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Conserved domains on  [gi|2017528048|emb|CAG0941696|]
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Mannosylfructose-phosphate phosphatase [Candidatus Brocadiaceae bacterium]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
5-264 3.22e-64

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd02605:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 245  Bit Score: 201.81  E-value: 3.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   5 LICTDLDRTLLPNGKQAESPEA-RALFARLMARHEVYLAFVSGRHRALVEQAIADYQLPTPDWVIADVGSSIY-AVHDDW 82
Cdd:cd02605     1 LLVSDLDETLVGHDTNLQALERlQDLLEQLTADNDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYyGESGYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  83 QAWHSWQHAIAVDWQdltaPDLQTLFTDL-TVLTLQESEKQNRYKLSYYLPLITDYNDLQlQMQQRLMEKNLAANLIYSI 161
Cdd:cd02605    81 EPDTYWNEVLSEGWE----RFLFEAIADLfKQLKPQSELEQNPHKISFYLDPQNDAAVIE-QLEEMLLKAGLTVRIIYSS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 162 DEAasiGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQAQQQANPEHLyc 241
Cdd:cd02605   156 GLA---YDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLA-- 230
                         250       260
                  ....*....|....*....|...
gi 2017528048 242 argdffgmNGNYSAGILEGIAHY 264
Cdd:cd02605   231 --------KGPYAGGILEGLAHF 245
 
Name Accession Description Interval E-value
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
5-264 3.22e-64

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 201.81  E-value: 3.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   5 LICTDLDRTLLPNGKQAESPEA-RALFARLMARHEVYLAFVSGRHRALVEQAIADYQLPTPDWVIADVGSSIY-AVHDDW 82
Cdd:cd02605     1 LLVSDLDETLVGHDTNLQALERlQDLLEQLTADNDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYyGESGYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  83 QAWHSWQHAIAVDWQdltaPDLQTLFTDL-TVLTLQESEKQNRYKLSYYLPLITDYNDLQlQMQQRLMEKNLAANLIYSI 161
Cdd:cd02605    81 EPDTYWNEVLSEGWE----RFLFEAIADLfKQLKPQSELEQNPHKISFYLDPQNDAAVIE-QLEEMLLKAGLTVRIIYSS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 162 DEAasiGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQAQQQANPEHLyc 241
Cdd:cd02605   156 GLA---YDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLA-- 230
                         250       260
                  ....*....|....*....|...
gi 2017528048 242 argdffgmNGNYSAGILEGIAHY 264
Cdd:cd02605   231 --------KGPYAGGILEGLAHF 245
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
2-265 6.60e-59

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 187.86  E-value: 6.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   2 PRLLICTDLDRTLLPngkqaesPEARALfARLMA-----RHEVYLAFVSGRHRALVEQAIADYQLPTPDWVIADVGSSIY 76
Cdd:pfam05116   1 PPLLLVSDLDNTLVD-------GDNEAL-ARLNQlleayRPDVGLVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  77 AVHDDwQAWHSWQHAIAVDWQdltaPD-LQTLFTDLTVLTLQESEKQNRYKLSYYLPLITDYNDLQlQMQQRLMEKNLAA 155
Cdd:pfam05116  73 YGPSL-VPDQSWQEHLDYHWD----RQaVVEALAKFPGLTLQPEEEQRPHKVSYFLDPEAAAAVLA-ELEQLLRKRGLDV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 156 NLIYSIDEAasiglLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQAQQQA- 234
Cdd:pfam05116 147 KVIYSSGRD-----LDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQPELLQWYLENAr 221
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2017528048 235 NPEHLYCArgdffgmNGNYSAGILEGIAHYH 265
Cdd:pfam05116 222 DNPRIYFA-------SGRCAGGILEGIRHFG 245
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
1-264 2.63e-30

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 112.54  E-value: 2.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   1 MPRLlICTDLDRTLLPNGKQAeSPEARALFARLMARHeVYLAFVSGRHRALVEQAIADYQLPtpDWVIADVGSSIYAVHD 80
Cdd:COG0561     1 MIKL-IALDLDGTLLNDDGEI-SPRTKEALRRLREKG-IKVVIATGRPLRSALPLLEELGLD--DPLITSNGALIYDPDG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  81 DWqawhswqhaiaVDWQDLTAPDLQTLFtdltvltlqesekqnryklsyylplitdyndlqlqmqQRLMEKNLAANLIYS 160
Cdd:COG0561    76 EV-----------LYERPLDPEDVREIL-------------------------------------ELLREHGLHLQVVVR 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 161 ideaASIGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQAQqqanpehlY 240
Cdd:COG0561   108 ----SGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAAD--------Y 175
                         250       260
                  ....*....|....*....|....
gi 2017528048 241 CARgdffgmnGNYSAGILEGIAHY 264
Cdd:COG0561   176 VTG-------SNDEDGVAEALEKL 192
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
3-264 6.97e-27

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.


