ID C6WQ55_ACTMD Unreviewed; 302 AA.
AC C6WQ55;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Acyl-CoA:diacylglycerol acyltransferase {ECO:0000256|ARBA:ARBA00032572};
DE EC=2.3.1.122 {ECO:0000256|ARBA:ARBA00012820};
DE EC=2.3.1.20 {ECO:0000256|ARBA:ARBA00013244};
GN OrderedLocusNames=Amir_1156 {ECO:0000313|EMBL:ACU35111.1};
OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinosynnema.
OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU35111.1, ECO:0000313|Proteomes:UP000002213};
RN [1] {ECO:0000313|EMBL:ACU35111.1, ECO:0000313|Proteomes:UP000002213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX PubMed=21304636; DOI=10.4056/sigs.21137;
RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL Stand. Genomic Sci. 1:46-53(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose
CC 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234;
CC EC=2.3.1.122; Evidence={ECO:0000256|ARBA:ARBA00000697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00001039};
CC -!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
CC {ECO:0000256|ARBA:ARBA00005874}.
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DR EMBL; CP001630; ACU35111.1; -; Genomic_DNA.
DR RefSeq; WP_015800001.1; NC_013093.1.
DR AlphaFoldDB; C6WQ55; -.
DR STRING; 446462.Amir_1156; -.
DR ESTHER; actmd-c6wq55; A85-Feruloyl-Esterase.
DR KEGG; ami:Amir_1156; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_059519_1_0_11; -.
DR OrthoDB; 3210113at2; -.
DR Proteomes; UP000002213; Chromosome.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050348; F:trehalose O-mycolyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..302
FT /note="Acyl-CoA:diacylglycerol acyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002973169"
FT REGION 35..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 32144 MW; 9EF1384EBB24E1ED CRC64;
MVSRRAVLGA LGALGALGAG AAGVSAALGG EEPLPPRANQ AVAGGAMSTP KGGSNGFKPA
VRRLLVQSER LFSAQRGKEI TFLTVAPPGV ETLKLPMVLL LHGLYGKAQD ALVGNLPDVL
VSAVAKGAVP PFGFVSVDGD NNYWHENVAG DDPMGMLLEE VPRWLADRGF SRPVACAGVS
MGGFGALLYA RRKLERKERI KAVAAISPGL LTSWTEMSKR KAFQDVGQWE SLDPLRHPDK
LKNLPVGVWV GDRDPFIEGT RKFIQTVRPE VGSVTPGGHN DEFYKTITPD VVRFLGKQLS
TT
//
