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Conserved domains on  [gi|520190500|dbj|BAM30179|]
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HAD superfamily hydrolase [Streptococcus pyogenes M1 476]

Protein Classification

YjjG family noncanonical pyrimidine nucleotidase( domain architecture ID 1007827)

YjjG family noncanonical pyrimidine nucleotidase similar to Streptococcus pneumoniae pyrimidine 5'-nucleotidase PynA that shows high phosphatase activity toward non-canonical pyrimidine nucleotides and three canonical nucleoside 5'-monophosphates (UMP, dUMP and dTMP)

CATH:  1.10.150.240|3.40.50.1000
EC:  3.1.3.5
Gene Ontology:  GO:0008253|GO:0046872

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YjjG/YfnB super family cl31454
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 7-227 1.90e-58

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


The actual alignment was detected with superfamily member TIGR02254:

Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 184.23  E-value: 1.90e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500    7 YNFLFFDLDHTLLDFDAAEEVALTKLLEEYQVIDIKAYKDYYKPMNQNLWKQLEGGDISKADLVNSRFALLFAHFGVTVD 86
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   87 GRQLAEGYQKHLKDQGQVYAGAKELLADLTAQgYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYD 166
Cdd:TIGR02254  81 EALLNQKYLRFLEEGHQLLPGAFELMENLQQK-FRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520190500  167 WMTQQVSNYQPDQALMIGDSLSADVQGGINAGMDTLWYNPKHLLNNSPVHPTYEVSDYQAL 227
Cdd:TIGR02254 160 YALERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEEL 220
 
Name Accession Description Interval E-value
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 7-227 1.90e-58

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 184.23  E-value: 1.90e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500    7 YNFLFFDLDHTLLDFDAAEEVALTKLLEEYQVIDIKAYKDYYKPMNQNLWKQLEGGDISKADLVNSRFALLFAHFGVTVD 86
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   87 GRQLAEGYQKHLKDQGQVYAGAKELLADLTAQgYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYD 166
Cdd:TIGR02254  81 EALLNQKYLRFLEEGHQLLPGAFELMENLQQK-FRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520190500  167 WMTQQVSNYQPDQALMIGDSLSADVQGGINAGMDTLWYNPKHLLNNSPVHPTYEVSDYQAL 227
Cdd:TIGR02254 160 YALERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEEL 220
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 10-231 6.12e-56

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: 177.91  E-value: 6.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  10 LFFDLDHTLLDFDAAEEVALTKLLEEYQVID-IKAYKDYYKPMNQNLWKQLEGGDISKADLvnsrFALLFAHFGVTvDGR 88
Cdd:COG1011    4 VLFDLDGTLLDFDPVIAEALRALAERLGLLDeAEELAEAYRAIEYALWRRYERGEITFAEL----LRRLLEELGLD-LAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  89 QLAEGYQKHLKDQGQVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYDWM 168
Cdd:COG1011   79 ELAEAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520190500 169 TQQvSNYQPDQALMIGDSLSADVQGGINAGMDTLWYNPKHLLNNSPVHPTYEVSDYQALLNCI 231
Cdd:COG1011  159 LER-LGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
PRK09449 PRK09449
dUMP phosphatase; Provisional
 7-229 5.79e-42

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 141.96  E-value: 5.79e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   7 YNFLFFDLDHTLLDFDAAEevALTKLLEEYQVIDIKAYKDYYKPMNQNLWKQLEGGDISKADLVNSRFALLFAHFGVTVD 86
Cdd:PRK09449   3 YDWILFDADETLFHFDAFA--GLQRMFSRYGVDFTAEDFQDYQAVNKPLWVDYQNGAITALQLQHTRFESWAEKLNVTPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  87 grQLAEGYQKHLKDQGQVYAGAKELLADLTAQgYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYD 166
Cdd:PRK09449  81 --ELNSAFLNAMAEICTPLPGAVELLNALRGK-VKMGIITNGFTELQQVRLERTGLRDYFDLLVISEQVGVAKPDVAIFD 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520190500 167 WMTQQVSNYQPDQALMIGDSLSADVQGGINAGMDTLWYNPKHLLNNSPVHPTYEVSDYQALLN 229
Cdd:PRK09449 158 YALEQMGNPDRSRVLMVGDNLHSDILGGINAGIDTCWLNAHGREQPEGIAPTYQVSSLSELEQ 220
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 105-205 4.48e-36

