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Conserved domains on  [gi|17557870|ref|NP_506040|]
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Phospholysine phosphohistidine inorganic pyrophosphate phosphatase [Caenorhabditis elegans]

Protein Classification

HAD-SF-IIA-hyp3 family protein( domain architecture ID 11492674)

HAD-SF-IIA-hyp3 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
7-262 1.21e-164

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


:

Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 456.25  E-value: 1.21e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870     7 VNGFLLDITGVLYNSIYKSdGVAVPKSAEAVNFLYQHS-KVKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQ 85
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAGG-GTAVPGSQEAVKRLRGASvKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870    86 YCRENKLRPHLFVRDDVLEYFDGIDTSSPNCVVMGEVEEGFSFDRINRAFRILIDMPKPLLITMGNGKFFQRVDGPCIDV 165
Cdd:TIGR01458  80 LLEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFRLLLDGAKPVLIAIGKGRYYKRKDGLALDV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   166 GAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGKWRP-DFEKMPVT 244
Cdd:TIGR01458 160 GPFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRTGKYRPsDEEKINVP 239
                         250
                  ....*....|....*...
gi 17557870   245 PDLTADCLYDAVKLIADN 262
Cdd:TIGR01458 240 PDLTCDSLPHAVDLILQH 257
 
Name Accession Description Interval E-value
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
7-262 1.21e-164

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 456.25  E-value: 1.21e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870     7 VNGFLLDITGVLYNSIYKSdGVAVPKSAEAVNFLYQHS-KVKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQ 85
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAGG-GTAVPGSQEAVKRLRGASvKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870    86 YCRENKLRPHLFVRDDVLEYFDGIDTSSPNCVVMGEVEEGFSFDRINRAFRILIDMPKPLLITMGNGKFFQRVDGPCIDV 165
Cdd:TIGR01458  80 LLEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFRLLLDGAKPVLIAIGKGRYYKRKDGLALDV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   166 GAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGKWRP-DFEKMPVT 244
Cdd:TIGR01458 160 GPFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRTGKYRPsDEEKINVP 239
                         250
                  ....*....|....*...
gi 17557870   245 PDLTADCLYDAVKLIADN 262
Cdd:TIGR01458 240 PDLTCDSLPHAVDLILQH 257
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
8-260 3.01e-134

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 378.93  E-value: 3.01e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   8 NGFLLDITGVLYNSIYksdgvAVPKSAEAVNFLY-QHSKVKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQY 86
Cdd:cd07509   1 KAVLLDLSGTLYISGA-----AIPGAAEALKRLRhAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  87 CRENKLRPHLFVRDDVLEYFDGIDTSSPNCVVMGEVEEGFSFDRINRAFRILIDmpKPLLITMGNGKFFQRVDGPCIDVG 166
Cdd:cd07509  76 LEEKGLRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLLD--GAPLIALHKGRYYKRKDGLALDPG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870 167 AFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGKWRPDFEKMP-VTP 245
Cdd:cd07509 154 AFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDEKKPnVPP 233
                       250
                ....*....|....*
gi 17557870 246 DLTADCLYDAVKLIA 260
Cdd:cd07509 234 DLTADSFADAVDHIL 248
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
9-254 2.40e-59

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 188.78  E-value: 2.40e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   9 GFLLDITGVLYNsiyksDGVAVPKSAEAVNFLYQHSK-VKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQYC 87
Cdd:COG0647  10 AFLLDLDGVLYR-----GDEPIPGAVEALARLRAAGKpVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  88 RENKLRPHLFV--RDDVLEYFDGI-----DTSSPNCVVMGEvEEGFSFDRINRAFRiLIDMPKPLLITMGNgKFFQRVDG 160
Cdd:COG0647  85 AERHPGARVYVigEEGLREELEEAgltlvDDEEPDAVVVGL-DRTFTYEKLAEALR-AIRRGAPFIATNPD-RTVPTEDG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870 161 PCIDVGAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGKWRP-DFE 239
Cdd:COG0647 162 LIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAeDLE 241
                       250
                ....*....|....*
gi 17557870 240 KMPVTPDLTADCLYD 254
Cdd:COG0647 242 AAPIRPDYVLDSLAE 256
Hydrolase_like pfam13242
HAD-hyrolase-like;
184-255 2.45e-19

