ID A0A126RG76_9SPHN Unreviewed; 231 AA.
AC A0A126RG76;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:AMK21064.1};
GN ORFNames=K426_00500 {ECO:0000313|EMBL:AMK21064.1};
OS Sphingobium sp. TKS.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1315974 {ECO:0000313|EMBL:AMK21064.1, ECO:0000313|Proteomes:UP000060779};
RN [1] {ECO:0000313|Proteomes:UP000060779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKS {ECO:0000313|Proteomes:UP000060779};
RA Tabata M.;
RT "Whole genome sequence of gamma-HCH degrading bacterium Sphingobium sp.
RT TKS.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMK21064.1, ECO:0000313|Proteomes:UP000060779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKS {ECO:0000313|EMBL:AMK21064.1,
RC ECO:0000313|Proteomes:UP000060779};
RX PubMed=27056231;
RA Tabata M., Ohhata S., Kawasumi T., Nikawadori Y., Kishida K., Sato T.,
RA Ohtsubo Y., Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of a gamma-Hexachlorocyclohexane Degrader,
RT Sphingobium sp. Strain TKS, Isolated from a gamma-Hexachlorocyclohexane-
RT Degrading Microbial Community.";
RL Genome Announc. 4:0-0(2016).
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 -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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DR EMBL; CP005083; AMK21064.1; -; Genomic_DNA.
DR RefSeq; WP_066552962.1; NZ_CP005083.1.
DR AlphaFoldDB; A0A126RG76; -.
DR STRING; 1315974.K426_00500; -.
DR KEGG; spht:K426_00500; -.
DR PATRIC; fig|1315974.3.peg.103; -.
DR OrthoDB; 5290997at2; -.
DR Proteomes; UP000060779; Chromosome 1.
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:AMK21064.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000060779};
KW Transferase {ECO:0000313|EMBL:AMK21064.1}.
FT DOMAIN 70..184
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 231 AA; 25212 MW; DBEF53B42391B078 CRC64;
MFTALRSLAF MLVFYVGSLL FVLAAMASNL VAPRSIPAVA THWSRFHRRC ARWLLGQKVR
VEGTLENGPY LYILKHESMF ETIDLLCLLD RPAIAAKREL FDIPLWGGIA RRYGLIPIER
TAGASALRAL RTAARATTAQ GRAVCLFPEG TRVPHGESPP LRAGFAGLYA LLGLPVVPIA
VDSGRVSPRG KFMKRPGTIT YKVGEIVPPG LDRREAEARV HAAINALNAS V
//