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Conserved domains on  [gi|489956272|ref|WP_003859579|]
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MULTISPECIES: mannosyl-3-phosphoglycerate phosphatase-related protein [Enterobacter]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK03669 super family cl30871
mannosyl-3-phosphoglycerate phosphatase-related protein;
1-265 4.31e-160

mannosyl-3-phosphoglycerate phosphatase-related protein;


The actual alignment was detected with superfamily member PRK03669:

Pssm-ID: 179628 [Multi-domain]  Cd Length: 271  Bit Score: 445.23  E-value: 4.31e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   1 MPSLEETLLVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGLPYIAENGAVIQPDV 80
Cdd:PRK03669   1 MLSLQDPLLIFTDLDGTLLDSHTYDWQPAAPWLTRLREAQVPVILCSSKTAAEMLPLQQTLGLQGLPLIAENGAVIQLDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  81 RWE---NAARFISEKKHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQMRY 157
Cdd:PRK03669  81 QWQdhpDFPRIISGISHGEIRQVLNTLREKEGFKFTTFDDVDDATIAEWTGLSRSQAALARLHEASVTLIWRDSDERMAQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272 158 FAAELARQRLKIVQGARFWHILDTCCGKDVAVHWLVDQYRLHEGYEPTTLGLGDGPNDAPLLDSVGFAVVVKGFNREGIS 237
Cdd:PRK03669 161 FTARLAELGLQFVQGARFWHVLDASAGKDQAANWLIATYQQLSGTRPTTLGLGDGPNDAPLLDVMDYAVVVKGLNREGVH 240

                        250       260
                 ....*....|....*....|....*...
gi 489956272 238 LINNDPARVYHTQHTGPTGWCEGLDYFL 265
Cdd:PRK03669 241 LQDDDPARVYRTQREGPEGWREGLDHFF 268
 
Name Accession Description Interval E-value
PRK03669 PRK03669
mannosyl-3-phosphoglycerate phosphatase-related protein;
1-265 4.31e-160

mannosyl-3-phosphoglycerate phosphatase-related protein;


Pssm-ID: 179628 [Multi-domain]  Cd Length: 271  Bit Score: 445.23  E-value: 4.31e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   1 MPSLEETLLVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGLPYIAENGAVIQPDV 80
Cdd:PRK03669   1 MLSLQDPLLIFTDLDGTLLDSHTYDWQPAAPWLTRLREAQVPVILCSSKTAAEMLPLQQTLGLQGLPLIAENGAVIQLDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  81 RWE---NAARFISEKKHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQMRY 157
Cdd:PRK03669  81 QWQdhpDFPRIISGISHGEIRQVLNTLREKEGFKFTTFDDVDDATIAEWTGLSRSQAALARLHEASVTLIWRDSDERMAQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272 158 FAAELARQRLKIVQGARFWHILDTCCGKDVAVHWLVDQYRLHEGYEPTTLGLGDGPNDAPLLDSVGFAVVVKGFNREGIS 237
Cdd:PRK03669 161 FTARLAELGLQFVQGARFWHVLDASAGKDQAANWLIATYQQLSGTRPTTLGLGDGPNDAPLLDVMDYAVVVKGLNREGVH 240

                        250       260
                 ....*....|....*....|....*...
gi 489956272 238 LINNDPARVYHTQHTGPTGWCEGLDYFL 265
Cdd:PRK03669 241 LQDDDPARVYRTQREGPEGWREGLDHFF 268
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 8-265 2.13e-116

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 334.49  E-value: 2.13e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   8 LLVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlPYIAENGAVIQPDVRWENAAR 87
Cdd:COG3769    4 LLVFTDLDGTLLDHDTYSWAAALPALARLKARGIPVILNTSKTAAEVEPLRQELGLSD-PFIVENGAAIFIPKGYFAFPS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  88 FISE----------KKHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQMRY 157
Cdd:COG3769   83 GTADidgywvielgKPYAEIRAVLEQLREELGFKFTGFGDMSAEEVAELTGLSLEQAALAKQREFSEPLLWLGSDEALER 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272 158 FAAELARQRLKIVQGARFWHILDtCCGKDVAVHWLVDQYRLHEGYEPTTLGLGDGPNDAPLLDSVGFAVVVKGFNREGIS 237
Cdd:COG3769  163 FIAALAALGLTVLRGGRFLHLMG-GADKGKAVRWLVEQYRQRFGKNVVTIALGDSPNDIPMLEAADIAVVIRSPHGAPPE 241

