GLPQ2_MYCTU
ID GLPQ2_MYCTU Reviewed; 264 AA.
AC O07244; F2GMB9; I6Y3H4; L0T6B1;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable glycerophosphodiester phosphodiesterase 2 {ECO:0000303|PubMed:9634230};
DE Short=Glycerophosphoryl diester phosphodiesterase 2;
DE EC=3.1.4.46 {ECO:0000305};
GN Name=glpQ2 {ECO:0000312|EMBL:CCP43047.1};
GN OrderedLocusNames=Rv0317c {ECO:0000312|EMBL:CCP43047.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1] {ECO:0000312|EMBL:CCP43047.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J.,
RA Squares R., Squares S., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-13, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.M111.011445;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Glycerophosphoryl diester phosphodiesterase hydrolyzes
CC deacylated phospholipids to G3P and the corresponding alcohols.
CC {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:83408; EC=3.1.4.46; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01041};
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP43047.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR EMBL; AL123456; CCP43047.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_214831.1; NC_000962.3.
DR RefSeq; WP_003401625.1; NZ_NVQJ01000026.1.
DR SMR; O07244; -.
DR STRING; 83332.Rv0317c; -.
DR PaxDb; O07244; -.
DR PRIDE; O07244; -.
DR DNASU; 886559; -.
DR GeneID; 45424284; -.
DR GeneID; 886559; -.
DR KEGG; mtu:Rv0317c; -.
DR PATRIC; fig|83332.111.peg.353; -.
DR TubercuList; Rv0317c; -.
DR eggNOG; COG0584; Bacteria.
DR OMA; AWDRVCV; -.
DR PhylomeDB; O07244; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:34915127"
FT CHAIN 2..264
FT /note="Probable glycerophosphodiester phosphodiesterase 2"
FT /id="PRO_0000455760"
FT DOMAIN 17..255
FT /note="GP-PDE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01041"
FT BINDING 50
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01041"
FT BINDING 52
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01041"
FT BINDING 65
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01041"
SQ SEQUENCE 264 AA; 29003 MW; F76F307016697CA1 CRC64;
MSDGGAPTVE FLRHGGRIAM AHRGFTSFRL PMNSMGAFQE AAKLGFRYIE TDVRATRDGV
AVILHDRRLA PGVGLSGAVD RLDWRDVRKA QLGAGQSIPT LEDLLTALPD MRVNIDIKAA
SAIEPTVNVI ERCNAHNRVL IGSFSERRRR RALRLLTKRV ASSAGTGALL AWLTARPLGS
RAYAWRMMRD IDCVQLPSRL GGVPVITPAR VRGFHAAGRQ VHAWTVDEPD VMHTLLDMDV
DGIITDRADL LRDVLIARGE WDGA
