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Conserved domains on  [gi|1002545195|gb|KXU16278|]
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2-haloalkanoic acid dehalogenase [Streptococcus oralis]

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

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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 ...
 3-227 2.61e-60

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: 188.85  E-value: 2.61e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   3 YKFLLFDLDHTLLDFDAAEDVALTQLLKEEGVADIQAYKDYYVPMNKTLWKDLEQKKISKQELVNTRFSRLFAYFGQGKD 82
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  83 GRLLAQRYQFYLAQQGQTLSGAHEFLDSLiERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFYE 162
Cdd:TIGR02254  81 EALLNQKYLRFLEEGHQLLPGAFELMENL-QQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002545195 163 KIGQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIWYNPHHLENHTQAQPTYEVHSYQDLLDCL 227
Cdd:TIGR02254 160 YALERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEELYEIL 224
 
Name Accession Description Interval E-value
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 3-227 2.61e-60

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: 188.85  E-value: 2.61e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   3 YKFLLFDLDHTLLDFDAAEDVALTQLLKEEGVADIQAYKDYYVPMNKTLWKDLEQKKISKQELVNTRFSRLFAYFGQGKD 82
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  83 GRLLAQRYQFYLAQQGQTLSGAHEFLDSLiERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFYE 162
Cdd:TIGR02254  81 EALLNQKYLRFLEEGHQLLPGAFELMENL-QQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002545195 163 KIGQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIWYNPHHLENHTQAQPTYEVHSYQDLLDCL 227
Cdd:TIGR02254 160 YALERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEELYEIL 224
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 3-227 4.86e-47

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: 154.80  E-value: 4.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   3 YKFLLFDLDHTLLDFDAAEDVALTQLLKEEGVAD-IQAYKDYYVPMNKTLWKDLEQKKISKQELvntrFSRLFAYFGQgK 81
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDeAEELAEAYRAIEYALWRRYERGEITFAEL----LRRLLEELGL-D 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  82 DGRLLAQRYQFYLAQQGQTLSGAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFY 161
Cdd:COG1011    76 LAEELAEAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIF 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002545195 162 EKIgQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIWYNPHHLENHTQAQPTYEVHSYQDLLDCL 227
Cdd:COG1011   156 ELA-LERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
PRK09449 PRK09449
dUMP phosphatase; Provisional
 1-227 2.34e-44

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 148.13  E-value: 2.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   1 MPYKFLLFDLDHTLLDFDAAEdvALTQLLKEEGVADIQAYKDYYVPMNKTLWKDLEQKKISKQELVNTRFS----RLfay 76
Cdd:PRK09449    1 MKYDWILFDADETLFHFDAFA--GLQRMFSRYGVDFTAEDFQDYQAVNKPLWVDYQNGAITALQLQHTRFEswaeKL--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  77 fgqGKDGRLLAQRYQFYLAQQGQTLSGAHEFLDSLIERdYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKP 156
Cdd:PRK09449   76 ---NVTPGELNSAFLNAMAEICTPLPGAVELLNALRGK-VKMGIITNGFTELQQVRLERTGLRDYFDLLVISEQVGVAKP 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002545195 157 DALFYEKIGQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIWYNPHHLENHTQAQPTYEVHSYQDLLDCL 227
Cdd:PRK09449  152 DVAIFDYALEQMGNPDRSRVLMVGDNLHSDILGGINAGIDTCWLNAHGREQPEGIAPTYQVSSLSELEQLL 222
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 101-201 4.85e-30

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: 107.63  E-value: 4.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195 101 LSGAHEFLDSLIERdYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFYEKIGQQIaGFSKEKTLMIG 180
Cdd:cd04305    11 LPGAKELLEELKKG-YKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQL-GVKPEETLMVG 88

                          90       100
                  ....*....|....*....|.
gi 1002545195 181 DSLTADIQGGNNADIDTIWYN 201
Cdd:cd04305    89 DSLESDILGAKNAGIKTVWFN 109
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 6-194 1.16e-14