                        250       260
                 ....*....|....*....|....*...
gi 489956272 238 LinNDPARVYHTQHTGPTGWCEGLDYFL 265
Cdd:COG3769  242 L--EDKPRVIRTPAPGPEGWNEAILDLL 267
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 9-258 7.26e-98

haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii mannosyl-3-phosphoglycerate phosphatase and Persephonella marina glucosyl-3-phosphoglycerate phosphatase; This family includes Pyrococcus horikoshii and Thermus thermophilus HB27 mannosyl-3-phosphoglycerate phosphatases (MpgPs) which catalyze the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG), and Persephonella marina glucosyl-3-phosphoglycerate phosphatase (GpgP) which catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to produce glucosylglycerate (GG). It also includes Methanococcoides burtonii MpgP protein which is able to dephosphorylate GPG to GG, and MPG to MG. Similar flexibilities in substrate specificity have been confirmed in vitro for the MpgPs from Thermus thermophiles and Pyrococcus horikoshii. Screens with natural substrates have not yet detected activity for another member Escherichia Coli YedP. 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: 319810 [Multi-domain]  Cd Length: 255  Bit Score: 286.95  E-value: 7.26e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   9 LVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGlGGLPYIAENGAVIQPDVRWENAARF 88
Cdd:cd07507    1 VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVEYLRKELG-IEDPFIVENGGAIFIPRGYFKFPGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  89 ISE----------KKHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQMRYF 158
Cdd:cd07507   80 CKSeggyevielgKPYREIRAALEKIREETGFKITGFGDLTEEEIAELTGLPRERAALAKEREYSETIILRSDEEEDEKV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272 159 AAELARQRLKIVQGARFWHILDTCCGKDVAVHWLVDQYRLHEGyEPTTLGLGDGPNDAPLLDSVGFAVVVKGFNREGISL 238
Cdd:cd07507  160 LEALEERGLKITKGGRFYHVLGAGADKGKAVAILAALYRQLYE-AIVTVGLGDSPNDLPMLEAVDIAFVVKSLNGKYESV 238

                        250       260
                 ....*....|....*....|
gi 489956272 239 InndPARVYHTQHTGPTGWC 258
Cdd:cd07507  239 I---LPGVLKAPAPGPEGWN 255
MPGP_rel TIGR02463
mannosyl-3-phosphoglycerate phosphatase-related protein; This family consists of members of ...
 9-229 3.88e-91

mannosyl-3-phosphoglycerate phosphatase-related protein; This family consists of members of the HAD superfamily, subfamily IIB. All members are closely related to mannosyl-3-phosphoglycerate phosphatase, the second enzyme in a two-step pathway for biosynthesis of mannosylglycerate, a compatible solute present in some thermophiles and in Dehalococcoides ethenogenes. However, members of this family are separable in a neighbor-joining tree constructed from a multiple sequence alignment and are found only in mesophiles that lack the companion mannosyl-3-phosphoglycerate synthase (TIGR02460). Members of this family are like to act on a compound related to yet distinct from mannosyl-3-phosphoglycerate. [Unknown function, General]


Pssm-ID: 131516  Cd Length: 221  Bit Score: 268.56  E-value: 3.88e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272    9 LVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGLPYIAENGAVIQPDVRWEN---A 85
Cdd:TIGR02463   1 WVFSDLDGTLLDSHSYDWQPAAPWLTRLQEAGIPVILCTSKTAAEVEYLQKALGLTGDPYIAENGAAIHLEELWREepgY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   86 ARFISEKKHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQMRYFAAELARQ 165
Cdd:TIGR02463  81 PRIILGISYGIIRLVLETLSEELHFKFTPFDDLSDAEIAELTGLSGSQAALAQDREASVPLLWRDSDSRMPRFTALLADL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956272  166 RLKIVQGARFWHILDTCCGKDVAVHWLVDQYRLHegyEPTTLGLGDGPNDAPLLDSVGFAVVVK 229
Cdd:TIGR02463 161 GLAIVQGNRFSHVLGASSSKGKAANWLKATYNQP---DVKTLGLGDGPNDLPLLEVADYAVVIK 221
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 10-77 2.04e-08

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 53.78  E-value: 2.04e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956272   10 VFTDLDGTLLDFH------TLDwqpAapwLEKLMDEQIPVILCSSKTASEMDDIQQELGLgGLPYIAENGAVIQ 77
Cdd:pfam08282   1 IASDLDGTLLNSDkkisekTKE---A---IKKLKEKGIKFVIATGRPYRAILPVIKELGL-DDPVICYNGALIY 67
 
