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Conserved domains on  [gi|19920940|ref|NP_609219|]
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uncharacterized protein Dmel_CG17294 [Drosophila melanogaster]

Protein Classification

HAD-IIA family hydrolase( domain architecture ID 11576289)

HAD (haloacid dehalogenase)-IIA family hydrolase such as vertebrate haloacid dehalogenase-like hydrolase domain-containing protein 2 and phospholysine phosphohistidine inorganic pyrophosphate phosphatase, which hydrolyzes imidodiphosphate, 3-phosphohistidine and 6-phospholysine, as well as inorganic diphosphate with lower efficiency

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 4-250 4.38e-132

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: 372.77  E-value: 4.38e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   4 KGALIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVENER 83
Cdd:cd07509   1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  84 LNPYYILSEDARQDFpPEDTRRYKDSVVIGLAPKAFNYEQLNEAFNVLLenKNHKLIAVHQGKYYKRAEGLALGPGCFVK 163
Cdd:cd07509  81 LRPHLLVDDDALEDF-IGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLL--DGAPLIALHKGRYYKRKDGLALDPGAFVT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 164 GLEFATGRTAKVIGKPNPYFFEGALAGR--DPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLPDV--KPSPPPTALL 239
Cdd:cd07509 158 GLEYATGIKATVVGKPSPEFFLSALRSLgvDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDekKPNVPPDLTA 237

                       250
                ....*....|.
gi 19920940 240 ENFAEAVDWII 250
Cdd:cd07509 238 DSFADAVDHIL 248
 
Name Accession Description Interval E-value
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 4-250 4.38e-132

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: 372.77  E-value: 4.38e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   4 KGALIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVENER 83
Cdd:cd07509   1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  84 LNPYYILSEDARQDFpPEDTRRYKDSVVIGLAPKAFNYEQLNEAFNVLLenKNHKLIAVHQGKYYKRAEGLALGPGCFVK 163
Cdd:cd07509  81 LRPHLLVDDDALEDF-IGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLL--DGAPLIALHKGRYYKRKDGLALDPGAFVT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 164 GLEFATGRTAKVIGKPNPYFFEGALAGR--DPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLPDV--KPSPPPTALL 239
Cdd:cd07509 158 GLEYATGIKATVVGKPSPEFFLSALRSLgvDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDekKPNVPPDLTA 237

                       250
                ....*....|.
gi 19920940 240 ENFAEAVDWII 250
Cdd:cd07509 238 DSFADAVDHIL 248
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 3-251 5.35e-80

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: 241.30  E-value: 5.35e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940     3 IKGALIDLSGTLHVEDEPT----PNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSY 78
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAGGgtavPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940    79 VENERLNPYYILSEDARQDFPPEDTRRyKDSVVIGLAPKAFNYEQLNEAFNVLLENKNHKLIAVHQGKYYKRAEGLALGP 158
Cdd:TIGR01458  81 LEEKQLRPMLLVDDRVLPDFDGIDTSD-PNCVVMGLAPEHFSYQILNQAFRLLLDGAKPVLIAIGKGRYYKRKDGLALDV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   159 GCFVKGLEFATGRTAKVIGKPNPYFFEGAL--AGRDPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLP--DVKPSPP 234
Cdd:TIGR01458 160 GPFVTALEYATDTKATVVGKPSKTFFLEALraTGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRTGKYRPsdEEKINVP 239

                         250
                  ....*....|....*..
gi 19920940   235 PTALLENFAEAVDWIIQ 251
Cdd:TIGR01458 240 PDLTCDSLPHAVDLILQ 256
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-244 2.38e-70

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 216.51  E-value: 2.38e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   1 MSIKGALIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVE 80
Cdd:COG0647   6 DRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  81 NERLN--PYYILSEDARQDFPPEDTRRYKDS----VVIGLAPkAFNYEQLNEAFNVLLENKnhKLIAVHQGKYYKRAEGL 154
Cdd:COG0647  86 ERHPGarVYVIGEEGLREELEEAGLTLVDDEepdaVVVGLDR-TFTYEKLAEALRAIRRGA--PFIATNPDRTVPTEDGL 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 155 ALGPGCFVKGLEFATGRTAKVIGKPNPYFFEGALA--GRDPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLP-DVKP 231
Cdd:COG0647 163 IPGAGALAAALEAATGGEPLVVGKPSPPIYELALErlGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAeDLEA 242

