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Database: UniProt
Entry: F4H5D7_CELFA
LinkDB: F4H5D7_CELFA
Original site: F4H5D7_CELFA 
ID   F4H5D7_CELFA            Unreviewed;       295 AA.
AC   F4H5D7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=haloalkane dehalogenase {ECO:0000256|ARBA:ARBA00012065};
DE            EC=3.8.1.5 {ECO:0000256|ARBA:ARBA00012065};
GN   OrderedLocusNames=Celf_3754 {ECO:0000313|EMBL:AEE47860.1};
OS   Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS   NCIMB 8980 / NCTC 7547).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE47860.1, ECO:0000313|Proteomes:UP000008460};
RN   [1] {ECO:0000313|EMBL:AEE47860.1, ECO:0000313|Proteomes:UP000008460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC   NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA   Woyke T.;
RT   "Complete sequence of Cellulomonas fimi ATCC 484.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-haloalkane + H2O = a halide anion + a primary alcohol +
CC         H(+); Xref=Rhea:RHEA:19081, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15734, ChEBI:CHEBI:16042, ChEBI:CHEBI:18060; EC=3.8.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001644};
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DR   EMBL; CP002666; AEE47860.1; -; Genomic_DNA.
DR   RefSeq; WP_013772883.1; NC_015514.1.
DR   AlphaFoldDB; F4H5D7; -.
DR   STRING; 590998.Celf_3754; -.
DR   KEGG; cfi:Celf_3754; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_13_3_11; -.
DR   OMA; HATVHEF; -.
DR   Proteomes; UP000008460; Chromosome.
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; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   PANTHER; PTHR43798:SF24; CIS-3-ALKYL-4-ALKYLOXETAN-2-ONE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AEE47860.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008460}.
FT   DOMAIN          35..272
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
SQ   SEQUENCE   295 AA;  32712 MW;  57153F7613DC7F00 CRC64;
     MTTRDWLDRT TYPWATRTLE VAGATVHLVE EGTGPTLLLL HGNPTWSYEW RDVIRHLRDD
     FRCVALDLPG LGLSTARPSF GGAPTDHARV VADVVAALDL RDWTLVAHDW GVPIGLAAAH
     RDPRRLGGLV VANSWAWPVD DDRHFTAFSR VMGGPLGRFG ARHANLVVRA MLPLGHRRRR
     LTRAELRHYR APLDTPDRRA ATSRFAREIV ASTDFLAGVA RALPDLADVP SLLLWADRDI
     AFREAELARW RAELPHADLV RLPGTGHFVP SDAPADVAAA IRAWHPALRT PATTR
//
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