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Conserved domains on  [gi|15831947|ref|NP_310720|]
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mannosyl-3-phosphoglycerate phosphatase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

mannosyl-3-phosphoglycerate phosphatase( domain architecture ID 11480019)

mannosyl-3-phosphoglycerate phosphatase is a HAD (haloacid dehalogenase) family hydrolase that catalyzes the hydrolysis of 2-O-(alpha-D-mannosyl)-3-phosphoglycerate to form 2-O-(alpha-D-mannosyl)-D-glycerate and phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK03669 PRK03669
mannosyl-3-phosphoglycerate phosphatase-related protein;
1-269 0e+00

mannosyl-3-phosphoglycerate phosphatase-related protein;


:

Pssm-ID: 179628 [Multi-domain]  Cd Length: 271  Bit Score: 509.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    1 MFSIQQPLLVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGLPLIAENGAVIQLAE 80
Cdd:PRK03669   1 MLSLQDPLLIFTDLDGTLLDSHTYDWQPAAPWLTRLREAQVPVILCSSKTAAEMLPLQQTLGLQGLPLIAENGAVIQLDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   81 QWQEIDGFPRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWRDSDERMAQ 160
Cdd:PRK03669  81 QWQDHPDFPRIISGISHGEIRQVLNTLREKEGFKFTTFDDVDDATIAEWTGLSRSQAALARLHEASVTLIWRDSDERMAQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  161 FTARLNELGLQFMQGARFWHVLDASAGKDQAANWIIATYQQLSGKRPTTLGLGDGPNDAPLLEVMDYAVIVKGLNREGVH 240
Cdd:PRK03669 161 FTARLAELGLQFVQGARFWHVLDASAGKDQAANWLIATYQQLSGTRPTTLGLGDGPNDAPLLDVMDYAVVVKGLNREGVH 240

                        250       260
                 ....*....|....*....|....*....
gi 15831947  241 LHDEDPARVWRTQREGPEGWREGLDHFFS 269
Cdd:PRK03669 241 LQDDDPARVYRTQREGPEGWREGLDHFFS 269
 
Name Accession Description Interval E-value
PRK03669 PRK03669
mannosyl-3-phosphoglycerate phosphatase-related protein;
1-269 0e+00

mannosyl-3-phosphoglycerate phosphatase-related protein;


Pssm-ID: 179628 [Multi-domain]  Cd Length: 271  Bit Score: 509.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    1 MFSIQQPLLVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGLPLIAENGAVIQLAE 80
Cdd:PRK03669   1 MLSLQDPLLIFTDLDGTLLDSHTYDWQPAAPWLTRLREAQVPVILCSSKTAAEMLPLQQTLGLQGLPLIAENGAVIQLDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   81 QWQEIDGFPRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWRDSDERMAQ 160
Cdd:PRK03669  81 QWQDHPDFPRIISGISHGEIRQVLNTLREKEGFKFTTFDDVDDATIAEWTGLSRSQAALARLHEASVTLIWRDSDERMAQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  161 FTARLNELGLQFMQGARFWHVLDASAGKDQAANWIIATYQQLSGKRPTTLGLGDGPNDAPLLEVMDYAVIVKGLNREGVH 240
Cdd:PRK03669 161 FTARLAELGLQFVQGARFWHVLDASAGKDQAANWLIATYQQLSGTRPTTLGLGDGPNDAPLLDVMDYAVVVKGLNREGVH 240

                        250       260
                 ....*....|....*....|....*....
gi 15831947  241 LHDEDPARVWRTQREGPEGWREGLDHFFS 269
Cdd:PRK03669 241 LQDDDPARVYRTQREGPEGWREGLDHFFS 269
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 9-268 6.06e-135