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: 69.54  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   6 LLFDLDHTLLDFDAAEDVALTQLL--KEEGVADIQAYKDYYVPMnKTLWKDLEQKKISKQELVNTRFSRLFAYFGQGKDG 83
Cdd:pfam00702   4 VVFDLDGTLTDGEPVVTEAIAELAseHPLAKAIVAAAEDLPIPV-EDFTARLLLGKRDWLEELDILRGLVETLEAEGLTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  84 RLLAQRYQFYLAQQGQTLSGAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFYEK 163
Cdd:pfam00702  83 VLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYLA 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1002545195 164 IGQQIaGFSKEKTLMIGDSLtADIQGGNNAD 194
Cdd:pfam00702 163 ALERL-GVKPEEVLMVGDGV-NDIPAAKAAG 191
 
Name Accession Description Interval E-value
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 3-227 2.61e-60

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: 188.85  E-value: 2.61e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   3 YKFLLFDLDHTLLDFDAAEDVALTQLLKEEGVADIQAYKDYYVPMNKTLWKDLEQKKISKQELVNTRFSRLFAYFGQGKD 82
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  83 GRLLAQRYQFYLAQQGQTLSGAHEFLDSLiERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFYE 162
Cdd:TIGR02254  81 EALLNQKYLRFLEEGHQLLPGAFELMENL-QQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002545195 163 KIGQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIWYNPHHLENHTQAQPTYEVHSYQDLLDCL 227
Cdd:TIGR02254 160 YALERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEELYEIL 224
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 3-227 4.86e-47

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: 154.80  E-value: 4.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   3 YKFLLFDLDHTLLDFDAAEDVALTQLLKEEGVAD-IQAYKDYYVPMNKTLWKDLEQKKISKQELvntrFSRLFAYFGQgK 81
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDeAEELAEAYRAIEYALWRRYERGEITFAEL----LRRLLEELGL-D 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  82 DGRLLAQRYQFYLAQQGQTLSGAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFY 161
Cdd:COG1011    76 LAEELAEAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIF 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002545195 162 EKIgQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIWYNPHHLENHTQAQPTYEVHSYQDLLDCL 227
Cdd:COG1011   156 ELA-LERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
PRK09449 PRK09449
dUMP phosphatase; Provisional
 1-227 2.34e-44

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 148.13  E-value: 2.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   1 MPYKFLLFDLDHTLLDFDAAEdvALTQLLKEEGVADIQAYKDYYVPMNKTLWKDLEQKKISKQELVNTRFS----RLfay 76
Cdd:PRK09449    1 MKYDWILFDADETLFHFDAFA--GLQRMFSRYGVDFTAEDFQDYQAVNKPLWVDYQNGAITALQLQHTRFEswaeKL--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  77 fgqGKDGRLLAQRYQFYLAQQGQTLSGAHEFLDSLIERdYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKP 156
Cdd:PRK09449   76 ---NVTPGELNSAFLNAMAEICTPLPGAVELLNALRGK-VKMGIITNGFTELQQVRLERTGLRDYFDLLVISEQVGVAKP 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002545195 157 DALFYEKIGQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIWYNPHHLENHTQAQPTYEVHSYQDLLDCL 227
Cdd:PRK09449  152 DVAIFDYALEQMGNPDRSRVLMVGDNLHSDILGGINAGIDTCWLNAHGREQPEGIAPTYQVSSLSELEQLL 222
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 101-201 4.85e-30

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: 107.63  E-value: 4.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195 101 LSGAHEFLDSLIERdYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFYEKIGQQIaGFSKEKTLMIG 180
Cdd:cd04305    11 LPGAKELLEELKKG-YKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQL-GVKPEETLMVG 88

                          90       100
                  ....*....|....*....|.
gi 1002545195 181 DSLTADIQGGNNADIDTIWYN 201
Cdd:cd04305    89 DSLESDILGAKNAGIKTVWFN 109
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-229 5.48e-26

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 100.39  E-value: 5.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   3 YKFLLFDLDHTLLDFDAAEDVALTQLLKEEG--VADIQAYKDYYVPMNKTLWKDLEQkkiskqELVNTRFSRLFAYFgqg 80
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGlpPLDLEELRALIGLGLRELLRRLLG------EDPDEELEELLARF--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  81 kdgrllAQRYQFYLAQQGQTLSGAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALF 160
Cdd:COG0546    72 ------RELYEEELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEP 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002545195 161 YEKIgQQIAGFSKEKTLMIGDSlTADIQGGNNADIDTIW--YNPHHLENHTQAQPTYEVHSYQDLLDCLDK 229
Cdd:COG0546   146 LLEA-LERLGLDPEEVLMVGDS-PHDIEAARAAGVPFIGvtWGYGSAEELEAAGADYVIDSLAELLALLAE 214
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
2-223 4.99e-16

