ID D5UF10_CELFN Unreviewed; 237 AA.
AC D5UF10;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:ADG74820.1};
GN OrderedLocusNames=Cfla_1925 {ECO:0000313|EMBL:ADG74820.1};
OS Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS 18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG74820.1, ECO:0000313|Proteomes:UP000000849};
RN [1] {ECO:0000313|EMBL:ADG74820.1, ECO:0000313|Proteomes:UP000000849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX PubMed=21304688; DOI=10.4056/sigs.1012662;
RA Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL Stand. Genomic Sci. 3:15-25(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; CP001964; ADG74820.1; -; Genomic_DNA.
DR AlphaFoldDB; D5UF10; -.
DR STRING; 446466.Cfla_1925; -.
DR KEGG; cfl:Cfla_1925; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_2_11; -.
DR OrthoDB; 9808424at2; -.
DR Proteomes; UP000000849; 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:ADG74820.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000849};
KW Transferase {ECO:0000313|EMBL:ADG74820.1}.
FT DOMAIN 55..164
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 237 AA; 25200 MW; C3E2A51A4607DBEB CRC64;
MTGVRRTTSA RDATAPHVPS AAGPAWSRWI GRFLARVVWD TRVVGAERVP RTGALVLAAN
HVTLLDGPLF IGVAPRPLHI LVKAEMFRGP LGWLLRAAGQ IPVDRTMGRP ALQSALGVLR
RGHAVGIFPE GTRGRGTAEQ VRAGAAWLAV HGGARVVPVA ILGTRRTGES PHGLPGPRRR
LVVEFGEPLD VTVEGLSRRE AIDRAAVAIR DAMAELVVAA QERTGISLPA DDPRAID
//