Name Accession Description Interval E-value
PRK03669 PRK03669
mannosyl-3-phosphoglycerate phosphatase-related protein;
1-265 4.31e-160

mannosyl-3-phosphoglycerate phosphatase-related protein;


Pssm-ID: 179628 [Multi-domain]  Cd Length: 271  Bit Score: 445.23  E-value: 4.31e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   1 MPSLEETLLVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGLPYIAENGAVIQPDV 80
Cdd:PRK03669   1 MLSLQDPLLIFTDLDGTLLDSHTYDWQPAAPWLTRLREAQVPVILCSSKTAAEMLPLQQTLGLQGLPLIAENGAVIQLDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  81 RWE---NAARFISEKKHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQMRY 157
Cdd:PRK03669  81 QWQdhpDFPRIISGISHGEIRQVLNTLREKEGFKFTTFDDVDDATIAEWTGLSRSQAALARLHEASVTLIWRDSDERMAQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272 158 FAAELARQRLKIVQGARFWHILDTCCGKDVAVHWLVDQYRLHEGYEPTTLGLGDGPNDAPLLDSVGFAVVVKGFNREGIS 237
Cdd:PRK03669 161 FTARLAELGLQFVQGARFWHVLDASAGKDQAANWLIATYQQLSGTRPTTLGLGDGPNDAPLLDVMDYAVVVKGLNREGVH 240

                        250       260
                 ....*....|....*....|....*...
gi 489956272 238 LINNDPARVYHTQHTGPTGWCEGLDYFL 265
Cdd:PRK03669 241 LQDDDPARVYRTQREGPEGWREGLDHFF 268
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 8-265 2.13e-116

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 334.49  E-value: 2.13e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   8 LLVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlPYIAENGAVIQPDVRWENAAR 87
Cdd:COG3769    4 LLVFTDLDGTLLDHDTYSWAAALPALARLKARGIPVILNTSKTAAEVEPLRQELGLSD-PFIVENGAAIFIPKGYFAFPS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  88 FISE----------KKHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQMRY 157
Cdd:COG3769   83 GTADidgywvielgKPYAEIRAVLEQLREELGFKFTGFGDMSAEEVAELTGLSLEQAALAKQREFSEPLLWLGSDEALER 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272 158 FAAELARQRLKIVQGARFWHILDtCCGKDVAVHWLVDQYRLHEGYEPTTLGLGDGPNDAPLLDSVGFAVVVKGFNREGIS 237
Cdd:COG3769  163 FIAALAALGLTVLRGGRFLHLMG-GADKGKAVRWLVEQYRQRFGKNVVTIALGDSPNDIPMLEAADIAVVIRSPHGAPPE 241

                        250       260
                 ....*....|....*....|....*...
gi 489956272 238 LinNDPARVYHTQHTGPTGWCEGLDYFL 265
Cdd:COG3769  242 L--EDKPRVIRTPAPGPEGWNEAILDLL 267
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 9-258 7.26e-98

haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii mannosyl-3-phosphoglycerate phosphatase and Persephonella marina glucosyl-3-phosphoglycerate phosphatase; This family includes Pyrococcus horikoshii and Thermus thermophilus HB27 mannosyl-3-phosphoglycerate phosphatases (MpgPs) which catalyze the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG), and Persephonella marina glucosyl-3-phosphoglycerate phosphatase (GpgP) which catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to produce glucosylglycerate (GG). It also includes Methanococcoides burtonii MpgP protein which is able to dephosphorylate GPG to GG, and MPG to MG. Similar flexibilities in substrate specificity have been confirmed in vitro for the MpgPs from Thermus thermophiles and Pyrococcus horikoshii. Screens with natural substrates have not yet detected activity for another member Escherichia Coli YedP. 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: 319810 [Multi-domain]  Cd Length: 255  Bit Score: 286.95  E-value: 7.26e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   9 LVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGlGGLPYIAENGAVIQPDVRWENAARF 88
Cdd:cd07507    1 VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVEYLRKELG-IEDPFIVENGGAIFIPRGYFKFPGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  89 ISE----------KKHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQMRYF 158
Cdd:cd07507   80 CKSeggyevielgKPYREIRAALEKIREETGFKITGFGDLTEEEIAELTGLPRERAALAKEREYSETIILRSDEEEDEKV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272 159 AAELARQRLKIVQGARFWHILDTCCGKDVAVHWLVDQYRLHEGyEPTTLGLGDGPNDAPLLDSVGFAVVVKGFNREGISL 238
Cdd:cd07507  160 LEALEERGLKITKGGRFYHVLGAGADKGKAVAILAALYRQLYE-AIVTVGLGDSPNDLPMLEAVDIAFVVKSLNGKYESV 238

