ID   D2J2T6_9HYPH            Unreviewed;       271 AA.
AC   D2J2T6;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Alpha/beta hydrolase fold protein {ECO:0000313|EMBL:ACZ73823.1};
GN   Name=aidH {ECO:0000313|EMBL:ACZ73823.1};
OS   Ochrobactrum sp. T63.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Ochrobactrum.
OX   NCBI_TaxID=680275 {ECO:0000313|EMBL:ACZ73823.1};
RN   [1] {ECO:0000313|EMBL:ACZ73823.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T63 {ECO:0000313|EMBL:ACZ73823.1};
RX   PubMed=20525860; DOI=10.1128/AEM.00477-10;
RA   Mei G.Y., Yan X.X., Turak A., Luo Z.Q., Zhang L.Q.;
RT   "AidH, an alpha/beta-hydrolase fold family member from an Ochrobactrum sp.
RT   strain, is a novel N-acylhomoserine lactonase.";
RL   Appl. Environ. Microbiol. 76:4933-4942(2010).
RN   [2] {ECO:0007829|PDB:4G5X, ECO:0007829|PDB:4G8B}
RP   X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS).
RX   PubMed=23275166; DOI=10.1107/S0907444912042369;
RA   Gao A., Mei G.Y., Liu S., Wang P., Tang Q., Liu Y.P., Wen H., An X.M.,
RA   Zhang L.Q., Yan X.X., Liang D.C.;
RT   "High-resolution structures of AidH complexes provide insights into a novel
RT   catalytic mechanism for N-acyl homoserine lactonase.";
RL   Acta Crystallogr. D 69:82-91(2013).
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DR   EMBL; GQ849010; ACZ73823.1; -; Genomic_DNA.
DR   PDB; 4G5X; X-ray; 1.29 A; A/B=1-271.
DR   PDB; 4G8B; X-ray; 1.30 A; A/B=1-271.
DR   PDB; 4G8C; X-ray; 1.11 A; A/B=1-271.
DR   PDB; 4G8D; X-ray; 1.35 A; A/B=1-271.
DR   PDB; 4G9E; X-ray; 1.09 A; A/B=1-271.
DR   PDB; 4G9G; X-ray; 1.35 A; A/B=1-271.
DR   PDBsum; 4G5X; -.
DR   PDBsum; 4G8B; -.
DR   PDBsum; 4G8C; -.
DR   PDBsum; 4G8D; -.
DR   PDBsum; 4G9E; -.
DR   PDBsum; 4G9G; -.
DR   AlphaFoldDB; D2J2T6; -.
DR   SMR; D2J2T6; -.
DR   ESTHER; 9rhiz-d2j2t6; AHL-acylase.
DR   BRENDA; 3.1.1.81; 14527.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IMP:CACAO.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4G5X, ECO:0007829|PDB:4G8B};
KW   Hydrolase {ECO:0000313|EMBL:ACZ73823.1}.
FT   DOMAIN          26..253
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
SQ   SEQUENCE   271 AA;  29549 MW;  992896298C1E9BEB CRC64;
     MTINYHELET SHGRIAVRES EGEGAPLLMI HGNSSSGAIF APQLEGEIGK KWRVIAPDLP
     GHGKSTDAID PDRSYSMEGY ADAMTEVMQQ LGIADAVVFG WSLGGHIGIE MIARYPEMRG
     LMITGTPPVA REEVGQGFKS GPDMALAGQE IFSERDVESY ARSTCGEPFE ASLLDIVART
     DGRARRIMFE KFGSGTGGNQ RDIVAEAQLP IAVVNGRDEP FVELDFVSKV KFGNLWEGKT
     HVIDNAGHAP FREAPAEFDA YLARFIRDCT Q
//