4-aminobutyrate aminotransferase PuuE - Escherichia coli (strain K12)

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P50457 (PUUE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	puuE
Synonyms:	goaG
Ordered Locus Names:	b1302, JW1295

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Protein existence	Evidence 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: K_M=0.0577 mM for SSA (at pH 7.8 and at 30 degrees Celsius) Ref.6 K_M=1.57 mM for GABA (at pH 7.8 and at 30 degrees Celsius) K_M=5.1 mM for KG (at pH 7.8 and at 30 degrees Celsius) K_M=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.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gamma-aminobutyric acid metabolic process Inferred from electronic annotation. Source: InterPro putrescine catabolic process Inferred from mutant phenotype Ref.5 Ref.6. Source: EcoCyc
Molecular_function	4-aminobutyrate transaminase activity Inferred from direct assay Ref.5 Ref.6. Source: EcoCyc pyridoxal phosphate binding Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 421

421

4-aminobutyrate aminotransferase PuuE

PRO_0000120388

Regions

Region

110 – 111

Pyridoxal phosphate binding By similarity

Region

238 – 241

Pyridoxal phosphate binding By similarity

Sites

Binding site

296

Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue

267

N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Mutagenesis

267

K → A: No GABA-AT activity. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P50457 [UniParc].

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

421

44,729

        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

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References

	« Hide 'large scale' referencesShow '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. 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 277:1453-1474(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.
PIR	A64879.
RefSeq	NP_415818.1. NC_000913.2. YP_489570.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P50457.
SMR	P50457. Positions 2-421.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9825N.
IntAct	P50457. 2 interactions.
MINT	MINT-1256713.
STRING	511145.b1302.
Proteomic databases
PaxDb	P50457.
PRIDE	P50457.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74384; AAC74384; b1302. BAA14871; BAA14871; BAA14871.
GeneID	12934532. 945446.
KEGG	ecj:Y75_p1277. eco:b1302.
PATRIC	32117876. VBIEscCol129921_1358.
Organism-specific databases
EchoBASE	EB2979.
EcoGene	EG13187. puuE.
Phylogenomic databases
eggNOG	COG0160.
HOGENOM	HOG000020206.
KO	K00823.
OMA	KLCERSA.
ProtClustDB	PRK09792.
Enzyme and pathway databases
BioCyc	EcoCyc:G6646-MONOMER. ECOL316407:JW1295-MONOMER. MetaCyc:G6646-MONOMER.
SABIO-RK	P50457.
UniPathway	UPA00188; UER00293.
Gene expression databases
Genevestigator	P50457.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR004632. 4NH2But_aminotransferase_bac. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
PANTHER	PTHR11986. PTHR11986. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00700. GABAtrnsam. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUUE_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents