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Q8Z747 (ABDH_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. Feed History...

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

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:STY1467, t1506
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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 caution

The sequence AAO69141.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAD01728.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Gamma-aminobutyraldehyde dehydrogenase HAMAP MF_01275
PRO_0000269699

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
Q8Z747 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: EE560746392178C8

FASTA47451,149
        10         20         30         40         50         60 
MQYQLLINGV LVDGEGERQS VYNPATGEVI LEIAEASPVQ VDAAVLAADS AFAEWGQTTP 

        70         80         90        100        110        120 
KARAECLLKL ADSIEQNALE FARLESQNCG KPLHCVINDE IPAIVDVFRF FAGAARCLSG 

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

       190        200        210        220        230        240 
ALKLAALAKD IFPPGVLNVL FGRGQTVGDV LTGHEKVRMV SLTGSIATGE HILRHTAPAI 

       250        260        270        280        290        300 
KRTHMELGGK APVIVFDDAD LDAVAQGVRT FGFYNAGQDC TAACRIYAQR GIYDALVEKL 

       310        320        330        340        350        360 
GNAVSSLKMG APEDKSTELG PLSSLAHLKR VTAAVEEAKA LSHIRVITGG SQTEGKGYYF 

       370        380        390        400        410        420 
APTLLADAKQ EDAIVQREVF GPVVSITVFD DEDQVLRWAN DSRYGLASSV WTQDVGRAHR 

       430        440        450        460        470 
LSARLQYGCT WINTHFMLVS EMPHGGQKQS GYGKDMSLYG LEDYTLVRHI MVKH

« Hide

References

[1]"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. expand/collapse author list , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:848-852(2001) [PubMed: 11677608] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.
[2]"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL627270 Genomic DNA. Translation: CAD01728.1. Different initiation.
AE014613 Genomic DNA. Translation: AAO69141.1. Different initiation.
RefSeqNP_455900.2. NC_003198.1.
NP_805292.2. NC_004631.1.

3D structure databases

HSSPHSSP built from PDB template 1WND based on UniProtKB P77674.
ProteinModelPortalQ8Z747.
SMRQ8Z747. Positions 1-474.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1070958.
1247857.
GenomeReviewsGene locus t1506 in contig AE014613_GR.
Gene locus STY1467 in contig AL513382_GR.
KEGGstt:t1506.
sty:STY1467.
PATRIC18540824. VBISalEnt120419_1477.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG752218.
OMAQVLRWAN.
ProtClustDBPRK13473.

Enzyme and pathway databases

BioCycSENT209261:T1506-MONOMER.
SENT220341:STY1467-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_SALTI
AccessionPrimary (citable) accession number: Q8Z747
Secondary accession number(s): Q7C9Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: January 25, 2012
This is version 74 of the entry and version 2 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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