ID   A5VY00_PSEP1            Unreviewed;       368 AA.
AC   A5VY00;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Alpha/beta hydrolase fold protein {ECO:0000313|EMBL:ABQ76760.1};
GN   OrderedLocusNames=Pput_0592 {ECO:0000313|EMBL:ABQ76760.1};
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ76760.1};
RN   [1] {ECO:0000313|EMBL:ABQ76760.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F1 {ECO:0000313|EMBL:ABQ76760.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938};
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DR   EMBL; CP000712; ABQ76760.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5VY00; -.
DR   ESTHER; psepu-acoc; AcoC_BiotinLipoyl-ABH.
DR   KEGG; ppf:Pput_0592; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_13_2_6; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR   PANTHER; PTHR43798:SF33; SERINE HYDROLASE-LIKE PROTEIN DDB_G0286239; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABQ76760.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823}.
FT   DOMAIN          4..79
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   368 AA;  39528 MW;  513B113BA951A2F4 CRC64;
     MSQIHTLTMP KWGLSMTEGR VDTWLKQEGD EISKGDEVLD VETDKISSSV EAPFSGVLRR
     QVAKPDETLP VGALLAVVVE GEAEESEIDA VVQRFQAEFV AEGGADQSQG PAPQKAEVGG
     RLLRWFELGE GGTPLVLVHG FGGDLNNWLF NHPALAAERR VIALDLPGHG ESAKALQRGD
     LDELSETVLA LLDHLDIAKA HLAGHSMGGA VSLNVARLAP QRVASLSLVA SAGLGEAING
     QYLQGFVTAA NRNALKPQMV QLFADPALVT RQMLEDMLKF KRLEGVDQAL QQLARALADG
     DRQRHDLRGV LGNHPALVVW GGKDAIIPAS HAEGLEAEVL VLPEAGHMVQ MEAAEQVNQQ
     LLAFLRKH
//