ID A0A3D9UZZ7_9MICO Unreviewed; 557 AA.
AC A0A3D9UZZ7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Putative phosphoserine phosphatase/1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000313|EMBL:REF31534.1};
GN ORFNames=DFJ65_2603 {ECO:0000313|EMBL:REF31534.1};
OS Calidifontibacter indicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Calidifontibacter.
OX NCBI_TaxID=419650 {ECO:0000313|EMBL:REF31534.1, ECO:0000313|Proteomes:UP000256253};
RN [1] {ECO:0000313|EMBL:REF31534.1, ECO:0000313|Proteomes:UP000256253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22967 {ECO:0000313|EMBL:REF31534.1,
RC ECO:0000313|Proteomes:UP000256253};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
CC {ECO:0000256|ARBA:ARBA00037183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:REF31534.1}.
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DR EMBL; QTUA01000001; REF31534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9UZZ7; -.
DR Proteomes; UP000256253; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.20.1440.100; SG protein - dephosphorylation function; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006385; HAD_hydro_SerB1.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR NCBIfam; TIGR01490; HAD-SF-IB-hyp1; 1.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF12710; HAD; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:REF31534.1};
KW Transferase {ECO:0000313|EMBL:REF31534.1}.
FT DOMAIN 265..387
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 479..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..515
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 59383 MW; ED310DC314DDCC94 CRC64;
MAGAAFFDLD RTLLRKASGP ALSRAMRESG VVSSKLPGES VLFWWMNAFG ETLGSIALAR
QAVLVAAGKP GGAFDDAARR AAQSLVDQIG PFAKILIAQH HEAGRKVVMA TTTPHHLIKP
LADALGFDDV IATRYQVGDD GLYNGKQDGR FVWSWGKLAS VKEWAREHDI DLSESFAYSD
SIYDVPLLGA VGNPGAVNPD PRLLVVAIAK RWPILSFEAP PGTLTFPVVN LEARRLAMML
TRPETFPYVR FEINGLENIP AEGAAILAGN HRSYFDMATM AVVMGRTGRG ASFLAKRELF
DVPLLGPVLR MLGGVRVDRD KRDPDAADPL EEAAVALAGG DLVGVMPQGT IPRGLDFFSD
TLEGYPGTAR LAAMSKAPVI PFAVSGTEVV WPRSSSTPNV LSFRNPPKIT VNIGTPVDLA
YDSEEADTER IMAAISRILP DDAKGLKATS IDQVASTYPG GRIPQQDLPD IERAIAANTA
KGRKATAKKA TAKAPAKKAT AKKTTAKKTT AKKTTAKKTA AKTPAKKTTA KRTAANTPAK
KTTTKKTSTR KTTGDAS
//
