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B5FUU8 (B5FUU8_SALDC) 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
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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:prr HAMAP MF_01275
Ordered Locus Names:SeD_A1744
OrganismSalmonella dublin (strain CT_02021853) [Complete proteome] [HAMAP] EMBL ACH77886.1
Taxonomic identifier439851 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella dublin

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
B5FUU8 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: C564F3A403C951C7

FASTA48151,963
        10         20         30         40         50         60 
MTIWENAMQY QLLINGVLVD GEGERQSVYN PATGEVILEI AEASPAQVDA AVLAADSAFA 

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

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

       190        200        210        220        230        240 
SEITPLTALK LAALAKDIFP PGVLNVLFGR 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 HGGQKQSGYG KDMSLYGLED YTLVRHIMVK 


H

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References

[1]"Complete genome of Salmonella dublin strain CT_02021853."
Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., Leclerc J., Cebula T., Sebastian Y.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001144 Genomic DNA. Translation: ACH77886.1.
RefSeqYP_002215549.1. NC_011205.1.

3D structure databases

ProteinModelPortalB5FUU8.
ModBaseSearch...

Protein-protein interaction databases

STRINGB5FUU8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6873612.
GenomeReviewsGene locus SeD_A1744 in contig CP001144_GR.
KEGGsed:SeD_A1744.
PATRIC18491655. VBISalEnt111443_1774.

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 nameB5FUU8_SALDC
AccessionPrimary (citable) accession number: B5FUU8
Entry history
Integrated into UniProtKB/TrEMBL: October 14, 2008
Last sequence update: October 14, 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)
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