1S2O


Conserved Protein Domain Family
SPP_plant-cyano

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TIGR01485: SPP_plant-cyano 
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sucrose-6F-phosphate phosphohydrolase
This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain.
Statistics
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PSSM-Id: 130549
View PSSM: TIGR01485
Aligned: 4 rows
Threshold Bit Score: 415.366
Threshold Setting Gi: 61679846
Created: 8-Oct-2014
Updated: 23-Jan-2015
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        3 QLLLISDLDNTWV----GDQQALEHLQEYLGDRRGNF--YLAYATGRSYHSARELQKQVGLMEPDYWLTAVGSEIYHP-- 74
gi 16605555   3 PFLFVTDLDDTLVyrttGDDSALPELNQLLKRHRQEYgtKIVYSTGRSPVLYKELQAQKNLLQPDALVLSVGTEIYLNg- 81
gi 11127755   9 RLMIVSDLDHTMVdhhdEENLSLLRFGALWESVYCEDs-LLVFSTGRSPTLYKELRKEKPMLTPDITIMSVGTEITYGe- 86
gi 6822073    9 RLILVADLDCTLVdhddPENNDLLRFNALWEAHYRHDs-LLVYCTGRSFSSYSSLRKKRPLLTPDIAVTSVGSEIVYGgg 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A       75 --EGLDQHWADYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETGIPVQVIFSSGK 152
gi 16605555  82 -aDTPDSDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASANVLPQLEAELQKSKLNVKLIYSSGI 160
gi 11127755  87 -aMVPDDGWEEYLNNKWDRNIVVAETVSFSELKLQPETEQRPHKVSFFVDKKNAQEVIKSVAERLDKCGLDAKIIYSGGQ 165
gi 6822073   88 esTVSDVVWTARLDYKWNRDIVVEETLKFPKLEPQPDKSQEEHKVSFFVGREDAVEIMKVLPGILEERGVDVKLVYSNGY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A      153 DVDLLPQRSNKGNATQYLQQHLAME---PSQTLVCGDSGNDIGLFET-SARGVIVRNAQPELLHWYDQWGDS--RHYRAQ 226
gi 16605555 161 DLDIVPHSSDKGQAMQFLRQKWKFA---AEQTVVCGDSGNDIALFAVgNERGIIVGNARKELLQWHNEHPAE--HRYLAS 235
gi 11127755 166 DLDILPQGAGKGQALAYLLEKLSSCgkpPNNTLVCGDSGNDAELFSIpGVHGVMVSNAQEELLQWYTENAKDnpKIIHSN 245
gi 6822073  168 AFDVLPRGAGKQGALTYLLDKLDIEgkqPSNTLVCGDSGNDAELFNIsDVYGVMVSNSHEELLQWYEENAKDnpKIFHAS 247
                       250
                ....*....|....*..
1S2O_A      227 SSHAGAILEAIAHFDFL 243
gi 16605555 236 CFCAGGIIEGLNYFGLL 252
gi 11127755 246 ERCAAGIIQAIGHFKLG 262
gi 6822073  248 ERCGAGMIEAIQRFNLG 264
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