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 73.70  E-value: 4.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   2 PYKFLLFDLDHTLLDFDAAEDVALTQLLKEEGVADIQAYKDYYVPMN-KTLWKDLEQK---KISKQELVNtRFSRLFayf 77
Cdd:COG0637     1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSrEDILRYLLEEyglDLPEEELAA-RKEELY--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  78 gqgkdgrllaqrYQFYLAQQGQTLSGAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPD 157
Cdd:COG0637    77 ------------RELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPD 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002545195 158 -ALFYEkiGQQIAGFSKEKTLMIGDSLtADIQGGNNADIDTIWYNPHHLENHTQAQPTYEVHSYQDL 223
Cdd:COG0637   145 pDIYLL--AAERLGVDPEECVVFEDSP-AGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 6-194 1.16e-14

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: 69.54  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   6 LLFDLDHTLLDFDAAEDVALTQLL--KEEGVADIQAYKDYYVPMnKTLWKDLEQKKISKQELVNTRFSRLFAYFGQGKDG 83
Cdd:pfam00702   4 VVFDLDGTLTDGEPVVTEAIAELAseHPLAKAIVAAAEDLPIPV-EDFTARLLLGKRDWLEELDILRGLVETLEAEGLTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  84 RLLAQRYQFYLAQQGQTLSGAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFYEK 163
Cdd:pfam00702  83 VLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYLA 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1002545195 164 IGQQIaGFSKEKTLMIGDSLtADIQGGNNAD 194
Cdd:pfam00702 163 ALERL-GVKPEEVLMVGDGV-NDIPAAKAAG 191
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-199 4.77e-14

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 67.61  E-value: 4.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   6 LLFDLDHTLLDFDAAEDVALTQLLKEEGVaDIQAYKDYYVPMNKTLWKDLEQKKISKQELVNTRFsrlfayfgqgkdgrl 85
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGY-GELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEF--------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  86 LAQRYQFYLAQQGQTL-SGAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFYEKI 164
Cdd:pfam13419  65 YLRKYNEELHDKLVKPyPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKA 144

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1002545195 165 GQQIaGFSKEKTLMIGDSLTaDIQGGNNADIDTIW 199
Cdd:pfam13419 145 LEQL-GLKPEEVIYVGDSPR-DIEAAKNAGIKVIA 177
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 6-193 5.28e-14

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: 67.42  E-value: 5.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   6 LLFDLDHTLLDFDAAEDVALTQLLKEEGVaDIQAYKDYyvpmnktlwkdLEQKKISKQELVNTRFSRLfayfgqgkdGRL 85
Cdd:TIGR01549   2 ILFDIDGTLVDIKFAIRRAFPQTFEEFGL-DPASFKAL-----------KQAGGLAEEEWYRIATSAL---------EEL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  86 LAQRYQFYLAQQgQTLSGAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLqTQKPDALFYEKIG 165
Cdd:TIGR01549  61 QGRFWSEYDAEE-AYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEP-GSKPEPEIFLAAL 138

                         170       180
                  ....*....|....*....|....*...
gi 1002545195 166 QQIAGFskEKTLMIGDSLtADIQGGNNA 193
Cdd:TIGR01549 139 ESLGVP--PEVLHVGDNL-NDIEGARNA 163
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 104-200 1.55e-13

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: 64.34  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195 104 AHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFYEKIgQQIAGFSKEKTLMIGDSL 183
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLL-LLKLGVDPEEVLFVGDSE 90

                          90
                  ....*....|....*..
gi 1002545195 184 TaDIQGGNNADIDTIWY 200
Cdd:cd01427    91 N-DIEAARAAGGRTVAV 106
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
155-224 8.56e-13

