ID   K9V8Y1_9CYAN            Unreviewed;      1303 AA.
AC   K9V8Y1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=glycerophosphodiester phosphodiesterase {ECO:0000256|ARBA:ARBA00012247};
DE            EC=3.1.4.46 {ECO:0000256|ARBA:ARBA00012247};
GN   ORFNames=Cal6303_4802 {ECO:0000313|EMBL:AFZ03700.1};
OS   Calothrix sp. PCC 6303.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ03700.1, ECO:0000313|Proteomes:UP000010477};
RN   [1] {ECO:0000313|EMBL:AFZ03700.1, ECO:0000313|Proteomes:UP000010477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ03700.1,
RC   ECO:0000313|Proteomes:UP000010477};
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00029315};
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DR   EMBL; CP003610; AFZ03700.1; -; Genomic_DNA.
DR   STRING; 1170562.Cal6303_4802; -.
DR   KEGG; calt:Cal6303_4802; -.
DR   PATRIC; fig|1170562.3.peg.5259; -.
DR   eggNOG; COG0584; Bacteria.
DR   eggNOG; COG2931; Bacteria.
DR   eggNOG; COG4222; Bacteria.
DR   HOGENOM; CLU_001601_0_0_3; -.
DR   OrthoDB; 384721at2; -.
DR   Proteomes; UP000010477; Chromosome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd08602; GDPD_ScGlpQ1_like; 2.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
DR   Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 2.
DR   InterPro; IPR030395; GP_PDE_dom.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR027372; Phytase-like_dom.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   PANTHER; PTHR43620:SF7; GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE GDPD6; 1.
DR   PANTHER; PTHR43620; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR   Pfam; PF03009; GDPD; 2.
DR   Pfam; PF00353; HemolysinCabind; 3.
DR   Pfam; PF13449; Phytase-like; 2.
DR   SUPFAM; SSF51120; beta-Roll; 2.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 2.
DR   PROSITE; PS51704; GP_PDE; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          180..530
FT                   /note="GP-PDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51704"
FT   DOMAIN          560..903
FT                   /note="GP-PDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51704"
SQ   SEQUENCE   1303 AA;  141389 MW;  BC906DD9FE144707 CRC64;
     MANVTLKGFA TLPADTFAAG PQSGKGISAN GRTGLFPGQP VQGFSGVQFA NENEFWFMAD
     NGFGAKTNSS DFLLRIYKVN PSFRGIENGD GTVQVGNFIQ LADPDKKATF KITNEGTSER
     LLTGADFDIE SFNIAKDNTI WIGDEFGPYL LHFDTTGKLL EAPIPTPNIV KLNTLNGEAP
     LVIGHRGASG ELPEHTLAAY KLAIDRGADF IEPDLVATKD GILVARHEPN IINTTDVADR
     PEFANRKTTK IVDGVAEEGF FVSDFTLAEL KTIRAKMPQD FRTQAFNGVL EIPTLDEIIN
     LVKQEEALTG KKIGIYPETK HPTYHDSLGL SLEEKLVDTL VKNNFTDPKR VFIQSFETSN
     LKELHSEIMP KAGIDIPLVQ LFDAADVRLD GSLIEVQPYD FVVNGDSRTY ADLRTREGLQ
     EIASYADGIG PWKRMIVSVK GVDSNNDGIA DDVNKDGVVN DADKTTLPPT SLVNDAHKAG
     LQVHPYTFRN EGRYLAKDYN GNPELEYQQF INLGVDGYFT DFPGTGDLVR DQIVSPFVRS
     PQNADVLKSN EFKTLDKNPP IVIGHRGASG DRPEHTLAAY KLAIASGADF IEPDLVVTKD
     GILVARHENA LAILNADGSL NNTDTSTDVY ERPEFANRLT TKVIDGRSVK GWFAEDFTLA
     ELKTLNAIER LPALRGTRFN NDKLQVPTLD EIIDLVQQVE KETGRKIGIY PETKHPTYFA
     TEGKYIDGTP INVSLGQKLI DTLVAQNFTD PKRVFIQSFE ISNLQELNDV IMPQAKVDLP
     LVQLFGGASD RPYDFRVKND PRTYGDLTKP AELTDIAKYA AGIGPNKRLI VPAGSDGKLL
     APTTLIQDAH SAGLLVHLYT LRSEPVFLAS EYKGNPVNEY KQFIELGVDG FFTDFPGLGD
     TIRDLYAGKP PVSNLGGSRG FEGMAISPDK TKLYPLLEGT VVGDAPGSLR IYDFDIATKQ
     YQGLVGYYQM ESSTNAIGDF AVINANEYLV IERDNNQGDA AKFKKIFKVD FSQKDANGFV
     AKEEIANLLN IQDPNDLNQD GSTTFEFPFV TIEDVLVIDE NTILVANDNN YPFSLGRPPA
     IDNNEILILG LDKPLKVDPR VGIAGQNLPK IEILGTKGDD VLYGSNLDEL FDAGEGNNTI
     YGNEGKNIFI AGNGNNIAYG GSSDDVFFFG KGNNVIYGNE GINKITTSSG NNLIYGGSQG
     DVIYTGAGND VIYANGGNNV ISSGTGNDTV YTGSGADKFI LDAGTGSATI IGYGANDQIS
     RGSTLAANSV LSVTITGNDT LISAGGDLLA TLKDVQLKSV SII
//