                        250       260
                 ....*....|....*....|
gi 489956272 239 InndPARVYHTQHTGPTGWC 258
Cdd:cd07507  239 I---LPGVLKAPAPGPEGWN 255
MPGP_rel TIGR02463
mannosyl-3-phosphoglycerate phosphatase-related protein; This family consists of members of ...
 9-229 3.88e-91

mannosyl-3-phosphoglycerate phosphatase-related protein; This family consists of members of the HAD superfamily, subfamily IIB. All members are closely related to mannosyl-3-phosphoglycerate phosphatase, the second enzyme in a two-step pathway for biosynthesis of mannosylglycerate, a compatible solute present in some thermophiles and in Dehalococcoides ethenogenes. However, members of this family are separable in a neighbor-joining tree constructed from a multiple sequence alignment and are found only in mesophiles that lack the companion mannosyl-3-phosphoglycerate synthase (TIGR02460). Members of this family are like to act on a compound related to yet distinct from mannosyl-3-phosphoglycerate. [Unknown function, General]


Pssm-ID: 131516  Cd Length: 221  Bit Score: 268.56  E-value: 3.88e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272    9 LVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGLPYIAENGAVIQPDVRWEN---A 85
Cdd:TIGR02463   1 WVFSDLDGTLLDSHSYDWQPAAPWLTRLQEAGIPVILCTSKTAAEVEYLQKALGLTGDPYIAENGAAIHLEELWREepgY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   86 ARFISEKKHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQMRYFAAELARQ 165
Cdd:TIGR02463  81 PRIILGISYGIIRLVLETLSEELHFKFTPFDDLSDAEIAELTGLSGSQAALAQDREASVPLLWRDSDSRMPRFTALLADL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956272  166 RLKIVQGARFWHILDTCCGKDVAVHWLVDQYRLHegyEPTTLGLGDGPNDAPLLDSVGFAVVVK 229
Cdd:TIGR02463 161 GLAIVQGNRFSHVLGASSSKGKAANWLKATYNQP---DVKTLGLGDGPNDLPLLEVADYAVVIK 221
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 9-265 4.97e-90

mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. Several members of this family from thermophiles (and from Dehalococcoides ethenogenes) are now known to act as mannosyl-3-phosphoglycerate (MPG) phosphatase. In these cases, the enzyme acts after MPG synthase to make the compatible solute mannosylglycerate. We propose that other mesophilic members of this family do not act as mannosyl-3-phosphoglycerate phosphatase. A member of this family is found in Escherichia coli, which appears to lack MPG synthase. Mannosylglycerate is imported in E. coli by phosphoenolpyruvate-dependent transporter (), but it appears the phosphorylation is not on the glycerate moiety, that the phosphorylated import is degraded by an alpha-mannosidase from an adjacent gene, and that E. coli would have no pathway to obtain MPG.


Pssm-ID: 130550 [Multi-domain]  Cd Length: 256  Bit Score: 266.96  E-value: 4.97e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272    9 LVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLgGLPYIAENGAVIQPDVRW---ENA 85
Cdd:TIGR01486   1 WIFTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKTAAEVEYLRKELGL-EDPFIVENGGAIYGPRGWrpePEY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   86 ARFISEKKHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQMryFAAELARQ 165
Cdd:TIGR01486  80 PVIALGIPYEKIRARLRELSEELGFKFRGLGDLTDEEIAELTGLSRELARLAQRREYSETILWSEERRER--FTEALVAV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  166 RLKIVQGARFWHILDTCCGKDVAVHWLVDQYRLHEGyEPTTLGLGDGPNDAPLLDSVGFAVVVKGFNREGISLINNDPAR 245
Cdd:TIGR01486 158 GLEVTHGGRFYHVLGAGSDKGKAVNALKAFYNQPGG-AIKVVGLGDSPNDLPLLEVVDLAVVVPGPNGPNVSLKPGDPGS 236

                         250       260
                  ....*....|....*....|
gi 489956272  246 VYHTQHTGPTGWCEGLDYFL 265
Cdd:TIGR01486 237 FLLTPAPGPEGWREALEHLL 256
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 7-261 1.02e-72

