ID B1YRF9_BURA4 Unreviewed; 371 AA.
AC B1YRF9;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Alpha/beta hydrolase fold protein {ECO:0000313|EMBL:ACB64233.1};
GN OrderedLocusNames=BamMC406_1748 {ECO:0000313|EMBL:ACB64233.1};
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB64233.1, ECO:0000313|Proteomes:UP000001680};
RN [1] {ECO:0000313|Proteomes:UP000001680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680};
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) 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; CP001025; ACB64233.1; -; Genomic_DNA.
DR RefSeq; WP_012364012.1; NC_010551.1.
DR AlphaFoldDB; B1YRF9; -.
DR ESTHER; burcm-q0beu2; AcoC_BiotinLipoyl-ABH.
DR KEGG; bac:BamMC406_1748; -.
DR HOGENOM; CLU_020336_13_2_4; -.
DR OrthoDB; 8562572at2; -.
DR Proteomes; UP000001680; Chromosome 1.
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; PTHR43194; HYDROLASE ALPHA/BETA FOLD FAMILY; 1.
DR PANTHER; PTHR43194:SF2; PEROXISOMAL MEMBRANE PROTEIN LPX1; 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:ACB64233.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 371 AA; 38963 MW; B11D1352A821663B CRC64;
MSIHMITMPK WGLSMEQGQV NGWLKAIGER VSKGDEVLDV ETDKISSGVE CAFDGTLRRQ
VAQEGETLPV GALLGVVAAA DASDADIDAA IAEFQRDFTP SAAADDAGGP QPEKAQIGGR
TIRFLKLGDG TGTPAVLIHG FGGDLNNWLF NHAELAAHRP VWALDLPGHG ESAKAVDTGS
LDELADAVLA LLDAQHIGRA HLIGHSMGGA VAMAAAERAP QRVASLTLIA SAGLGADINR
GYIDGFVAGN SRNTLKPHLG ALFADHALVT RQLVEDLVKY KRLEGVQAAL EKIANAAFDG
AAQRRVFRDR VASLAPRTLV IWGERDEVIP AQHAQGLPDG VQAEVIAGSG HMVQMEAAAD
VNRLIVAFLG D
//