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: 123.04  E-value: 4.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500 105 YAGAKELLADLTaQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYDWMTQQVsNYQPDQALMIG 184
Cdd:cd04305   11 LPGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQL-GVKPEETLMVG 88

                         90       100
                 ....*....|....*....|.
gi 520190500 185 DSLSADVQGGINAGMDTLWYN 205
Cdd:cd04305   89 DSLESDILGAKNAGIKTVWFN 109
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
12-203 7.81e-16

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 72.62  E-value: 7.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   12 FDLDHTLLDFDAAEEVALTKLLEEYQVIDIKAyKDYYKPMNQNLWKQLEGGDISKadLVNSRFALLFAHFGvtvdgrqlA 91
Cdd:pfam13419   3 FDFDGTLLDTEELIIKSFNYLLEEFGYGELSE-EEILKFIGLPLREIFRYLGVSE--DEEEKIEFYLRKYN--------E 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   92 EGYQKHLKdqgqVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPK-KAFYDWMTQ 170
Cdd:pfam13419  72 ELHDKLVK----PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDpDPILKALEQ 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 520190500  171 QvsNYQPDQALMIGDSLSaDVQGGINAGMDTLW 203
Cdd:pfam13419 148 L--GLKPEEVIYVGDSPR-DIEAAKNAGIKVIA 177
 
Name Accession Description Interval E-value
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 7-227 1.90e-58

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 184.23  E-value: 1.90e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500    7 YNFLFFDLDHTLLDFDAAEEVALTKLLEEYQVIDIKAYKDYYKPMNQNLWKQLEGGDISKADLVNSRFALLFAHFGVTVD 86
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   87 GRQLAEGYQKHLKDQGQVYAGAKELLADLTAQgYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYD 166
Cdd:TIGR02254  81 EALLNQKYLRFLEEGHQLLPGAFELMENLQQK-FRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520190500  167 WMTQQVSNYQPDQALMIGDSLSADVQGGINAGMDTLWYNPKHLLNNSPVHPTYEVSDYQAL 227
Cdd:TIGR02254 160 YALERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEEL 220
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 10-231 6.12e-56

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: 177.91  E-value: 6.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  10 LFFDLDHTLLDFDAAEEVALTKLLEEYQVID-IKAYKDYYKPMNQNLWKQLEGGDISKADLvnsrFALLFAHFGVTvDGR 88
Cdd:COG1011    4 VLFDLDGTLLDFDPVIAEALRALAERLGLLDeAEELAEAYRAIEYALWRRYERGEITFAEL----LRRLLEELGLD-LAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  89 QLAEGYQKHLKDQGQVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYDWM 168
Cdd:COG1011   79 ELAEAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520190500 169 TQQvSNYQPDQALMIGDSLSADVQGGINAGMDTLWYNPKHLLNNSPVHPTYEVSDYQALLNCI 231
Cdd:COG1011  159 LER-LGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
PRK09449 PRK09449
dUMP phosphatase; Provisional
 7-229 5.79e-42

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 141.96  E-value: 5.79e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   7 YNFLFFDLDHTLLDFDAAEevALTKLLEEYQVIDIKAYKDYYKPMNQNLWKQLEGGDISKADLVNSRFALLFAHFGVTVD 86
Cdd:PRK09449   3 YDWILFDADETLFHFDAFA--GLQRMFSRYGVDFTAEDFQDYQAVNKPLWVDYQNGAITALQLQHTRFESWAEKLNVTPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  87 grQLAEGYQKHLKDQGQVYAGAKELLADLTAQgYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYD 166
Cdd:PRK09449  81 --ELNSAFLNAMAEICTPLPGAVELLNALRGK-VKMGIITNGFTELQQVRLERTGLRDYFDLLVISEQVGVAKPDVAIFD 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520190500 167 WMTQQVSNYQPDQALMIGDSLSADVQGGINAGMDTLWYNPKHLLNNSPVHPTYEVSDYQALLN 229
Cdd:PRK09449 158 YALEQMGNPDRSRVLMVGDNLHSDILGGINAGIDTCWLNAHGREQPEGIAPTYQVSSLSELEQ 220
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 105-205 4.48e-36