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 223.66  E-value: 1.02e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   7 TLLVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlPYIAENGAVI---------- 76
Cdd:PRK00192   4 KLLVFTDLDGTLLDHHTYSYEPAKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGLED-PFIVENGAAIyipknyfpfq 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  77 QPDVRWENAARFIS-EKKHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQM 155
Cdd:PRK00192  83 PDGERLKGDYWVIElGPPYEELREILDEISDELGYPLKGFGDLSAEEVAELTGLSGESARLAKDREFSEPFLWNGSEAAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272 156 RYFAAELARQRLKIVQGARFWHILDTcCGKDVAVHWLVDQYRLHegYEPTTLGLGDGPNDAPLLDSVGFAVVVKGFNREG 235
Cdd:PRK00192 163 ERFEEALKRLGLKVTRGGRFLHLLGG-GDKGKAVRWLKELYRRQ--DGVETIALGDSPNDLPMLEAADIAVVVPGPDGPN 239

                        250       260
                 ....*....|....*....|....*..
gi 489956272 236 ISLIN-NDPARVYHTQHTGPTGWCEGL 261
Cdd:PRK00192 240 PPLLPgIADGEFILASAPGPEGWAEAI 266
osmo_MPG_phos TIGR02461
mannosyl-3-phosphoglycerate phosphatase; Members of this family are ...
 9-228 1.15e-35

mannosyl-3-phosphoglycerate phosphatase; Members of this family are mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70). It acts sequentially after mannosyl-3-phosphoglycerate synthase (EC 2.4.1.217) in a two-step pathway of biosynthesis of the compatible solute mannosylglycerate, a typical osmolyte of thermophiles.


Pssm-ID: 131514  Cd Length: 225  Bit Score: 126.82  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272    9 LVFTDLDGTLLDfHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlPYIAENGAVI---QPDVRWENA 85
Cdd:TIGR02461   1 VIFTDLDGTLLD-PGYEPGPAREALEELKDLGFPIVFVSSKTRAEQEYYREELGVEP-PFIVENGGAIyipRGYFPFPVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   86 ARFISE--------KKHDDIRQCIARVRQEMHLKFttFDDVDEHVVAEWTGLSRPRSVLARKHEASVTlIWRDSDEQMRY 157
Cdd:TIGR02461  79 AGREVGnyevielgKPYAKIRAALKEAENEAGIKG--YGDSTAEEVARLTGLPREAARLAKRREYSET-IFLWSREGWEA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956272  158 FAAELARQRLKIVQGARFWHILDTcCGKDVAVHWLVDQYRLHEGyEPTTLGLGDGPNDAPLLDSVGFAVVV 228
Cdd:TIGR02461 156 VLVTARARGLEYTHGGRFYTVHGG-SDKGKAIKRLLDLYKLRPG-AIESVGLGDSENDFPMFEAVDLAFLV 224
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 9-228 3.68e-33

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: 119.79  E-value: 3.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272    9 LVFTDLDGTLLDFHTLDWQPAAPW-LEKLMDEQIPVILCSSKTASEMDDIQQELGLgGLPYIAENGAVIQPD-----VRW 82
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHELSPETIEaLERLREAGVKVVIVTGRSLAEIKELLKQLNL-PLPLIAENGALIFYPgeilyIEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   83 ENAARFISEKKHDDIRqCIARVRQEmHLKFTTFDDVDEHVVAEWTGLSRPRsVLARKHEASVTLIWRDsDEQMRyfaael 162
Cdd:TIGR01484  80 SDVFEEILGIKFEEIG-AELKSLSE-HYVGTFIEDKAIAVAIHYVGAELGQ-ELDSKMRERLEKIGRN-DLELE------ 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956272  163 arqrlKIVQGARFWHILDTCCGKDVAVHWLVDQYrlhEGYEPTTLGLGDGPNDAPLLDSVGFAVVV 228
Cdd:TIGR01484 150 -----AIYSGKTDLEVLPAGVNKGSALQALLQEL---NGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK14502 PRK14502
bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; ...
 1-266 5.19e-23

bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; Provisional


Pssm-ID: 184713 [Multi-domain]  Cd Length: 694  Bit Score: 98.08  E-value: 5.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   1 MPSLEE-TLLVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlPYIAENGAVI--- 76
Cdd:PRK14502 409 LPSSGQfKKIVYTDLDGTLLNPLTYSYSTALDALRLLKDKELPLVFCSAKTMGEQDLYRNELGIKD-PFITENGGAIfip 487

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  77 -----QPDVRWENAARFISEK---KHDDIRQCIARVRQEM-----------HLKFTTFDDVDEHVVAEWTGLSRPRSVLA 137
Cdd:PRK14502 488 kdyfrLPFAYDRVAGNYLVIElgmAYKDIRHILKKALAEActeiensekagNIFITSFGDMSVEDVSRLTDLNLKQAELA 567