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 79.58  E-value: 2.45e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17557870   184 GKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGK-WRPDFEKMPVTPDLTADCLYDA 255
Cdd:pfam13242   3 GKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVtRPADLEKAPIRPDYVVDDLAEA 75
PRK10444 PRK10444
HAD-IIA family hydrolase;
13-254 1.70e-09

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 56.72  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   13 DITGVLYNsiyksDGVAVPKSAEAVN-FLYQHSKVKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQYCRENK 91
Cdd:PRK10444   7 DIDGVLMH-----DNVAVPGAAEFLHrILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   92 LRPHLFVRDDVLE---YFDG--IDTSSPNCVVMGEVEEgFSFDRINRAFRILidmpkpllitmGNGKFFQRVD----GPC 162
Cdd:PRK10444  82 GKKAYVIGEGALIhelYKAGftITDINPDFVIVGETRS-YNWDMMHKAAYFV-----------ANGARFIATNpdthGRG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  163 ID--VGAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDV-GGAQAcGMRGVQVRTGKWR-PDF 238
Cdd:PRK10444 150 FYpaCGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDIlAGFQA-GLETILVLSGVSTlDDI 228
                        250
                 ....*....|....*.
gi 17557870  239 EKMPVTPDLTADCLYD 254
Cdd:PRK10444 229 DSMPFRPSWIYPSVAD 244
 
Name Accession Description Interval E-value
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
7-262 1.21e-164

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 456.25  E-value: 1.21e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870     7 VNGFLLDITGVLYNSIYKSdGVAVPKSAEAVNFLYQHS-KVKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQ 85
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAGG-GTAVPGSQEAVKRLRGASvKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870    86 YCRENKLRPHLFVRDDVLEYFDGIDTSSPNCVVMGEVEEGFSFDRINRAFRILIDMPKPLLITMGNGKFFQRVDGPCIDV 165
Cdd:TIGR01458  80 LLEEKQLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPEHFSYQILNQAFRLLLDGAKPVLIAIGKGRYYKRKDGLALDV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   166 GAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGKWRP-DFEKMPVT 244
Cdd:TIGR01458 160 GPFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRTGKYRPsDEEKINVP 239
                         250
                  ....*....|....*...
gi 17557870   245 PDLTADCLYDAVKLIADN 262
Cdd:TIGR01458 240 PDLTCDSLPHAVDLILQH 257
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
8-260 3.01e-134

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 378.93  E-value: 3.01e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   8 NGFLLDITGVLYNSIYksdgvAVPKSAEAVNFLY-QHSKVKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQY 86
Cdd:cd07509   1 KAVLLDLSGTLYISGA-----AIPGAAEALKRLRhAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  87 CRENKLRPHLFVRDDVLEYFDGIDTSSPNCVVMGEVEEGFSFDRINRAFRILIDmpKPLLITMGNGKFFQRVDGPCIDVG 166
Cdd:cd07509  76 LEEKGLRPHLLVDDDALEDFIGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLLD--GAPLIALHKGRYYKRKDGLALDPG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870 167 AFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGKWRPDFEKMP-VTP 245
Cdd:cd07509 154 AFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDEKKPnVPP 233
                       250
                ....*....|....*
gi 17557870 246 DLTADCLYDAVKLIA 260
Cdd:cd07509 234 DLTADSFADAVDHIL 248
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
9-254 2.40e-59