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: 123.04  E-value: 4.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500 105 YAGAKELLADLTaQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYDWMTQQVsNYQPDQALMIG 184
Cdd:cd04305   11 LPGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQL-GVKPEETLMVG 88

                         90       100
                 ....*....|....*....|.
gi 520190500 185 DSLSADVQGGINAGMDTLWYN 205
Cdd:cd04305   89 DSLESDILGAKNAGIKTVWFN 109
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
7-233 1.98e-28

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 106.55  E-value: 1.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   7 YNFLFFDLDHTLLDFDAAEEVALTKLLEEYQ--VIDIKAYKDYYKPMNQNLWKQLEGGDISKadlvnsRFALLFAHFgvt 84
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGlpPLDLEELRALIGLGLRELLRRLLGEDPDE------ELEELLARF--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  85 vdgrqlAEGYQKHLKDQGQVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAF 164
Cdd:COG0546   72 ------RELYEEELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEP 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520190500 165 YDWMTQQvSNYQPDQALMIGDSLSaDVQGGINAGMDT---LW-YNPKHLLNNSpvHPTYEVSDYQALLNCIAE 233
Cdd:COG0546  146 LLEALER-LGLDPEEVLMVGDSPH-DIEAARAAGVPFigvTWgYGSAEELEAA--GADYVIDSLAELLALLAE 214
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
10-227 3.13e-18

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 79.48  E-value: 3.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  10 LFFDLDHTLLDFDAAEEVALTKLLEEYQVidikaykdyykPMNQNLWKQLEGGdiSKADLVnsrfALLFAHFGVTVDGRQ 89
Cdd:COG0637    5 VIFDMDGTLVDSEPLHARAWREAFAELGI-----------DLTEEEYRRLMGR--SREDIL----RYLLEEYGLDLPEEE 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  90 LA----EGYQKHLKDQG-QVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAF 164
Cdd:COG0637   68 LAarkeELYRELLAEEGlPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDI 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520190500 165 YDWMTQQVsNYQPDQALMIGDSLsADVQGGINAGMDTLWYNPKHLLNNSPVHPTYEVSDYQAL 227
Cdd:COG0637  148 YLLAAERL-GVDPEECVVFEDSP-AGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 10-198 9.07e-18

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; 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/E), (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 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe 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 relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 77.44  E-value: 9.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   10 LFFDLDHTLLDFDAAEEVALTKLLEEYQvIDIKAYKDYYK--PMNQNLWKqleggdiskaDLVNSRFALLFAHFgvtvdg 87
Cdd:TIGR01549   2 ILFDIDGTLVDIKFAIRRAFPQTFEEFG-LDPASFKALKQagGLAEEEWY----------RIATSALEELQGRF------ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   88 RQLAEGYQKHlkdqgqvYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSqKPKKAFYDW 167
Cdd:TIGR01549  65 WSEYDAEEAY-------IRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGS-KPEPEIFLA 136

                         170       180       190
                  ....*....|....*....|....*....|.
gi 520190500  168 MTQQVSnyQPDQALMIGDSLSaDVQGGINAG 198
Cdd:TIGR01549 137 ALESLG--VPPEVLHVGDNLN-DIEGARNAG 164
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
12-203 7.81e-16

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 72.62  E-value: 7.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   12 FDLDHTLLDFDAAEEVALTKLLEEYQVIDIKAyKDYYKPMNQNLWKQLEGGDISKadLVNSRFALLFAHFGvtvdgrqlA 91
Cdd:pfam13419   3 FDFDGTLLDTEELIIKSFNYLLEEFGYGELSE-EEILKFIGLPLREIFRYLGVSE--DEEEKIEFYLRKYN--------E 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   92 EGYQKHLKdqgqVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPK-KAFYDWMTQ 170
Cdd:pfam13419  72 ELHDKLVK----PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDpDPILKALEQ 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 520190500  171 QvsNYQPDQALMIGDSLSaDVQGGINAGMDTLW 203
Cdd:pfam13419 148 L--GLKPEEVIYVGDSPR-DIEAAKNAGIKVIA 177
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 10-198 2.52e-15

