ID C9ZCS0_STRSW Unreviewed; 344 AA.
AC C9ZCS0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=SCAB_78951 {ECO:0000313|EMBL:CBG74859.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG74859.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG74859.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG74859.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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; FN554889; CBG74859.1; -; Genomic_DNA.
DR RefSeq; WP_013005309.1; NC_013929.1.
DR AlphaFoldDB; C9ZCS0; -.
DR STRING; 680198.SCAB_78951; -.
DR ESTHER; strsw-c9zcs0; A85-Mycolyl-transferase.
DR GeneID; 24308573; -.
DR KEGG; scb:SCAB_78951; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_026624_1_0_11; -.
DR Proteomes; UP000001444; 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; ENTEROCHELIN ESTERASE-RELATED; 1.
DR PANTHER; PTHR48098:SF7; SECRETED PROTEIN-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:UP000001444};
KW Transferase {ECO:0000313|EMBL:CBG74859.1}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 344 AA; 36009 MW; 047D7FD66B49C618 CRC64;
MTDPVNHSPR TGRRNGTTGS SRRSVTRAAA ATALAALVGA STARTAAAAT PGTAPRARTA
PVPGGRSVTR LGARTLDVSL PSAALGRNAP VRLILPSSFD ARPARTYPVL YLLHGAHDDH
TSWTRETDIE AFTAGRELIV AMPDAGPTGI PTAWRDGPDY ETFQVSEVPA LLARDYRASG
VRVVAGVSTG GYGAMAHAAR HPGTYAAAAS YSGILDTMAP GVPSLMDAIV DRENLAPRSL
WGNPILDLLT WRDFNPRSRA AGLRGTALYV SSGSGVVGGL GDWLPEALES LLWPSAHAFT
DTLALLRVPV TTHFYAGGGH GWAYWKREFG ASWPMLAGAL GVPA
//
