ATDA1_ACISP
ID ATDA1_ACISP Reviewed; 500 AA.
AC Q44249;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Gamma-glutamylanilide synthase {ECO:0000303|PubMed:23893114};
DE Short=Gamma-GA {ECO:0000303|PubMed:23893114};
DE EC=6.3.1.18 {ECO:0000269|PubMed:23893114};
DE AltName: Full=Glutamine synthetase-like protein {ECO:0000303|PubMed:23893114};
GN Name=atdA1 {ECO:0000303|PubMed:23893114};
OS Acinetobacter sp.
OG Plasmid pYA1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=472;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YAA; PLASMID=pYA1;
RA Fujii T., Takeo M., Maeda Y.;
RT "Plasmid-encoded genes specifying aniline oxidation from Acinetobacter sp.
RT strain YAA.";
RL Microbiology (Mosc.) 143:93-99(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YAA; PLASMID=pYA1;
RA Takeo M., Fujii T., Maeda Y.;
RT "Sequence analysis of the genes encoding a multicomponent dioxygenase
RT involved in oxidation of aniline and o-toluidine in Acinetobacter sp.
RT strain YAA.";
RL J. Ferment. Bioeng. 85:17-24(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=YAA; PLASMID=pYA1;
RX PubMed=23893114; DOI=10.1128/jb.00397-13;
RA Takeo M., Ohara A., Sakae S., Okamoto Y., Kitamura C., Kato D., Negoro S.;
RT "Function of a glutamine synthetase-like protein in bacterial aniline
RT oxidation via gamma-glutamylanilide.";
RL J. Bacteriol. 195:4406-4414(2013).
CC -!- FUNCTION: Involved in the initial oxidation of aniline to catechol by
CC the release of its amino group. Catalyzes the ATP-dependent ligation of
CC L-glutamate to aniline to yield gamma-glutamylanilide. AtdA1 has a
CC broad substrate range and is able to convert the following anilines:
CC aniline (100%), o-chloroaniline (92%), m-chloroaniline (69%), p-
CC chloroaniline (92%), o-methylaniline (40%), m-methylaniline (27%), and
CC p-methylaniline (45%). It can also accept chlorinated and methylated
CC forms of aniline, preferably in the o- and p-positions.
CC {ECO:0000269|PubMed:23893114}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aniline + ATP + L-glutamate = ADP + N(5)-phenyl-L-glutamine +
CC phosphate; Xref=Rhea:RHEA:41648, ChEBI:CHEBI:17296,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:78375, ChEBI:CHEBI:456216; EC=6.3.1.18;
CC Evidence={ECO:0000269|PubMed:23893114};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between 8 and 10. {ECO:0000269|PubMed:23893114};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:23893114};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:23893114}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; D86080; BAA13010.1; -; Genomic_DNA.
DR AlphaFoldDB; Q44249; -.
DR SMR; Q44249; -.
DR KEGG; ag:BAA13010; -.
DR BioCyc; MetaCyc:MON-15722; -.
DR GO; GO:0016880; F:acid-ammonia (or amide) 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: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; Plasmid.
FT CHAIN 1..500
FT /note="Gamma-glutamylanilide synthase"
FT /id="PRO_0000435684"
FT DOMAIN 32..136
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 143..500
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ SEQUENCE 500 AA; 54993 MW; DAFBF5AA25917D8B CRC64;
MSEKLDFITK NNLWTDKQRD AADKVLAEID SLGLEMIRLS WADQYGLLRG KALSVAALKA
AFSEGSEVTM APFSFNLVSE WVFNPFTAGG GFGIDEFDEL GGVPSVVMVP DPTTFKVLPW
ADKTGWMLAD LHWKSGEPFP LCPRGIMKKA VKSLSDEGYL FKCGIELEWY LTKIVDRSLS
PESLGAPGVQ PDAIQVQPVA QGYSYLLEYH LDQVDDIMSK VRKGLLELNL PLRSIEDELA
PSQMETTFDV MEGLEAADAA LLIKSAIKQI CSRHGYHATF MCKPAINGFS VASGWHMHQS
LVDKDTRKNL FIPSEGEVVS PLGRAYAGGL LANGSAASSF TTPTVNGYRR RQPHSLAPDR
RAWAKENKAA MVRVISATGD PASRIENRIG EPGANPYLYM ASQIVSGLDG IKIKRDPGGL
QGAPYGAQVP MLPTALAEAL DALEHDSELF RSCFGDTFIK YWLQLRRSEW ARFLDAEGAE
AAEPTGAVTQ WEQKEYFNLL