Pssm-ID: 130549  Cd Length: 249  Bit Score: 104.89  E-value: 6.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   3 RLLICTDLDRTLL--PNGKQAESPEARALFARlMARHEVYLAFVSGRHRALVEQAIADYQLPTPDWVIADVGSSIY---- 76
Cdd:TIGR01485   1 RLLLVSDLDNTLVdhTDGDNQALLRLNALLED-HRGEDSLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYygga 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  77 -AVHDDWQAWHS--WQHAIavdwqdltapdLQTLFTDLTVLTLQESEKQNRYKLSYYLPLITDYNDLQlQMQQRLMEKNL 153
Cdd:TIGR01485  80 eVPDQHWAEYLSekWQRDI-----------VVAITDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIK-QLTEMLKETGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 154 AANLIYSIDEAasiglLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVL-ISHIPSVLVANADDNVRQQAQQ 232
Cdd:TIGR01485 148 DVKLIYSSGKD-----LDILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFeIGSVRGVIVSNAQEELLQWYDE 222
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2017528048 233 QANpEHLYCArgdffgmNGNYSAGILEGIAHY 264
Cdd:TIGR01485 223 NAK-DKIYHA-------SERCAGGIIEAIAHF 246
PLN02382 PLN02382
probable sucrose-phosphatase
2-264 2.74e-22

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 95.44  E-value: 2.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   2 PRLLICTDLDRTLLPNGkqaeSPEARAL--FARLMA---RHEVYLAFVSGRHRALVEQAIADYQLPTPDWVIADVGSSI- 75
Cdd:PLN02382    8 PRLMIVSDLDHTMVDHH----DPENLSLlrFNALWEaeyRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEIa 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  76 YA---VHDDwqAW-----HSWQHAIAVDwqdltapdlQTLftDLTVLTLQESEKQNRYKLSYYLplitDYNDLQLQMQ-- 145
Cdd:PLN02382   84 YGesmVPDH--GWveylnKKWDREIVVE---------ETS--KFPELKLQPETEQRPHKVSFYV----DKKKAQEVIKel 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 146 -QRLMEKNLAANLIYS--IDeaasiglLDVLPKRANKLHAIEFLMQQ---QGFTDENTVFAGDSGNDlAVLIShIPSV-- 217
Cdd:PLN02382  147 sERLEKRGLDVKIIYSggID-------LDVLPQGAGKGQALAYLLKKlkaEGKAPVNTLVCGDSGND-AELFS-VPDVyg 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2017528048 218 -LVANADDNVRQ-QAQQQANPEHLY-----CArgdffgmngnysAGILEGIAHY 264
Cdd:PLN02382  218 vMVSNAQEELLQwYAENAKDNPKIIhaterCA------------AGIIQAIGHF 259
 
Name Accession Description Interval E-value
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
5-264 3.22e-64

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 201.81  E-value: 3.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   5 LICTDLDRTLLPNGKQAESPEA-RALFARLMARHEVYLAFVSGRHRALVEQAIADYQLPTPDWVIADVGSSIY-AVHDDW 82
Cdd:cd02605     1 LLVSDLDETLVGHDTNLQALERlQDLLEQLTADNDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYyGESGYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  83 QAWHSWQHAIAVDWQdltaPDLQTLFTDL-TVLTLQESEKQNRYKLSYYLPLITDYNDLQlQMQQRLMEKNLAANLIYSI 161
Cdd:cd02605    81 EPDTYWNEVLSEGWE----RFLFEAIADLfKQLKPQSELEQNPHKISFYLDPQNDAAVIE-QLEEMLLKAGLTVRIIYSS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 162 DEAasiGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQAQQQANPEHLyc 241
Cdd:cd02605   156 GLA---YDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLA-- 230
                         250       260
                  ....*....|....*....|...
gi 2017528048 242 argdffgmNGNYSAGILEGIAHY 264
Cdd:cd02605   231 --------KGPYAGGILEGLAHF 245
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
2-265 6.60e-59

