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Protein

4-aminobutyrate aminotransferase PuuE

Gene

puuE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Enzyme regulationi

Completely inhibited by succinate and low-aeration conditions.1 Publication

Kineticsi

  1. KM=0.0577 mM for SSA (at pH 7.8 and at 30 degrees Celsius)1 Publication
  2. KM=1.57 mM for GABA (at pH 7.8 and at 30 degrees Celsius)1 Publication
  3. KM=5.1 mM for KG (at pH 7.8 and at 30 degrees Celsius)1 Publication
  4. KM=18 mM for L-glutamate (at pH 7.8 and at 30 degrees Celsius)1 Publication

pH dependencei

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.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei296 – 2961Pyridoxal phosphateBy similarity

GO - Molecular functioni

  1. 4-aminobutyrate transaminase activity Source: EcoCyc
  2. pyridoxal phosphate binding Source: EcoCyc

GO - Biological processi

  1. gamma-aminobutyric acid metabolic process Source: InterPro
  2. putrescine catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:G6646-MONOMER.
ECOL316407:JW1295-MONOMER.
MetaCyc:G6646-MONOMER.
SABIO-RKP50457.
UniPathwayiUPA00188; UER00293.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:puuE
Synonyms:goaG
Ordered Locus Names:b1302, JW1295
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG13187. puuE.

Pathology & Biotechi

Disruption phenotypei

Cells show only 35% of the wild-type activity.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi267 – 2671K → A: No GABA-AT activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4214214-aminobutyrate aminotransferase PuuEPRO_0000120388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei267 – 2671N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiP50457.
PRIDEiP50457.

Expressioni

Inductioni

By putrescine.1 Publication

Gene expression databases

GenevestigatoriP50457.

Interactioni

Protein-protein interaction databases

DIPiDIP-9825N.
IntActiP50457. 3 interactions.
MINTiMINT-1256713.
STRINGi511145.b1302.

Structurei

3D structure databases

ProteinModelPortaliP50457.
SMRiP50457. Positions 2-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni110 – 1112Pyridoxal phosphate bindingBy similarity
Regioni238 – 2414Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0160.
HOGENOMiHOG000020206.
InParanoidiP50457.
KOiK00823.
OMAiGQRLTNT.
OrthoDBiEOG6QVRHN.
PhylomeDBiP50457.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004632. 4NH2But_aminotransferase_bac.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00700. GABAtrnsam. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50457-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNNEFHQRR LSATPRGVGV MCNFFAQSAE NATLKDVEGN EYIDFAAGIA
60 70 80 90 100
VLNTGHRHPD LVAAVEQQLQ QFTHTAYQIV PYESYVTLAE KINALAPVSG
110 120 130 140 150
QAKTAFFTTG AEAVENAVKI ARAHTGRPGV IAFSGGFHGR TYMTMALTGK
160 170 180 190 200
VAPYKIGFGP FPGSVYHVPY PSDLHGISTQ DSLDAIERLF KSDIEAKQVA
210 220 230 240 250
AIIFEPVQGE GGFNVAPKEL VAAIRRLCDE HGIVMIADEV QSGFARTGKL
260 270 280 290 300
FAMDHYADKP DLMTMAKSLA GGMPLSGVVG NANIMDAPAP GGLGGTYAGN
310 320 330 340 350
PLAVAAAHAV LNIIDKESLC ERANQLGQRL KNTLIDAKES VPAIAAVRGL
360 370 380 390 400
GSMIAVEFND PQTGEPSAAI AQKIQQRALA QGLLLLTCGA YGNVIRFLYP
410 420
LTIPDAQFDA AMKILQDALS D
Length:421
Mass (Da):44,729
Last modified:October 1, 1996 - v1
Checksum:iA2C17A885FEBE4EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38543 Genomic DNA. Translation: AAC45301.1.
U00096 Genomic DNA. Translation: AAC74384.1.
AP009048 Genomic DNA. Translation: BAA14871.1.
PIRiA64879.
RefSeqiNP_415818.1. NC_000913.3.
YP_489570.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74384; AAC74384; b1302.
BAA14871; BAA14871; BAA14871.
GeneIDi12934532.
945446.
KEGGiecj:Y75_p1277.
eco:b1302.
PATRICi32117876. VBIEscCol129921_1358.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38543 Genomic DNA. Translation: AAC45301.1.
U00096 Genomic DNA. Translation: AAC74384.1.
AP009048 Genomic DNA. Translation: BAA14871.1.
PIRiA64879.
RefSeqiNP_415818.1. NC_000913.3.
YP_489570.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP50457.
SMRiP50457. Positions 2-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9825N.
IntActiP50457. 3 interactions.
MINTiMINT-1256713.
STRINGi511145.b1302.

Proteomic databases

PaxDbiP50457.
PRIDEiP50457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74384; AAC74384; b1302.
BAA14871; BAA14871; BAA14871.
GeneIDi12934532.
945446.
KEGGiecj:Y75_p1277.
eco:b1302.
PATRICi32117876. VBIEscCol129921_1358.

Organism-specific databases

EchoBASEiEB2979.
EcoGeneiEG13187. puuE.

Phylogenomic databases

eggNOGiCOG0160.
HOGENOMiHOG000020206.
InParanoidiP50457.
KOiK00823.
OMAiGQRLTNT.
OrthoDBiEOG6QVRHN.
PhylomeDBiP50457.

Enzyme and pathway databases

UniPathwayiUPA00188; UER00293.
BioCyciEcoCyc:G6646-MONOMER.
ECOL316407:JW1295-MONOMER.
MetaCyc:G6646-MONOMER.
SABIO-RKP50457.

Miscellaneous databases

PROiP50457.

Gene expression databases

GenevestigatoriP50457.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004632. 4NH2But_aminotransferase_bac.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00700. GABAtrnsam. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Jovanovic G.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.

Entry informationi

Entry nameiPUUE_ECOLI
AccessioniPrimary (citable) accession number: P50457
Secondary accession number(s): P78150
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.