Skip Header

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

B4TIM0 (B4TIM0_SALHS) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 25. 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 ACF67285.1
Synonyms:prr HAMAP MF_01275
Ordered Locus Names:SeHA_C1777
OrganismSalmonella heidelberg (strain SL476) [Complete proteome] [HAMAP] EMBL ACF67285.1
Taxonomic identifier454169 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella enterica subsp. enterica serovar Heidelberg

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
B4TIM0 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 6A44022C5049CE71

FASTA48151,948
        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 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 QVLRWANDSH YGLASSVWTQ 

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


H

« Hide

References

[1]"Complete genome of Salmonella heidelberg strain SL476."
Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., Leclerc J., Cebula T., Sebastian Y.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001120 Genomic DNA. Translation: ACF67285.1.
RefSeqYP_002045639.1. NC_011083.1.

3D structure databases

ProteinModelPortalB4TIM0.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4TIM0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6492410.
GenomeReviewsGene locus SeHA_C1777 in contig CP001120_GR.
KEGGseh:SeHA_C1777.
PATRIC18511246. VBISalEnt43179_1730.

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 nameB4TIM0_SALHS
AccessionPrimary (citable) accession number: B4TIM0
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: December 14, 2011
This is version 25 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