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: 380.98  E-value: 6.06e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947     9 LVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQgLPLIAENGAVIQLAEQWQEIDGF 88
Cdd:TIGR01486   1 WIFTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKTAAEVEYLRKELGLE-DPFIVENGGAIYGPRGWRPEPEY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    89 PRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWrdSDERMAQFTARLNEL 168
Cdd:TIGR01486  80 PVIALGIPYEKIRARLRELSEELGFKFRGLGDLTDEEIAELTGLSRELARLAQRREYSETILW--SEERRERFTEALVAV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   169 GLQFMQGARFWHVLDASAGKDQAANWIIATYQQLsGKRPTTLGLGDGPNDAPLLEVMDYAVIVKGLNREGVHLHDEDPAR 248
Cdd:TIGR01486 158 GLEVTHGGRFYHVLGAGSDKGKAVNALKAFYNQP-GGAIKVVGLGDSPNDLPLLEVVDLAVVVPGPNGPNVSLKPGDPGS 236

                         250       260
                  ....*....|....*....|
gi 15831947   249 VWRTQREGPEGWREGLDHFF 268
Cdd:TIGR01486 237 FLLTPAPGPEGWREALEHLL 256
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 5-269 2.56e-128

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 364.92  E-value: 2.56e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   5 QQPLLVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGlPLIAENGAVIQLAEQW-- 82
Cdd:COG3769   1 MPPLLVFTDLDGTLLDHDTYSWAAALPALARLKARGIPVILNTSKTAAEVEPLRQELGLSD-PFIVENGAAIFIPKGYfa 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  83 -----QEIDGFPRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWRDSDER 157
Cdd:COG3769  80 fpsgtADIDGYWVIELGKPYAEIRAVLEQLREELGFKFTGFGDMSAEEVAELTGLSLEQAALAKQREFSEPLLWLGSDEA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947 158 MAQFTARLNELGLQFMQGARFWHVLDAsAGKDQAANWIIATYQQLSGKRPTTLGLGDGPNDAPLLEVMDYAVIVKGLNRE 237
Cdd:COG3769 160 LERFIAALAALGLTVLRGGRFLHLMGG-ADKGKAVRWLVEQYRQRFGKNVVTIALGDSPNDIPMLEAADIAVVIRSPHGA 238

                       250       260       270
                ....*....|....*....|....*....|..
gi 15831947 238 GVHLhdEDPARVWRTQREGPEGWREGLDHFFS 269
Cdd:COG3769 239 PPEL--EDKPRVIRTPAPGPEGWNEAILDLLE 268
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 9-261 5.88e-125

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: 355.90  E-value: 5.88e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   9 LVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGlQGLPLIAENGAVIQLAEQWQEID-- 86
Cdd:cd07507   1 VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVEYLRKELG-IEDPFIVENGGAIFIPRGYFKFPgr 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  87 -----GFPRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWRDSDERMAQF 161
Cdd:cd07507  80 cksegGYEVIELGKPYREIRAALEKIREETGFKITGFGDLTEEEIAELTGLPRERAALAKEREYSETIILRSDEEEDEKV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947 162 TARLNELGLQFMQGARFWHVLDASAGKDQAANWIIATYQQLSGkRPTTLGLGDGPNDAPLLEVMDYAVIVKGLNREGVHL 241
Cdd:cd07507 160 LEALEERGLKITKGGRFYHVLGAGADKGKAVAILAALYRQLYE-AIVTVGLGDSPNDLPMLEAVDIAFVVKSLNGKYESV 238

                       250       260
                ....*....|....*....|
gi 15831947 242 HdedPARVWRTQREGPEGWR 261
Cdd:cd07507 239 I---LPGVLKAPAPGPEGWN 255
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 10-232 6.23e-11

