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Database: UniProt
Entry: D0LZ00_HALO1
LinkDB: D0LZ00_HALO1
Original site: D0LZ00_HALO1 
ID   D0LZ00_HALO1            Unreviewed;       282 AA.
AC   D0LZ00;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:ACY14470.1};
GN   OrderedLocusNames=Hoch_1923 {ECO:0000313|EMBL:ACY14470.1};
OS   Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC   Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX   NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY14470.1, ECO:0000313|Proteomes:UP000001880};
RN   [1] {ECO:0000313|EMBL:ACY14470.1, ECO:0000313|Proteomes:UP000001880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC   {ECO:0000313|Proteomes:UP000001880};
RX   PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA   Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA   Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA   Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL   Stand. Genomic Sci. 2:96-106(2010).
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};
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DR   EMBL; CP001804; ACY14470.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0LZ00; -.
DR   STRING; 502025.Hoch_1923; -.
DR   KEGG; hoh:Hoch_1923; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_986147_0_0_7; -.
DR   Proteomes; UP000001880; Chromosome.
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:ACY14470.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW   Transferase {ECO:0000313|EMBL:ACY14470.1}.
FT   DOMAIN          59..191
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   282 AA;  32155 MW;  2D19ADA1876C2171 CRC64;
     MERVALSLGR FVNERSIPKR LQDRYLHAVT KTWVRPAIGS RVYVDGIDWL RDLEPERGVM
     LVANHRSFFD LYLVMLAMHD SGAEWIERMF FPVRSNFFYE KALGVALNMF VGGGSMYPPI
     FRDRSKRSLN RDSVDRVIRF LQQPGTVIGM HPEGTRGKGP DPYELLPAQP GAGQIMLQAR
     PIVVPLFING LSNDIPSALG DTYRKNARRE NPIIISFGQA FDYSEFLTQK PRATLYKRCA
     DLLLNEVRTL GERERGLRAA CTVGEIDDSD PAWLRNRLAA RR
//
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