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: 71.46  E-value: 2.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   10 LFFDLDHTLLDFDAAEEVALTKLLEEYQV--IDIKAYKDYYKPMNQNLWKQLEGGD--ISKADLVNSRFALLFAHFGVTV 85
Cdd:pfam00702   4 VVFDLDGTLTDGEPVVTEAIAELASEHPLakAIVAAAEDLPIPVEDFTARLLLGKRdwLEELDILRGLVETLEAEGLTVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   86 DGRQLAEgyqKHLKDQGQVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFY 165
Cdd:pfam00702  84 LVELLGV---IALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 520190500  166 DWMTQQVsNYQPDQALMIGDSLsADVQGGINAG 198
Cdd:pfam00702 161 LAALERL-GVKPEEVLMVGDGV-NDIPAAKAAG 191
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 108-204 2.49e-14

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: 66.65  E-value: 2.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500 108 AKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYDWMTQQVsNYQPDQALMIGDSL 187
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKL-GVDPEEVLFVGDSE 90

                         90
                 ....*....|....*..
gi 520190500 188 SaDVQGGINAGMDTLWY 204
Cdd:cd01427   91 N-DIEAARAAGGRTVAV 106
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 108-207 1.24e-12

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: 62.69  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500 108 AKELLADLTAQGYNLYAATNgIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYDWMTQQVSNyQPDQALMIGDSL 187
Cdd:cd16415   12 AVETLKDLKEKGLKLAVVSN-FDRRLRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGV-SPEEALHVGDDL 89

                         90       100
                 ....*....|....*....|
gi 520190500 188 SADVQGGINAGMDTLWYNPK 207
Cdd:cd16415   90 KNDYLGARAVGWHALLVDRE 109
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 10-204 4.25e-12

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: 62.44  E-value: 4.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   10 LFFDLDHTLLDFDAAEEVALTKllEEYQVIDIKAYKDYYKPM--NQNLWKQLEGGDISKADlvnsrFALLFAHFGVTvdg 87
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAKLINR--EELGLVPDELGVSAVGRLelALRRFKAQYGRTISPED-----AQLLYKQLFYE--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   88 rqlaegyQKHLKDQGQVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQAsGLAPYFKAIFISEQSGSQKPKKAFYDW 167
Cdd:TIGR01509  72 -------QIEEEAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKLVLALL-GLRDLFDVVIDSSDVGLGKPDPDIYLQ 143

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 520190500  168 MtQQVSNYQPDQALMIGDSLsADVQGGINAGMDTLWY 204
Cdd:TIGR01509 144 A-LKALGLEPSECVFVDDSP-AGIEAAKAAGMHTVGV 178
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
94-233 1.87e-11

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 61.36  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  94 YQKHLKDQGQVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIfISEQSGSQKPKKAFYDWMTQQVS 173
Cdd:PRK13222  84 YAENVAGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVV-IGGDSLPNKKPDPAPLLLACEKL 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520190500 174 NYQPDQALMIGDSLSaDVQGGINAGMDTLW----YNPKHLLNNSpvHPTYEVSDYQALLNCIAE 233
Cdd:PRK13222 163 GLDPEEMLFVGDSRN-DIQAARAAGCPSVGvtygYNYGEPIALS--EPDVVIDHFAELLPLLGL 223
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
159-228 5.77e-11

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 60.51  E-value: 5.77e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520190500 159 KPKKAFYDwMTQQVSNYQPDQALMIGDSLSADVQGGINAGMDTLW-----YNPKHLLnNSPVHPTYEVSDYQALL 228
Cdd:COG0647  186 KPSPPIYE-LALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLvltgvTTAEDLE-AAPIRPDYVLDSLAELL 258
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 94-201 1.46e-10

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: 58.79  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  94 YQKHLKDQGQVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFiseqSGSQKPKK-----AFYDWM 168
Cdd:cd16417   78 YAETLSVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVL----GGDSLPEKkpdpaPLLHAC 153

                         90       100       110
                 ....*....|....*....|....*....|...
gi 520190500 169 tqQVSNYQPDQALMIGDSLSaDVQGGINAGMDT 201
Cdd:cd16417  154 --EKLGIAPAQMLMVGDSRN-DILAARAAGCPS 183
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 12-223 1.96e-10

