PUUA_ECOLI
ID PUUA_ECOLI Reviewed; 472 AA.
AC P78061; P78287;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Gamma-glutamylputrescine synthetase PuuA {ECO:0000303|PubMed:18495664};
DE Short=Gamma-Glu-Put synthetase;
DE EC=6.3.1.11 {ECO:0000269|PubMed:18495664};
DE AltName: Full=Glutamate--putrescine ligase {ECO:0000303|PubMed:18495664};
GN Name=puuA {ECO:0000303|PubMed:18495664}; Synonyms=ycjK;
GN OrderedLocusNames=b1297, JW5201;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INDUCTION BY COLD SHOCK.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14527658; DOI=10.1016/s0923-2508(03)00167-0;
RA Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G.,
RA Deho G.;
RT "Changes in Escherichia coli transcriptome during acclimatization at low
RT temperature.";
RL Res. Microbiol. 154:573-580(2003).
RN [5]
RP FUNCTION AS A GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE, AND NOMENCLATURE.
RC STRAIN=K12;
RX PubMed=15590624; DOI=10.1074/jbc.m411114200;
RA Kurihara S., Oda S., Kato K., Kim H.G., Koyanagi T., Kumagai H., Suzuki H.;
RT "A novel putrescine utilization pathway involves gamma-glutamylated
RT intermediates of Escherichia coli K-12.";
RL J. Biol. Chem. 280:4602-4608(2005).
RN [6]
RP FUNCTION IN PUTRESCINE DEGRADATION, CATALYTIC ACTIVITY, COFACTOR,
RP MUTAGENESIS OF HIS-282 AND ARG-357, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, INDUCTION, SUBUNIT, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=18495664; DOI=10.1074/jbc.m800133200;
RA Kurihara S., Oda S., Tsuboi Y., Kim H.G., Oshida M., Kumagai H., Suzuki H.;
RT "gamma-Glutamylputrescine synthetase in the putrescine utilization pathway
RT of Escherichia coli K-12.";
RL J. Biol. Chem. 283:19981-19990(2008).
CC -!- FUNCTION: Involved in the breakdown of putrescine. Catalyzes the ATP-
CC dependent gamma-glutamylation of putrescine, producing gamma-L-
CC glutamylputrescine. Absolutely essential to utilize putrescine as both
CC nitrogen and carbon sources and to decrease the toxicity of putrescine,
CC which can lead to inhibition of cell growth and protein synthesis. In
CC vitro is also able to use several diamines, and spermidine and
CC spermine, instead of putrescine, but with a much lower activity, and
CC cannot catalyze the gamma-glutamylation of ornithine or GABA
CC (PubMed:18495664). {ECO:0000269|PubMed:15590624,
CC ECO:0000269|PubMed:18495664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + putrescine = ADP + gamma-L-
CC glutamylputrescine + H(+) + phosphate; Xref=Rhea:RHEA:13633,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58731, ChEBI:CHEBI:326268,
CC ChEBI:CHEBI:456216; EC=6.3.1.11;
CC Evidence={ECO:0000269|PubMed:18495664};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13634;
CC Evidence={ECO:0000269|PubMed:18495664};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18495664};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18495664};
CC Note=Requires Mg(2+), that can be substituted by Mn(2+).
CC {ECO:0000269|PubMed:18495664};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.07 mM for glutamate (at pH 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18495664};
CC KM=2.25 mM for ATP (at pH 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18495664};
CC KM=44.6 mM for putrescine (at pH 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18495664};
CC Vmax=6.71 umol/min/mg enzyme with putrescine as substrate (at pH 8
CC and at 37 degrees Celsius) {ECO:0000269|PubMed:18495664};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:18495664};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC aminobutanoate from putrescine: step 1/4.
CC {ECO:0000269|PubMed:18495664}.
CC -!- SUBUNIT: Dodecamer. {ECO:0000269|PubMed:18495664}.
