Skip Header

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

B5RA85 (B5RA85_SALG2) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 26. Feed History...

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

Names and origin

Protein namesRecommended name:
Gamma-aminobutyraldehyde dehydrogenase HAMAP MF_01275
EC=1.2.1.19 HAMAP MF_01275
Alternative name(s):
1-pyrroline dehydrogenase HAMAP MF_01275
4-aminobutanal dehydrogenase HAMAP MF_01275
Gene names
Name:ydcW EMBL CAR37392.1
Synonyms:prr HAMAP MF_01275
Ordered Locus Names:SG1526
OrganismSalmonella gallinarum (strain 287/91 / NCTC 13346) [Complete proteome] [HAMAP]
Taxonomic identifier550538 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella gallinarum

Protein attributes

Sequence length481 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 By similarity. HAMAP MF_01275

Sequence similarities

Belongs to the aldehyde dehydrogenase family. Gamma-aminobutyraldehyde dehydrogenase subfamily. HAMAP MF_01275

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding179 – 1824NAD By similarity HAMAP MF_01275
Nucleotide binding232 – 2387NAD By similarity HAMAP MF_01275

Sites

Active site2531 By similarity HAMAP MF_01275
Active site2871Nucleophile By similarity HAMAP MF_01275
Binding site1531NAD; via carbonyl oxygen By similarity HAMAP MF_01275
Binding site2161NAD By similarity HAMAP MF_01275

Sequences

Sequence LengthMass (Da)Tools
B5RA85 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: 41F315C910D9EB12

FASTA48151,997
        10         20         30         40         50         60 
MTIWENAMQY QLLINGVLVD GEGERQSVYN PATGEVILEI AEASPAQVDA AVLAADSAFA 

        70         80         90        100        110        120 
EWGQTTPKAR AECLLKLADS IEQNALEFAR LESQNCGKPL HCVINDEIPA IVDVFRFFAG 

       130        140        150        160        170        180 
AARCLSGLAA GEYLEGHTSM IRRDPIGVVA SIAPWNYPLM MAAWKLAPAL AAGNCVVIKP 

       190        200        210        220        230        240 
SEITPLTALK LAALAKDIFP PGGLNVLFGR GQTVGDVLTG HEKVRMVSLT GSIATGEHIL 

       250        260        270        280        290        300 
RHTAPAIKRT HMELGGKAPV IVFDDADLDA VAQGVRTFGF YNAGQDCTAA CRIYAQRGIY 

       310        320        330        340        350        360 
DALVEKLGNA VSSLKMGAPE DESTELGPLS SLAHLKRVTA AVEEAKALSH IRVITGGSQT 

       370        380        390        400        410        420 
EGKGYYFAPT LLADAKQEDA IVQREVFGPV VSITVFDDED QVLRWANDSR YGLASSVWTQ 

       430        440        450        460        470        480 
DVGRAHRLSA RLQYGCTWIN THFMLVSEMP HGEQKQSGYG KDMSLYGLED YTLVRHIMVK 


H

« Hide

References

[1]"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways."
Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. expand/collapse author list , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.
Genome Res. 18:1624-1637(2008) [PubMed: 18583645] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM933173 Genomic DNA. Translation: CAR37392.1.
RefSeqYP_002226522.1. NC_011274.1.

3D structure databases

ProteinModelPortalB5RA85.
ModBaseSearch...

Protein-protein interaction databases

STRINGB5RA85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6925485.
GenomeReviewsGene locus SG1526 in contig AM933173_GR.
KEGGseg:SG1526.
PATRIC18501384. VBISalEnt1629_1624.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG752218.
OMAQVLRWAN.
ProtClustDBPRK13473.

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.
PROSITEPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB5RA85_SALG2
AccessionPrimary (citable) accession number: B5RA85
Entry history
Integrated into UniProtKB/TrEMBL: November 4, 2008
Last sequence update: November 4, 2008
Last modified: December 14, 2011
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info