ID A0A0A7IA89_9BIFI Unreviewed; 315 AA.
AC A0A0A7IA89;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acyl-phosphate glycerol 3-phosphate acyltransferase {ECO:0000313|EMBL:AIZ15734.1};
GN ORFNames=AH67_01260 {ECO:0000313|EMBL:AIZ15734.1};
OS Bifidobacterium pseudolongum PV8-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447715 {ECO:0000313|EMBL:AIZ15734.1, ECO:0000313|Proteomes:UP000030636};
RN [1] {ECO:0000313|EMBL:AIZ15734.1, ECO:0000313|Proteomes:UP000030636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV8-2 {ECO:0000313|EMBL:AIZ15734.1,
RC ECO:0000313|Proteomes:UP000030636};
RX PubMed=25614573;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Stevens M.J.,
RA Jans C.;
RT "Bifidobacterium pseudolongum Strain PV8-2, Isolated from a Stool Sample of
RT an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(2015).
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; CP007457; AIZ15734.1; -; Genomic_DNA.
DR RefSeq; WP_039171039.1; NZ_CP007457.1.
DR AlphaFoldDB; A0A0A7IA89; -.
DR STRING; 1447715.AH67_01260; -.
DR KEGG; bpsp:AH67_01260; -.
DR HOGENOM; CLU_027938_4_1_11; -.
DR OrthoDB; 9806008at2; -.
DR Proteomes; UP000030636; 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:AIZ15734.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030636};
KW Transferase {ECO:0000313|EMBL:AIZ15734.1}.
FT DOMAIN 88..212
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 315 AA; 35731 MW; 192BD35724F42C3A CRC64;
MASKGKPSPR SAVRPLSHAQ VAKLAAQYDL VDPTRPYPTG RIEPNEQEIN EQNPKLTGRL
MEGCAKVLRA SCRLRAWGLE NVPVDGPYIT AATHVTQFDV FVPMIAMFEM GRRPRYMAKA
EMGTWPIIGK WFRAVGMQPV PRRSGKARQI EEESISILTG GRPLTIWPEG TVTRDPQKWP
MSMKNGVGFI ALEASRRLGR QIPLYCAVTW GAASINHFWP WPRKNVVMCY DVRLDYSDLL
EDVDDWGPEP PVEYANELAR RIRVRMKNVM ANIRGEQPPK GFFDYRIMKE VPETEPFADP
HQVDARALAH AQPRA
//