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272 138 RKHEASVTLIWRDSDEQMRYFAAELARQRLKIVQGARFWHIldtCCGKD--VAVHWLVDQYRLHEGyEPTTLGLGDGPND 215
Cdd:PRK14502 568 KQREYSETVHIEGDKRSTNIVLNHIQQSGLEYSFGGRFYEV---TGGNDkgKAIKILNELFRLNFG-NIHTFGLGDSEND 643

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489956272 216 APLLDSVGFAVVVKGFNREGISLINNDPARVyhtQHTGPTGWCEGLDYFLR 266
Cdd:PRK14502 644 YSMLETVDSPILVQRPGNKWHKMRLRNPSYV---KGVGPEGFSRAVTDIIL 691
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 9-228 3.23e-14

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: 69.01  E-value: 3.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   9 LVFTDLDGTLLDF-HTLDwQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlPYIAENGAVIqpdvrwenaar 87
Cdd:COG0561    4 LIALDLDGTLLNDdGEIS-PRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDD-PLITSNGALI----------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  88 fisekkHDDIRQCIARVrqemhlkfttfdDVDEHVVAEWTGlsrprsvLARKHEASVTLIWRDSDeqmryfaaelarqrl 167
Cdd:COG0561   71 ------YDPDGEVLYER------------PLDPEDVREILE-------LLREHGLHLQVVVRSGP--------------- 110

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956272 168 kivqgaRFWHILDTCCGKDVAVHWLVDQYrlheGYEPT-TLGLGDGPNDAPLLDSVGFAVVV 228
Cdd:COG0561  111 ------GFLEILPKGVSKGSALKKLAERL----GIPPEeVIAFGDSGNDLEMLEAAGLGVAM 162
PRK12702 PRK12702
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 9-259 7.79e-11

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 105866  Cd Length: 302  Bit Score: 61.24  E-value: 7.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   9 LVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlPYIAENG-AVIQP--------- 78
Cdd:PRK12702   3 LVLSSLDGSLLDLEFNSYGAARQALAALERRSIPLVLYSLRTRAQLEHLCRQLRLEH-PFICEDGsAIYVPehyfpagil 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  79 DVRWENAARFISEK---KHDDIRQCIARVRQEMHLKFTTFDDVDEHVVAEWTGLSRPRSVLARKHEASVTLIWRDSDEQM 155
Cdd:PRK12702  82 DEQWQHRPPYYVCAlglPYPCLRHILQQVRQDSHLDLIGFGDWTASELAAATGIPLEEAERAQKREYSEIFSYSGDPARL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272 156 R-YFAAELAR--QRLKIVQGARF-----WHILD----------TCCGKDVAVHWLVDQYRLHEGyEPTTLGLGDGPNDAP 217
Cdd:PRK12702 162 ReAFAQQEANltQHLLRLHQLHFsdlpqWYLTGwmqptlaaepNSLPGEQAVQLLLDCYQRHLG-PIKALGIGCSPPDLA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489956272 218 LLDSVGFAVVV-----KGFNREGISLINNDPARVYH-TQHTGPTGWCE 259
Cdd:PRK12702 241 FLRWSEQKVVLpspiaDSLWKEALRLGGPEVQPQWQlAQLPGPEGWNE 288
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 10-77 2.04e-08

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 53.78  E-value: 2.04e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956272   10 VFTDLDGTLLDFH------TLDwqpAapwLEKLMDEQIPVILCSSKTASEMDDIQQELGLgGLPYIAENGAVIQ 77
Cdd:pfam08282   1 IASDLDGTLLNSDkkisekTKE---A---IKKLKEKGIKFVIATGRPYRAILPVIKELGL-DDPVICYNGALIY 67
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 9-226 2.23e-08

