IPUC_PSESP
ID IPUC_PSESP Reviewed; 459 AA.
AC Q936T0;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Glutamate--isopropylamine ligase;
DE EC=6.3.2.-;
DE AltName: Full=Gamma-glutamylisopropylamide synthetase;
DE Short=GIPA synthetase;
GN Name=ipuC;
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, AND SUBSTRATE SPECIFICITY.
RC STRAIN=KIE171;
RX PubMed=11976110; DOI=10.1128/aem.68.5.2368-2375.2002;
RA de Azevedo Waesch S.I., van der Ploeg J.R., Maire T., Lebreton A.,
RA Kiener A., Leisinger T.;
RT "Transformation of isopropylamine to L-alaninol by Pseudomonas sp. strain
RT KIE171 involves N-glutamylated intermediates.";
RL Appl. Environ. Microbiol. 68:2368-2375(2002).
CC -!- FUNCTION: Involved in the degradation of isopropylamine, which is a
CC constituent of the herbicides atrazine. Catalyzes the ATP-dependent
CC formation of gamma-glutamyl-isopropylamide from isopropylamine and L-
CC glutamate. It can also use aminoalkanes, amino-alcohols (L-alaninol and
CC D-alaninol) and amino-esters as substrates.
CC {ECO:0000269|PubMed:11976110}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + isopropylamine + L-glutamate = ADP + gamma-L-glutamyl-
CC isopropylamide + H(+) + phosphate; Xref=Rhea:RHEA:21048,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57492, ChEBI:CHEBI:85420,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:11976110};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to transform
CC isopropylamine to L-alaninol. {ECO:0000269|PubMed:11976110}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; AJ311159; CAC81335.1; -; Genomic_DNA.
DR AlphaFoldDB; Q936T0; -.
DR SMR; Q936T0; -.
DR BioCyc; MetaCyc:MON-13561; -.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:InterPro.
DR GO; GO:0019624; P:atrazine catabolic process to isopropylamine; IMP:UniProtKB.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
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 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; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding.
FT CHAIN 1..459
FT /note="Glutamate--isopropylamine ligase"
FT /id="PRO_0000428935"
FT DOMAIN 19..115
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 122..459
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ SEQUENCE 459 AA; 50586 MW; CBEF4392500A2436 CRC64;
MSEENKKQIL KVRDFIEKHN IDTIRLGAVD IDGVWRGKQV GAEYFLNKAA LDGTQISNIL
FGWDVADHLV DGLEFTGWDS GYPDIALIPD LSTLSLVPWQ EKTASVLCDI QHLNGEPLNL
SPRNLLRKAI EKAEQLGYKC YAAYEFEFYL LNDSIASISA DQWRSINPVE KSGHCYSMLH
HSSSSDIMGE VRKYMRDAGI VLEATNSEHG PGQYEINIKY DDALKAADDA IFVKNGIKEI
AAKHGMTATF MAKPSAEWSG SSGHVHMSLS DLAGTPVFAN PENPGALSEV GYNFLAGMVA
LAREMSAIYL PNINSYKRTA GASWAGGNSS WGFDNRTVSH RAITSAGSAA RVENRIPGAD
TNPYLVIAAS LLSGLYGIEN KLKPKDPILG NAYKVSPELA RPLAASLEEA AGIFRESEMA
RVIFPNEFVE HYAQMKVWEI KQSNSFVNNW ELARYLDII
