ID A0A0N9UXT3_SPHMC Unreviewed; 783 AA.
AC A0A0N9UXT3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432};
DE EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113};
GN ORFNames=AN936_15740 {ECO:0000313|EMBL:ALH81754.1};
OS Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH81754.1, ECO:0000313|Proteomes:UP000058074};
RN [1] {ECO:0000313|EMBL:ALH81754.1, ECO:0000313|Proteomes:UP000058074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EY-1 {ECO:0000313|EMBL:ALH81754.1,
RC ECO:0000313|Proteomes:UP000058074};
RX PubMed=26634754;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL Genome Announc. 3:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000510};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004765}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
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DR EMBL; CP012700; ALH81754.1; -; Genomic_DNA.
DR RefSeq; WP_054588905.1; NZ_CP012700.1.
DR AlphaFoldDB; A0A0N9UXT3; -.
DR KEGG; smag:AN936_15740; -.
DR PATRIC; fig|33050.5.peg.3264; -.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000058074; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR SMART; SM00563; PlsC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:ALH81754.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000058074};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ALH81754.1}.
FT DOMAIN 277..404
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 783 AA; 86704 MW; 1F9CCDAA93394871 CRC64;
MADGTPRTEI VAEEAADRLY IIDARNRVER RILLDWIHAT AGDLGGDRAP QWASLSIADG
DHALDLDQLK ARLAGAPGRQ VVPLRVAWRI PGFERDRALK FRHLIFGDPR QPGPLRSQFI
LWRDRRRAQI LVGEAATQAA LKDRFLAQTG GGDGGEEGGA EYAGFVARQA GLALDVAERG
IRGSRYKVPR FVADGLRTSP KFRAALAELS ETLGRPVGDL YREARPLMKE VIARPSALFL
DLRAKLDRMM FGGYAPEMEA DAVELARLRS ILREHPTCIL FTHKTYIDGA TPSRLLYEND
MPMLHSFGGA NLDIAVMGEF FRRSGMIFIR RSFQGQPVYK VVLRHYIAWL LAKRFPLSWA
FEGTRSRLGK LMPPKYGLMK YVLDAAHATG TRDVHFVPFV TSFDLIRDVE EYAAEQTGRN
KKPESLSWFL GYMRSLRAPS GRIRLDIGNP VVIDMAPGPD DKRALEKIAF AVAVEANRVT
PLTVTSVMCL ILLGTAPRGV TATELLATIA AVADWARARG IRLSKELESG DDAALSATVD
TLVASGLLTR YEAGSESVYS IDPAKHPMAS YYRNIIVHHF LDRAMIEIAL FELRDGDSKD
ATAAFWAKID RLRDLFKFEF FYPPRGEHMA ALQAELERID PVWDRRLASG DRGVAQLIRR
CQPLVGHAIL LPFAEAYSVV ADLAARARPG EEIDEKTLLD AALVEGKQAY LLRRISSEAA
IGKLLFANGL SLMRHMGMAG TATPDSLNAR RALLMELRGL ANVMESMRLA TLALADRLPP
SGG
//