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 61.10  E-value: 6.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    10 VFSDLDGTLLDShsyDWQP-----AApwLSRLREANVPVILCSSKTSAEMLYLQKMLGLQgLPLIAENGAVIQlAEQWQE 84
Cdd:pfam08282   1 IASDLDGTLLNS---DKKIsektkEA--IKKLKEKGIKFVIATGRPYRAILPVIKELGLD-DPVICYNGALIY-DENGKI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    85 IdgfprIISGISHGEISQVLNTLRE-KEHFKFTTFDD--VDDATIAEWTGLSRSQAALTQLHEASVTLIWRDS------- 154
Cdd:pfam08282  74 L-----YSNPISKEAVKEIIEYLKEnNLEILLYTDDGvyILNDNELEKILKELNYTKSFVPEIDDFELLEDEDinkilil 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   155 --DERMAQFTARLNELGLQFMQGARFWH-VLDASAGKDQAANWI--IATYQQLSGKRptTLGLGDGPNDAPLLEVMDYAV 229
Cdd:pfam08282 149 ldEEDLDELEKELKELFGSLITITSSGPgYLEIMPKGVSKGTALkaLAKHLNISLEE--VIAFGDGENDIEMLEAAGLGV 226


                  ...
gi 15831947   230 IVK 232
Cdd:pfam08282 227 AMG 229
 
Name Accession Description Interval E-value
PRK03669 PRK03669
mannosyl-3-phosphoglycerate phosphatase-related protein;
1-269 0e+00

mannosyl-3-phosphoglycerate phosphatase-related protein;


Pssm-ID: 179628 [Multi-domain]  Cd Length: 271  Bit Score: 509.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    1 MFSIQQPLLVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGLPLIAENGAVIQLAE 80
Cdd:PRK03669   1 MLSLQDPLLIFTDLDGTLLDSHTYDWQPAAPWLTRLREAQVPVILCSSKTAAEMLPLQQTLGLQGLPLIAENGAVIQLDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   81 QWQEIDGFPRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWRDSDERMAQ 160
Cdd:PRK03669  81 QWQDHPDFPRIISGISHGEIRQVLNTLREKEGFKFTTFDDVDDATIAEWTGLSRSQAALARLHEASVTLIWRDSDERMAQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  161 FTARLNELGLQFMQGARFWHVLDASAGKDQAANWIIATYQQLSGKRPTTLGLGDGPNDAPLLEVMDYAVIVKGLNREGVH 240
Cdd:PRK03669 161 FTARLAELGLQFVQGARFWHVLDASAGKDQAANWLIATYQQLSGTRPTTLGLGDGPNDAPLLDVMDYAVVVKGLNREGVH 240

                        250       260
                 ....*....|....*....|....*....
gi 15831947  241 LHDEDPARVWRTQREGPEGWREGLDHFFS 269
Cdd:PRK03669 241 LQDDDPARVYRTQREGPEGWREGLDHFFS 269
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 9-268 6.06e-135

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: 380.98  E-value: 6.06e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947     9 LVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQgLPLIAENGAVIQLAEQWQEIDGF 88
Cdd:TIGR01486   1 WIFTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKTAAEVEYLRKELGLE-DPFIVENGGAIYGPRGWRPEPEY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    89 PRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWrdSDERMAQFTARLNEL 168
Cdd:TIGR01486  80 PVIALGIPYEKIRARLRELSEELGFKFRGLGDLTDEEIAELTGLSRELARLAQRREYSETILW--SEERRERFTEALVAV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   169 GLQFMQGARFWHVLDASAGKDQAANWIIATYQQLsGKRPTTLGLGDGPNDAPLLEVMDYAVIVKGLNREGVHLHDEDPAR 248
Cdd:TIGR01486 158 GLEVTHGGRFYHVLGAGSDKGKAVNALKAFYNQP-GGAIKVVGLGDSPNDLPLLEVVDLAVVVPGPNGPNVSLKPGDPGS 236

                         250       260
                  ....*....|....*....|
gi 15831947   249 VWRTQREGPEGWREGLDHFF 268
Cdd:TIGR01486 237 FLLTPAPGPEGWREALEHLL 256
MPGP_rel TIGR02463
mannosyl-3-phosphoglycerate phosphatase-related protein; This family consists of members of ...
 9-232 1.46e-133