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: 58.43  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  12 FDLDHTLLDF----DAAEEVALTKLLEEYQVIDIKAYKDYYKPMNQNLWKQLEggDISKADLvnsRFALlfAHFGVTVD- 86
Cdd:cd02588    5 FDVYGTLIDWhsglAAAERAFPGRGEELSRLWRQKQLEYTWLVTLMGPYVDFD--ELTRDAL---RATA--AELGLELDe 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  87 --GRQLAEGYqKHLKdqgqVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAF 164
Cdd:cd02588   78 sdLDELGDAY-LRLP----PFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAV 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520190500 165 YDwMTQQVSNYQPDQALMIgdSLSA-DVQGGINAGMDTLWYN-PKHLLNNSPVHPTYEVSD 223
Cdd:cd02588  153 YE-LAAERLGVPPDEILHV--ASHAwDLAGARALGLRTAWINrPGEVPDPLGPAPDFVVPD 210
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 94-202 5.20e-09

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: 54.52  E-value: 5.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  94 YQKHLKDQG----QVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSqKPKKAfyDWMT 169
Cdd:cd04302   68 YREYYKEKGlfenEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGS-RVHKA--DVIR 144

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 520190500 170 QQVSNYQ--PDQALMIGDSlSADVQGGINAGMDTL 202
Cdd:cd04302  145 YALDTLGiaPEQAVMIGDR-KHDIIGARANGIDSI 178
Hydrolase_like pfam13242
HAD-hyrolase-like;
159-223 1.24e-08

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 50.31  E-value: 1.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520190500  159 KPKKAFYDwMTQQVSNYQPDQALMIGDSLSADVQGGINAGMDTLWY----NPKHLLNNSPVHPTYEVSD 223
Cdd:pfam13242   4 KPNPGMLE-RALARLGLDPERTVMIGDRLDTDILGAREAGARTILVltgvTRPADLEKAPIRPDYVVDD 71
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 7-229 1.54e-08

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. 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: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 53.05  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   7 YNFLFFDLDHTLLD-----FDAAEEVALTKLLEEYQVIDIKAYkdYYKPMNQNLWKQLEGGDISKADLVNSRfallfahf 81
Cdd:cd02616    1 ITTILFDLDGTLIDtneliIKSFNHTLKEYGLEGYTREEVLPF--IGPPLRETFEKIDPDKLEDMVEEFRKY-------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  82 gvtvdgrqlaegYQKHLKDQGQVYAGAKELLADLTAQGYNLYAATNGIA-TIQQGrLQASGLAPYFKAIFISEQSGSQKP 160
Cdd:cd02616   71 ------------YREHNDDLTKEYPGVYETLARLKSQGIKLGVVTTKLReTALKG-LKLLGLDKYFDVIVGGDDVTHHKP 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520190500 161 K-----KAFydwmtqQVSNYQPDQALMIGDSlSADVQGGINAGMDT---LW-YNPKHLLNNSpvHPTYEVSDYQALLN 229
Cdd:cd02616  138 DpepvlKAL------ELLGAEPEEALMVGDS-PHDILAGKNAGVKTvgvTWgYKGREYLKAF--NPDFIIDKMSDLLT 206
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 100-206 1.71e-08

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: 51.64  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  100 DQGQVYAGAKELLADLTAQGYNLYAATN--GIA-----TIQQGRLQAS--GLAPYFKAIFISEqsGSQKPKKAFYDWMTQ 170
Cdd:TIGR01662  22 DERILYPEVPDALAELKEAGYKVVIVTNqsGIGrgyfsRSFSGRVARRleELGVPIDILYACP--GCRKPKPGMFLEALK 99

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 520190500  171 QVSNYQPDQALMIGDSLSADVQGGINAGMDTLWYNP 206
Cdd:TIGR01662 100 RFNEIDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 8-201 2.75e-08

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: 51.96  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500   8 NFLFFDLDHTLLDFDAAEEVA-LTKLLeeyqVIDIKAYKDYYKPmnQNLWKQLEGGDISKADlvnsrFALLFAHfgvtVD 86
Cdd:cd02603    2 RAVLFDFGGVLIDPDPAAAVArFEALT----GEPSEFVLDTEGL--AGAFLELERGRITEEE-----FWEELRE----EL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  87 GRQLAEGYQKHLKDQGQVYAGAK-ELLADLTAQGYNLYAATN---GIATIQQGRLQASGLapYFKAIFISEQSGSQKPKK 162
Cdd:cd02603   67 GRPLSAELFEELVLAAVDPNPEMlDLLEALRAKGYKVYLLSNtwpDHFKFQLELLPRRGD--LFDGVVESCRLGVRKPDP 144

