ID H6MU85_GORPV Unreviewed; 319 AA.
AC H6MU85;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=GPOL_c04920 {ECO:0000313|EMBL:AFA71562.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA71562.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA71562.1, ECO:0000313|Proteomes:UP000009154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA Liebl W., Daniel R., Steinbuchel A.;
RT "Involvement of two latex-clearing proteins during rubber degradation and
RT insights into the subsequent degradation pathway revealed by the genome
RT sequence of Gordonia polyisoprenivorans strain VH2.";
RL Appl. Environ. Microbiol. 78:2874-2887(2012).
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; CP003119; AFA71562.1; -; Genomic_DNA.
DR RefSeq; WP_006369317.1; NC_016906.1.
DR AlphaFoldDB; H6MU85; -.
DR STRING; 1112204.GPOL_c04920; -.
DR KEGG; gpo:GPOL_c04920; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_026624_0_0_11; -.
DR Proteomes; UP000009154; 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 PANTHER; PTHR48098:SF1; DIACYLGLYCEROL ACYLTRANSFERASE_MYCOLYLTRANSFERASE AG85A; 1.
DR PANTHER; PTHR48098; ENTEROCHELIN ESTERASE-RELATED; 1.
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:UP000009154};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..319
FT /note="Acyl-CoA:diacylglycerol acyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003604340"
SQ SEQUENCE 319 AA; 34224 MW; B3B86868111A665B CRC64;
MLTRARKRLV AGMVALAAVA GVTTVAAPAA HAANGCGVEN VYSAAMHRSV PVCIVDGGGG
GPKPTLYLLD GLRAPNNNSG WLINTDVARW MGGKGTNVVI PFGGGGSFYT DWERPDPKLG
INKWETFLTR ELPAYMAKQH NSDNKRNGIA GLSMSGTSAL NLASRHPNFY KAVASYSGYP
TVTMPGFTQG IQASVSTMGG DPNNMWGFYP AGEWFQNDPF LSAGNLSGHR VFISAGTGMG
SRYDSSITPG SPNFNAVHFA QMVPLEVAAS TSSQIYIARL RTLPIQLTTR ITPDGDHWWD
YWQADFKQSW GSTFAPAFF
//
