位置:首页 > 蛋白库 > PLSY_MALP2
PLSY_MALP2
ID   PLSY_MALP2              Reviewed;         272 AA.
AC   P59248;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE   AltName: Full=Acyl-PO4 G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE   AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE   AltName: Full=G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE            Short=GPAT {ECO:0000255|HAMAP-Rule:MF_01043};
DE            EC=2.3.1.275 {ECO:0000255|HAMAP-Rule:MF_01043};
DE   AltName: Full=Lysophosphatidic acid synthase {ECO:0000255|HAMAP-Rule:MF_01043};
DE            Short=LPA synthase {ECO:0000255|HAMAP-Rule:MF_01043};
GN   Name=plsY {ECO:0000255|HAMAP-Rule:MF_01043}; OrderedLocusNames=MYPE4020;
OS   Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX   NCBI_TaxID=272633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2;
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT   bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(2002).
CC   -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate
CC       (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic
CC       acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor,
CC       but not acyl-CoA or acyl-ACP. {ECO:0000255|HAMAP-Rule:MF_01043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-
CC         glycero-3-phosphate + phosphate; Xref=Rhea:RHEA:34075,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970,
CC         ChEBI:CHEBI:59918; EC=2.3.1.275; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01043};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC       Rule:MF_01043}.
CC   -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000255|HAMAP-
CC       Rule:MF_01043}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01043};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01043}.
CC   -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000255|HAMAP-
CC       Rule:MF_01043}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000026; BAC44192.1; -; Genomic_DNA.
DR   RefSeq; WP_011077228.1; NC_004432.1.
DR   AlphaFoldDB; P59248; -.
DR   SMR; P59248; -.
DR   STRING; 272633.26453861; -.
DR   EnsemblBacteria; BAC44192; BAC44192; BAC44192.
DR   KEGG; mpe:MYPE4020; -.
DR   eggNOG; COG0344; Bacteria.
DR   HOGENOM; CLU_081254_3_0_14; -.
DR   OMA; WRHRGNL; -.
DR   OrthoDB; 1691856at2; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000002522; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01043; PlsY; 1.
DR   InterPro; IPR003811; G3P_acylTferase_PlsY.
DR   PANTHER; PTHR30309; PTHR30309; 1.
DR   Pfam; PF02660; G3P_acyltransf; 1.
DR   SMART; SM01207; G3P_acyltransf; 1.
DR   TIGRFAMs; TIGR00023; TIGR00023; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..272
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000188405"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
SQ   SEQUENCE   272 AA;  30650 MW;  87E9B53B6858A4EF CRC64;
     MNIGNLIGII ILFLFIGYFI GNILFGILIS KSQGVDIRTL GSGNVGATNV TRNLGRISGA
     IVMVLDFFKS WFSTFVCLLI YKALRYSIGD ESAYANAGVI IYLGGFAAII GHCFPCFYFY
     TLFKTKFNFE EAKKYSGGKG VSSAAGFAAS ISPWMFFICF VLFWSICLIS KYVSLASIVT
     VFLLPIWSLI PHLNYFYMLD VAQANINPIP PFNRPFEIAA IFNYSLNWWY ILVTFLLELL
     TAVLVIYRHK ENIVRLIKGE ERKAFAKKTN TH
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024