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Database: UniProt
Entry: S5Y8V1_PARAH
LinkDB: S5Y8V1_PARAH
Original site: S5Y8V1_PARAH 
ID   S5Y8V1_PARAH            Unreviewed;       284 AA.
AC   S5Y8V1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:AGT07778.1};
DE            EC=2.3.1.51 {ECO:0000313|EMBL:AGT07778.1};
GN   ORFNames=JCM7686_0669 {ECO:0000313|EMBL:AGT07778.1};
OS   Paracoccus aminophilus JCM 7686.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT07778.1, ECO:0000313|Proteomes:UP000015480};
RN   [1] {ECO:0000313|EMBL:AGT07778.1, ECO:0000313|Proteomes:UP000015480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT07778.1};
RX   PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA   Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA   Schluter A., Puhler A., Bartosik D.;
RT   "Architecture and functions of a multipartite genome of the methylotrophic
RT   bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT   chromids.";
RL   BMC Genomics 15:124-124(2014).
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DR   EMBL; CP006650; AGT07778.1; -; Genomic_DNA.
DR   RefSeq; WP_020949417.1; NC_022041.1.
DR   AlphaFoldDB; S5Y8V1; -.
DR   STRING; 1367847.JCM7686_0669; -.
DR   KEGG; pami:JCM7686_0669; -.
DR   PATRIC; fig|1367847.3.peg.620; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_0_1_5; -.
DR   OrthoDB; 9806880at2; -.
DR   Proteomes; UP000015480; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR23063:SF52; LYSOPHOSPHATIDYLCHOLINE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 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:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:AGT07778.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015480};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGT07778.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          97..212
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   284 AA;  31132 MW;  2D106386BA8C3138 CRC64;
     MSEAPRTAAT WLGDDQPAPL PRPSALGWAL VVLRGLPIIL TLVLGVLFLL PLRLIERLFT
     GPRRPVTGPW VQGVCRICLF FMGLRWRRVG RPMKGAGAAV ANHASWLDIL VLNAAMPVFF
     VSKSEVASWP GINILTRVTN THFVTRDPKL ARQQAEEFAE RTRAGHRLLF FPEGTSSDSQ
     RVLPFKPTLF QGFLDPALPP DLAIQPVTAC YQAPPGEDPR FYGWWGNLEL GPHLLAVLSR
     PRQGAVTVIL HPPIPVAGES RKTLSAKAEA AVRSGFLPDP KAKA
//
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