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Protein

Gamma-glutamylputrescine synthetase PuuA

Gene

puuA

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

Functioni

Involved in the breakdown of putrescine via the biosynthesis of gamma-L-glutamylputrescine. It is able to use several diamines, spermidine and spermine. Absolutely essential to utilize putrescine as both nitrogen and carbon sources and to decrease the toxicity of putrescine, which can lead to inhibition of cell growth and protein synthesis.2 Publications

Catalytic activityi

ATP + L-glutamate + putrescine = ADP + phosphate + gamma-L-glutamylputrescine.

Kineticsi

  1. KM=2.07 mM for glutamate (at pH 8 and at 37 degrees Celsius)1 Publication
  2. KM=2.25 mM for ATP (at pH 8 and at 37 degrees Celsius)1 Publication
  3. KM=44.6 mM for putrescine (at pH 8 and at 37 degrees Celsius)1 Publication
  1. Vmax=6.71 µmol/min/mg enzyme (at pH 8 and at 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 9.1 Publication

Pathwayi: putrescine degradation

This protein is involved in step 1 of the subpathway that synthesizes 4-aminobutanoate from putrescine.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Gamma-glutamylputrescine synthetase PuuA (puuA)
  2. Gamma-glutamylputrescine oxidoreductase (puuB)
  3. Aldehyde dehydrogenase PuuC (puuC)
  4. Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (puuD)
This subpathway is part of the pathway putrescine degradation, which is itself part of Amine and polyamine degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-aminobutanoate from putrescine, the pathway putrescine degradation and in Amine and polyamine degradation.

GO - Molecular functioni

GO - Biological processi

  • glutamine biosynthetic process Source: InterPro
  • putrescine catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6644-MONOMER.
ECOL316407:JW5201-MONOMER.
MetaCyc:G6644-MONOMER.
RETL1328306-WGS:GSTH-1322-MONOMER.
RETL1328306-WGS:GSTH-719-MONOMER.
UniPathwayiUPA00188; UER00880.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamylputrescine synthetase PuuA (EC:6.3.1.11)
Short name:
Gamma-Glu-Put synthetase
Alternative name(s):
Glutamate--putrescine ligase
Gene namesi
Name:puuA
Synonyms:ycjK
Ordered Locus Names:b1297, JW5201
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13908. puuA.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi282 – 2821H → N: Activity is impaired to 9% of wild-type. 1 Publication
Mutagenesisi357 – 3571R → Q: Activity is impaired to 3% of wild-type. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 472472Gamma-glutamylputrescine synthetase PuuAPRO_0000153280Add
BLAST

Proteomic databases

PaxDbiP78061.

Expressioni

Inductioni

Induced by putrescine and repressed by PuuR. Transiently induced by cold shock.2 Publications

Interactioni

Subunit structurei

Dodecamer.1 Publication

Protein-protein interaction databases

BioGridi4260944. 8 interactions.
STRINGi511145.b1297.

