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C3TAP2 (C3TAP2_ECOLX) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 22. 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 1 HAMAP MF_01275

EC=1.2.1.19 HAMAP MF_01275
Alternative name(s):
1-pyrroline dehydrogenase 1 HAMAP MF_01275
4-aminobutanal dehydrogenase 1 HAMAP MF_01275
Gene names
Name:prr1 HAMAP MF_01275
ORF Names:ECs2048 EMBL ACI83776.1
OrganismEscherichia coli EMBL ACI83776.1
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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

Sequences

Sequence LengthMass (Da)Tools
C3TAP2 [UniParc].

Last modified June 16, 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]"A precise reconstruction of the emergence and constrained radiations of Escherichia coli O157 portrayed by backbone concatenomic analysis."
Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J., Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E., Sawyer S.A., Whittam T.S., Tarr P.I.
Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009) [PubMed: 19439656] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 493/89 EMBL ACI83776.1, 86-24 EMBL ACI83777.1, 87-14 EMBL ACI83778.1 and TW14359 EMBL ACI83780.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU901230 Genomic DNA. Translation: ACI83776.1.
EU901231 Genomic DNA. Translation: ACI83777.1.
EU901232 Genomic DNA. Translation: ACI83778.1.
EU901234 Genomic DNA. Translation: ACI83780.1.

3D structure databases

ProteinModelPortalC3TAP2.
SMRC3TAP2. Positions 1-474.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
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 nameC3TAP2_ECOLX
AccessionPrimary (citable) accession number: C3TAP2
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: January 25, 2012
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)