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 65.52  E-value: 8.56e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002545195 155 KPDALFYEKIgQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIW-----YNPHHLENHTQaQPTYEVHSYQDLL 224
Cdd:COG0647   186 KPSPPIYELA-LERLGVDPERVLMVGDRLDTDILGANAAGLDTLLvltgvTTAEDLEAAPI-RPDYVLDSLAELL 258
Hydrolase_like pfam13242
HAD-hyrolase-like;
155-223 1.12e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 56.08  E-value: 1.12e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002545195 155 KPDALFYEKIGQQIaGFSKEKTLMIGDSLTADIQGGNNADIDTIW-----YNPHHLEnHTQAQPTYEVHSYQDL 223
Cdd:pfam13242   4 KPNPGMLERALARL-GLDPERTVMIGDRLDTDILGAREAGARTILvltgvTRPADLE-KAPIRPDYVVDDLAEA 75
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-229 1.60e-09

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 55.97  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   1 MPYKFLLFDLDHTLLD----FDAAEDVALTQL-LKEEGVADIQAYKDYYVPMnktlwkdleqkkiskqeLVntrfSRLFA 75
Cdd:PRK13222    4 MDIRAVAFDLDGTLVDsapdLAAAVNAALAALgLPPAGEERVRTWVGNGADV-----------------LV----ERALT 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  76 YFGQGKDGRLLAQRYQFYLAQQGQTLS-------GAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFIS 148
Cdd:PRK13222   63 WAGREPDEELLEKLRELFDRHYAENVAggsrlypGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195 149 EQLQTQKPDAL-FYEKIGQqiAGFSKEKTLMIGDSLTaDIQGGNNADIDTIW----YNphHLENHTQAQPTYEVHSYQDL 223
Cdd:PRK13222  143 DSLPNKKPDPApLLLACEK--LGLDPEEMLFVGDSRN-DIQAARAAGCPSVGvtygYN--YGEPIALSEPDVVIDHFAEL 217


                  ....*.
gi 1002545195 224 LDCLDK 229
Cdd:PRK13222  218 LPLLGL 223
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 6-200 2.54e-09

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: 54.73  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   6 LLFDLDHTLLDFDAAEDVALTQLLKEegvadiqaykdyYVPmnktlwKDLEQKKISKQELVNTRFSRLFAYFGQGKDGRL 85
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAKLINREELG------------LVP------DELGVSAVGRLELALRRFKAQYGRTISPEDAQL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  86 L-AQRYQFYLAQQGQT--LSGAHEFLDSLIERDYDLYAATNGITAIQTgRLAQSDLAAYFNQVFISEQLQTQKPDALFYE 162
Cdd:TIGR01509  64 LyKQLFYEQIEEEAKLkpLPGVRALLEALRARGKKLALLTNSPRAHKL-VLALLGLRDLFDVVIDSSDVGLGKPDPDIYL 142

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1002545195 163 KiGQQIAGFSKEKTLMIGDSLtADIQGGNNADIDTIWY 200
Cdd:TIGR01509 143 Q-ALKALGLEPSECVFVDDSP-AGIEAAKAAGMHTVGV 178
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 5-224 3.11e-07

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: 49.16  E-value: 3.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   5 FLLFDLDHTLLDfdAAED--VALTQLLKEegvadiqaykdyyvpMNKTLWkDLEQ---------KKISKQELVNTRfsrl 73
Cdd:cd16417     1 LVAFDLDGTLVD--SAPDlaEAANAMLAA---------------LGLPPL-PEETvrtwigngaDVLVERALTGAR---- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  74 fayfGQGKDGRLLAQRYQFYLAQQGQTLS-------GAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVF 146
Cdd:cd16417    59 ----EAEPDEELFKEARALFDRHYAETLSvhshlypGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195 147 ISEQLQTQKPDAL-FYEKIGQqiAGFSKEKTLMIGDSLTaDIQGGNNADIDTIW----YNphHLENHTQAQPTYEVHSYQ 221
Cdd:cd16417   135 GGDSLPEKKPDPApLLHACEK--LGIAPAQMLMVGDSRN-DILAARAAGCPSVGltygYN--YGEDIAASGPDAVIDSLA 209


                  ...
gi 1002545195 222 DLL 224
Cdd:cd16417   210 ELL 212
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 4-225 3.43e-07