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: 53.43  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272    9 LVFTDLDGTLL-DFHTLDwQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlPYIAENGAVIQpdvrwENAAR 87
Cdd:TIGR00099   1 LIFIDLDGTLLnDDHTIS-PSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDT-PFITANGAAVI-----DDQGE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   88 FISEKK-HDDIRQCIARVRQEMHLKFTTFDDVDEHV---------VAEWTGLSRPRSVLARKHEAS-VTLIWR--DSDEQ 154
Cdd:TIGR00099  74 ILYKKPlDLDLVEEILNFLKKHGLDVILYGDDSIYAskndpeyftIFKKFLGEPKLEVVDIQYLPDdILKILLlfLDPED 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956272  155 MRYFAAEL--ARQRLKIVQGARFWHILDTC---CGKDVAVHWLVDqyrlHEGYEPT-TLGLGDGPNDAPLLDSVGFAV 226
Cdd:TIGR00099 154 LDLLIEALnkLELEENVSVVSSGPYSIEITakgVSKGSALQSLAE----ALGISLEdVIAFGDGMNDIEMLEAAGYGV 227
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 9-229 6.10e-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: 52.21  E-value: 6.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   9 LVFTDLDGTLLDF------HTLDwqpAapwLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlPYIAENGAVIQpdvrw 82
Cdd:cd07516    1 LIALDLDGTLLNSdkeispRTKE---A---IKKAKEKGIKVVIATGRPLRGAQPYLEELGLDS-PLITFNGALVY----- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  83 ENAARFISEKK--HDDIRQcIARVRQEMHLKFTTFDDVD-------EHVVAEWTGLSRPRSVLARKHEASVT-LIWRDSD 152
Cdd:cd07516   69 DPTGKEILERLisKEDVKE-LEEFLRKLGIGINIYTNDDwadtiyeENEDDEIIKPAEILDDLLLPPDEDITkILFVGED 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272 153 EQMRYFAAELARQ---RLKIVQGArfWHILDTC---CGKDVAVHWLVDQYrlheGYEP-TTLGLGDGPNDAPLLDSVGFA 225
Cdd:cd07516  148 EELDELIAKLPEEffdDLSVVRSA--PFYLEIMpkgVSKGNALKKLAEYL----GISLeEVIAFGDNENDLSMLEYAGLG 221


                 ....
gi 489956272 226 VVVK 229
Cdd:cd07516  222 VAMG 225
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 9-228 2.35e-07

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: 50.12  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272    9 LVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlPYIAENGAVIqpdvRWENAARF 88
Cdd:TIGR01487   3 LVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSG-PVVAENGGVI----FYNKEDIF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   89 ISEKKhddiRQCIARVRQEMHlkfttfddvdehvvaewtglsRPRSVLARKHEASVTLIWRDSD--EQMRYFAAELarqR 166
Cdd:TIGR01487  78 LANME----EEWFLDEEKKKR---------------------FPRDRLSNEYPRASLVIMREGKdvDEVREIIKER---G 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956272  167 LKIVQGARFWHILDTCCGKDVAVHWLVDQYrlheGYEPT-TLGLGDGPNDAPLLDSVGFAVVV 228
Cdd:TIGR01487 130 LNLVASGFAIHIMKKGVDKGVGVEKLKELL----GIKPEeVAAIGDSENDIDLFRVVGFKVAV 188
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 10-228 4.65e-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: 49.38  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   10 VFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlPYIAENGAVI----QPDVRWena 85
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPD-PVIAENGGEIsyneGLDDIF--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   86 arFISEKKHddirqCIARVRQEMHLKFTTFDdvdehvvaewtgLSRPRsvlarkhEASVTLIWRDSDEQMRYFAAELARQ 165
Cdd:TIGR01482  77 --LAYLEEE-----WFLDIVIAKTFPFSRLK------------VQYPR-------RASLVKMRYGIDVDTVREIIKELGL 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956272  166 RLKIVQGARFWHILDTCCGKDVAVHWLVDQYrlheGYEPT-TLGLGDGPNDAPLLDSVGFAVVV 228
Cdd:TIGR01482 131 NLVAVDSGFDIHILPQGVNKGVAVKKLKEKL----GIKPGeTLVCGDSENDIDLFEVPGFGVAV 190
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 9-76 4.79e-06

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: 46.04  E-value: 4.79e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956272   9 LVFTDLDGTLL-DFHTLDWQPAAPWLEKLMDEQIPVILCS----SKTASEMDDIQQELglgglPYIAENGAVI 76
Cdd:cd07518    2 LIATDMDGTFLnDDKTYDHERFFAILDQLLKKGIKFVVASgrqyYQLISFFPEIKDEM-----SFVAENGAVV 69
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 9-226 1.68e-05

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: 44.52  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   9 LVFTDLDGTLLDFHTLDWQPAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGlpYIAENGAVIQpdvrweNAARF 88
Cdd:cd07517    2 IVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDS--YVSYNGQYVF------FEGEV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  89 ISEKKHDdirqciarvRQEMHlKFTTFDDVDEHVVAewtglsrprsvlarkHEASVTLIWRDSDEQmrYFAAElaRQRLK 168
Cdd:cd07517   74 IYKNPLP---------QELVE-RLTEFAKEQGHPVS---------------FYGQLLLFEDEEEEQ--KYEEL--RPELR 124