                       250
                ....*....|....
gi 19920940 232 SPP-PTALLENFAE 244
Cdd:COG0647 243 APIrPDYVLDSLAE 256
Hydrolase_like pfam13242
HAD-hyrolase-like;
175-245 1.31e-22

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 88.06  E-value: 1.31e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19920940   175 VIGKPNPYFFEGALA--GRDPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLPD--VKPSPPPTALLENFAEA 245
Cdd:pfam13242   1 VCGKPNPGMLERALArlGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPAdlEKAPIRPDYVVDDLAEA 75
PLN02645 PLN02645
phosphoglycolate phosphatase
 7-223 4.09e-12

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 64.73  E-value: 4.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940    7 LIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVENERLNP 86
Cdd:PLN02645  32 IFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYLKSINFPK 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   87 ---YYILSEDARQD------FP----PEDTRRYKD--------------SVVIGLAPKaFNYEQLNEAFNVLLENKNHKL 139
Cdd:PLN02645 112 dkkVYVIGEEGILEelelagFQylggPEDGDKKIElkpgflmehdkdvgAVVVGFDRY-INYYKIQYATLCIRENPGCLF 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  140 IAVHQGK--YYKRAEGLAlGPGCFVKGLEFATGRTAKVIGKPNPYFFEGALA--GRDPASCVMIGDDANDDIVGAMSMGM 215
Cdd:PLN02645 191 IATNRDAvtHLTDAQEWA-GAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANkfGIEKSQICMVGDRLDTDILFGQNGGC 269


                 ....*...
gi 19920940  216 QGILVKTG 223
Cdd:PLN02645 270 KTLLVLSG 277
 
Name Accession Description Interval E-value
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 4-250 4.38e-132

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: 372.77  E-value: 4.38e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   4 KGALIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVENER 83
Cdd:cd07509   1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  84 LNPYYILSEDARQDFpPEDTRRYKDSVVIGLAPKAFNYEQLNEAFNVLLenKNHKLIAVHQGKYYKRAEGLALGPGCFVK 163
Cdd:cd07509  81 LRPHLLVDDDALEDF-IGIDTSDPNAVVIGDAGEHFNYQTLNRAFRLLL--DGAPLIALHKGRYYKRKDGLALDPGAFVT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 164 GLEFATGRTAKVIGKPNPYFFEGALAGR--DPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLPDV--KPSPPPTALL 239
Cdd:cd07509 158 GLEYATGIKATVVGKPSPEFFLSALRSLgvDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDekKPNVPPDLTA 237

                       250
                ....*....|.
gi 19920940 240 ENFAEAVDWII 250
Cdd:cd07509 238 DSFADAVDHIL 248
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 3-251 5.35e-80

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: 241.30  E-value: 5.35e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940     3 IKGALIDLSGTLHVEDEPT----PNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSY 78
Cdd:TIGR01458   1 VKGVLLDISGVLYISDAGGgtavPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940    79 VENERLNPYYILSEDARQDFPPEDTRRyKDSVVIGLAPKAFNYEQLNEAFNVLLENKNHKLIAVHQGKYYKRAEGLALGP 158
Cdd:TIGR01458  81 LEEKQLRPMLLVDDRVLPDFDGIDTSD-PNCVVMGLAPEHFSYQILNQAFRLLLDGAKPVLIAIGKGRYYKRKDGLALDV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   159 GCFVKGLEFATGRTAKVIGKPNPYFFEGAL--AGRDPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLP--DVKPSPP 234
Cdd:TIGR01458 160 GPFVTALEYATDTKATVVGKPSKTFFLEALraTGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRTGKYRPsdEEKINVP 239

                         250
                  ....*....|....*..
gi 19920940   235 PTALLENFAEAVDWIIQ 251
Cdd:TIGR01458 240 PDLTCDSLPHAVDLILQ 256
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-244 2.38e-70