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: 49.19  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   4 KFLLFDLDHTLLDFDAaedvaltqllkeeGVADIQAYKDYYVPMNKTLWKDLEQkkiskqelvntRFSRLFAYFGQGKD- 82
Cdd:cd02588     1 KALVFDVYGTLIDWHS-------------GLAAAERAFPGRGEELSRLWRQKQL-----------EYTWLVTLMGPYVDf 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  83 GRLLAQRYQFYLAQQGQTLSGAH------------------EFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQ 144
Cdd:cd02588    57 DELTRDALRATAAELGLELDESDldelgdaylrlppfpdvvAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDA 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195 145 VFISEQLQTQKPDALFYEKIGQQIaGFSKEKTLMIGDSlTADIQGGNNADIDTIWYN-PHHLENHTQAQPTYEVHSYQDL 223
Cdd:cd02588   137 VLSAEDVRAYKPAPAVYELAAERL-GVPPDEILHVASH-AWDLAGARALGLRTAWINrPGEVPDPLGPAPDFVVPDLGEL 214


                  ..
gi 1002545195 224 LD 225
Cdd:cd02588   215 AD 216
HAD-like cd07515
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 101-214 1.40e-06

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: 46.26  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195 101 LSGAHEFLDSLIErDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFI-SEQlqtqkpDALFYEKIgQQIAGFSKEKTLMI 179
Cdd:cd07515    19 LPGVREALAALKA-DYRLVLITKGDLLDQEQKLARSGLSDYFDAVEVvSEK------DPDTYRRV-LSRYGIGPERFVMV 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002545195 180 GDSLTADIQ-----GGNNADIdtiwynPHHLENHTQAQPT 214
Cdd:cd07515    91 GNSLRSDILpvlaaGGWGVHI------PYELTWKEEADEP 124
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 155-222 1.50e-06

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: 47.59  E-value: 1.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002545195 155 KPDALFYEKiGQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIWY-----NPHHLEnHTQAQPTYEVHSYQD 222
Cdd:cd07530   177 KPEPIMMRA-ALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVltgvtTREDLA-KPPYRPTYIVPSLRE 247
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 155-199 2.85e-05

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


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 43.85  E-value: 2.85e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1002545195 155 KPDALFYEKIGQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIW 199
Cdd:TIGR01460 188 KPSPAIYRAALNLLQARPERRDVMVGDNLRTDILGAKNAGFDTLL 232
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
 155-199 7.10e-05

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: 42.57  E-value: 7.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1002545195 155 KPDALFYEKIGQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIW 199
Cdd:TIGR01459 195 KPYPAIFHKALKECSNIPKNRMLMVGDSFYTDILGANRLGIDTAL 239
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 3-204 7.89e-05

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


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 42.33  E-value: 7.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   3 YKFLLFDLDHTLLDFDAAEDVALtQLLKEEGVADI----QAYKDYY---VPMNKtlWKDLEQkkISKQELvntrfSRLFA 75
Cdd:TIGR01428   1 IKALVFDVYGTLFDVHSVAERAA-ELYGGRGEALSqlwrQKQLEYSwlrTLMGP--YKDFWD--LTREAL-----RYLLG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  76 YFGQGKDGRLLAQRYQFYLaqqgqTLSgAH----EFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQL 151
Cdd:TIGR01428  71 RLGLEDDESAADRLAEAYL-----RLP-PHpdvpAGLRALKERGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAV 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002545195 152 QTQKPDALFYEkIGQQIAGFSKEKTLMIGDSLtADIQGGNNADIDTIWYN-PHH 204
Cdd:TIGR01428 145 RAYKPAPQVYQ-LALEALGVPPDEVLFVASNP-WDLGGAKKFGFKTAWINrPGE 196
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 4-211 8.43e-05

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 41.95  E-value: 8.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   4 KFLLFDLDHTLLDFDAAEDValtQLLKEEGVADIQAYKDYYVPmnKTLWKDLEQKKISKQElvntrFSRLFA-YFGQGKD 82
Cdd:cd02603     2 RAVLFDFGGVLIDPDPAAAV---ARFEALTGEPSEFVLDTEGL--AGAFLELERGRITEEE-----FWEELReELGRPLS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  83 GRLLAQRYQFYLAQQGQTLsgahEFLDSLIERDYDLYAATN-GITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFY 161
Cdd:cd02603    72 AELFEELVLAAVDPNPEML----DLLEALRAKGYKVYLLSNtWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIY 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002545195 162 EkIGQQIAGFSKEKTLMIGDSLtADIQGGNNADIDTIwynphHLENHTQA 211
Cdd:cd02603   148 Q-LALERLGVKPEEVLFIDDRE-ENVEAARALGIHAI-----LVTDAEDA 190
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 3-225 2.66e-04