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: 376.41  E-value: 1.46e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947     9 LVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGLPLIAENGAVIQLAEQWQEIDGF 88
Cdd:TIGR02463   1 WVFSDLDGTLLDSHSYDWQPAAPWLTRLQEAGIPVILCTSKTAAEVEYLQKALGLTGDPYIAENGAAIHLEELWREEPGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    89 PRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWRDSDERMAQFTARLNEL 168
Cdd:TIGR02463  81 PRIILGISYGIIRLVLETLSEELHFKFTPFDDLSDAEIAELTGLSGSQAALAQDREASVPLLWRDSDSRMPRFTALLADL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831947   169 GLQFMQGARFWHVLDASAGKDQAANWIIATYQQlsgKRPTTLGLGDGPNDAPLLEVMDYAVIVK 232
Cdd:TIGR02463 161 GLAIVQGNRFSHVLGASSSKGKAANWLKATYNQ---PDVKTLGLGDGPNDLPLLEVADYAVVIK 221
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 5-269 2.56e-128

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 364.92  E-value: 2.56e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   5 QQPLLVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGlPLIAENGAVIQLAEQW-- 82
Cdd:COG3769   1 MPPLLVFTDLDGTLLDHDTYSWAAALPALARLKARGIPVILNTSKTAAEVEPLRQELGLSD-PFIVENGAAIFIPKGYfa 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  83 -----QEIDGFPRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWRDSDER 157
Cdd:COG3769  80 fpsgtADIDGYWVIELGKPYAEIRAVLEQLREELGFKFTGFGDMSAEEVAELTGLSLEQAALAKQREFSEPLLWLGSDEA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947 158 MAQFTARLNELGLQFMQGARFWHVLDAsAGKDQAANWIIATYQQLSGKRPTTLGLGDGPNDAPLLEVMDYAVIVKGLNRE 237
Cdd:COG3769 160 LERFIAALAALGLTVLRGGRFLHLMGG-ADKGKAVRWLVEQYRQRFGKNVVTIALGDSPNDIPMLEAADIAVVIRSPHGA 238

                       250       260       270
                ....*....|....*....|....*....|..
gi 15831947 238 GVHLhdEDPARVWRTQREGPEGWREGLDHFFS 269
Cdd:COG3769 239 PPEL--EDKPRVIRTPAPGPEGWNEAILDLLE 268
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 9-261 5.88e-125

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: 355.90  E-value: 5.88e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   9 LVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGlQGLPLIAENGAVIQLAEQWQEID-- 86
Cdd:cd07507   1 VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVEYLRKELG-IEDPFIVENGGAIFIPRGYFKFPgr 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  87 -----GFPRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWRDSDERMAQF 161
Cdd:cd07507  80 cksegGYEVIELGKPYREIRAALEKIREETGFKITGFGDLTEEEIAELTGLPRERAALAKEREYSETIILRSDEEEDEKV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947 162 TARLNELGLQFMQGARFWHVLDASAGKDQAANWIIATYQQLSGkRPTTLGLGDGPNDAPLLEVMDYAVIVKGLNREGVHL 241
Cdd:cd07507 160 LEALEERGLKITKGGRFYHVLGAGADKGKAVAILAALYRQLYE-AIVTVGLGDSPNDLPMLEAVDIAFVVKSLNGKYESV 238

                       250       260
                ....*....|....*....|
gi 15831947 242 HdedPARVWRTQREGPEGWR 261
Cdd:cd07507 239 I---LPGVLKAPAPGPEGWN 255
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 7-269 1.75e-84