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 216.51  E-value: 2.38e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   1 MSIKGALIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVE 80
Cdd:COG0647   6 DRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  81 NERLN--PYYILSEDARQDFPPEDTRRYKDS----VVIGLAPkAFNYEQLNEAFNVLLENKnhKLIAVHQGKYYKRAEGL 154
Cdd:COG0647  86 ERHPGarVYVIGEEGLREELEEAGLTLVDDEepdaVVVGLDR-TFTYEKLAEALRAIRRGA--PFIATNPDRTVPTEDGL 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 155 ALGPGCFVKGLEFATGRTAKVIGKPNPYFFEGALA--GRDPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLP-DVKP 231
Cdd:COG0647 163 IPGAGALAAALEAATGGEPLVVGKPSPPIYELALErlGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAeDLEA 242

                       250
                ....*....|....
gi 19920940 232 SPP-PTALLENFAE 244
Cdd:COG0647 243 APIrPDYVLDSLAE 256
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 4-244 3.65e-37

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: 131.18  E-value: 3.65e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   4 KGALIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYV-ENE 82
Cdd:cd07530   1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLaEQL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  83 RLNPYYILSE----DARQDFPPEDTRRYKDSVVIGLAPKaFNYEQLNEAfnVLLENKNHKLIAVHQGKYYKRAEGLALGP 158
Cdd:cd07530  81 PGAKVYVIGEeglrTALHEAGLTLTDENPDYVVVGLDRD-LTYEKLAEA--TLAIRNGAKFIATNPDLTLPTERGLLPGN 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 159 GCFVKGLEFATGRTAKVIGKPNPYFFEGALA--GRDPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLP-DVKPSP-P 234
Cdd:cd07530 158 GSVVAALEAATGVKPLFIGKPEPIMMRAALEklGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTReDLAKPPyR 237

                       250
                ....*....|
gi 19920940 235 PTALLENFAE 244
Cdd:cd07530 238 PTYIVPSLRE 247
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 7-223 4.15e-32

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: 117.81  E-value: 4.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940     7 LIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRI-GFQLDASEIYSSLSAAVSYV----EN 81
Cdd:TIGR01460   2 LFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLlGVDVSPDQIITSGSVTKDLLrqrfEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940    82 ERlnPYYILSEDARQDFP------------PEDTRRYKDSVVIGLAPKAFNYEQLNEAFNVLLENKNHkLIAVHQGKYYK 149
Cdd:TIGR01460  82 EK--VYVIGVGELRESLEglgfrndffddiDHLAIEKIPAAVIVGEPSDFSYDELAKAAYLLAEGDVP-FIAANRDDLVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19920940   150 RAEG-LALGPGCFVKGLEFATGRTAKVIGKPNPYFFEGALA--GRDPAS-CVMIGDDANDDIVGAMSMGMQGILVKTG 223
Cdd:TIGR01460 159 LGDGrFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNllQARPERrDVMVGDNLRTDILGAKNAGFDTLLVLTG 236
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 7-223 6.29e-29

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: 110.55  E-value: 6.29e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   7 LIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQ-LDASEIYSSLSAAVSYVENERLN 85
Cdd:cd07510   5 LFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTgLKEEEIFSSAYCAARYLRQRLPG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  86 PY----YILSEDA-RQDF------------PPEDTRRYKDSVVIGLAPKA----------FNYEQLNEAFNVLLeNKNHK 138
Cdd:cd07510  85 PAdgkvYVLGGEGlRAELeaagvahlggpdDGLRRAAPKDWLLAGLDPDVgavlvgldehVNYLKLAKATQYLR-DPGCL 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 139 LIAVHQGKYYKRAEGLAL-GPGCFVKGLEFATGRTAKVIGKPNPYFFEGALA--GRDPASCVMIGDDANDDIVGAMSMGM 215
Cdd:cd07510 164 FVATNRDPWHPLSDGSFIpGTGSLVAALETASGRQAIVVGKPSRFMFDCISSkfSIDPARTCMVGDRLDTDILFGQNCGL 243


                ....*...
gi 19920940 216 QGILVKTG 223
Cdd:cd07510 244 KTLLVLTG 251
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 4-223 1.55e-27

