GDE1_ASHGO
ID GDE1_ASHGO Reviewed; 1321 AA.
AC Q74ZH9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Glycerophosphocholine phosphodiesterase GDE1;
DE EC=3.1.4.2 {ECO:0000250|UniProtKB:Q02979};
DE AltName: Full=Glycerophosphodiester phosphodiesterase GDE1;
GN Name=GDE1; OrderedLocusNames=AGR223W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 327; 335 AND 340.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Glycerophosphocholine glycerophosphodiesterase responsible
CC for the hydrolysis of intracellular glycerophosphocholine into
CC glycerol-phosphate and choline. The choline is used for phosphatidyl-
CC choline synthesis. Required for utilization of glycerophosphocholine as
CC phosphate source. {ECO:0000250|UniProtKB:Q02979}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 3-phosphocholine = choline + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:16061, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:57597; EC=3.1.4.2;
CC Evidence={ECO:0000250|UniProtKB:Q02979};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16062;
CC Evidence={ECO:0000250|UniProtKB:Q02979};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q02979}.
CC -!- SIMILARITY: Belongs to the GDE1 family. {ECO:0000305}.
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DR EMBL; AE016820; AAS54713.2; -; Genomic_DNA.
DR RefSeq; NP_986889.2; NM_211951.2.
DR AlphaFoldDB; Q74ZH9; -.
DR SMR; Q74ZH9; -.
DR STRING; 33169.AAS54713; -.
DR EnsemblFungi; AAS54713; AAS54713; AGOS_AGR223W.
DR GeneID; 4623191; -.
DR KEGG; ago:AGOS_AGR223W; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1162; Eukaryota.
DR eggNOG; KOG2421; Eukaryota.
DR HOGENOM; CLU_005444_1_0_1; -.
DR InParanoid; Q74ZH9; -.
DR OMA; HSTQLDT; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047389; F:glycerophosphocholine phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR033506; Gde1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR004331; SPX_dom.
DR PANTHER; PTHR22958:SF1; PTHR22958:SF1; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF03009; GDPD; 1.
DR Pfam; PF03105; SPX; 2.
DR SMART; SM00248; ANK; 7.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51704; GP_PDE; 1.
DR PROSITE; PS51382; SPX; 1.
PE 3: Inferred from homology;
KW ANK repeat; Cytoplasm; Hydrolase; Reference proteome; Repeat.
FT CHAIN 1..1321
FT /note="Glycerophosphocholine phosphodiesterase GDE1"
FT /id="PRO_0000233008"
FT DOMAIN 1..209
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT REPEAT 417..446
FT /note="ANK 1"
FT REPEAT 463..495
FT /note="ANK 2"
FT REPEAT 497..524
FT /note="ANK 3"
FT REPEAT 529..558
FT /note="ANK 4"
FT REPEAT 563..592
FT /note="ANK 5"
FT REPEAT 596..626
FT /note="ANK 6"
FT DOMAIN 972..1311
FT /note="GP-PDE"
FT REGION 630..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1321 AA; 147076 MW; 95CF4D85909CC556 CRC64;
MKFGKTFPNH QVPEWAHKYV NYKGLKKQIK EITLVQDALF RQEQGAASQD GPARRRGRES
KEQYLGHPEV KKLLAAFFFA LDRDIEKVDG FYNMQFMEYD RRLRKLLSSA QLADITSVQR
GATGYLHAPL PQYIAYGERE RDGLPERYVP PHATDMSEDL AEVLTILLEL RSHFRNLKWY
GELNKRAFTK IMKKLDKKVG TNQQHSYFQA RIKPLEFADD TPIVKALATI NEILDRISPC
VKDLQDKLRG EDRRLLQGSS SPIDVASQLV TKDDGAGLIN ELISMYRSVV LIPTRTLVTL
LNKSALSRSF SCVDEILGII PTLGDPSDIN GRNFFHHHVI ALGKKRTKSL EERDNINSLL
SDSLDLEAAI PPEPNTRLVG AFGPDGVNSD DSPAPLSHIL QQLPAHLRPS LLQRDNYKRT
PLHYSAQYGL CEVTRIILQA LSEWDAWNAD VAIDDIDVWG DSENLTPLHL AVIGTHPLTV
STLLSFMNPE KSLNSPRLLH LATRLNSPSL LNSLLSAKGF DIDYQEPENL ETALYVACKL
DIYEAAEYLV KQGANMELGE KLFGWTPIFA AATEGYARIV QLLVDHGAKY DLFDESGWTP
MEHAALRGHL DISQLIRITD NKAITRPKFA TDWNKSTRPT ETTNGLLSAL TPSESGSTTT
GSENKSSSLT PSTSNEMYAL PARSSTSIDK ISEPNKGNHR KVLKSQLSHG KVQTIKDTQL
PQQPIKSFGH SFLQKDESVI LLTLGTNDNR STIPAVSLNK VPVAKASSTE LDTALSLLVT
CMDNLDAEPV MLDLPLHENL DSVTFKVPYK KDSSYTIFFD IVPTYGYSMA NMNRENSSGM
HSNVGNSTGP AYLDAQVGQC GSRLHYDQLG RDTPNTYDQR SRHQASQQKE QIATKKQSKI
LGRAVALLDS APTSVGPNRR SIAEAITIPI IGSDTLEVLG IIRFDFLVVT PFVHKNLSVG
PAETYWKSLV STRVIGHRGL GKNMNTNKSL QLGENTVESF IAAASLGASY VEFDVQLTKD
NIPVVYHDFL VAESGVDIPM HELTLEQFLD LNGERQRHQD AREAHRNHRS PNGRRLSMDD
SSAELIKRSL MMRGDEDRTA RDLNTIYGDR MRLTRTFKKN AFKANSRGHA IASSFVTLKE
LFKKIPQNVG FNIECKYPMV DEAEEEDIGP IAVEMNHWID TVLEVVYDNV EGRDVIFSSF
QPDVCLMLSL KQPSFPILFL TEGGTAKRCD IRAASLQNAI RFAHRWNLLG IVSAAAPIVI
APRLAQIVKS SGLVCVTYGV ENNDPEIARV EMDAGVDAVI VDSVLAVRKG LTREAQDADT
L
