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Database: UniProt
Entry: O06441_RHOSO
LinkDB: O06441_RHOSO
Original site: O06441_RHOSO 
ID   O06441_RHOSO            Unreviewed;       322 AA.
AC   O06441;
DT   01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Heroin esterase {ECO:0000313|EMBL:AAC45283.1};
GN   Name=her {ECO:0000313|EMBL:AAC45283.1};
OS   Rhodococcus sp.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1831 {ECO:0000313|EMBL:AAC45283.1};
RN   [1] {ECO:0000313|EMBL:AAC45283.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H1 {ECO:0000313|EMBL:AAC45283.1};
RX   PubMed=9143135;
RA   Rathbone D.A., Holt P.J., Lowe C.R., Bruce N.C.;
RT   "Molecular analysis of the Rhodococcus sp. strain H1 her gene and
RT   characterization of its product, a heroin esterase, expressed in
RT   Escherichia coli.";
RL   Appl. Environ. Microbiol. 63:2062-2066(1997).
RN   [2] {ECO:0007829|PDB:1LZK, ECO:0007829|PDB:1LZL}
RP   X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 1-307.
RX   PubMed=12421810; DOI=10.1074/jbc.M210103200;
RA   Zhu X., Larsen N.A., Basran A., Bruce N.C., Wilson I.A.;
RT   "Observation of an arsenic adduct in an acetyl esterase crystal
RT   structure.";
RL   J. Biol. Chem. 278:2008-2014(2003).
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DR   EMBL; U70619; AAC45283.1; -; Genomic_DNA.
DR   PDB; 1LZK; X-ray; 1.45 A; A=1-307.
DR   PDB; 1LZL; X-ray; 1.30 A; A=1-307.
DR   PDBsum; 1LZK; -.
DR   PDBsum; 1LZL; -.
DR   AlphaFoldDB; O06441; -.
DR   SMR; O06441; -.
DR   ESTHER; rhosp-hercx; Hormone-sensitive_lipase_like.
DR   EvolutionaryTrace; O06441; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   PANTHER; PTHR48081:SF31; ALPHA_BETA HYDROLASE FOLD-3 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1LZK, ECO:0007829|PDB:1LZL}.
FT   DOMAIN          82..292
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
SQ   SEQUENCE   322 AA;  34240 MW;  93B01D5C760B4A1E CRC64;
     MTTFPTLDPE LAAALTMLPK VDFADLPNAR ATYDALIGAM LADLSFDGVS LRELSAPGLD
     GDPEVKIRFV TPDNTAGPVP VLLWIHGGGF AIGTAESSDP FCVEVARELG FAVANVEYRL
     APETTFPGPV NDCYAALLYI HAHAEELGID PSRIAVGGES AGGGLAAGTV LKARDEGVVP
     VAFQFLEIPE LDDRLETVSM TNFVDTPLWH RPNAILSWKY YLGESYSGPE DPDVSIYAAP
     SRATDLTGLP PTYLSTMELD PLRDEGIEYA LRLLQAGVSV ELHSFPGTFH GSALVATAGV
     RERGAAKPHC DPERVAFAVA VS
//
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