRIYAQQ.
ProtClustDBPRK13473.

Enzyme and pathway databases

BioCycECOL83334:ECS2048-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_ECO57
AccessionPrimary (citable) accession number: Q8X9W5
Secondary accession number(s): Q7AE53
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 73 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

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