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 187.86  E-value: 6.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   2 PRLLICTDLDRTLLPngkqaesPEARALfARLMA-----RHEVYLAFVSGRHRALVEQAIADYQLPTPDWVIADVGSSIY 76
Cdd:pfam05116   1 PPLLLVSDLDNTLVD-------GDNEAL-ARLNQlleayRPDVGLVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  77 AVHDDwQAWHSWQHAIAVDWQdltaPD-LQTLFTDLTVLTLQESEKQNRYKLSYYLPLITDYNDLQlQMQQRLMEKNLAA 155
Cdd:pfam05116  73 YGPSL-VPDQSWQEHLDYHWD----RQaVVEALAKFPGLTLQPEEEQRPHKVSYFLDPEAAAAVLA-ELEQLLRKRGLDV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 156 NLIYSIDEAasiglLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQAQQQA- 234
Cdd:pfam05116 147 KVIYSSGRD-----LDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQPELLQWYLENAr 221
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2017528048 235 NPEHLYCArgdffgmNGNYSAGILEGIAHYH 265
Cdd:pfam05116 222 DNPRIYFA-------SGRCAGGILEGIRHFG 245
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
1-264 2.63e-30

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 112.54  E-value: 2.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   1 MPRLlICTDLDRTLLPNGKQAeSPEARALFARLMARHeVYLAFVSGRHRALVEQAIADYQLPtpDWVIADVGSSIYAVHD 80
Cdd:COG0561     1 MIKL-IALDLDGTLLNDDGEI-SPRTKEALRRLREKG-IKVVIATGRPLRSALPLLEELGLD--DPLITSNGALIYDPDG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  81 DWqawhswqhaiaVDWQDLTAPDLQTLFtdltvltlqesekqnryklsyylplitdyndlqlqmqQRLMEKNLAANLIYS 160
Cdd:COG0561    76 EV-----------LYERPLDPEDVREIL-------------------------------------ELLREHGLHLQVVVR 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 161 ideaASIGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQAQqqanpehlY 240
Cdd:COG0561   108 ----SGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAAD--------Y 175
                         250       260
                  ....*....|....*....|....
gi 2017528048 241 CARgdffgmnGNYSAGILEGIAHY 264
Cdd:COG0561   176 VTG-------SNDEDGVAEALEKL 192
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
3-264 6.97e-27

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.


Pssm-ID: 130549  Cd Length: 249  Bit Score: 104.89  E-value: 6.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   3 RLLICTDLDRTLL--PNGKQAESPEARALFARlMARHEVYLAFVSGRHRALVEQAIADYQLPTPDWVIADVGSSIY---- 76
Cdd:TIGR01485   1 RLLLVSDLDNTLVdhTDGDNQALLRLNALLED-HRGEDSLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYygga 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  77 -AVHDDWQAWHS--WQHAIavdwqdltapdLQTLFTDLTVLTLQESEKQNRYKLSYYLPLITDYNDLQlQMQQRLMEKNL 153
Cdd:TIGR01485  80 eVPDQHWAEYLSekWQRDI-----------VVAITDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIK-QLTEMLKETGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 154 AANLIYSIDEAasiglLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVL-ISHIPSVLVANADDNVRQQAQQ 232
Cdd:TIGR01485 148 DVKLIYSSGKD-----LDILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFeIGSVRGVIVSNAQEELLQWYDE 222
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2017528048 233 QANpEHLYCArgdffgmNGNYSAGILEGIAHY 264
Cdd:TIGR01485 223 NAK-DKIYHA-------SERCAGGIIEAIAHF 246
PLN02382 PLN02382
probable sucrose-phosphatase
2-264 2.74e-22

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 95.44  E-value: 2.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   2 PRLLICTDLDRTLLPNGkqaeSPEARAL--FARLMA---RHEVYLAFVSGRHRALVEQAIADYQLPTPDWVIADVGSSI- 75
Cdd:PLN02382    8 PRLMIVSDLDHTMVDHH----DPENLSLlrFNALWEaeyRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEIa 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  76 YA---VHDDwqAW-----HSWQHAIAVDwqdltapdlQTLftDLTVLTLQESEKQNRYKLSYYLplitDYNDLQLQMQ-- 145
Cdd:PLN02382   84 YGesmVPDH--GWveylnKKWDREIVVE---------ETS--KFPELKLQPETEQRPHKVSFYV----DKKKAQEVIKel 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 146 -QRLMEKNLAANLIYS--IDeaasiglLDVLPKRANKLHAIEFLMQQ---QGFTDENTVFAGDSGNDlAVLIShIPSV-- 217
Cdd:PLN02382  147 sERLEKRGLDVKIIYSggID-------LDVLPQGAGKGQALAYLLKKlkaEGKAPVNTLVCGDSGND-AELFS-VPDVyg 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2017528048 218 -LVANADDNVRQ-QAQQQANPEHLY-----CArgdffgmngnysAGILEGIAHY 264
Cdd:PLN02382  218 vMVSNAQEELLQwYAENAKDNPKIIhaterCA------------AGIIQAIGHF 259
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
6-240 1.32e-17