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: 106.11  E-value: 1.55e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   4 KGALIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYV-ENE 82
Cdd:cd07531   1 KGYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFLaREK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  83 RLNPYYILSEDARQD------FPPEDTRRyKDSVVIGLAPKAFNYEQLNEAFNVLLenKNHKLIAVHQGKYYKRAEGLAL 156
Cdd:cd07531  81 PNAKVFVTGEEGLIEelrlagLEIVDKYD-EAEYVVVGSNRKITYELLTKAFRACL--RGARYIATNPDRIFPAEDGPIP 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 157 GPGCFVKGLEFATGRTAKVI-GKPNPYFFEGA--LAGRDPASCVMIGDDANDDIVGAMSMGMQGILVKTG 223
Cdd:cd07531 158 DTAAIIGAIEWCTGREPEVVvGKPSEVMAREAldILGLDAKDCAIVGDQIDVDIAMGKAIGMETALVLTG 227
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 5-223 7.03e-24

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: 96.66  E-value: 7.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   5 GALIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVENERL 84
Cdd:cd07508   1 LVISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKATARFLRSRKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  85 NP--YYILSEDARQDF----------PPEDTRRYK------------DSVVIGLApKAFNYEQLNEAFnVLLENKNHKLI 140
Cdd:cd07508  81 GKkvYVLGEEGLKEELraagfriaggPSKGIETYAelvehleddenvDAVIVGSD-FKLNFAKLRKAC-RYLRNPGCLFI 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 141 AVHQGKYYKRA-EGLALGPGCFVKGLEFATGRTAKVIGKPNPYFFEGAL--AGRDPASCVMIGDDANDDIVGAMSMGMQG 217
Cdd:cd07508 159 ATAPDRIHPLKdGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALekFGIDPERVLFVGDRLATDVLFGKACGFQT 238


                ....*.
gi 19920940 218 ILVKTG 223
Cdd:cd07508 239 LLVLTG 244
Hydrolase_like pfam13242
HAD-hyrolase-like;
175-245 1.31e-22

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 88.06  E-value: 1.31e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19920940   175 VIGKPNPYFFEGALA--GRDPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLPD--VKPSPPPTALLENFAEA 245
Cdd:pfam13242   1 VCGKPNPGMLERALArlGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPAdlEKAPIRPDYVVDDLAEA 75
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 2-225 1.28e-19

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: 85.43  E-value: 1.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   2 SIKGALIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVEN 81
Cdd:cd07532   5 NIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIADYLKE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  82 ERLNPY--------------------YILSEDARQDFPPEDTRR--YKD----SVVIGLaPKAFNYEQLNEAFNVLLeNK 135
Cdd:cd07532  85 KGFKKKvyvigeegirkeleeagivsCGGDGEDEKDDSMGDFAHnlELDpdvgAVVVGR-DEHFSYPKLMKACNYLR-NP 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 136 NHKLIAVHQGKYYKRAEGLAL-GPGCFVKGLEFATGRTAKVIGKPNPYFFEGAL--AGRDPASCVMIGDDANDDIVGAMS 212
Cdd:cd07532 163 DVLFLATNMDATFPGPVGRVIpGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMksGVIKPERTLMIGDRLKTDILFANN 242

                       250
                ....*....|...
gi 19920940 213 MGMQGILVKTGKY 225
Cdd:cd07532 243 CGFQSLLVGTGVN 255
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 7-98 4.09e-18

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 77.12  E-value: 4.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940     7 LIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVE--NERL 84
Cdd:pfam13344   2 LFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKerKFGK 81

                          90
                  ....*....|....
gi 19920940    85 NPYYILSEDARQDF 98
Cdd:pfam13344  82 KVLVIGSEGLREEL 95
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 7-244 1.45e-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: 79.40  E-value: 1.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   7 LIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVENERLNP 86
Cdd:cd16422   3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  87 --YYILSEDARQDFPP---EDTRRYKDSVVIGLaPKAFNYEQLNEAfnVLLENKNHKLIAVHQGKYYKRAEGLALGPGCF 161
Cdd:cd16422  83 kiFLLGTKSLREEFEKagfTLDGDDIDVVVLGF-DTELTYEKLRTA--CLLLRRGIPYIATHPDINCPSEEGPIPDAGSI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 162 VKGLEFATGRTAK-VIGKPNPYFFEGALAGRD--PASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLPDV--KPSPPPT 236
Cdd:cd16422 160 IALIETSTGRRPDlVIGKPNPIILDPVLEKFDysKEETVMVGDRLYTDIVLGINAGVDSILVLSGETTREDleDLERKPT 239