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 188.78  E-value: 2.40e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   9 GFLLDITGVLYNsiyksDGVAVPKSAEAVNFLYQHSK-VKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQYC 87
Cdd:COG0647  10 AFLLDLDGVLYR-----GDEPIPGAVEALARLRAAGKpVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  88 RENKLRPHLFV--RDDVLEYFDGI-----DTSSPNCVVMGEvEEGFSFDRINRAFRiLIDMPKPLLITMGNgKFFQRVDG 160
Cdd:COG0647  85 AERHPGARVYVigEEGLREELEEAgltlvDDEEPDAVVVGL-DRTFTYEKLAEALR-AIRRGAPFIATNPD-RTVPTEDG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870 161 PCIDVGAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGKWRP-DFE 239
Cdd:COG0647 162 LIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAeDLE 241
                       250
                ....*....|....*
gi 17557870 240 KMPVTPDLTADCLYD 254
Cdd:COG0647 242 AAPIRPDYVLDSLAE 256
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
9-256 5.07e-31

UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar phosphatase; Bacillus subtilis AraL is a phosphatase displaying activity towards different sugar phosphate substrates; it is encoded by the arabinose metabolic operon araABDLMNPQ-abfA and may play a role in the dephosphorylation of substrates related to l-arabinose metabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319833 [Multi-domain]  Cd Length: 252  Bit Score: 115.74  E-value: 5.07e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   9 GFLLDITGVlynsIYKSDgVAVPKSAEAVNFLYQHSK-VKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQYC 87
Cdd:cd07531   2 GYIIDLDGT----IGKGV-TLIPGAVEGVKTLRRLGKkIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  88 RENKLRPHLFVRD-----DVLEyFDGIDTSSP---NCVVMGEVEEGFSFDRINRAFRILIDMPKplLITMGNGKFFQRVD 159
Cdd:cd07531  77 AREKPNAKVFVTGeegliEELR-LAGLEIVDKydeAEYVVVGSNRKITYELLTKAFRACLRGAR--YIATNPDRIFPAED 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870 160 GPCIDVGAFAAALKFSTN--CEVLnIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTG-KWRP 236
Cdd:cd07531 154 GPIPDTAAIIGAIEWCTGrePEVV-VGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMETALVLTGvTTRE 232
                       250       260
                ....*....|....*....|
gi 17557870 237 DFEKMPVTPDLTADCLYDAV 256
Cdd:cd07531 233 NLDRHGYKPDYVLNSIKDLV 252
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
9-254 2.40e-30

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. 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: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 114.38  E-value: 2.40e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   9 GFLLDITGVLYNsiyksDGVAVPKSAEAVNFLYQHSK-VKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQYC 87
Cdd:cd07508   1 LVISDCDGVLWH-----DERAIPGAAEFLEALKEAGKkIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKATARFL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  88 RENK----------------LRPHLFV--------RDDVLEYFDGI-DTSSPNCVVMGeVEEGFSFDRINRAFRILIDmP 142
Cdd:cd07508  76 RSRKfgkkvyvlgeeglkeeLRAAGFRiaggpskgIETYAELVEHLeDDENVDAVIVG-SDFKLNFAKLRKACRYLRN-P 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870 143 KPLLI-----TMGNGKffqrVDGPCIDVGAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVG 217
Cdd:cd07508 154 GCLFIatapdRIHPLK----DGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVL 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17557870 218 GAQACGMRGVQVRTGKWRPD----FEKMPVTPDLTADCLYD 254
Cdd:cd07508 230 FGKACGFQTLLVLTGVTTLEdlqaYIDHELVPDYYADSLAD 270
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
9-254 1.01e-27

