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P50457 (PUUE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-aminobutyrate aminotransferase PuuE

EC=2.6.1.19
Alternative name(s):
GABA aminotransferase
Short name=GABA-AT
Gamma-amino-N-butyrate transaminase
Short name=GABA transaminase
Glutamate:succinic semialdehyde transaminase
Gene names
Name:puuE
Synonyms:goaG
Ordered Locus Names:b1302, JW1295
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA). PuuE is important for utilization of putrescine as the sole nitrogen or carbon source. Ref.5 Ref.6

Catalytic activity

4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Completely inhibited by succinate and low-aeration conditions. Ref.6

Pathway

Amine and polyamine degradation; putrescine degradation; succinate semialdehyde from 4-aminobutanoate: step 1/1.

Induction

By putrescine. Ref.6

Disruption phenotype

Cells show only 35% of the wild-type activity. Ref.6

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.0577 mM for SSA (at pH 7.8 and at 30 degrees Celsius) Ref.6

KM=1.57 mM for GABA (at pH 7.8 and at 30 degrees Celsius)

KM=5.1 mM for KG (at pH 7.8 and at 30 degrees Celsius)

KM=18 mM for L-glutamate (at pH 7.8 and at 30 degrees Celsius)

pH dependence:

Optimum pH is 9 for the forward reaction which is the transfer reaction of the amino group from GABA to beta-ketoglutarate, and pH 8 for the reverse reaction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4214214-aminobutyrate aminotransferase PuuE
PRO_0000120388

Regions

Region110 – 1112Pyridoxal phosphate binding By similarity
Region238 – 2414Pyridoxal phosphate binding By similarity

Sites

Binding site2961Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Mutagenesis2671K → A: No GABA-AT activity. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P50457 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A2C17A885FEBE4EB

FASTA42144,729
        10         20         30         40         50         60 
MSNNEFHQRR LSATPRGVGV MCNFFAQSAE NATLKDVEGN EYIDFAAGIA VLNTGHRHPD 

        70         80         90        100        110        120 
LVAAVEQQLQ QFTHTAYQIV PYESYVTLAE KINALAPVSG QAKTAFFTTG AEAVENAVKI 

       130        140        150        160        170        180 
ARAHTGRPGV IAFSGGFHGR TYMTMALTGK VAPYKIGFGP FPGSVYHVPY PSDLHGISTQ 

       190        200        210        220        230        240 
DSLDAIERLF KSDIEAKQVA AIIFEPVQGE GGFNVAPKEL VAAIRRLCDE HGIVMIADEV 

       250        260        270        280        290        300 
QSGFARTGKL FAMDHYADKP DLMTMAKSLA GGMPLSGVVG NANIMDAPAP GGLGGTYAGN 

       310        320        330        340        350        360 
PLAVAAAHAV LNIIDKESLC ERANQLGQRL KNTLIDAKES VPAIAAVRGL GSMIAVEFND 

       370        380        390        400        410        420 
PQTGEPSAAI AQKIQQRALA QGLLLLTCGA YGNVIRFLYP LTIPDAQFDA AMKILQDALS 


D 

« Hide

References

« Hide 'large scale' references
[1]Jovanovic G.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"A novel putrescine utilization pathway involves gamma-glutamylated intermediates of Escherichia coli K-12."
Kurihara S., Oda S., Kato K., Kim H.G., Koyanagi T., Kumagai H., Suzuki H.
J. Biol. Chem. 280:4602-4608(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A GABA AMINOTRANSFERASE, NOMENCLATURE.
Strain: K12.
[6]"A putrescine-inducible pathway comprising PuuE-YneI in which gamma-aminobutyrate is degraded into succinate in Escherichia coli K-12."
Kurihara S., Kato K., Asada K., Kumagai H., Suzuki H.
J. Bacteriol. 192:4582-4591(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PUTRESCINE DEGRADATION AND AS A GABA AMINOTRANSFERASE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-267, DISRUPTION PHENOTYPE, ENZYME REGULATION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38543 Genomic DNA. Translation: AAC45301.1.
U00096 Genomic DNA. Translation: AAC74384.1.
AP009048 Genomic DNA. Translation: BAA14871.1.
PIRA64879.
RefSeqNP_415818.1. NC_000913.3.
YP_489570.1. NC_007779.1.

3D structure databases

ProteinModelPortalP50457.
SMRP50457. Positions 2-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9825N.
IntActP50457. 3 interactions.
MINTMINT-1256713.
STRING511145.b1302.

Proteomic databases

PaxDbP50457.
PRIDEP50457.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74384; AAC74384; b1302.
BAA14871; BAA14871; BAA14871.
GeneID12934532.
945446.
KEGGecj:Y75_p1277.
eco:b1302.
PATRIC32117876. VBIEscCol129921_1358.

Organism-specific databases

EchoBASEEB2979.
EcoGeneEG13187. puuE.

Phylogenomic databases

eggNOGCOG0160.
HOGENOMHOG000020206.
KOK00823.
OMAGQRLTNT.
OrthoDBEOG6QVRHN.
PhylomeDBP50457.
ProtClustDBPRK09792.

Enzyme and pathway databases

BioCycEcoCyc:G6646-MONOMER.
ECOL316407:JW1295-MONOMER.
MetaCyc:G6646-MONOMER.
SABIO-RKP50457.
UniPathwayUPA00188; UER00293.

Gene expression databases

GenevestigatorP50457.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004632. 4NH2But_aminotransferase_bac.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00700. GABAtrnsam. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP50457.

Entry information

Entry namePUUE_ECOLI
AccessionPrimary (citable) accession number: P50457
Secondary accession number(s): P78150
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene