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Conserved domains on  [gi|446308319|ref|WP_000386174|]
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MULTISPECIES: HAD-IIB family hydrolase [Bacillus]

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 ...
 18-276 4.28e-54

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: 175.62  E-value: 4.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  18 IVFSDFDETYFPHQltaerkSQIQALE--QTIVEK-SRISGLLFGLVTGSNIEAVLEKMKRGgFQYLPHFIASDLGTEIH 94
Cdd:cd02605    1 LLVSDLDETLVGHD------TNLQALErlQDLLEQlTADNDVILVYATGRSPESVLELIKEV-MLPKPDFIISDVGTEIY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  95 YFNKlKQGEIDKEWLSRFDNGnYHPDKIKEIVDLLAskniALDSQSQMGASKYKSNYYYFSKNekdDQLNLNHIRQVASD 174
Cdd:cd02605   74 YGES-GYLEPDTYWNEVLSEG-WERFLFEAIADLFK----QLKPQSELEQNPHKISFYLDPQN---DAAVIEQLEEMLLK 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319 175 FKISININQCNPLAgdpenaYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAK 254
Cdd:cd02605  145 AGLTVRIIYSSGLA------YDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELL 218

                        250       260
                 ....*....|....*....|....*..
gi 446308319 255 NGHERLTI-----GSYSEGILNTIKEL 276
Cdd:cd02605  219 KWADRVTRsrlakGPYAGGILEGLAHF 245
 
Name Accession Description Interval E-value
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 18-276 4.28e-54

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: 175.62  E-value: 4.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  18 IVFSDFDETYFPHQltaerkSQIQALE--QTIVEK-SRISGLLFGLVTGSNIEAVLEKMKRGgFQYLPHFIASDLGTEIH 94
Cdd:cd02605    1 LLVSDLDETLVGHD------TNLQALErlQDLLEQlTADNDVILVYATGRSPESVLELIKEV-MLPKPDFIISDVGTEIY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  95 YFNKlKQGEIDKEWLSRFDNGnYHPDKIKEIVDLLAskniALDSQSQMGASKYKSNYYYFSKNekdDQLNLNHIRQVASD 174
Cdd:cd02605   74 YGES-GYLEPDTYWNEVLSEG-WERFLFEAIADLFK----QLKPQSELEQNPHKISFYLDPQN---DAAVIEQLEEMLLK 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319 175 FKISININQCNPLAgdpenaYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAK 254
Cdd:cd02605  145 AGLTVRIIYSSGLA------YDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELL 218

                        250       260
                 ....*....|....*....|....*..
gi 446308319 255 NGHERLTI-----GSYSEGILNTIKEL 276
Cdd:cd02605  219 KWADRVTRsrlakGPYAGGILEGLAHF 245
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 15-276 5.36e-24

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: 95.59  E-value: 5.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  15 PKYIVFSDFDETYFP--HQLTAERKSQIQALEQtiveksriSGLLFGLVTGSNIEAVLEKMKRGGfqyLPHFIASDLGTE 92
Cdd:COG0561    1 MIKLIALDLDGTLLNddGEISPRTKEALRRLRE--------KGIKVVIATGRPLRSALPLLEELG---LDDPLITSNGAL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  93 IHYFnklkQGEIDKEwlSRFDngnyhPDKIKEIVDLLASKNIALdsqsqmgaskyksNYYYFSknekddqlnlnhirqva 172
Cdd:COG0561   70 IYDP----DGEVLYE--RPLD-----PEDVREILELLREHGLHL-------------QVVVRS----------------- 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319 173 sdfkisininqcnplagdpeNAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSE 252
Cdd:COG0561  109 --------------------GPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                        250       260
                 ....*....|....*....|....
gi 446308319 253 AKNGHERLTIGSYSEGILNTIKEL 276
Cdd:COG0561  169 VKAAADYVTGSNDEDGVAEALEKL 192
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 15-274 1.25e-14

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: 71.53  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   15 PKYIVFSDFDETYFPHqltaERksqiQALEQ--TIVEKSRIsGLLFGLVTGSNIEAVLEKMKRggFQYL-PHFIASDLGT 91
Cdd:pfam05116   1 PPLLLVSDLDNTLVDG----DN----EALARlnQLLEAYRP-DVGLVFATGRSLDSAKELLKE--KPLPtPDYLITSVGT 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   92 EIHYFNKLkqgEIDKEWLSRFDNGnYHPDKIKEIVDLLAskNIALDSQSQMGAskYKSNYYYfsknEKDDQLNL-----N 166
Cdd:pfam05116  70 EIYYGPSL---VPDQSWQEHLDYH-WDRQAVVEALAKFP--GLTLQPEEEQRP--HKVSYFL----DPEAAAAVlaeleQ 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  167 HIRQVASDFKISINinqcnplagdpeNAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLL 246
Cdd:pfam05116 138 LLRKRGLDVKVIYS------------SGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVV 205