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 106.52  E-value: 1.01e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   9 GFLLDITGVLYNsiyksDGVAVPKSAEAVNFLY-QHSKVKFLSNakgNSNR---NVARRLQRLGINVREEDVITPAPVVA 84
Cdd:cd07530   2 GYLIDLDGTVYR-----GGTAIPGAVEFIERLReKGIPFLFLTN---NSTRtpeDVAAKLAEMGIDVPEEDVYTSALATA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  85 QYCRENKLRPHLFV------RDDVLEYFDGIDTSSPNCVVMGEVEEgFSFDRINRAfrilidmpkPLLITMGnGKFF--- 155
Cdd:cd07530  74 QYLAEQLPGAKVYVigeeglRTALHEAGLTLTDENPDYVVVGLDRD-LTYEKLAEA---------TLAIRNG-AKFIatn 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870 156 -----QRVDGPCIDVGAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVR 230
Cdd:cd07530 143 pdltlPTERGLLPGNGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVL 222
                       250       260
                ....*....|....*....|....*
gi 17557870 231 TGKWRP-DFEKMPVTPDLTADCLYD 254
Cdd:cd07530 223 TGVTTReDLAKPPYRPTYIVPSLRE 247
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
10-232 5.88e-27

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: 104.33  E-value: 5.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870    10 FLLDITGVLYNsiyksDGVAVPKSAEAVNFLYQHSK-VKFLSNAKGNSNRNVARRLQRL-GINVREEDVITPAPVVAQYC 87
Cdd:TIGR01460   1 FLFDIDGVLWL-----GHKPIPGAAEALNRLRAKGKpVVFLTNNSSRSEEDYAEKLSSLlGVDVSPDQIITSGSVTKDLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870    88 RE---------------NKLRPHLFVRDDVLEYFDGIDTSSPNCVVMGEVEEGFSFDRINRAFRILIDmPKPLLITMGNG 152
Cdd:TIGR01460  76 RQrfegekvyvigvgelRESLEGLGFRNDFFDDIDHLAIEKIPAAVIVGEPSDFSYDELAKAAYLLAE-GDVPFIAANRD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   153 KFFQRVDG-PCIDVGAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEI-VMVGDDLMSDVGGAQACGMRGVQVR 230
Cdd:TIGR01460 155 DLVRLGDGrFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRdVMVGDNLRTDILGAKNAGFDTLLVL 234

                  ..
gi 17557870   231 TG 232
Cdd:TIGR01460 235 TG 236
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
10-232 3.00e-23

UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium falciparum PNPase; Plasmodium falciparum para nitrophenyl phosphate phosphatase (PNPase) catalyzes the dephosphorylation of thiamine monophosphate to thiamine, other substrates on which its active are nucleotides, phosphorylated sugars, pyridoxal-5-phosphate, and paranitrophenyl phosphate. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319834 [Multi-domain]  Cd Length: 286  Bit Score: 95.83  E-value: 3.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  10 FLLDITGVLYNsiyksDGVAVPKSAEAVNFLYQHSK-VKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQYCR 88
Cdd:cd07532   9 VIFDADGVLWT-----GDKPIPGAVEVFNALLDKGKkVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIADYLK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  89 ENKLRPHLFV--------------------------RDDVLEYFDGIDTS-SPNCVVMGEvEEGFSFDRINRAFRILIDm 141
Cdd:cd07532  84 EKGFKKKVYVigeegirkeleeagivscggdgedekDDSMGDFAHNLELDpDVGAVVVGR-DEHFSYPKLMKACNYLRN- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870 142 PKPLLITMGNGKFFQRVDGPCI-DVGAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQ 220
Cdd:cd07532 162 PDVLFLATNMDATFPGPVGRVIpGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFAN 241
                       250
                ....*....|..
gi 17557870 221 ACGMRGVQVRTG 232
Cdd:cd07532 242 NCGFQSLLVGTG 253
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
7-232 5.57e-20

phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In mammals, PGP is found in many tissues, notably in red blood cells where P-glycolate is and important activator of the hydrolysis of 2,3-bisphosphoglycerate, a major modifier of the oxygen affinity of hemoglobin. Pyridoxal phosphate (PLP, Vitamin B6) phosphatase is involved in the degradation of PLP in mammals and is widely distributed in human tissues including erythrocyes. The enzymes described here are members of the Haloacid dehalogenase superfamily of hydrolase enzymes (pfam00702). Unlike the bacterial PGP equivalog (TIGR01449), which is a member of class (subfamily) I, these enzymes are members of class (subfamily) II. These two families have almost certainly arisen from convergent evolution (although these two ancestors may themselves have diverged from a more distant HAD superfamily progenitor). The primary seed sequence for this model comes from Chlamydomonas reinhardtii, a photosynthetic alga. The enzyme has been purified and characterized and these data are fully consistent with the assignment of function as a PGPase involved in photorespiration. The second seed, from Homo sapiens chromosome 22 has been characterized as a pyridoxal phosphatase. Biochemical characterization of partially purified PGP's from various tissues including red blood cells have been performed while one gene for PGP has been localized to chromosome 16p13.3. The sequence used here maps to chromosome 22. There is indeed a related gene on chromosome 16 (and it is expressed, since EST's are found) which shows 46% identity. The chromosome 16 gene is not in evidence in nraa but translated from the genomic sequence. The third seed, from C. elegans, is only supported by sequence similarity. This model is limited to eukaryotic species including S. pombe and S. cerevisiae, although several archaea score between the trusted and noise cutoffs. This model is closely related to a family of bacterial sequences including the E. coli NagD and B. subtilus AraL genes which are characterized by the ability to hydrolyze para-nitrophenylphosphate (pNPPases or NPPases). The chlamydomonas PGPase d


Pssm-ID: 273635 [Multi-domain]  Cd Length: 279  Bit Score: 86.84  E-value: 5.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870     7 VNGFLLDITGVLYNSiyksdGVAVPKSAEAVNFLYQHSK-VKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQ 85
Cdd:TIGR01452   2 AQGFIFDCDGVLWLG-----ERVVPGAPELLDRLARAGKqILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870    86 YCRENKLRP-HLFV------RDDV----LEYF-DGIDTSSPNCVVMGEV--------------EEGFSFDRINRAFRILI 139
Cdd:TIGR01452  77 LLRQPPDAGkAVYVigeeglRAELdaagIRLAgDPGEKKQDEADGFMYDikldervgavvvgyDEHFSYVKLMEACAHLR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   140 DmPKPLLITMGNGKFFQRVDGPCI-DVGAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGG 218
Cdd:TIGR01452 157 E-PGCLFVATNRDPWHPLSDGSRTpGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILF 235
                         250
                  ....*....|....
gi 17557870   219 AQACGMRGVQVRTG 232
Cdd:TIGR01452 236 GHRCGMTTVLVLSG 249
Hydrolase_like pfam13242
HAD-hyrolase-like;
184-255 2.45e-19

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 79.58  E-value: 2.45e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17557870   184 GKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGK-WRPDFEKMPVTPDLTADCLYDA 255
Cdd:pfam13242   3 GKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVtRPADLEKAPIRPDYVVDDLAEA 75
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
7-232 2.45e-18

UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase; This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It belongs to the UmpH/NagD phosphatase family, and 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: 319813 [Multi-domain]  Cd Length: 282  Bit Score: 82.05  E-value: 2.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   7 VNGFLLDITGVLYNSiyksdGVAVPKSAEAVNFLYQHSK-VKFLSNAKGNSNRNVARRLQRLGINV-REEDVITPAPVVA 84
Cdd:cd07510   1 VDTFLFDCDGVLWNG-----EKAIPGAPETLNLLRSLGKrLVFVTNNSTKSREAYAKKFARLGFTGlKEEEIFSSAYCAA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  85 QYCREN-------------------KLR----PHLFVRDDVLEYFDGIDTSSP------NCVVMGeVEEGFSFDRINRAF 135
Cdd:cd07510  76 RYLRQRlpgpadgkvyvlggeglraELEaagvAHLGGPDDGLRRAAPKDWLLAgldpdvGAVLVG-LDEHVNYLKLAKAT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870 136 RILIDmPKPLLITMGNGKFFQRVDGPCI-DVGAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMS 214
Cdd:cd07510 155 QYLRD-PGCLFVATNRDPWHPLSDGSFIpGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDT 233
                       250
                ....*....|....*...
gi 17557870 215 DVGGAQACGMRGVQVRTG 232
Cdd:cd07510 234 DILFGQNCGLKTLLVLTG 251
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
10-250 1.01e-17

