ID F5XRW4_MICPN Unreviewed; 260 AA.
AC F5XRW4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:BAK37177.1};
GN OrderedLocusNames=MLP_41630 {ECO:0000313|EMBL:BAK37177.1};
OS Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK37177.1, ECO:0000313|Proteomes:UP000007947};
RN [1] {ECO:0000313|EMBL:BAK37177.1, ECO:0000313|Proteomes:UP000007947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA Yamazaki S., Fujita N.;
RT "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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; AP012204; BAK37177.1; -; Genomic_DNA.
DR RefSeq; WP_013865014.1; NC_015635.1.
DR AlphaFoldDB; F5XRW4; -.
DR STRING; 1032480.MLP_41630; -.
DR KEGG; mph:MLP_41630; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_0_11; -.
DR OrthoDB; 9808424at2; -.
DR Proteomes; UP000007947; 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:BAK37177.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007947};
KW Transferase {ECO:0000313|EMBL:BAK37177.1}.
FT DOMAIN 35..155
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 260 AA; 28127 MW; D2E42D9F185EB522 CRC64;
MFYWIFKWSL FVPVVRLIWR PKVTGLENVP DSGPAIVVCN HTSAVETFIV PAMISRRLTF
PAKAELFTQG GGIGKRIVAW FLAAVGQLPM DRSGGRASAG SMDGVLQVLK NGELLAIFPE
GTRSPDGRLY KGKTGVARLV LQAKVPVIPI GIRDSVARRT KRLGIPYYPR TKISIGPPIE
FDRYAAAATD RNVIRYVTDE IMAAVQAQSG QEYVDAYAAS VKSALAEGRQ LPSAVVVARP
GLGRPVPPVP GDEQVQDEAS
//