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 520190500 163 AFYDWMTQQvSNYQPDQALMIgDSLSADVQGGINAGMDT 201
Cdd:cd02603  145 EIYQLALER-LGVKPEEVLFI-DDREENVEAARALGIHA 181
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 11-201 7.29e-08

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. 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: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 50.45  E-value: 7.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  11 FFDLDHTLLDFDAAEEVALTKLLEEYqVIDIKAYKDYYkpmnqnlwkqleggdISKADLVNSrfalLFAHFGVTVDGRQL 90
Cdd:cd07523    3 IWDLDGTLLDSYPAMTKALSETLADF-GIPQDLETVYK---------------IIKESSVQF----AIQYYAEVPDLEEE 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  91 AEGYQKHLKDQGQVYAGAKELLADLTAQGYNLYAAT---NGIATIqqgrLQASGLAPYFKAIFISEQSGSQKPKKAFYDW 167
Cdd:cd07523   63 YKELEAEYLAKPILFPGAKAVLRWIKEQGGKNFLMThrdHSALTI----LKKDGIASYFTEIVTSDNGFPRKPNPEAINY 138

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 520190500 168 MTQQvsnYQ--PDQALMIGDSlSADVQGGINAGMDT 201
Cdd:cd07523  139 LLNK---YQlnPEETVMIGDR-ELDIEAGHNAGIST 170
HAD-like cd07515
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 103-198 9.93e-08

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: 319817 [Multi-domain]  Cd Length: 131  Bit Score: 49.34  E-value: 9.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500 103 QVYAGAKELLADLTAqGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISeqsgSQKPKKAFYDWMtqqvSNYQ--PDQA 180
Cdd:cd07515   17 ELLPGVREALAALKA-DYRLVLITKGDLLDQEQKLARSGLSDYFDAVEVV----SEKDPDTYRRVL----SRYGigPERF 87

                         90
                 ....*....|....*...
gi 520190500 181 LMIGDSLSADVQGGINAG 198
Cdd:cd07515   88 VMVGNSLRSDILPVLAAG 105
PRK10748 PRK10748
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;
110-207 4.86e-07

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


Pssm-ID: 182696 [Multi-domain]  Cd Length: 238  Bit Score: 48.96  E-value: 4.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500 110 ELLADLtAQGYNLYAATNGIAtiqqgRLQASGLAPYFKAIFISEQSGSQKPKKAFYDWMTQQVsNYQPDQALMIGDSLSA 189
Cdd:PRK10748 120 DTLKQL-AKKWPLVAITNGNA-----QPELFGLGDYFEFVLRAGPHGRSKPFSDMYHLAAEKL-NVPIGEILHVGDDLTT 192

                         90
                 ....*....|....*...
gi 520190500 190 DVQGGINAGMDTLWYNPK 207
Cdd:PRK10748 193 DVAGAIRCGMQACWINPE 210
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 10-128 5.75e-07

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 48.68  E-value: 5.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  10 LFFDLDHTLLDFDAAEEVAltKLLEEYQVIDIKAYKDyykpMNQNLWKQLEGGDISKADLVNSRFALLfAhfGVTVDgrQ 89
Cdd:COG0560    6 AVFDLDGTLIAGESIDELA--RFLGRRGLVDRREVLE----EVAAITERAMAGELDFEESLRFRVALL-A--GLPEE--E 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 520190500  90 LAEGYQKHLKDQGQVYAGAKELLADLTAQGYNLYAATNG 128
Cdd:COG0560   75 LEELAERLFEEVPRLYPGARELIAEHRAAGHKVAIVSGG 113
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 105-208 2.75e-06

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: 46.24  E-value: 2.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500 105 YAGAKELLADLTAQGYNLYAATN--GIAT----------IQQgRLQASgLAP---YFKAIFI-----SEQSGSQKPK--- 161
Cdd:COG0241   30 LPGVLEALARLNEAGYRLVVVTNqsGIGRglfteedlnaVHA-KMLEL-LAAeggRIDAIYYcphhpDDNCDCRKPKpgm 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 520190500 162 --KAFYDWmtqqvsNYQPDQALMIGDSLSaDVQGGINAGMDTLWYNPKH 208
Cdd:COG0241  108 llQAAERL------GIDLSNSYMIGDRLS-DLQAAKAAGCKGILVLTGK 149
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 83-199 1.25e-05