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized subfamily belongs to the UmpH/NagD phosphatase family and 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: 319858 [Multi-domain]  Cd Length: 247  Bit Score: 79.79  E-value: 1.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  10 FLLDITGvlynSIYKSDGVaVPKSAEAVNFLYQHSK-VKFLSNakgNSNRNVA---RRLQRLGINVREEDVITPAPVVAQ 85
Cdd:cd16422   2 FIFDMDG----TIYLGDDL-IPGTLEFLERLHEKKRrYIFLTN---NSSKNLAdyvEKLNRLGIDAGLDRVFTSGEATID 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  86 YCRENKLRPHLF------VRDDVLEYFDGIDTSSPNCVVMGeVEEGFSFDRINRAFrILIDMPKPLLITMGNgKFFQRVD 159
Cdd:cd16422  74 HLKKEFIKPKIFllgtksLREEFEKAGFTLDGDDIDVVVLG-FDTELTYEKLRTAC-LLLRRGIPYIATHPD-INCPSEE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870 160 GPCIDVGAFAAALKFSTNC-EVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGKWRP-D 237
Cdd:cd16422 151 GPIPDAGSIIALIETSTGRrPDLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILVLSGETTReD 230
                       250
                ....*....|...
gi 17557870 238 FEKMPVTPDLTAD 250
Cdd:cd16422 231 LEDLERKPTYVFD 243
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
10-108 3.22e-15

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 69.42  E-value: 3.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870    10 FLLDITGVLYNsiyksDGVAVPKSAEAVNFLYQHSK-VKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQYCR 88
Cdd:pfam13344   1 FLFDIDGVLWR-----GGEPIPGAAEALRALRAAGKpVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLK 75
                          90       100
                  ....*....|....*....|..
gi 17557870    89 ENKLRPHLFV--RDDVLEYFDG 108
Cdd:pfam13344  76 ERKFGKKVLVigSEGLREELEE 97
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
179-259 7.92e-14

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 68.52  E-value: 7.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870 179 EVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGKWRPDFEkmpVTPDLTADCLYDAVKL 258
Cdd:COG1011 143 EEVGVRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAE---PRPDYVISDLAELLEL 219

                .
gi 17557870 259 I 259
Cdd:COG1011 220 L 220
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
165-230 1.89e-10

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];


Pssm-ID: 441782  Cd Length: 164  Bit Score: 58.22  E-value: 1.89e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17557870 165 VGAFAAALKFSTnceVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVR 230
Cdd:COG2179  74 VKRFAEKLGIPY---IARAKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVK 136
PRK10444 PRK10444
HAD-IIA family hydrolase;
13-254 1.70e-09

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 56.72  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   13 DITGVLYNsiyksDGVAVPKSAEAVN-FLYQHSKVKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVAQYCRENK 91
Cdd:PRK10444   7 DIDGVLMH-----DNVAVPGAAEFLHrILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   92 LRPHLFVRDDVLE---YFDG--IDTSSPNCVVMGEVEEgFSFDRINRAFRILidmpkpllitmGNGKFFQRVD----GPC 162
Cdd:PRK10444  82 GKKAYVIGEGALIhelYKAGftITDINPDFVIVGETRS-YNWDMMHKAAYFV-----------ANGARFIATNpdthGRG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  163 ID--VGAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDV-GGAQAcGMRGVQVRTGKWR-PDF 238
Cdd:PRK10444 150 FYpaCGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDIlAGFQA-GLETILVLSGVSTlDDI 228
                        250
                 ....*....|....*.
gi 17557870  239 EKMPVTPDLTADCLYD 254
Cdd:PRK10444 229 DSMPFRPSWIYPSVAD 244
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
185-230 2.07e-09