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 253.71  E-value: 1.75e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    7 PLLVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGlPLIAENGAVIQLAEQWQ--- 83
Cdd:PRK00192   4 KLLVFTDLDGTLLDHHTYSYEPAKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGLED-PFIVENGAAIYIPKNYFpfq 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   84 -----EIDGFPRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWRDSDERM 158
Cdd:PRK00192  83 pdgerLKGDYWVIELGPPYEELREILDEISDELGYPLKGFGDLSAEEVAELTGLSGESARLAKDREFSEPFLWNGSEAAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  159 AQFTARLNELGLQFMQGARFWHVLDAsAGKDQAANWIIATYQQLSGkrPTTLGLGDGPNDAPLLEVMDYAVIVKGLNREG 238
Cdd:PRK00192 163 ERFEEALKRLGLKVTRGGRFLHLLGG-GDKGKAVRWLKELYRRQDG--VETIALGDSPNDLPMLEAADIAVVVPGPDGPN 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 15831947  239 VHLHDE-DPARVWRTQREGPEGWREGLDHFFS 269
Cdd:PRK00192 240 PPLLPGiADGEFILASAPGPEGWAEAINKLLS 271
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 9-231 9.45e-56

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: 178.34  E-value: 9.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947     9 LVFSDLDGTLLDSHSYDWQPAAPW-LSRLREANVPVILCSSKTSAEMLYLQKMLGLQgLPLIAENGAVIQLAEQWQEI-- 85
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHELSPETIEaLERLREAGVKVVIVTGRSLAEIKELLKQLNLP-LPLIAENGALIFYPGEILYIep 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    86 DGFPRIISGISHGEISQVLNTLreKEHFKFTTFDDVDDATIAEWTGLSRSQAaLTQLHEASVTLIWRdsdeRMAQFTARl 165
Cdd:TIGR01484  80 SDVFEEILGIKFEEIGAELKSL--SEHYVGTFIEDKAIAVAIHYVGAELGQE-LDSKMRERLEKIGR----NDLELEAI- 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831947   166 nelglqfMQGARFWHVLDASAGKDQAANWIIATYQqlsGKRPTTLGLGDGPNDAPLLEVMDYAVIV 231
Cdd:TIGR01484 152 -------YSGKTDLEVLPAGVNKGSALQALLQELN---GKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK14502 PRK14502
bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; ...
 9-260 2.56e-23

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


Pssm-ID: 184713 [Multi-domain]  Cd Length: 694  Bit Score: 98.85  E-value: 2.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    9 LVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGlPLIAENGAVIQLAEQW------ 82
Cdd:PRK14502 418 IVYTDLDGTLLNPLTYSYSTALDALRLLKDKELPLVFCSAKTMGEQDLYRNELGIKD-PFITENGGAIFIPKDYfrlpfa 496

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   83 --QEIDGFPRIISGISHGEISQVLNTLREKE-----------HFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTL 149
Cdd:PRK14502 497 ydRVAGNYLVIELGMAYKDIRHILKKALAEActeiensekagNIFITSFGDMSVEDVSRLTDLNLKQAELAKQREYSETV 576

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  150 IWRDSDERMAQFTARLNELGLQFMQGARFWHVldaSAGKDQA-ANWIIATYQQLSGKRPTTLGLGDGPNDAPLLEVMDYA 228
Cdd:PRK14502 577 HIEGDKRSTNIVLNHIQQSGLEYSFGGRFYEV---TGGNDKGkAIKILNELFRLNFGNIHTFGLGDSENDYSMLETVDSP 653

                        250       260       270
                 ....*....|....*....|....*....|..
gi 15831947  229 VIVKGLNREGVHLHDEDPARVwrtQREGPEGW 260
Cdd:PRK14502 654 ILVQRPGNKWHKMRLRNPSYV---KGVGPEGF 682
PRK12702 PRK12702
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 9-262 1.91e-16