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: 44.70  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  83 VTVDGRQLAEGYQKH------LKDQG-QVYAGAKELLADLTAQGYNLYAATNgiatiqQGR------LQASGLAPYFKAI 149
Cdd:cd07533   57 ATPALVAVAERYKEAfdilrlLPEHAePLFPGVREALDALAAQGVLLAVATG------KSRrgldrvLEQHGLGGYFDAT 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 520190500 150 FISEQSGSqKPkkafYDWMTQQVSNY---QPDQALMIGDSlSADVQGGINAGM 199
Cdd:cd07533  131 RTADDTPS-KP----HPEMLREILAElgvDPSRAVMVGDT-AYDMQMAANAGA 177
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 105-201 1.26e-05

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 44.64  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500 105 YAGAKELLADLTAQGYNLYAATNGI-ATIQQGrLQASGLAPYFKAIFISEQSGSQKP-----KKAFydwmtqQVSNYQPD 178
Cdd:PRK13288  84 YETVYETLKTLKKQGYKLGIVTTKMrDTVEMG-LKLTGLDEFFDVVITLDDVEHAKPdpepvLKAL------ELLGAKPE 156

                         90       100
                 ....*....|....*....|...
gi 520190500 179 QALMIGDSlSADVQGGINAGMDT 201
Cdd:PRK13288 157 EALMVGDN-HHDILAGKNAGTKT 178
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 12-199 2.54e-05

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 43.84  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  12 FDLDHTLLDFDAAEEVALTKLLEEyqvidikaykDYYKPMNQNLWKQLEGGDiskadlVNSRFALLFAHFGVTVDGRQLA 91
Cdd:cd07512    4 FDLDGTLIDSAPDLHAALNAVLAA----------EGLAPLSLAEVRSFVGHG------APALIRRAFAAAGEDLDGPLHD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  92 EGYQKHLK-------DQGQVYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAF 164
Cdd:cd07512   68 ALLARFLDhyeadppGLTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAP 147

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 520190500 165 YDwMTQQVSNYQPDQALMIGDSLSaDVQGGINAGM 199
Cdd:cd07512  148 LR-AAIRRLGGDVSRALMVGDSET-DAATARAAGV 180
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 178-223 2.90e-05

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: 43.73  E-value: 2.90e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 520190500 178 DQALMIGDSLSADVQGGINAGMDTLWY-----NPKHLLnNSPVHPTYEVSD 223
Cdd:cd07530  195 EETLMVGDRLDTDIAAGIAAGIDTLLVltgvtTREDLA-KPPYRPTYIVPS 244
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 11-217 6.35e-05

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 42.76  E-value: 6.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  11 FFDLDHTLLDfdaaeevaltklleeYQVIDIKAYKDYYKPMNQNL-----WKQLEG---GDIskADLVNSRfallfahFG 82
Cdd:PRK10563   8 FFDCDGTLVD---------------SEVICSRAYVTMFAEFGITLsleevFKRFKGvklYEI--IDIISKE-------HG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  83 VTVDGRQLAEGYQKHLK----DQGQVYAGAKELLADLTAQgynLYAATNGIATIQQGRLQASGLAPYFkaifiseqsgsq 158
Cdd:PRK10563  64 VTLAKAELEPVYRAEVArlfdSELEPIAGANALLESITVP---MCVVSNGPVSKMQHSLGKTGMLHYF------------ 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500 159 kPKKAF--YDwmtqqVSNYQPDQALM----------------IGDSlSADVQGGINAGMDTLWY--NPkhllNNSPV-HP 217
Cdd:PRK10563 129 -PDKLFsgYD-----IQRWKPDPALMfhaaeamnvnvencilVDDS-SAGAQSGIAAGMEVFYFcaDP----HNKPIdHP 197
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
 136-203 1.56e-04

HAD-superfamily class IIA hydrolase, TIGR01459; 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 gram negative and primarily alpha proteobacteria. Only one sequence hase been annotated as other than "hypothetical." That one, from Brucella, is annotated as related to NagD, but only by sequence similarity and should be treated with some skepticism. (See comments for Class IIA subfamily model)