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 79.43  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   6 ICTDLDRTLL-PNGKQAESPEAralFARLMARHEVYLAFVSGRHRALVEQAiaDYQLPTPDWVIADVGSSIYAVHDDWQA 84
Cdd:TIGR01482   1 IASDIDGTLTdPNRAINESALE---AIRKAESKGIPVVLVTGNSVQFARAL--AKLIGTPDPVIAENGGEISYNEGLDDI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  85 WHSW--QHAIAVDWQDLTAPdlqtlftdLTVLTLQESEKQNRYKLSYYLplitdyndlQLQMQQRLMEKnLAANLiysiD 162
Cdd:TIGR01482  76 FLAYleEEWFLDIVIAKTFP--------FSRLKVQYPRRASLVKMRYGI---------DVDTVREIIKE-LGLNL----V 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017528048 163 EAASIGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQAQQQANPEHLY 240
Cdd:TIGR01482 134 AVDSGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWADYVTESPYGE 211
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
6-230 4.25e-16

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 75.74  E-value: 4.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   6 ICTDLDRTLLPNGKQAeSPEARALFARLMARhEVYLAFVSGRHRALVEQAIADYQLPTPdwVIADVGSSIYAVHD----- 80
Cdd:pfam08282   1 IASDLDGTLLNSDKKI-SEKTKEAIKKLKEK-GIKFVIATGRPYRAILPVIKELGLDDP--VICYNGALIYDENGkilys 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  81 --------------------DWQAWH--SWQHAIAVDWQDLTAPDLQTLFTDLTVLTLQESEKQNRYKLSyylpLITDYN 138
Cdd:pfam08282  77 npiskeavkeiieylkennlEILLYTddGVYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDINKIL----ILLDEE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 139 DLQlQMQQRLmEKNLAANLIYSIdeaASIGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAvLISHIP-SV 217
Cdd:pfam08282 153 DLD-ELEKEL-KELFGSLITITS---SGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIE-MLEAAGlGV 226
                         250
                  ....*....|...
gi 2017528048 218 LVANADDNVRQQA 230
Cdd:pfam08282 227 AMGNASPEVKAAA 239
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
5-210 1.41e-15

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 73.57  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   5 LICTDLDRTLLPNGKQAESPEARALFARLMARhEVYLAFVSGRHRALVeQAIADyQLPTPDWVIADVGSSIYAVH----- 79
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHELSPETIEALERLREA-GVKVVIVTGRSLAEI-KELLK-QLNLPLPLIAENGALIFYPGeilyi 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  80 ---DDWQAWHSWQHAIAVDwqDLTApdlqtlFTDLTVLTLQEsekqnRYKLSYylplITDYNDLQlqMQQRLMEKNLAAN 156
Cdd:TIGR01484  78 epsDVFEEILGIKFEEIGA--ELKS------LSEHYVGTFIE-----DKAIAV----AIHYVGAE--LGQELDSKMRERL 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 157 LIYSIDEAA------SIGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVL 210
Cdd:TIGR01484 139 EKIGRNDLEleaiysGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMF 198
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
5-230 2.89e-10

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 59.20  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   5 LICTDLDRTLLPNGKQAeSPEARALFARLMAR-HEVYLAfvSGRHRALVEQAIADYQLPTP------DWVIADVGSSIYa 77
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTI-SPSTKEALAKLREKgIKVVLA--TGRPYKEVKNILKELGLDTPfitangAAVIDDQGEILY- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  78 vhddwqawhswQHAIAVD-----WQDLTAPDLQTLFTDLTVLTLQ----ESEKQNRYKLSYYLP---------------- 132
Cdd:TIGR00099  77 -----------KKPLDLDlveeiLNFLKKHGLDVILYGDDSIYASkndpEYFTIFKKFLGEPKLevvdiqylpddilkil 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 133 -LITDYNDLQlQMQQRLMEKNLAANLIYSIdeaASIGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLI 211
Cdd:TIGR00099 146 lLFLDPEDLD-LLIEALNKLELEENVSVVS---SGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLE 221
                         250
                  ....*....|....*....
gi 2017528048 212 SHIPSVLVANADDNVRQQA 230
Cdd:TIGR00099 222 AAGYGVAMGNADEELKALA 240
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
5-231 3.08e-09