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 105866  Cd Length: 302  Bit Score: 77.42  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    9 LVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGlPLIAENGAVIQ----------L 78
Cdd:PRK12702   3 LVLSSLDGSLLDLEFNSYGAARQALAALERRSIPLVLYSLRTRAQLEHLCRQLRLEH-PFICEDGSAIYvpehyfpagiL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   79 AEQWQEIDGFPRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWRDSDERM 158
Cdd:PRK12702  82 DEQWQHRPPYYVCALGLPYPCLRHILQQVRQDSHLDLIGFGDWTASELAAATGIPLEEAERAQKREYSEIFSYSGDPARL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  159 ----AQFTARLNELGLQFMQ----GARFWHVLD----------ASAGKDQAANWIIATYQQLSGKrPTTLGLGDGPNDAP 220
Cdd:PRK12702 162 reafAQQEANLTQHLLRLHQlhfsDLPQWYLTGwmqptlaaepNSLPGEQAVQLLLDCYQRHLGP-IKALGIGCSPPDLA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15831947  221 LLEVMDYAV-----IVKGLNREGVHLHDEDPARVWRTQR-EGPEGWRE 262
Cdd:PRK12702 241 FLRWSEQKVvlpspIADSLWKEALRLGGPEVQPQWQLAQlPGPEGWNE 288
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 9-231 1.56e-13

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: 68.45  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947     9 LVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGlPLIAENGAVIQLaEQWQEIDGF 88
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDT-PFITANGAAVID-DQGEILYKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    89 PriisgISHGEISQVLNTLREKE---HFK-----FTTFDDVDDATIAEWTGLSRSQ-AALTQLHEASVTLIWR--DSDER 157
Cdd:TIGR00099  79 P-----LDLDLVEEILNFLKKHGldvILYgddsiYASKNDPEYFTIFKKFLGEPKLeVVDIQYLPDDILKILLlfLDPED 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831947   158 MAQFTARLNELGLQFMQGARFWH-----VLDASAGKDQAANWiIATYQQLSGKRptTLGLGDGPNDAPLLEVMDYAVIV 231
Cdd:TIGR00099 154 LDLLIEALNKLELEENVSVVSSGpysieITAKGVSKGSALQS-LAEALGISLED--VIAFGDGMNDIEMLEAAGYGVAM 229
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 9-231 6.71e-12

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: 62.85  E-value: 6.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   9 LVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGlPLIAENGAVIQlaeqwqeiDGF 88
Cdd:COG0561   4 LIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDD-PLITSNGALIY--------DPD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  89 PRII--SGISHGEISQVLNTLREkehfkfttfddvddatiaewtglsrsqaaltqlHEASVTLIWRDSDermaqftarln 166
Cdd:COG0561  75 GEVLyeRPLDPEDVREILELLRE---------------------------------HGLHLQVVVRSGP----------- 110

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831947 167 elglqfmqgaRFWHVLDASAGKDQAANWIIatyQQLSGKRPTTLGLGDGPNDAPLLEVMDYAVIV 231
Cdd:COG0561 111 ----------GFLEILPKGVSKGSALKKLA---ERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAM 162
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 10-232 6.23e-11

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 61.10  E-value: 6.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    10 VFSDLDGTLLDShsyDWQP-----AApwLSRLREANVPVILCSSKTSAEMLYLQKMLGLQgLPLIAENGAVIQlAEQWQE 84
Cdd:pfam08282   1 IASDLDGTLLNS---DKKIsektkEA--IKKLKEKGIKFVIATGRPYRAILPVIKELGLD-DPVICYNGALIY-DENGKI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    85 IdgfprIISGISHGEISQVLNTLRE-KEHFKFTTFDD--VDDATIAEWTGLSRSQAALTQLHEASVTLIWRDS------- 154
Cdd:pfam08282  74 L-----YSNPISKEAVKEIIEYLKEnNLEILLYTDDGvyILNDNELEKILKELNYTKSFVPEIDDFELLEDEDinkilil 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   155 --DERMAQFTARLNELGLQFMQGARFWH-VLDASAGKDQAANWI--IATYQQLSGKRptTLGLGDGPNDAPLLEVMDYAV 229
Cdd:pfam08282 149 ldEEDLDELEKELKELFGSLITITSSGPgYLEIMPKGVSKGTALkaLAKHLNISLEE--VIAFGDGENDIEMLEAAGLGV 226