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; 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: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 54.22  E-value: 2.07e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 17557870 185 KPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVR 230
Cdd:cd16415  62 KPDPRIFQKALERLGVSPEEALHVGDDLKNDYLGARAVGWHALLVD 107
PLN02645 PLN02645
phosphoglycolate phosphatase
6-258 4.55e-09

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 55.87  E-value: 4.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870    6 AVNGFLLDITGVlynsIYKSDGVaVPKSAEAVNFL-YQHSKVKFLSNAKGNSNRNVARRLQRLGINVREEDVITPAPVVA 84
Cdd:PLN02645  27 SVETFIFDCDGV----IWKGDKL-IEGVPETLDMLrSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870   85 QYCRENKLRPHLFV----RDDVLEYFDGID--------------TSSPNCVV-----MGEVEEGF----SFDRINRAFRI 137
Cdd:PLN02645 102 AYLKSINFPKDKKVyvigEEGILEELELAGfqylggpedgdkkiELKPGFLMehdkdVGAVVVGFdryiNYYKIQYATLC 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870  138 LIDMPKPLLI---TMGNGKFFQRVDGPciDVGAFAAALKFSTNCEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMS 214
Cdd:PLN02645 182 IRENPGCLFIatnRDAVTHLTDAQEWA--GAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLDT 259
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 17557870  215 DVGGAQACGMRGVQVRTGKWRPDFEKMP---VTPDLTADCLYDAVKL 258
Cdd:PLN02645 260 DILFGQNGGCKTLLVLSGVTSESMLLSPenkIQPDFYTSKISDFLTL 306
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
184-229 1.46e-08

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: 51.50  E-value: 1.46e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 17557870 184 GKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQV 229
Cdd:cd16416  63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTILV 108
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
178-227 5.98e-08

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 49.85  E-value: 5.98e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 17557870 178 CEVLNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGV 227
Cdd:cd04305  57 SEEVGVQKPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
7-223 6.89e-08

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 51.43  E-value: 6.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870     7 VNGFLLDITGVLYNSiyksdgvaVPKSAEAVNFL-YQHSKVKFLSNAKGNSNRNVARRLQRLGINVREedvitpapvvaq 85
Cdd:pfam00702   1 IKAVVFDLDGTLTDG--------EPVVTEAIAELaSEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRD------------ 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557870    86 YCRENklrPHLFVRDDVLEYFDGIDTSSPNCVVMGEVEEGFSFDRINRAFRILIDM-PKPLLITMGNGKFFQRVdgpCID 164
Cdd:pfam00702  61 WLEEL---DILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERgIKVAILTGDNPEAAEAL---LRL 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17557870   165 VGAFAAALKFSTNCEVlNIGKPSRFYFEQGMNALGMKPEEIVMVGDDLMsDVGGAQACG 223
Cdd:pfam00702 135 LGLDDYFDVVISGDDV-GVGKPKPEIYLAALERLGVKPEEVLMVGDGVN-DIPAAKAAG 191
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
184-260 2.19e-07

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 50.31  E-value: 2.19e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17557870 184 GKPSRFYFEQGMNALGMKPEEIVMVGDDLmSDVGGAQACGMRGVQVRTGKWRPDfEKMPVTPDLTADCLYDAVKLIA 260
Cdd:COG0546 139 AKPKPEPLLEALERLGLDPEEVLMVGDSP-HDIEAARAAGVPFIGVTWGYGSAE-ELEAAGADYVIDSLAELLALLA 213
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
185-243 3.03e-06

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.


