GLPQ_BACSU
ID GLPQ_BACSU Reviewed; 293 AA.
AC P37965;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Glycerophosphodiester phosphodiesterase;
DE Short=Glycerophosphoryl diester phosphodiesterase;
DE EC=3.1.4.46;
GN Name=glpQ; Synonyms=ybeD; OrderedLocusNames=BSU02130;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BR95;
RX PubMed=8012593; DOI=10.1099/00221287-140-4-723;
RA Nilsson R.P., Beijer L., Rutberg B.;
RT "The glpT and glpQ genes of the glycerol regulon in Bacillus subtilis.";
RL Microbiology 140:723-730(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT Bacillus subtilis chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Glycerophosphoryl diester phosphodiesterase hydrolyzes
CC deacylated phospholipids to G3P and the corresponding alcohols.
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;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; Z26522; CAA81292.1; -; Genomic_DNA.
DR EMBL; AB006424; BAA33110.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12007.1; -; Genomic_DNA.
DR PIR; I40418; I40418.
DR RefSeq; NP_388095.1; NC_000964.3.
DR RefSeq; WP_003246382.1; NZ_JNCM01000030.1.
DR PDB; 5T91; X-ray; 1.53 A; A=27-293.
DR PDB; 5T9B; X-ray; 1.62 A; G=27-293.
DR PDB; 5T9C; X-ray; 1.48 A; E=27-293.
DR PDBsum; 5T91; -.
DR PDBsum; 5T9B; -.
DR PDBsum; 5T9C; -.
DR AlphaFoldDB; P37965; -.
DR SMR; P37965; -.
DR IntAct; P37965; 1.
DR STRING; 224308.BSU02130; -.
DR PaxDb; P37965; -.
DR PRIDE; P37965; -.
DR EnsemblBacteria; CAB12007; CAB12007; BSU_02130.
DR GeneID; 938446; -.
DR KEGG; bsu:BSU02130; -.
DR PATRIC; fig|224308.179.peg.219; -.
DR eggNOG; COG0584; Bacteria.
DR InParanoid; P37965; -.
DR OMA; CRHENDI; -.
DR PhylomeDB; P37965; -.
DR BioCyc; BSUB:BSU02130-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
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 3D-structure; Calcium; Glycerol metabolism; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..293
FT /note="Glycerophosphodiester phosphodiesterase"
FT /id="PRO_0000200573"
FT DOMAIN 38..290
FT /note="GP-PDE"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5T9C"
FT TURN 43..49
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:5T9C"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:5T9C"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:5T9C"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:5T9C"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5T9C"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:5T9C"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:5T9C"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:5T9C"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:5T9C"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:5T9C"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:5T9C"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:5T9C"
SQ SEQUENCE 293 AA; 32959 MW; 8A7149CA6322F082 CRC64;
MRKNRILALF VLSLGLLSFM VTPVSAASKG NLLSPDRILT VAHRGASGYV PEHTILSYET
AQKMKADFIE LDLQMTKDGK LIVMHDEKLD RTTNGMGWVK DHTLADIKKL DAGSWFNEAY
PEKAKPQYVG LKVPTLEEVL DRFGKHANYY IETKSPDTYP GMEEKLIASL QKHKLLGKHS
KPGQVIIQSF SKESLVKVHQ LQPNLPTVQL LEAKQMASMT DAALEEIKTY AVGAGPDYKA
LNQENVRMIR SHGLLLHPYT VNNEADMHRL LDWGVTGVFT NYPDLFHKVK KGY