                ....*...
gi 19920940 237 ALLENFAE 244
Cdd:cd16422 240 YVFDNVGE 247
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 178-249 6.87e-13

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: 65.82  E-value: 6.87e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19920940 178 KPNPYFFEGALA--GRDPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLPDvkPSPPPTALLENFAEAVDWI 249
Cdd:COG1011 149 KPDPEIFELALErlGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAP--AEPRPDYVISDLAELLELL 220
PLN02645 PLN02645
phosphoglycolate phosphatase
 7-223 4.09e-12

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 64.73  E-value: 4.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940    7 LIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVENERLNP 86
Cdd:PLN02645  32 IFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYLKSINFPK 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   87 ---YYILSEDARQD------FP----PEDTRRYKD--------------SVVIGLAPKaFNYEQLNEAFNVLLENKNHKL 139
Cdd:PLN02645 112 dkkVYVIGEEGILEelelagFQylggPEDGDKKIElkpgflmehdkdvgAVVVGFDRY-INYYKIQYATLCIRENPGCLF 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  140 IAVHQGK--YYKRAEGLAlGPGCFVKGLEFATGRTAKVIGKPNPYFFEGALA--GRDPASCVMIGDDANDDIVGAMSMGM 215
Cdd:PLN02645 191 IATNRDAvtHLTDAQEWA-GAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANkfGIEKSQICMVGDRLDTDILFGQNGGC 269


                 ....*...
gi 19920940  216 QGILVKTG 223
Cdd:PLN02645 270 KTLLVLSG 277
PRK10444 PRK10444
HAD-IIA family hydrolase;
3-233 7.46e-12

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 63.27  E-value: 7.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940    3 IKGALIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKDSKATLHERLCRIGFQLDASEIYSSLSAAVSYVENE 82
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   83 RLNPYYILSEDA------RQDFPPEDTRryKDSVVIGlAPKAFNYEQLNEAFNVLLENKnhKLIAVHQGKYykraeGLAL 156
Cdd:PRK10444  81 EGKKAYVIGEGAlihelyKAGFTITDIN--PDFVIVG-ETRSYNWDMMHKAAYFVANGA--RFIATNPDTH-----GRGF 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  157 GPGC--FVKGLEFATGRTAKVIGKPNPYFFEGALAGRDPAS--CVMIGDDANDDIVGAMSMGMQGILVKTG-KYLPDVKP 231
Cdd:PRK10444 151 YPACgaLCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSeeTVIVGDNLRTDILAGFQAGLETILVLSGvSTLDDIDS 230


                 ..
gi 19920940  232 SP 233
Cdd:PRK10444 231 MP 232
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 7-240 1.13e-10

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; 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: 319827 [Multi-domain]  Cd Length: 253  Bit Score: 60.03  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   7 LIDLSGTLHVEDEPTPNAVEALKRLRDSGVLVKFVTNTTKdSKATLHERLCRIGFQLDASE-IYSS-------------L 72
Cdd:cd07525   4 LLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTNAPR-PAESVVRQLAKLGVPPSTYDaIITSgevtrellareagL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  73 SAAVSYVENERLNPYYilsEDARQDFPPEDTRRyKDSVVIGLAPKAFNY-EQLNEAFNVLLENKnHKLIAVHQGKYYKRA 151
Cdd:cd07525  83 GRKVYHLGPERDANVL---EGLDVVATDDAEKA-EFILCTGLYDDETETpEDYRKLLKAAAARG-LPLICANPDLVVPRG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 152 EGLALGPGCFVKGLEfATGRTAKVIGKPNPYFFEGALA---GRDPASCVMIGDDANDDIVGAMSMGMQGILVKTGKYLPD 228
Cdd:cd07525 158 GKLIYCAGALAELYE-ELGGEVIYFGKPHPPIYDLALArlgRPAKARILAVGDGLHTDILGANAAGLDSLFVTGGIHRRL 236

