AHLLB_AGRFC
ID AHLLB_AGRFC Reviewed; 276 AA.
AC A9CKY2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=N-acyl homoserine lactonase AiiB {ECO:0000303|PubMed:17900178};
DE Short=AHL-lactonase AiiB {ECO:0000303|PubMed:17900178};
DE EC=3.1.1.81;
GN Name=aiiB {ECO:0000312|EMBL:AAK91031.1}; OrderedLocusNames=Atu6071;
GN ORFNames=AGR_pTi_140;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OG Plasmid pTiC58 {ECO:0000305, ECO:0000312|EMBL:AAK91031.1}.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1] {ECO:0000312|EMBL:AAK91031.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ZINC, CATALYTIC
RP ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17900178; DOI=10.1021/bi7012849;
RA Liu D., Thomas P.W., Momb J., Hoang Q.Q., Petsko G.A., Ringe D., Fast W.;
RT "Structure and specificity of a quorum-quenching lactonase (AiiB) from
RT Agrobacterium tumefaciens.";
RL Biochemistry 46:11789-11799(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
CC + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81;
CC Evidence={ECO:0000269|PubMed:17900178};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17900178};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:17900178};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 mM for N-butyryl-(RS)-homoserine lactone (with zinc as
CC cofactor) {ECO:0000269|PubMed:17900178};
CC KM=1.6 mM for N-hexanoyl-(S)-homoserine lactone (with zinc as
CC cofactor) {ECO:0000269|PubMed:17900178};
CC KM=4.6 mM for N-(beta-ketocaproyl)-(RS)-homoserine lactone (with zinc
CC as cofactor) {ECO:0000269|PubMed:17900178};
CC KM=1.0 mM for N-octanoyl-(S)-homoserine lactone (with zinc as
CC cofactor) {ECO:0000269|PubMed:17900178};
CC KM=2.5 mM for N-(3-oxo-octanoyl)-(S)-homoserine lactone (with zinc as
CC cofactor) {ECO:0000269|PubMed:17900178};
CC KM=0.11 mM for N-decanoyl-(S)-homoserine lactone (with zinc as
CC cofactor) {ECO:0000269|PubMed:17900178};
CC KM=7.7 mM for N-t-butyloxycarbonyl-(RS)-homoserine lactone (with zinc
CC as cofactor) {ECO:0000269|PubMed:17900178};
CC KM=0.77 mM for N-carbobenzyloxy-(S)-homoserine lactone (with zinc as
CC cofactor) {ECO:0000269|PubMed:17900178};
CC KM=5.9 mM for N-hexanoyl-(S)-homoserine lactone (with cobalt as
CC cofactor) {ECO:0000269|PubMed:17900178};
CC KM=7.3 mM for N-(beta-ketocaproyl)-(RS)-homoserine lactone (with
CC cobalt as cofactor) {ECO:0000269|PubMed:17900178};
CC KM=7.0 mM for N-(3-oxo-octanoyl)-(S)-homoserine lactone (with cobalt
CC as cofactor) {ECO:0000269|PubMed:17900178};
CC KM=1.6 mM for N-carbobenzyloxy-(S)-homoserine lactone (with cobalt as
CC cofactor) {ECO:0000269|PubMed:17900178};
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; AE007871; AAK91031.1; -; Genomic_DNA.
DR PIR; AE3236; AE3236.
DR RefSeq; NP_396590.1; NC_003065.3.
DR RefSeq; WP_010974862.1; NC_003065.3.
DR PDB; 2R2D; X-ray; 1.75 A; A/B/C/D/E/F=1-276.
DR PDBsum; 2R2D; -.
DR AlphaFoldDB; A9CKY2; -.
DR SMR; A9CKY2; -.
DR EnsemblBacteria; AAK91031; AAK91031; Atu6071.
DR KEGG; atu:Atu6071; -.
DR PATRIC; fig|176299.10.peg.5278; -.
DR HOGENOM; CLU_030571_3_2_5; -.
DR OMA; GMMTYQH; -.
DR PhylomeDB; A9CKY2; -.
DR BioCyc; AGRO:ATU6071-MON; -.
DR EvolutionaryTrace; A9CKY2; -.
DR Proteomes; UP000000813; Plasmid Ti.
DR GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Plasmid; Reference proteome; Zinc.
FT CHAIN 1..276
FT /note="N-acyl homoserine lactonase AiiB"
FT /id="PRO_0000405125"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17900178"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17900178"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17900178"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17900178"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17900178"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17900178"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17900178"
FT STRAND 4..16
FT /evidence="ECO:0007829|PDB:2R2D"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 38..49
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2R2D"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:2R2D"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:2R2D"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:2R2D"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2R2D"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:2R2D"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2R2D"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 182..201
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:2R2D"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:2R2D"
FT HELIX 234..250
FT /evidence="ECO:0007829|PDB:2R2D"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:2R2D"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:2R2D"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:2R2D"
SQ SEQUENCE 276 AA; 30562 MW; 6AD213ADB02C7DA3 CRC64;
MGNKLFVLDL GEIRVDENFI IANSTFVTPQ KPTVSSRLID IPVSAYLIQC TDATVLYDTG
CHPECMGTNG RWPAQSQLNA PYIGASECNL PERLRQLGLS PDDISTVVLS HLHNDHAGCV
EYFGKSRLIA HEDEFATAVR YFATGDHSSP YIVKDIEAWL ATPRNWDLVG RDERERELAP
GVNLLNFGTG HASGMLGLAV RLEKQPGFLL VSDACYTATN YGPPARRAGV LHDTIGYDRT
VSHIRQYAES RSLTVLFGHD REQFASLIKS TDGFYE
