ID A0A8L7TBK0_BRUMA Unreviewed; 472 AA. AC A0A8L7TBK0; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 02-OCT-2024, entry version 8. DE RecName: Full=glycerophosphocholine cholinephosphodiesterase {ECO:0000256|ARBA:ARBA00012318}; DE EC=3.1.4.38 {ECO:0000256|ARBA:ARBA00012318}; DE AltName: Full=Choline-specific glycerophosphodiester phosphodiesterase {ECO:0000256|ARBA:ARBA00032556}; DE AltName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 6 {ECO:0000256|ARBA:ARBA00031167}; GN Name=Bm1_06255 {ECO:0000313|WBParaSite:Bm5521.1}; OS Brugia malayi (Filarial nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia. OX NCBI_TaxID=6279 {ECO:0000313|Proteomes:UP000006672, ECO:0000313|WBParaSite:Bm5521.1}; RN [1] {ECO:0000313|Proteomes:UP000006672} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FR3 {ECO:0000313|Proteomes:UP000006672}; RX PubMed=17885136; DOI=10.1126/science.1145406; RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E., RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T., RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L., RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M., RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J., RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F., RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W., RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M., RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J., RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E., RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G., RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B., RA Blaxter M.L., Scott A.L.; RT "Draft genome of the filarial nematode parasite Brugia malayi."; RL Science 317:1756-1760(2007). RN [2] {ECO:0000313|WBParaSite:Bm5521.1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (APR-2022) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine CC + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + H(+) + CC phosphocholine; Xref=Rhea:RHEA:41003, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:34071, ChEBI:CHEBI:74344, CC ChEBI:CHEBI:295975; Evidence={ECO:0000256|ARBA:ARBA00000776}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41004; CC Evidence={ECO:0000256|ARBA:ARBA00000776}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O = CC 1-(9Z,12Z-octadecadienoyl)-sn-glycerol + H(+) + phosphocholine; CC Xref=Rhea:RHEA:41115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28733, ChEBI:CHEBI:75561, ChEBI:CHEBI:295975; CC Evidence={ECO:0000256|ARBA:ARBA00000637}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41116; CC Evidence={ECO:0000256|ARBA:ARBA00000637}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z- CC octadecenoyl)-sn-glycerol + H(+) + phosphocholine; CC Xref=Rhea:RHEA:41091, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28610, ChEBI:CHEBI:75757, ChEBI:CHEBI:295975; CC Evidence={ECO:0000256|ARBA:ARBA00024461}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41092; CC Evidence={ECO:0000256|ARBA:ARBA00024461}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-alkyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn- CC glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:36083, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15850, CC ChEBI:CHEBI:30909, ChEBI:CHEBI:295975; CC Evidence={ECO:0000256|ARBA:ARBA00000101}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36084; CC Evidence={ECO:0000256|ARBA:ARBA00000101}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + H2O = 1-dodecanoyl- CC sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41127, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74966, CC ChEBI:CHEBI:75529, ChEBI:CHEBI:295975; CC Evidence={ECO:0000256|ARBA:ARBA00001317}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41128; CC Evidence={ECO:0000256|ARBA:ARBA00001317}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1- CC hexadecanoyl-sn-glycerol + H(+) + phosphocholine; CC Xref=Rhea:RHEA:41119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75542, ChEBI:CHEBI:295975; CC Evidence={ECO:0000256|ARBA:ARBA00000008}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41120; CC Evidence={ECO:0000256|ARBA:ARBA00000008}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1- CC tetradecanoyl-sn-glycerol + H(+) + phosphocholine; CC Xref=Rhea:RHEA:40999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:64489, ChEBI:CHEBI:75536, ChEBI:CHEBI:295975; CC Evidence={ECO:0000256|ARBA:ARBA00000256}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41000; CC Evidence={ECO:0000256|ARBA:ARBA00000256}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) + CC phosphocholine; Xref=Rhea:RHEA:19545, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:17754, CC ChEBI:CHEBI:295975; EC=3.1.4.38; CC Evidence={ECO:0000256|ARBA:ARBA00001458}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19546; CC Evidence={ECO:0000256|ARBA:ARBA00001458}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + sphing-4-enine-phosphocholine = H(+) + phosphocholine + CC sphing-4-enine; Xref=Rhea:RHEA:41095, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57756, ChEBI:CHEBI:58906, CC ChEBI:CHEBI:295975; Evidence={ECO:0000256|ARBA:ARBA00000756}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41096; CC Evidence={ECO:0000256|ARBA:ARBA00000756}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- CC glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:44720, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58168, CC ChEBI:CHEBI:64683, ChEBI:CHEBI:295975; CC Evidence={ECO:0000256|ARBA:ARBA00000769}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44721; CC Evidence={ECO:0000256|ARBA:ARBA00000769}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycero-2-phosphocholine + H2O = glycerol + H(+) + CC phosphocholine; Xref=Rhea:RHEA:61684, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:144950, CC ChEBI:CHEBI:295975; Evidence={ECO:0000256|ARBA:ARBA00000554}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61685; CC Evidence={ECO:0000256|ARBA:ARBA00000554}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase CC family. {ECO:0000256|ARBA:ARBA00010594}. 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 RefSeq; XP_001892720.1; XM_001892685.1. DR GeneID; 6096178; -. DR KEGG; bmy:BM_BM5521; -. DR WBParaSite; Bm5521.1; Bm5521.1; WBGene00225782. DR CTD; 6096178; -. DR Proteomes; UP000006672; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR CDD; cd16018; Enpp; 1. DR Gene3D; 3.30.1360.180; -; 1. DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1. DR InterPro; IPR017850; Alkaline_phosphatase_core_sf. DR InterPro; IPR002591; Phosphodiest/P_Trfase. DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1. DR PANTHER; PTHR10151:SF66; GLYCEROPHOSPHOCHOLINE CHOLINEPHOSPHODIESTERASE ENPP6; 1. DR Pfam; PF01663; Phosphodiest; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1. PE 3: Inferred from homology; KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000006672}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1..17 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 18..472 FT /note="glycerophosphocholine cholinephosphodiesterase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5035475406" FT TRANSMEM 445..468 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 472 AA; 54980 MW; 3A5957A4C8CA4680 CRC64; MWYCQYIFCI IAHFVAATEK IPCGQNLIVF IIDGYGKALL NQSDIGFRLL TQNGVYSDFL KPVYPTHNYP NWMSLVTGLY AENHGFGANY MWDRVKNRRF WKGETNRVGD SWWPDGVVPA WYTTGKSNVD VHCYWMPGCD LPYQDIIVQV PQERKYNASL PEQTDALMSY FPEIIERITK YQPYRQQFFL IRYAGVQAAL ETFGLRSDEL KQALINVDLS LLLLQQKLDA EKLFESTNLM VISTHGLYTV EQEEQFFIEE CLTDYSKIQK VVNHHAMMMI FTNPDEANEV FFELKLCDQW APMGDYDENE QPLVSVYQTT ELPDRFHWKN FQYMPEIVLI TRPGATVLTR ELPSLPPHDE QERDILLTGG WDNENLNMHG IFFARGPAFK EDYEASDINV VDIYQVMMNI FGIEPPHRHN GTWSNVEDFL SSGWETRSVP ENMRAFTVTS CQISLMCFTI LISSFMIYDQ FL //