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Database: UniProt
Entry: H5UUS4_9MICO
LinkDB: H5UUS4_9MICO
Original site: H5UUS4_9MICO 
ID   H5UUS4_9MICO            Unreviewed;       336 AA.
AC   H5UUS4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:GAB49482.1};
GN   ORFNames=MOPEL_130_00890 {ECO:0000313|EMBL:GAB49482.1};
OS   Mobilicoccus pelagius NBRC 104925.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC   Mobilicoccus.
OX   NCBI_TaxID=1089455 {ECO:0000313|EMBL:GAB49482.1, ECO:0000313|Proteomes:UP000004367};
RN   [1] {ECO:0000313|EMBL:GAB49482.1, ECO:0000313|Proteomes:UP000004367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 104925 {ECO:0000313|EMBL:GAB49482.1,
RC   ECO:0000313|Proteomes:UP000004367};
RA   Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Mobilicoccus pelagius NBRC 104925.";
RL   Submitted (FEB-2012) 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:GAB49482.1}.
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DR   EMBL; BAFE01000089; GAB49482.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5UUS4; -.
DR   STRING; 1089455.MOPEL_130_00890; -.
DR   eggNOG; COG0204; Bacteria.
DR   OrthoDB; 9808424at2; -.
DR   Proteomes; UP000004367; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
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   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:GAB49482.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004367};
KW   Transferase {ECO:0000313|EMBL:GAB49482.1}.
FT   DOMAIN          35..154
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          298..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   336 AA;  36029 MW;  5C83707722675B15 CRC64;
     MLYWFFKLVL IGPVLRVLFR PWVEGAEHVP AHGPAILASN HLSFSDSIFL PLMCPRRITF
     PAKSDYFTQP GLVGRLKKAF FQGTGQIPID RSGGAASKVA MDAGLAVLQR GELFGIYPEG
     TRSPDGRLYR GKTGIARLAL AAGVPIIPVA MIDTDKAQPT GQRIPTIMQV GMRFGPPMDF
     SEYADRADDH EVLREITDEV MAALQELSGQ EYVDEYAATV KEQLAARAND LLAAARAEGA
     NVQARASDLV ASAKAESATV QANVQARASD LVASAKAEGA QAQARAEELI QAARTEVEQR
     RRRRAASEGA TVADAAPVEA DGQDDVGDDG SSRTRP
//
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