(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 110.
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-phosphoester + 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}.
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   SMR; P37965; -.
DR   IntAct; P37965; 1.
DR   STRING; 224308.BSU02130; -.
DR   PaxDb; P37965; -.
DR   PRIDE; P37965; -.
DR   EnsemblBacteria; CAB12007; CAB12007; BSU02130.
DR   GeneID; 938446; -.
DR   KEGG; bsu:BSU02130; -.
DR   PATRIC; fig|224308.179.peg.219; -.
DR   eggNOG; ENOG4107VXM; Bacteria.
DR   eggNOG; COG0584; LUCA.
DR   HOGENOM; HOG000004695; -.
DR   InParanoid; P37965; -.
DR   KO; K01126; -.
DR   OMA; RFYAIDF; -.
DR   PhylomeDB; P37965; -.
DR   BioCyc; BSUB:BSU02130-MONOMER; -.
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;
DR   PRODOM; P37965.
DR   SWISS-2DPAGE; P37965.
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   METAL           70
FT                   /note="Calcium"
FT                   /evidence="ECO:0000250"
FT   METAL           72
FT                   /note="Calcium"
FT                   /evidence="ECO:0000250"
FT   METAL           152
FT                   /note="Calcium"
FT                   /evidence="ECO:0000250"
FT   STRAND          39..42
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   TURN            43..49
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           55..63
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   STRAND          67..75
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   STRAND          81..83
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   STRAND          85..89
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   TURN            90..92
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           99..101
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           104..107
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           114..119
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           121..123
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           126..128
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           136..143
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           144..146
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   STRAND          149..153
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           156..158
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           162..172
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   STRAND          177..180
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   STRAND          184..190
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           192..201
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   STRAND          207..211
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           213..217
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           221..228
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   STRAND          232..237
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           238..240
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           243..251
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           264..273
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   STRAND          277..281
FT                   /evidence="ECO:0000244|PDB:5T9C"
FT   HELIX           283..290
FT                   /evidence="ECO:0000244|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
//

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