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 446308319  247 ENATSE-----AKNGHERLTI----GSYSEGILNTIK 274
Cdd:pfam05116 206 GNAQPEllqwyLENARDNPRIyfasGRCAGGILEGIR 242
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 18-244 5.38e-13

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: 66.25  E-value: 5.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   18 IVFSDFDETYFPHQ---LTAERKSQIQALEQTiveksrisGLLFGLVTGSNIEAVLEKMKrggFQYLPHFIASDLGTEIH 94
Cdd:TIGR01484   1 LLFFDLDGTLLDPNaheLSPETIEALERLREA--------GVKVVIVTGRSLAEIKELLK---QLNLPLPLIAENGALIF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   95 Y-----FNKLKQGEidKEWLSRFDNGNYHPdkIKEIVDLLASKNIALDSQSQmgaskyksNYYYFSKNEKDDqlnlnhir 169
Cdd:TIGR01484  70 YpgeilYIEPSDVF--EEILGIKFEEIGAE--LKSLSEHYVGTFIEDKAIAV--------AIHYVGAELGQE-------- 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446308319  170 qVASDFKISININQCNPLAGD--PENAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGY 244
Cdd:TIGR01484 130 -LDSKMRERLEKIGRNDLELEaiYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAV 205
PLN02382 PLN02382
probable sucrose-phosphatase
 193-258 4.30e-05

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 4.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446308319 193 NAYDIDFIPLGTGKDEIVRYILAKFKIDR---QNAIAFGDSGNDLKmLQAVK--FGYLLENATSEAKNGHE 258
Cdd:PLN02382 163 GGIDLDVLPQGAGKGQALAYLLKKLKAEGkapVNTLVCGDSGNDAE-LFSVPdvYGVMVSNAQEELLQWYA 232
 
Name Accession Description Interval E-value
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 18-276 4.28e-54

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: 175.62  E-value: 4.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  18 IVFSDFDETYFPHQltaerkSQIQALE--QTIVEK-SRISGLLFGLVTGSNIEAVLEKMKRGgFQYLPHFIASDLGTEIH 94
Cdd:cd02605    1 LLVSDLDETLVGHD------TNLQALErlQDLLEQlTADNDVILVYATGRSPESVLELIKEV-MLPKPDFIISDVGTEIY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  95 YFNKlKQGEIDKEWLSRFDNGnYHPDKIKEIVDLLAskniALDSQSQMGASKYKSNYYYFSKNekdDQLNLNHIRQVASD 174
Cdd:cd02605   74 YGES-GYLEPDTYWNEVLSEG-WERFLFEAIADLFK----QLKPQSELEQNPHKISFYLDPQN---DAAVIEQLEEMLLK 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319 175 FKISININQCNPLAgdpenaYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAK 254
Cdd:cd02605  145 AGLTVRIIYSSGLA------YDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELL 218

                        250       260
                 ....*....|....*....|....*..
gi 446308319 255 NGHERLTI-----GSYSEGILNTIKEL 276
Cdd:cd02605  219 KWADRVTRsrlakGPYAGGILEGLAHF 245
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 15-276 5.36e-24

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: 95.59  E-value: 5.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  15 PKYIVFSDFDETYFP--HQLTAERKSQIQALEQtiveksriSGLLFGLVTGSNIEAVLEKMKRGGfqyLPHFIASDLGTE 92
Cdd:COG0561    1 MIKLIALDLDGTLLNddGEISPRTKEALRRLRE--------KGIKVVIATGRPLRSALPLLEELG---LDDPLITSNGAL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  93 IHYFnklkQGEIDKEwlSRFDngnyhPDKIKEIVDLLASKNIALdsqsqmgaskyksNYYYFSknekddqlnlnhirqva 172
Cdd:COG0561   70 IYDP----DGEVLYE--RPLD-----PEDVREILELLREHGLHL-------------QVVVRS----------------- 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319 173 sdfkisininqcnplagdpeNAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSE 252
Cdd:COG0561  109 --------------------GPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                        250       260
                 ....*....|....*....|....
gi 446308319 253 AKNGHERLTIGSYSEGILNTIKEL 276
Cdd:COG0561  169 VKAAADYVTGSNDEDGVAEALEKL 192
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 15-274 1.25e-14

