ID I4VNU4_9GAMM Unreviewed; 262 AA.
AC I4VNU4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acyltransferase family protein {ECO:0000313|EMBL:EIL88885.1};
GN ORFNames=UU9_11595 {ECO:0000313|EMBL:EIL88885.1};
OS Rhodanobacter fulvus Jip2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL88885.1, ECO:0000313|Proteomes:UP000004210};
RN [1] {ECO:0000313|EMBL:EIL88885.1, ECO:0000313|Proteomes:UP000004210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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}.
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:EIL88885.1}.
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DR EMBL; AJXU01000044; EIL88885.1; -; Genomic_DNA.
DR AlphaFoldDB; I4VNU4; -.
DR STRING; 1163408.UU9_11595; -.
DR PATRIC; fig|1163408.3.peg.2370; -.
DR eggNOG; COG0204; Bacteria.
DR OrthoDB; 9812274at2; -.
DR Proteomes; UP000004210; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:EIL88885.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000004210};
KW Transferase {ECO:0000313|EMBL:EIL88885.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..202
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 262 AA; 29071 MW; 0ACD02EF73D66970 CRC64;
MAVAAHLMHR RRDAWLWRLL ATGASFAVFG IGGVILRVLI LPMFALLPGG PLARRRRARA
AISRAFHLHV QFMYRTRVLD FRIDGAERLG RPGQLVVANH PSLIDVVFLI SQMRDTNCVV
KASLWSNPCM HGAVRAAQYI SNNGSPEMLE QAANVLRGGE TLVMFPEGTR TTPGQPPVFH
RGAAAIALRG ARTITPVFIS VAPTTLTKAE PWYHIPWRRV MVHLRVGDDI DPASFDNAPM
PIASRRLNQH LHHLFLQGLD AP
//