                       250
                ....*....|....*..
gi 19920940 229 -----VKPSPPPTALLE 240
Cdd:cd07525 237 aaeagIKSQIVPDFVIP 253
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-252 6.76e-09

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 53.95  E-value: 6.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   1 MSIKGALIDLSGTL--------HVED-EPTPNAVEALKRLRDSGVLVKFVTNttkdskatlherlcrigfQldaseiyss 71
Cdd:COG0241   1 MMKKAVFLDRDGTInedvgyvkSPEEfEFLPGVLEALARLNEAGYRLVVVTN------------------Q--------- 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  72 lsaavsyvenerlnpyyilSEDARQDFPPEDtrrykdsvviglapkafnYEQLNEAFNVLLENKNHKLIAVhqgkYY--- 148
Cdd:COG0241  54 -------------------SGIGRGLFTEED------------------LNAVHAKMLELLAAEGGRIDAI----YYcph 92

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 149 KRAEGLAlgpgCfvkglefatgRtakvigKPNPYFFEGALA--GRDPASCVMIGDDANdDIVGAMSMGMQGILVKTGKYL 226
Cdd:COG0241  93 HPDDNCD----C----------R------KPKPGMLLQAAErlGIDLSNSYMIGDRLS-DLQAAKAAGCKGILVLTGKGA 151

                       250       260
                ....*....|....*....|....*.
gi 19920940 227 PDVKpSPPPTALLENFAEAVDWIIQK 252
Cdd:COG0241 152 EELA-EALPDTVADDLAEAVDYLLAE 176
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
177-249 3.79e-08

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 52.24  E-value: 3.79e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19920940 177 GKPNPYFFEGALA--GRDPASCVMIGDDANdDIVGAMSMGMQGILVKTGKYLPDVKPSPPPTALLENFAEAVDWI 249
Cdd:COG0546 139 AKPKPEPLLEALErlGLDPEEVLMVGDSPH-DIEAARAAGVPFIGVTWGYGSAEELEAAGADYVIDSLAELLALL 212
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 176-218 2.62e-07

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: 47.92  E-value: 2.62e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 19920940 176 IGKPNPYFFEGAL--AGRDPASCVMIGDDANDDIVGAMSMGMQGI 218
Cdd:cd04305  62 VQKPNPEIFDYALnqLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-205 1.65e-06

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: 47.20  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940     3 IKGALIDLSGTLHvedEPTPNAVEALKRLRDSGVLVKfvtnttkdskaTLHERLCRIGFQLDAseiYSSLSAAVSYVENE 82
Cdd:pfam00702   1 IKAVVFDLDGTLT---DGEPVVTEAIAELASEHPLAK-----------AIVAAAEDLPIPVED---FTARLLLGKRDWLE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940    83 RLNPYYILSEDARQDFPPEDTRRYKDsvVIGLAPKAFNYEQLNEAFNvLLENKNHKLIAVHqGKYYKRAEGLALGPGCFV 162
Cdd:pfam00702  64 ELDILRGLVETLEAEGLTVVLVELLG--VIALADELKLYPGAAEALK-ALKERGIKVAILT-GDNPEAAEALLRLLGLDD 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 19920940   163 KgLEFATGRTAKVIGKPNPYFFEGALA--GRDPASCVMIGDDAND 205
Cdd:pfam00702 140 Y-FDVVISGDDVGVGKPKPEIYLAALErlGVKPEEVLMVGDGVND 183
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 178-234 2.08e-05

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: 43.05  E-value: 2.08e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19920940 178 KPNPYFFEGAL--AGRDPASCVMIGDDANDDIVGAMSMGMQGILV---KTGKYLPDVKPSPP 234
Cdd:cd16415  62 KPDPRIFQKALerLGVSPEEALHVGDDLKNDYLGARAVGWHALLVdreGALHELPSLANLLE 123
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
178-254 5.42e-05

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 42.50  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940  178 KPNPYFFEgALAGR---DPASCVMIGDDAnDDIVGAMSMGMQGILVKTGKYL-PDVKPSPPPTALLENFAEAVDWIIQKN 253
Cdd:PRK08942 103 KPKPGMLL-SIAERlniDLAGSPMVGDSL-RDLQAAAAAGVTPVLVRTGKGVtTLAEGAAPGTWVLDSLADLPQALKKQQ 180