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: 71.53  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   15 PKYIVFSDFDETYFPHqltaERksqiQALEQ--TIVEKSRIsGLLFGLVTGSNIEAVLEKMKRggFQYL-PHFIASDLGT 91
Cdd:pfam05116   1 PPLLLVSDLDNTLVDG----DN----EALARlnQLLEAYRP-DVGLVFATGRSLDSAKELLKE--KPLPtPDYLITSVGT 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   92 EIHYFNKLkqgEIDKEWLSRFDNGnYHPDKIKEIVDLLAskNIALDSQSQMGAskYKSNYYYfsknEKDDQLNL-----N 166
Cdd:pfam05116  70 EIYYGPSL---VPDQSWQEHLDYH-WDRQAVVEALAKFP--GLTLQPEEEQRP--HKVSYFL----DPEAAAAVlaeleQ 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  167 HIRQVASDFKISINinqcnplagdpeNAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLL 246
Cdd:pfam05116 138 LLRKRGLDVKVIYS------------SGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVV 205

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 446308319  247 ENATSE-----AKNGHERLTI----GSYSEGILNTIK 274
Cdd:pfam05116 206 GNAQPEllqwyLENARDNPRIyfasGRCAGGILEGIR 242
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 197-274 1.80e-14

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: 69.92  E-value: 1.80e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446308319 197 IDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAKNgHERLTIGSYSE-GILNTIK 274
Cdd:cd07518  107 IDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKA-AAKYVAPSNNEnGVLQVIE 184
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 18-244 5.38e-13

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: 66.25  E-value: 5.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   18 IVFSDFDETYFPHQ---LTAERKSQIQALEQTiveksrisGLLFGLVTGSNIEAVLEKMKrggFQYLPHFIASDLGTEIH 94
Cdd:TIGR01484   1 LLFFDLDGTLLDPNaheLSPETIEALERLREA--------GVKVVIVTGRSLAEIKELLK---QLNLPLPLIAENGALIF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   95 Y-----FNKLKQGEidKEWLSRFDNGNYHPdkIKEIVDLLASKNIALDSQSQmgaskyksNYYYFSKNEKDDqlnlnhir 169
Cdd:TIGR01484  70 YpgeilYIEPSDVF--EEILGIKFEEIGAE--LKSLSEHYVGTFIEDKAIAV--------AIHYVGAELGQE-------- 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446308319  170 qVASDFKISININQCNPLAGD--PENAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGY 244
Cdd:TIGR01484 130 -LDSKMRERLEKIGRNDLELEaiYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAV 205
sucr_syn_bact_C TIGR02471
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate ...
 58-274 2.41e-12

sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate synthase (SPS) and sucrose phosphate phosphatase (SPP) are the last two enzymes of sucrose biosynthesis. In cyanobacteria and plants, the C-terminal region of most or all versions of SPS has a domain homologous to the known SPP. This domain may serve a binding or regulatory rather than catalytic function. Sequences in this family are bacterial C-terminal regions found in all but two of the putative bacterial sucrose phosphate synthases described by TIGR02472.


Pssm-ID: 131524  Cd Length: 236  Bit Score: 64.79  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   58 FGLVTGSNIEAVLEKMKRGGFQyLPHFIASDLGTEIHYFNKLKqgeIDKEWLSRFDngnyHPDKIKEIVDLLAS-KNIAL 136
Cdd:TIGR02471  33 FGIATGRSVESAKSRYAKLNLP-SPDVLIARVGTEIYYGPELQ---PDRFWQKHID----HDWRRQAVVEALADiPGLTL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  137 -DSQSQmgaSKYKSNYYYFSKNEKDDQLNLNHIRQVASDFKISININQCnplagdpenaydIDFIPLGTGKDEIVRYILA 215
Cdd:TIGR02471 105 qDDQEQ---GPFKISYLLDPEGEPILPQIRQRLRQQSQAAKVILSCGWF------------LDVLPLRASKGLALRYLSY 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446308319  216 KFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAKNGHERLTI----GSYSEGILNTIK 274
Cdd:TIGR02471 170 RWGLPLEQILVAGDSGNDEEMLRGLTLGVVVGNHDPELEGLRHQQRIyfanNPHAFGILEGIN 232
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 18-273 1.69e-11