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 56.06  E-value: 3.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   5 LICTDLDRTLLPNGKQAeSPEARALFARLMARHeVYLAFVSGRH-RALveQAIADyQLPTPDWVIADVGSSIYAVH---- 79
Cdd:cd07516     1 LIALDLDGTLLNSDKEI-SPRTKEAIKKAKEKG-IKVVIATGRPlRGA--QPYLE-ELGLDSPLITFNGALVYDPTgkei 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  80 -------DDWQAW--HSWQHAIAVDWQDLTAPDLQTLFTDLTVLTLQESEKQNRYKLSYYLP----LITDYNDLQLQMQQ 146
Cdd:cd07516    76 lerliskEDVKELeeFLRKLGIGINIYTNDDWADTIYEENEDDEIIKPAEILDDLLLPPDEDitkiLFVGEDEELDELIA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 147 RLMEK-NLAANLIYSideaaSIGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAvLISHIP-SVLVANADD 224
Cdd:cd07516   156 KLPEEfFDDLSVVRS-----APFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLS-MLEYAGlGVAMGNAID 229

                  ....*..
gi 2017528048 225 NVRQQAQ 231
Cdd:cd07516   230 EVKEAAD 236
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
5-236 5.32e-09

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 54.51  E-value: 5.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   5 LICTDLDRTLLPNGKQAESPEARALFARLMARHevyLAFV--SGRHRALVEQAIADYQLPTpdWVIADVGSSIYavhddw 82
Cdd:cd07518     2 LIATDMDGTFLNDDKTYDHERFFAILDQLLKKG---IKFVvaSGRQYYQLISFFPEIKDEM--SFVAENGAVVY------ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  83 qawhswqHAIAVDWQDLTAPDLQTLFTDltvltlqesekqnryKLSYYLPLITDYNdlqlqmqqrlmeknlaanliysid 162
Cdd:cd07518    71 -------FKFTLNVPDEAAPDIIDELNQ---------------KFGGILRAVTSGF------------------------ 104
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017528048 163 eaasiGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQAQQQANP 236
Cdd:cd07518   105 -----GSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAAKYVAPS 173
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
169-235 5.63e-05

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 43.29  E-value: 5.63e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017528048 169 LLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVL-ISHIPsvlVA-NADDNVRQQAQQQAN 235
Cdd:COG0560   146 VVGPIVDGEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLeAAGLP---VAvNPDPALREAADRERG 211
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
4-202 1.38e-04

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 42.28  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048   4 LLICtDLDRTLLPNGKQAE----SPEARALFARLMARHEVYLAFVSGRHRALVEQAIADYQLptpdWVIADVGSSI-YAV 78
Cdd:cd01627     1 LLFL-DYDGTLAPIVPDPDaavpSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGI----GLAGEHGAEIrLPG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048  79 HDDWQawHSWQHAIAvDWQDLTAPDLQtLFTDLTVLTLQEsEKQNRYKLSYYLpliTDYNDLQ--LQMQQRLMEKNLAAN 156
Cdd:cd01627    76 GGEWV--TLAPKADL-EWKEEVEAIFK-YFTERTPGSLVE-DKGASLAWHYRN---ADPEGARaaLELALHLASDLLKAL 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2017528048 157 LIYSIDEAasiglLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGD 202
Cdd:cd01627   148 EVVPGKKV-----VEVRPVGVNKGEAVERILGELPFAGDFVLCAGD 188
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
164-231 1.54e-04

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 40.97  E-value: 1.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017528048 164 AASIGLLDVLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQAQ 231
Cdd:cd01630    62 AKELGIEDLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAAD 129
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
172-230 5.63e-04

phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases.


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 40.11  E-value: 5.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017528048 172 VLPKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQA 230
Cdd:TIGR01487 141 IMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEIA 199
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
178-264 3.75e-03

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 36.80  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528048 178 NKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQAQqqanpehlYCARgdffgmnGNYSAGI 257
Cdd:cd07514    67 DKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAAD--------YVTD-------ASYGDGV 131

                  ....*..
gi 2017528048 258 LEGIAHY 264
Cdd:cd07514   132 LEAIDKL 138
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
158-230 7.79e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 36.87  E-value: 7.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017528048 158 IYSIDEAASIGLLDvlpKRANKLHAIEFLMQQQGFTDENTVFAGDSGNDLAVLISHIPSVLVANADDNVRQQA 230
Cdd:PRK01158  140 LEIVDSGFAIHIKS---PGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAA 209
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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