CC -!- INDUCTION: Induced by putrescine and repressed by PuuR. Transiently
CC induced by cold shock. {ECO:0000269|PubMed:14527658,
CC ECO:0000269|PubMed:18495664}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene cannot grow on putrescine
CC as the sole source of carbon or nitrogen.
CC {ECO:0000269|PubMed:18495664}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; U00096; AAC74379.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA14857.2; -; Genomic_DNA.
DR PIR; D64878; D64878.
DR RefSeq; NP_415813.4; NC_000913.3.
DR RefSeq; WP_001296746.1; NZ_STEB01000005.1.
DR AlphaFoldDB; P78061; -.
DR SMR; P78061; -.
DR BioGRID; 4260944; 13.
DR STRING; 511145.b1297; -.
DR jPOST; P78061; -.
DR PaxDb; P78061; -.
DR PRIDE; P78061; -.
DR EnsemblBacteria; AAC74379; AAC74379; b1297.
DR EnsemblBacteria; BAA14857; BAA14857; BAA14857.
DR GeneID; 66674875; -.
DR GeneID; 946202; -.
DR KEGG; ecj:JW5201; -.
DR KEGG; eco:b1297; -.
DR PATRIC; fig|511145.12.peg.1352; -.
DR EchoBASE; EB3667; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_017290_0_0_6; -.
DR InParanoid; P78061; -.
DR OMA; NPGQHEI; -.
DR PhylomeDB; P78061; -.
DR BioCyc; EcoCyc:G6644-MON; -.
DR BioCyc; MetaCyc:G6644-MON; -.
DR UniPathway; UPA00188; UER00880.
DR PRO; PR:P78061; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:InterPro.
DR GO; GO:0034024; F:glutamate-putrescine ligase activity; IDA:EcoCyc.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006598; P:polyamine catabolic process; IBA:GO_Central.
DR GO; GO:0009447; P:putrescine catabolic process; IMP:EcoCyc.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR036651; Gln_synt_N.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR027303; Gln_synth_gly_rich_site.
DR Pfam; PF00120; Gln-synt_C; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Magnesium; Manganese; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..472
FT /note="Gamma-glutamylputrescine synthetase PuuA"
FT /id="PRO_0000153280"
FT DOMAIN 35..129
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 136..472
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT MUTAGEN 282
FT /note="H->N: Activity is impaired to 9% of wild-type."
FT /evidence="ECO:0000269|PubMed:18495664"
FT MUTAGEN 357
FT /note="R->Q: Activity is impaired to 3% of wild-type."
FT /evidence="ECO:0000269|PubMed:18495664"
SQ SEQUENCE 472 AA; 53177 MW; 9D2224C5A9FCC0A3 CRC64;
METNIVEVEN FVQQSEERRG SAFTQEVKRY LERYPNTQYV DVLLTDLNGC FRGKRIPVSS
LKKLEKGCYF PASVFAMDIL GNVVEEAGLG QEMGEPDRTC VPVLGSLTPS AADPEFIGQM
LLTMVDEDGA PFDVEPRNVL NRLWQQLRQR GLFPVVAVEL EFYLLDRQRD AEGYLQPPCA
PGTDDRNTQS QVYSVDNLNH FADVLNDIDE LAQLQLIPAD GAVAEASPGQ FEINLYHTDN
VLEACDDALA LKRLVRLMAE KHKMHATFMA KPYEEHAGSG MHIHISMQNN RGENVLSDAE
GEDSPLLKKM LAGMIDLMPS SMALLAPNVN SYRRFQPGMY VPTQASWGHN NRTVALRIPC
GDRHNHRVEY RVAGADANPY LVMAAIFAGI LHGLDNELPL QEEVEGNGLE QEGLPFPIRQ
SDALGEFIEN DHLRRYLGER FCHVYHACKN DELLQFERLI TETEIEWMLK NA
