ID Q5KIN5_CRYNJ Unreviewed; 783 AA.
AC Q5KIN5; Q55TQ0;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN OrderedLocusNames=CND02330 {ECO:0000313|EMBL:AAW43127.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW43127.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW43127.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Catalytic subunit in the complex catalyzing the transfer of
CC N-acetylglucosamine from UDP-N-acetylglucosamine to
CC phosphatidylinositol, the first step of GPI biosynthesis.
CC {ECO:0000256|ARBA:ARBA00003265}.
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|RuleBase:RU361267};
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|RuleBase:RU361267}.
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DR EMBL; AE017344; AAW43127.1; -; Genomic_DNA.
DR RefSeq; XP_570434.1; XM_570434.1.
DR AlphaFoldDB; Q5KIN5; -.
DR STRING; 214684.Q5KIN5; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PaxDb; 214684-Q5KIN5; -.
DR EnsemblFungi; AAW43127; AAW43127; CND02330.
DR GeneID; 3257167; -.
DR KEGG; cne:CND02330; -.
DR VEuPathDB; FungiDB:CND02330; -.
DR eggNOG; KOG1111; Eukaryota.
DR eggNOG; KOG2848; Eukaryota.
DR HOGENOM; CLU_019267_0_0_1; -.
DR InParanoid; Q5KIN5; -.
DR OMA; MSEDMAV; -.
DR OrthoDB; 24420at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002149; Chromosome 4.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IBA:GO_Central.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR CDD; cd03796; GT4_PIG-A-like; 1.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR039507; PIG-A/GPI3.
DR InterPro; IPR013234; PIGA_GPI_anchor_biosynthesis.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR00530; AGP_acyltrn; 1.
DR PANTHER; PTHR45871; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL BIOSYNTHETIC PROTEIN; 1.
DR PANTHER; PTHR45871:SF1; PHOSPHATIDYLINOSITOL N-ACETYLGLUCOSAMINYLTRANSFERASE SUBUNIT A; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF08288; PIGA; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361267};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361267};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..204
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 255..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 87490 MW; 7675CA2D1397B083 CRC64;
MWKVIYYLNL ALYTILLIST SFLAVLIAIV CSLTGRRLNT NYFVARTFYC IAGTILGWKF
QVEGEQYLWE LSGEHGGGKA NEKGRSMVMV GNHQSFVDIL YLGRIFPKHA AIMAKKSIQW
IPGLGWFMMM SGTVFINRSN NKSAIASLQH AGEEMKRKRI SLWIFPEGTR HNTPEPELLN
FKKGAFYLAV QAGVPIVPVV CENYNHLFNG KSHFRRGTLR IKVLPPISTT GLTAADVPGL
IERTRNAMLE TLQEISTPSQ STSQAGSPDP LLGRSGRERE DYYTSGSPAP PQSVPSTAEI
GTEEEAEAAV EDAIGREEAD NGERHVPVVG KNNKEDETMS SPRRLVIAMV SDFFFPVIGG
VEGHIYSLSV ELMRRGHKVI VITHSHPDRL GIHYLEPSLK VYYLPYLPIA SSASLPNFLL
FLPYFRHIIL TENIQLVHGH GALSSLAHEA VIHAPLLGVK AVFTDHSLFG FGDAVGVLTN
KLLGAALRCV DEVICVSNTG RENTVLRAQL DPSIVSVIPN ALEAEHFKPD PFRADPDWIT
IVVISRLVHR KGIDLLISSA PQICALFPKV RFIVGGDGPK MVELEQMREK YELQGRVELL
GRVNPGDVRD VLTKGQIYLS NSLTEAFGIS IIEAASAGLF VVATKVGGVP EILPQDMIEF
CRADEDDVIR ALTHAIHTIQ SSRHSPWSAH IRVRDMYSWS HVSSRAEIVY LRAMSRPHRE
IGERMRRYLE LGPVFGVVMC CILAVEHYFF WLLEWWNPRD KLRQVISFPG VERFEDRGKN
NKK
//