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956272 169 IVQgarfWH-----ILDTCCGKDVAVHWLVDQYrlheGYEPT-TLGLGDGPNDAPLLDSVGFAV 226
Cdd:cd07517  125 FVR----WHplstdVIPKGGSKAKGIQKVIEHL----GIKKEeTMAFGDGLNDIEMLEAVGIGI 180
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 9-102 4.21e-05

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All 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. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 41.61  E-value: 4.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   9 LVFTDLDGTLLdfhtldwqpAAPWLEKLMDEQIPVILCSSKTASEMDDIQQELGLGGL--PYIAENGAVIqpDVRWENAA 86
Cdd:cd01427    1 AVLFDLDGTLL---------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLfdGIIGSDGGGT--PKPKPKPL 69

                         90
                 ....*....|....*.
gi 489956272  87 RFISEKKHDDIRQCIA 102
Cdd:cd01427   70 LLLLLKLGVDPEEVLF 85
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 9-196 1.44e-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: 41.89  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   9 LVFTDLDGTLLDFhTLDWQPAAPW------LEKLM-DEQIPVILCSsktASEMDDIQQELGLGGLPYIAENGAviqpDVR 81
Cdd:cd01627    1 LLFLDYDGTLAPI-VPDPDAAVPSpelleaLKKLAaDPKNAVAIVS---GRDLDDLDKWLGLPGIGLAGEHGA----EIR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  82 WENAARFISEKKHDDIRqciaRVRQEMHlkfttfddvdehvVAEWTGLSRPRSVLARKhEASVTLIWRDSDEQMRYFAAE 161
Cdd:cd01627   73 LPGGGEWVTLAPKADLE----WKEEVEA-------------IFKYFTERTPGSLVEDK-GASLAWHYRNADPEGARAALE 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489956272 162 LAR-------QRLKIVQG-------ARFWHildtccgKDVAVHWLVDQY 196
Cdd:cd01627  135 LALhlasdllKALEVVPGkkvvevrPVGVN-------KGEAVERILGEL 176
T6PP TIGR00685
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ...
 9-235 6.81e-04

trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an important osmolyte for dessication and/or salt tolerance in a number of prokaryotic and eukaryotic species, including E. coli, Saccharomyces cerevisiae, and Arabidopsis thaliana. Many bacteria also utilize trehalose in the synthesis of trehalolipids, specialized cell wall constituents believed to be involved in the uptake of hydrophobic substances. Trehalose dimycolate (TDM, cord factor) and related substances are important constituents of the mycobacterial waxy coat and responsible for various clinically important immunological interactions with host organism. This enzyme, trehalose-phosphatase, removes a phosphate group in the final step of trehalose biosynthesis. The trehalose-phosphatase from Saccharomyces cerevisiae is fused to the synthase. At least 18 distinct sequences from Arabidopsis have been identified, roughly half of these are of the fungal type, with a fused synthase and half are like the bacterial members having only the phosphatase domain. It has been suggested that trehalose is being used in Arabidopsis as a regulatory molecule in development and possibly other processes. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273219 [Multi-domain]  Cd Length: 244  Bit Score: 40.20  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272    9 LVFTDLDGTLLDFHTldwQPAAPW--------LEKLM---DEQIPVIlcsskTASEMDDIQQELGLGGLPYIAENGAVIQ 77
Cdd:TIGR00685   5 AFFFDYDGTLSEIVP---DPDAAVvsdrlltiLQKLAarpHNAIWII-----SGRKFLEKWLGVKLPGLGLAGEHGCEMK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272   78 PDV---RWENAARFISEkkhddIRQCIARVRQEmhlkFTTFDDV---DEHVVAEWTGLSRPRSVLARKHEASVTliwrds 151
Cdd:TIGR00685  77 DNGscqDWVNLTEKIPS-----WKVRANELREE----ITTRPGVfieRKGVALAWHYRQAPVPELARFRAKELK------ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956272  152 dEQMRYFAA-ELARQRLKIVQGARFWHildtccgKDVAVHWLVDqyrlHEGYEPTT-LGLGDGpndapLLDSVGFAVVVK 229
Cdd:TIGR00685 142 -EKILSFTDlEVMDGKAVVELKPRFVN-------KGEIVKRLLW----HQPGSGISpVYLGDD-----ITDEDAFRVVNN 204


                  ....*.
gi 489956272  230 GFNREG 235
Cdd:TIGR00685 205 QWGNYG 210
 
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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