Pssm-ID: 273744  Cd Length: 170  Bit Score: 46.24  E-value: 3.03e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17557870   185 KPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMRGVQVRTGKwRPD--FEKMPV 243
Cdd:TIGR01668  91 KPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLV-HPDqwFIKRIW 150
PRK10748 PRK10748
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;
185-225 1.52e-04

5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;


Pssm-ID: 182696 [Multi-domain]  Cd Length: 238  Bit Score: 42.03  E-value: 1.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 17557870  185 KPSRFYFEQGMNALGMKPEEIVMVGDDLMSDVGGAQACGMR 225
Cdd:PRK10748 163 KPFSDMYHLAAEKLNVPIGEILHVGDDLTTDVAGAIRCGMQ 203
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
185-229 2.04e-04

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. 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: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 41.18  E-value: 2.04e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17557870 185 KPSRFYFEQGMNALGMKPEEIVMVgDDLMSDVGGAQACGMRGVQV 229
Cdd:cd02603 141 KPDPEIYQLALERLGVKPEEVLFI-DDREENVEAARALGIHAILV 184
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
183-229 5.98e-04

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: 38.53  E-value: 5.98e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 17557870 183 IGKPSRFYFEQGMNALGMKPEEIVMVGDDLmSDVGGAQACGMRGVQV 229
Cdd:cd01427  61 TPKPKPKPLLLLLLKLGVDPEEVLFVGDSE-NDIEAARAAGGRTVAV 106
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
185-249 7.13e-04

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 39.94  E-value: 7.13e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17557870 185 KPSRFYFEQGMNALGMKPEEIVMVgddlmS----DVGGAQACGMRGVQVRtgkwRPD--FEKMPVTPDLTA 249
Cdd:cd02588 147 KPAPAVYELAAERLGVPPDEILHV-----AshawDLAGARALGLRTAWIN----RPGevPDPLGPAPDFVV 208
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
184-232 2.19e-03

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 38.15  E-value: 2.19e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17557870 184 GKPSRFYFEQGMNALGMKPEEIVMVGDDLMsDVGGAQACGMRGVQVRTG 232
Cdd:cd07533 138 SKPHPEMLREILAELGVDPSRAVMVGDTAY-DMQMAANAGAHAVGVAWG 185
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
195-231 2.39e-03

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 37.38  E-value: 2.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 17557870   195 MNALgmKPEEIVMVGDDLMSDVGGAQACGMRGVQVRT 231
Cdd:TIGR01662 101 FNEI--DPEESVYVGDQDLTDLQAAKRVGLATILVAP 135
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
185-232 2.46e-03

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and 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 (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. 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: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 37.98  E-value: 2.46e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17557870 185 KPSRFYFEQGMNALGMKPEEIVMVGDDLmSDVGGAQACGMRGVQVRTG 232
Cdd:cd16417 143 KPDPAPLLHACEKLGIAPAQMLMVGDSR-NDILAARAAGCPSVGLTYG 189
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
165-229 2.65e-03

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies 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. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 37.78  E-value: 2.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17557870   165 VGAFAAALKFSTNCEVLNiGKPSRFYFEQGMNALGMKPEEIVMVgDDLMSDVGGAQACGMRGVQV 229
Cdd:TIGR01509 116 LGLRDLFDVVIDSSDVGL-GKPDPDIYLQALKALGLEPSECVFV-DDSPAGIEAAKAAGMHTVGV 178
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
185-230 4.08e-03

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 37.32  E-value: 4.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 17557870   185 KPSRFYFEQGMNALGMKPEEIVMVGDDlMSDVGGAQACGMRGVQVR 230
Cdd:TIGR01428 148 KPAPQVYQLALEALGVPPDEVLFVASN-PWDLGGAKKFGFKTAWIN 192
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
198-232 5.71e-03

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. 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: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 37.19  E-value: 5.71e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 17557870 198 LGMKPEEIVMVGDDlMSDVGGAQACGMRGVQVRTG 232
Cdd:cd04302 150 LGIAPEQAVMIGDR-KHDIIGARANGIDSIGVLYG 183
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
195-238 8.56e-03

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 36.71  E-value: 8.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17557870  195 MNALGMKPEEIVMVGDDLmSDVGGAQACGMRGVQVRTG--------KWRPDF 238
Cdd:PRK13222 159 CEKLGLDPEEMLFVGDSR-NDIQAARAAGCPSVGVTYGynygepiaLSEPDV 209
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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