ID D2YIE9_VIBMI Unreviewed; 528 AA.
AC D2YIE9;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=cyclic-guanylate-specific phosphodiesterase {ECO:0000256|ARBA:ARBA00012282};
DE EC=3.1.4.52 {ECO:0000256|ARBA:ARBA00012282};
GN ORFNames=VMB_32960 {ECO:0000313|EMBL:EEW05470.1};
OS Vibrio mimicus VM603.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=671074 {ECO:0000313|EMBL:EEW05470.1, ECO:0000313|Proteomes:UP000004827};
RN [1] {ECO:0000313|EMBL:EEW05470.1, ECO:0000313|Proteomes:UP000004827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VM603 {ECO:0000313|EMBL:EEW05470.1,
RC ECO:0000313|Proteomes:UP000004827};
RX PubMed=19860885; DOI=10.1186/1471-2148-9-258;
RA Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T.,
RA Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.;
RT "Genomic taxonomy of Vibrios.";
RL BMC Evol. Biol. 9:258-258(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine +
CC H(+); Xref=Rhea:RHEA:24902, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58754, ChEBI:CHEBI:58805; EC=3.1.4.52;
CC Evidence={ECO:0000256|ARBA:ARBA00034290};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEW05470.1}.
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DR EMBL; ACYU01000179; EEW05470.1; -; Genomic_DNA.
DR RefSeq; WP_001150561.1; NZ_ACYU01000179.1.
DR AlphaFoldDB; D2YIE9; -.
DR Proteomes; UP000004827; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IEA:UniProtKB-EC.
DR CDD; cd01948; EAL; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR InterPro; IPR024744; CSS-motif_dom.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR PANTHER; PTHR33121:SF80; CYCLIC DI-GMP PHOSPHODIESTERASE PDEL-RELATED; 1.
DR Pfam; PF12792; CSS-motif; 1.
DR Pfam; PF00563; EAL; 1.
DR SMART; SM00052; EAL; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR PROSITE; PS50883; EAL; 1.
PE 4: Predicted;
KW c-di-GMP {ECO:0000256|ARBA:ARBA00022636};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 252..504
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 528 AA; 59865 MW; DBFC7A041D78C7A8 CRC64;
MQDFFHETFI RRSTHAFWAF LFPLVIGLLL ITWQTSHDLK NDIRDNLKAG NALLDSLVQH
AEIANERAAP YLRMSCDNAQ PYLADLVAIT PDVRSIHLSE NNKIYCDSLG GKRIRPINES
LGTNEELLLL QGNKWSPHHS ALIFFRDYDE GTVFSGVSSY YLRNILSLIK SYGSTSLHIG
ERWFNDKGLV THRSNPTTIE QNSLKYPYSL STFLTVEDYW DYFIDAKHTS LLLLLVMSFG
VGSYAFWRQG QINALDPEIR RAIRAQEFEP YIQPIMDIHG RLASAEVLMR WQHPSAGLIR
PDLFIPLAEE SGLIVPMTSQ VMAKVRDQLG PYQSKIPSDF HISFNISAKH CVNSDLVKDC
QHFLSAFNHP SLLSLELTER ELIEDTEEAR KLFAKLNQIG VRLAIDDFGT GHSSLNYLQT
FQFDVLKIDQ SFVRMIGSNA VASHIVDTLL NLAQRLNMQT VAEGIETEEQ VTYFAARGVD
YMQGYFYASP MPMDDFLTHL VIGTWESSNA PTQLTQALSL NLAENGAI
//