Pssm-ID: 130526 [Multi-domain]  Cd Length: 242  Bit Score: 41.80  E-value: 1.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520190500  136 RLQASGLAPYFKAIFISE---QSGSQ-----KPKKAFYDWMTQQVSNYQPDQALMIGDSLSADVQGGINAGMDTLW 203
Cdd:TIGR01459 164 RGINQHGIYRYGAGYYAElikQLGGKviysgKPYPAIFHKALKECSNIPKNRMLMVGDSFYTDILGANRLGIDTAL 239
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 133-203 3.55e-04

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: 40.39  E-value: 3.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520190500  133 QQGRLQAsGLAPYFKAIfiSEQSGSQ-----KPKKAFYDWMTQQVSNYQPDQALMIGDSLSADVQGGINAGMDTLW 203
Cdd:TIGR01460 160 GDGRFRP-GAGAIAAGI--KELSGREptvvgKPSPAIYRAALNLLQARPERRDVMVGDNLRTDILGAKNAGFDTLL 232
COG5610 COG5610
Predicted sugar hydrolase, contains GT1 and HAD domains [General function prediction only];
146-210 4.53e-04

Predicted sugar hydrolase, contains GT1 and HAD domains [General function prediction only];


Pssm-ID: 444341 [Multi-domain]  Cd Length: 501  Bit Score: 40.95  E-value: 4.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520190500 146 FKAIFISEQSGSQKPKKAFYDWMTQQVSNyQPDQALMIGDSLSADVQGGINAGMDTLWYNPKHLL 210
Cdd:COG5610  160 FDPLYVSSDYGLSKASGELFDYVLEEEGV-DPKQILHIGDNPRSDVQRPRKLGIQALHYPRASLS 223
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 80-201 5.26e-04

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It 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: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 39.14  E-value: 5.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500  80 HFGVTVDGRQLAEGYQK-HLKDQGQVYAGAKELLADLTAQGYNLYAATN-GIATIQQGRLQASGLAPYFKAIFISEQSGS 157
Cdd:cd07505   17 HRQAWQLLERKNALLLElIASEGLKLKPGVVELLDALKAAGIPVAVATSsSRRNVELLLLELGLLRGYFDVIVSGDDVER 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 520190500 158 QKPKKAFYdWMTQQVSNYQPDQALMIGDSLSAdVQGGINAGMDT 201
Cdd:cd07505   97 GKPAPDIY-LLAAERLGVDPERCLVFEDSLAG-IEAAKAAGMTV 138
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 159-202 6.61e-04

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: 40.00  E-value: 6.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 520190500 159 KPKKAFYDWMTQQVSNYQPDQALMIGDSLSADVQGGINAGMDTL 202
Cdd:cd07525  183 KPHPPIYDLALARLGRPAKARILAVGDGLHTDILGANAAGLDSL 226
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 155-201 3.44e-03

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 36.09  E-value: 3.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 520190500 155 SGSQKPKKAFYDWmTQQVSNYQPDQALMIGDSLSADVQGGINAGMDT 201
Cdd:cd16416   60 ARAGKPRPRAFRR-ALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYT 105
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 159-199 5.07e-03

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: 37.26  E-value: 5.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 520190500 159 KPKKAFYDWMTQQVsNYQPDQALMIGDSLSADVQGGINAGM 199
Cdd:cd07509  172 KPSPEFFLSALRSL-GVDPEEAVMIGDDLRDDVGGAQACGM 211
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 176-203 6.09e-03

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: 36.90  E-value: 6.09e-03
                         10        20
                 ....*....|....*....|....*...
gi 520190500 176 QPDQALMIGDSLSADVQGGINAGMDTLW 203
Cdd:cd07532  222 KPERTLMIGDRLKTDILFANNCGFQSLL 249
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 104-228 6.34e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 36.77  E-value: 6.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520190500 104 VYAGAKELLADLTAQGYNLYAATNGIATIQQGRLQASGLAPYFKAIFISEQSGSQKPKKAFYdWMTQQVSNYQPDQALMI 183
Cdd:PRK13223 102 VYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAAL-LFVMKMAGVPPSQSLFV 180

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 520190500 184 GDSLSaDVQGGINAGMD--TLWYNPKHLLNNSPVHPTYEVSDYQALL 228
Cdd:PRK13223 181 GDSRS-DVLAAKAAGVQcvALSYGYNHGRPIAEESPALVIDDLRALL 226
 
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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