Structurei

3D structure databases

ProteinModelPortaliP78061.
SMRiP78061. Positions 21-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiENOG4105CFQ. Bacteria.
COG0174. LUCA.
HOGENOMiHOG000005154.
InParanoidiP78061.
KOiK09470.
OMAiAADHNAF.
OrthoDBiEOG6B360N.
PhylomeDBiP78061.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_b-grasp.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
[Graphical view]
SMARTiSM01230. Gln-synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P78061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METNIVEVEN FVQQSEERRG SAFTQEVKRY LERYPNTQYV DVLLTDLNGC
60 70 80 90 100
FRGKRIPVSS LKKLEKGCYF PASVFAMDIL GNVVEEAGLG QEMGEPDRTC
110 120 130 140 150
VPVLGSLTPS AADPEFIGQM LLTMVDEDGA PFDVEPRNVL NRLWQQLRQR
160 170 180 190 200
GLFPVVAVEL EFYLLDRQRD AEGYLQPPCA PGTDDRNTQS QVYSVDNLNH
210 220 230 240 250
FADVLNDIDE LAQLQLIPAD GAVAEASPGQ FEINLYHTDN VLEACDDALA
260 270 280 290 300
LKRLVRLMAE KHKMHATFMA KPYEEHAGSG MHIHISMQNN RGENVLSDAE
310 320 330 340 350
GEDSPLLKKM LAGMIDLMPS SMALLAPNVN SYRRFQPGMY VPTQASWGHN
360 370 380 390 400
NRTVALRIPC GDRHNHRVEY RVAGADANPY LVMAAIFAGI LHGLDNELPL
410 420 430 440 450
QEEVEGNGLE QEGLPFPIRQ SDALGEFIEN DHLRRYLGER FCHVYHACKN
460 470
DELLQFERLI TETEIEWMLK NA
Length:472
Mass (Da):53,177
Last modified:July 11, 2001 - v2
Checksum:i9D2224C5A9FCC0A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74379.2.
AP009048 Genomic DNA. Translation: BAA14857.2.
PIRiD64878.
RefSeqiNP_415813.4. NC_000913.3.
WP_001296746.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74379; AAC74379; b1297.
BAA14857; BAA14857; BAA14857.
GeneIDi946202.
KEGGiecj:JW5201.
eco:b1297.
PATRICi32117864. VBIEscCol129921_1352.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74379.2.
AP009048 Genomic DNA. Translation: BAA14857.2.
PIRiD64878.
RefSeqiNP_415813.4. NC_000913.3.
WP_001296746.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP78061.
SMRiP78061. Positions 21-467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260944. 8 interactions.
STRINGi511145.b1297.

Proteomic databases

PaxDbiP78061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74379; AAC74379; b1297.
BAA14857; BAA14857; BAA14857.
GeneIDi946202.
KEGGiecj:JW5201.
eco:b1297.
PATRICi32117864. VBIEscCol129921_1352.

Organism-specific databases

EchoBASEiEB3667.
EcoGeneiEG13908. puuA.

Phylogenomic databases

eggNOGiENOG4105CFQ. Bacteria.
COG0174. LUCA.
HOGENOMiHOG000005154.
InParanoidiP78061.
KOiK09470.
OMAiAADHNAF.
OrthoDBiEOG6B360N.
PhylomeDBiP78061.

Enzyme and pathway databases

UniPathwayiUPA00188; UER00880.
BioCyciEcoCyc:G6644-MONOMER.
ECOL316407:JW5201-MONOMER.
MetaCyc:G6644-MONOMER.
RETL1328306-WGS:GSTH-1322-MONOMER.
RETL1328306-WGS:GSTH-719-MONOMER.

Miscellaneous databases

PROiP78061.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_b-grasp.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
[Graphical view]
SMARTiSM01230. Gln-synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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], SEQUENCE REVISION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Changes in Escherichia coli transcriptome during acclimatization at low temperature."
    Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G., Deho G.
    Res. Microbiol. 154:573-580(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY COLD SHOCK.
    Strain: K12 / MG1655 / ATCC 47076.
  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 GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE, NOMENCLATURE.
    Strain: K12.
  6. "gamma-Glutamylputrescine synthetase in the putrescine utilization pathway of Escherichia coli K-12."
    Kurihara S., Oda S., Tsuboi Y., Kim H.G., Oshida M., Kumagai H., Suzuki H.
    J. Biol. Chem. 283:19981-19990(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PUTRESCINE DEGRADATION AND AS A GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE, MUTAGENESIS OF HIS-282 AND ARG-357, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBUNIT, SUBSTRATE SPECIFICITY.
    Strain: K12.

Entry informationi

Entry nameiPUUA_ECOLI
AccessioniPrimary (citable) accession number: P78061
Secondary accession number(s): P78287
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 11, 2001
Last modified: May 11, 2016
This is version 118 of the entry and version 2 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

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 one 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.