                  ...
gi 15831947   230 IVK 232
Cdd:pfam08282 227 AMG 229
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 9-126 3.22e-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: 52.98  E-value: 3.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   9 LVFSDLDGTLLDSHSYdwqpaapwLS--------RLREANVPVILCSSKTSAEMLYLQKMLGLqGLPLIAENGAVIQLAE 80
Cdd:cd07516   1 LIALDLDGTLLNSDKE--------ISprtkeaikKAKEKGIKVVIATGRPLRGAQPYLEELGL-DSPLITFNGALVYDPT 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15831947  81 QWqeidgfpRIISGISHGEISQVLNTLREKEHFKFTTF-DDVDDATI 126
Cdd:cd07516  72 GK-------EILERLISKEDVKELEEFLRKLGIGINIYtNDDWADTI 111
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 9-76 6.27e-07

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: 47.01  E-value: 6.27e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   9 LVFSDLDGTLLdshsydwqpAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGL--PLIAENGAVI 76
Cdd:cd01427   1 AVLFDLDGTLL---------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLfdGIIGSDGGGT 61
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 10-231 6.36e-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: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    10 VFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGlPLIAENGAVI------------Q 77
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPD-PVIAENGGEIsyneglddiflaY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    78 LAEQWQEIDgfpriisgishgeisqvlntlREKEHFKFTTFDdvddatiaewtglsrsqaaLTQLHEASVTLIWRDSDER 157
Cdd:TIGR01482  80 LEEEWFLDI---------------------VIAKTFPFSRLK-------------------VQYPRRASLVKMRYGIDVD 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831947   158 MAQftARLNELGLQ-FMQGARF-WHVLDASAGKDQAanwiIATYQQLSGKRPT-TLGLGDGPNDAPLLEVMDYAVIV 231
Cdd:TIGR01482 120 TVR--EIIKELGLNlVAVDSGFdIHILPQGVNKGVA----VKKLKEKLGIKPGeTLVCGDSENDIDLFEVPGFGVAV 190
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 10-126 1.38e-05

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 45.01  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    10 VFSDLDGTLLDSHsyDWQPAAP-WLSRLREANVPVILC---SSKTSAEML-YLQKMLGLQGLPL-IAENGAVIQ-LAEQW 82
Cdd:TIGR01460   1 FLFDIDGVLWLGH--KPIPGAAeALNRLRAKGKPVVFLtnnSSRSEEDYAeKLSSLLGVDVSPDqIITSGSVTKdLLRQR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15831947    83 QEIDGfpriISGISHGEISQVLntlrEKEHFKFTTFDDVDDATI 126
Cdd:TIGR01460  79 FEGEK----VYVIGVGELRESL----EGLGFRNDFFDDIDHLAI 114
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 13-75 1.85e-05

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: 43.35  E-value: 1.85e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831947  13 DLDGTLLD---SHSYDwqpAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGlPLIAENGAV 75
Cdd:cd07514   5 DIDGTLTDrrrSIDLR---AIEAIRKLEKAGIPVVLVTGNSLPVARALAKYLGLSG-PVVAENGGV 66
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 7-231 9.33e-05

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: 42.42  E-value: 9.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947     7 PLLVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGlPLIAENGAVI---------- 76
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSG-PVVAENGGVIfynkedifla 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947    77 QLAEQWqEIDGFPRIISgishgEISQVLNTLREKEHFKFTTFDDVDdaTIAEWtglsrsqaaltqlheasvtliwrdsde 156
Cdd:TIGR01487  80 NMEEEW-FLDEEKKKRF-----PRDRLSNEYPRASLVIMREGKDVD--EVREI--------------------------- 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831947   157 rmaqftarLNELGLQFMQGARFWHVLDASAGKDQAanwiIATYQQLSG-KRPTTLGLGDGPNDAPLLEVMDYAVIV 231
Cdd:TIGR01487 125 --------IKERGLNLVASGFAIHIMKKGVDKGVG----VEKLKELLGiKPEEVAAIGDSENDIDLFRVVGFKVAV 188
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 9-76 1.49e-04