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: 62.67  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   18 IVFSDFDET-YFP-HQLTAERKSQIQALeqtiveksRISGLLFGLVTGSNIEAVLEKMKRGGFQYLphFIASDlGTEIHY 95
Cdd:TIGR00099   1 LIFIDLDGTlLNDdHTISPSTKEALAKL--------REKGIKVVLATGRPYKEVKNILKELGLDTP--FITAN-GAAVID 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   96 FNklkQGEIDKEWLSRfdngnyhpDKIKEIVDLLASKNIaldsqsQMGASKYKSNYYYFSKNE----KDDQLNLNHIRQV 171
Cdd:TIGR00099  70 DQ---GEILYKKPLDL--------DLVEEILNFLKKHGL------DVILYGDDSIYASKNDPEyftiFKKFLGEPKLEVV 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  172 ASDFKISININQCNpLAGDPE-----------------------NAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFG 228
Cdd:TIGR00099 133 DIQYLPDDILKILL-LFLDPEdldlliealnkleleenvsvvssGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFG 211

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 446308319  229 DSGNDLKMLQAVKFGYLLENATSEAKNgHERLTIGSYSE-GILNTI 273
Cdd:TIGR00099 212 DGMNDIEMLEAAGYGVAMGNADEELKA-LADYVTDSNNEdGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 19-255 4.02e-11

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 61.87  E-value: 4.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   19 VFSDFDETYFP--HQLTAERKSQIQALEQtiveksriSGLLFGLVTGSNIEAVLEKMKRGGFQylPHFIASDlGTEIHYF 96
Cdd:pfam08282   1 IASDLDGTLLNsdKKISEKTKEAIKKLKE--------KGIKFVIATGRPYRAILPVIKELGLD--DPVICYN-GALIYDE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   97 NK--LKQGEIDKEwlsrfdngnyhpdKIKEIVDLLASKNIAL----------DSQSQMGASKYKSNYYYFSKNEKDDQLN 164
Cdd:pfam08282  70 NGkiLYSNPISKE-------------AVKEIIEYLKENNLEIllytddgvyiLNDNELEKILKELNYTKSFVPEIDDFEL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  165 LNHIR----QVASDFKISININQ-CNPLAGDPENAYD-----IDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDL 234
Cdd:pfam08282 137 LEDEDinkiLILLDEEDLDELEKeLKELFGSLITITSsgpgyLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDI 216

                         250       260
                  ....*....|....*....|.
gi 446308319  235 KMLQAVKFGYLLENATSEAKN 255
Cdd:pfam08282 217 EMLEAAGLGVAMGNASPEVKA 237
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 18-276 1.01e-10

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. 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: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 59.93  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  18 IVFSDFDETYFPHQltaerkSQIQALEQTIVEKSRISGLLFGLVTGSNIEAVLEKMKRGGfqylPHFIASDLGTEIHYFN 97
Cdd:cd07517    2 IVFFDIDGTLLDED------TTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALG----IDSYVSYNGQYVFFEG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  98 K-LKQGEIDKEwlsrfdngnyhpdKIKEIVDLLASKNIALDSQSQMGAskyksnyyYFSKNEKDDQLNLnhirqvASDFK 176
Cdd:cd07517   72 EvIYKNPLPQE-------------LVERLTEFAKEQGHPVSFYGQLLL--------FEDEEEEQKYEEL------RPELR 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319 177 ISINinqcnplagdpeNAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAKNG 256
Cdd:cd07517  125 FVRW------------HPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEI 192

                        250       260
                 ....*....|....*....|
gi 446308319 257 HERLTIGSYSEGILNTIKEL 276
Cdd:cd07517  193 ADYVTKDVDEDGILKALKHF 212
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 203-276 7.09e-09

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: 53.36  E-value: 7.09e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446308319 203 GTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAKNGHERLTIGSYSEGILNTIKEL 276
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKL 138
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 154-255 2.01e-08

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: 53.75  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319 154 FSKNEKDDQLnlnhIRQVASDFKISININQCNPlagdpenaYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGND 233
Cdd:cd07516  144 VGEDEELDEL----IAKLPEEFFDDLSVVRSAP--------FYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNEND 211

                         90       100
                 ....*....|....*....|..
gi 446308319 234 LKMLQAVKFGYLLENATSEAKN 255
Cdd:cd07516  212 LSMLEYAGLGVAMGNAIDEVKE 233
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 197-244 7.66e-08

