Skip Header

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

C6UU28 (C6UU28_ECO5T) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 24. 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 ACT71749.1
Synonyms:prr HAMAP MF_01275
Ordered Locus Names:ECSP_1924
OrganismEscherichia coli O157:H7 (strain TW14359 / EHEC) [Complete proteome] [HAMAP]
Taxonomic identifier544404 [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 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 binding172 – 1754NAD By similarity HAMAP MF_01275
Nucleotide binding225 – 2317NAD By similarity HAMAP MF_01275

Sites

Active site2461 By similarity HAMAP MF_01275
Active site2801Nucleophile By similarity HAMAP MF_01275
Binding site1461NAD; via carbonyl oxygen By similarity HAMAP MF_01275
Binding site2091NAD By similarity HAMAP MF_01275

Sequences

Sequence LengthMass (Da)Tools
C6UU28 [UniParc].

Last modified September 22, 2009. 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

References

[1]"Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-associated outbreak isolate indicates candidate genes that may enhance virulence."
Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C., Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H., Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K. expand/collapse author list , Samadpour M., Whittam T.S., Kaul R., Brittnacher M., Miller S.I.
Infect. Immun. 77:3713-3721(2009) [PubMed: 19564389] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001368 Genomic DNA. Translation: ACT71749.1.
RefSeqYP_003077825.1. NC_013008.1.

3D structure databases

ProteinModelPortalC6UU28.
SMRC6UU28. Positions 1-474.
ModBaseSearch...

Protein-protein interaction databases

STRINGC6UU28.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000165814; EBESCP00000155934; EBESCG00000167163.
GeneID8216490.
GenomeReviewsGene locus ECSP_1924 in contig CP001368_GR.
KEGGetw:ECSP_1924.
PATRIC18387814. VBIEscCol9396_1959.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009175.
OMACRIYAQQ.
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 nameC6UU28_ECO5T
AccessionPrimary (citable) accession number: C6UU28
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: December 14, 2011
This is version 24 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