                 .
gi 19920940  254 Q 254
Cdd:PRK08942 181 K 181
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 167-245 2.47e-04

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: 40.84  E-value: 2.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 167 FATGRTA-KVIGKPNPYFFEGALA--GRDPASCVMIGDDANDdivgaMSM----GMQGILVKTGKYLPDVKPSPPPTALL 239
Cdd:cd07533 127 FDATRTAdDTPSKPHPEMLREILAelGVDPSRAVMVGDTAYD-----MQMaanaGAHAVGVAWGYHSLEDLRSAGADAVV 201


                ....*.
gi 19920940 240 ENFAEA 245
Cdd:cd07533 202 DHFSEL 207
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 132-220 4.79e-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: 4.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940 132 LENKNHKLIAVhQGKYYKRAEGLA--LGPGCFVKGLeFATGRTAKVIGKPNPYFFEGALAGRDPASCVMIGDDANdDIVG 209
Cdd:cd01427  19 LRAAGIKLAIV-TNRSREALRALLekLGLGDLFDGI-IGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN-DIEA 95

                        90
                ....*....|.
gi 19920940 210 AMSMGMQGILV 220
Cdd:cd01427  96 ARAAGGRTVAV 106
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 176-250 5.25e-04

HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog.


Pssm-ID: 200106 [Multi-domain]  Cd Length: 321  Bit Score: 40.63  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920940   176 IGKPNPYFFEGA----------LAGRDPAS-----CVMIGDDANDDIVGAMSMGMQGILVKTGKY--LPDVKPSpPPTAL 238
Cdd:TIGR01456 231 LGKPTKLTYDFAedvlidwekrLSGTKPSTspfhaLYMVGDNPASDIIGAQNYGWFSCLVKTGVYngGDDLKEC-KPTLI 309

                          90
                  ....*....|..
gi 19920940   239 LENFAEAVDWII 250
Cdd:TIGR01456 310 VNDVFDAVTKIL 321
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 178-221 2.27e-03

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: 38.09  E-value: 2.27e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 19920940 178 KPNPYFFEGALA--GRDPASCVMIgDDANDDIVGAMSMGMQGILVK 221
Cdd:cd02603 141 KPDPEIYQLALErlGVKPEEVLFI-DDREENVEAARALGIHAILVT 185
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 172-220 2.28e-03

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 38.00  E-value: 2.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 19920940 172 TAKVIGKPNPYFFEGAL--AGRDPASCVMIgDDANDDIVGAMSMGMQGILV 220
Cdd:cd02604 131 YAGPDPKPHPAAFEKAIreAGLDPKRAAFF-DDSIRNLLAAKALGMKTVLV 180
PRK06769 PRK06769
HAD-IIIA family hydrolase;
190-250 3.58e-03

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 37.40  E-value: 3.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19920940  190 GRDPASCVMIGDDANDdIVGAMSMGMQGILVKTG-------KY---LPDVKPSppptALLENFAEAVDWII 250
Cdd:PRK06769 107 GLDLTQCAVIGDRWTD-IVAAAKVNATTILVRTGagydalhTYrdkWAHIEPN----YIAENFEDAVNWIL 172
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 178-220 3.65e-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: 36.61  E-value: 3.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 19920940   178 KPNPYFFEGAL---AGRDPASCVMIGDDANDDIVGAMSMGMQGILV 220
Cdd:TIGR01662  88 KPKPGMFLEALkrfNEIDPEESVYVGDQDLTDLQAAKRVGLATILV 133
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
178-251 5.67e-03

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 37.10  E-value: 5.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19920940  178 KPNP----YFFEgaLAGRDPASCVMIGDDANdDIVGAMSMGMQGILVKTGKYLPDVKPSPPPTALLENFAEAVDWIIQ 251
Cdd:PRK13222 149 KPDPapllLACE--KLGLDPEEMLFVGDSRN-DIQAARAAGCPSVGVTYGYNYGEPIALSEPDVVIDHFAELLPLLGL 223
 
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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