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: 41.42  E-value: 1.49e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831947   9 LVFSDLDGTLLDS-HSYDWQPAAPWLSRLREANVPVILCSSKtsaEMLYLQKMLG--LQGLPLIAENGAVI 76
Cdd:cd07518   2 LIATDMDGTFLNDdKTYDHERFFAILDQLLKKGIKFVVASGR---QYYQLISFFPeiKDEMSFVAENGAVV 69
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 9-267 4.38e-04

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: 40.80  E-value: 4.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   9 LVFSDLDGTLLDSHsyDWQPAAPWLSRLRE---ANVPVILCSSKTSAEMLYLQKMlGLQGLP------------LIAENG 73
Cdd:cd02605   1 LLVSDLDETLVGHD--TNLQALERLQDLLEqltADNDVILVYATGRSPESVLELI-KEVMLPkpdfiisdvgteIYYGES 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  74 AVIQLAEQWqeidgfpriisgishgeiSQVLNTLREKEhfkftTFDDVDDATIAEWTGLSRSQAAltqlHEASVTLIWRD 153
Cdd:cd02605  78 GYLEPDTYW------------------NEVLSEGWERF-----LFEAIADLFKQLKPQSELEQNP----HKISFYLDPQN 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947 154 SDERMAQFTARLNELGLQF-----MQGARFWHVLDASAGKDQAANWIIATYQqLSGKRptTLGLGDGPNDAPLLEVMDYA 228
Cdd:cd02605 131 DAAVIEQLEEMLLKAGLTVriiysSGLAYDLDILPLGAGKGEALRYLQEKWN-FPPER--TLVCGDSGNDIALLSTGTRG 207

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15831947 229 VIVKGLNREGVHLHDEdPARVWRTQREGPEGWREGLDHF 267
Cdd:cd02605 208 VIVGNAQPELLKWADR-VTRSRLAKGPYAGGILEGLAHF 245
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 10-66 3.45e-03

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; The haloacid dehalogenase-like (HAD) hydrolases are 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 include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members 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: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 36.48  E-value: 3.45e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831947  10 VFSDLDGTLLdshSYDWQPAAP----WLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGL 66
Cdd:cd16416   2 VITDLDNTLL---AWDNPDLTPevkaWLADLKEAGIKVVLVSNNNERRVAKVIEKLDLPFV 59
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 9-150 4.08e-03

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: 37.59  E-value: 4.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   9 LVFSDLDGTLLDSHSYDWQPAAPWLSRLREANVPVILCSSKTSAEMLYLQKMLGLQGlpLIAENGAVIQLAEQwqeidgf 88
Cdd:cd07517   2 IVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDS--YVSYNGQYVFFEGE------- 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947  89 prII--SGISHGEISQVLNTLREKEHF------KFTTFDDVDDATIAEwtglSRSQAALTQLHEASVTLI 150
Cdd:cd07517  73 --VIykNPLPQELVERLTEFAKEQGHPvsfygqLLLFEDEEEEQKYEE----LRPELRFVRWHPLSTDVI 136
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
9-72 5.94e-03

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 37.40  E-value: 5.94e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831947   9 LVFSDLDGTLLDshsyDWQP---AAPWLSRLREANVPVILC---SSKTSAEmlYLQKMLGLqGLPLIAEN 72
Cdd:COG0647  10 AFLLDLDGVLYR----GDEPipgAVEALARLRAAGKPVLFLtnnSSRTPED--VAEKLRRL-GIPVAEDE 72
 
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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