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: 51.76  E-value: 7.66e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446308319 197 IDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGY 244
Cdd:COG0560  147 VGPIVDGEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPV 194
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 19-275 7.87e-07

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: 49.00  E-value: 7.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   19 VFSDFDETYFPHQlTAERKSQIQALEqtiveKSRISGLLFGLVTGSNIEAVLEKMKRGGfqyLPHFIASDLGTEIHYFNK 98
Cdd:TIGR01482   1 IASDIDGTLTDPN-RAINESALEAIR-----KAESKGIPVVLVTGNSVQFARALAKLIG---TPDPVIAENGGEISYNEG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319   99 LKQGeidkeWLSRFDNgNYHPDKIKEIVDLLAskniALDSQSQMGASKYKSNYYyfsknekddqLNLNHIRQVASdfKIS 178
Cdd:TIGR01482  72 LDDI-----FLAYLEE-EWFLDIVIAKTFPFS----RLKVQYPRRASLVKMRYG----------IDVDTVREIIK--ELG 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446308319  179 ININQCNplagdpeNAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAKNGHE 258
Cdd:TIGR01482 130 LNLVAVD-------SGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWAD 202

                         250
                  ....*....|....*..
gi 446308319  259 RLTIGSYSEGILNTIKE 275
Cdd:TIGR01482 203 YVTESPYGEGGAEAIGE 219
PLN02382 PLN02382
probable sucrose-phosphatase
 193-258 4.30e-05

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 4.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446308319 193 NAYDIDFIPLGTGKDEIVRYILAKFKIDR---QNAIAFGDSGNDLKmLQAVK--FGYLLENATSEAKNGHE 258
Cdd:PLN02382 163 GGIDLDVLPQGAGKGQALAYLLKKLKAEGkapVNTLVCGDSGNDAE-LFSVPdvYGVMVSNAQEELLQWYA 232
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 222-277 9.93e-05

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 42.70  E-value: 9.93e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446308319 222 QNAIAFGDSGNDLKMLQAVKFGYLLENATSEAKNgHERLTIGSYSE-GILNTIKELV 277
Cdd:PRK10530 216 KNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKA-RADLVIGDNTTpSIAEFIYSHV 271
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 193-252 1.08e-04

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: 42.49  E-value: 1.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446308319  193 NAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVK-FGYLLENATSE 252
Cdd:TIGR01485 155 SGKDLDILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSvRGVIVSNAQEE 215
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 168-240 2.06e-04

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 41.19  E-value: 2.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446308319  168 IRQVASdfKISININQCNPLA----GDPENAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAV 240
Cdd:TIGR01488 103 VEPVAE--KLGIDDVFANRLEfddnGLLTGPIEGQVNPEGECKGKVLKELLEESKITLKKIIAVGDSVNDLPMLKLA 177
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 203-277 2.95e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 41.11  E-value: 2.95e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446308319 203 GTGkdeiVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAKNGHERLTIGSYSEGILNTIKELV 277
Cdd:PRK01158 159 GTG----LKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVTEKSYGEGVAEAIEHLL 229
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 187-240 5.76e-04

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 39.88  E-value: 5.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446308319  187 LAGDPENAYDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAV 240
Cdd:pfam00702 137 LDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAA 190
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 205-277 9.84e-04

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 39.68  E-value: 9.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446308319 205 GKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAKNGHERLTIGSYSEGILNTIKELV 277
Cdd:PRK10513 196 NKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEKYV 268
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 203-243 2.65e-03

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 37.91  E-value: 2.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446308319 203 GTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFG 243
Cdd:cd07500  135 AQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLG 175
PLN02887 PLN02887
hydrolase family protein
 197-254 3.33e-03

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 38.70  E-value: 3.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446308319 197 IDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAK 254
Cdd:PLN02887 499 LEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASLGVALSNGAEKTK 556
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 203-252 4.41e-03

Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 37.88  E-value: 4.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446308319 203 GTGKDEIVRYILAKFKIDRQNA---IAFGDSGNDLKMLQAVKFGYLLENATSE 252
Cdd:COG3769  186 GADKGKAVRWLVEQYRQRFGKNvvtIALGDSPNDIPMLEAADIAVVIRSPHGA 238
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 195-269 8.80e-03

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: 36.64  E-value: 8.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446308319  195 YDIDFIPLGTGKDEIVRYILAKFKIDRQNAIAFGDSGNDLKMLQAVKFGYLLENATSEAKNGHERLTIGSYSEGI 269
Cdd:TIGR01487 137 FAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEIADYVTSNPYGEGV 211
 
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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