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: 40.73  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   3 YKFLLFDLDHTLLDfdAAEDV--ALTQLLKE---EGVADIQAYKDYYVPMNKTLWKDLEQKKISKQELV-------NTRF 70
Cdd:cd02616     1 ITTILFDLDGTLID--TNELIikSFNHTLKEyglEGYTREEVLPFIGPPLRETFEKIDPDKLEDMVEEFrkyyrehNDDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  71 SRLFAyfgqgkdgrllaqryqfylaqqgqtlsGAHEFLDSLIERDYDLYAATNGI--TAIQTgrLAQSDLAAYFNQVFIS 148
Cdd:cd02616    79 TKEYP---------------------------GVYETLARLKSQGIKLGVVTTKLreTALKG--LKLLGLDKYFDVIVGG 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002545195 149 EQLQTQKPDALFYEKiGQQIAGFSKEKTLMIGDSlTADIQGGNNADIDT--IWYNPHHLENHTQAQPTYEVHSYQDLLD 225
Cdd:cd02616   130 DDVTHHKPDPEPVLK-ALELLGAEPEEALMVGDS-PHDILAGKNAGVKTvgVTWGYKGREYLKAFNPDFIIDKMSDLLT 206
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
167-202 2.79e-04

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 40.11  E-value: 2.79e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1002545195 167 QIAGFSKEKTLMIGDSLTADIQGGNNADIDTIWYNP 202
Cdd:COG2179   102 KLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKP 137
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 6-195 2.81e-04

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: 40.76  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   6 LLFDLDHTLLDFDAAEDVALTQLLKEEGVADIqaykdyyvpmnktlwkDLEQKKISKQELVNTRFSRLFAYFGQGKDGRL 85
Cdd:cd07512     2 VIFDLDGTLIDSAPDLHAALNAVLAAEGLAPL----------------SLAEVRSFVGHGAPALIRRAFAAAGEDLDGPL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  86 LAQRYQFYLAQ-----QGQT--LSGAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPD- 157
Cdd:cd07512    66 HDALLARFLDHyeadpPGLTrpYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDp 145

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1002545195 158 ALFYEKIgqQIAGFSKEKTLMIGDSLTaDIQGGNNADI 195
Cdd:cd07512   146 APLRAAI--RRLGGDVSRALMVGDSET-DAATARAAGV 180
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 155-198 4.45e-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: 40.39  E-value: 4.45e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002545195 155 KPDALFYEKIGQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTI 198
Cdd:cd07525   183 KPHPPIYDLALARLGRPAKARILAVGDGLHTDILGANAAGLDSL 226
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 103-230 5.22e-04

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 40.01  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195 103 GAHEFLDSLIERDYDLYAATNGITAIQTGRLAQSDLAAYFNQVFISEQLQTQKPDALFYEKIGQQIaGFSKEKTLMIGDS 182
Cdd:PRK13288   86 TVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELL-GAKPEEALMVGDN 164

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002545195 183 lTADIQGGNNADIDTI---W--YNPHHLENHtqaQPTYEVHSYQDLLDCLDKL 230
Cdd:PRK13288  165 -HHDILAGKNAGTKTAgvaWtiKGREYLEQY---KPDFMLDKMSDLLAIVGDM 213
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 173-198 2.78e-03

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


Pssm-ID: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 36.48  E-value: 2.78e-03
                          10        20
                  ....*....|....*....|....*.
gi 1002545195 173 KEKTLMIGDSLTADIQGGNNADIDTI 198
Cdd:cd16416    81 PEQVAMVGDQLFTDILGGNRAGLYTI 106
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 155-198 4.03e-03

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: 37.37  E-value: 4.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002545195 155 KPDALFYEKIGQQIaGFSKEKTLMIGDSLTADIQGGNNADIDTI 198
Cdd:cd07510   204 KPSRFMFDCISSKF-SIDPARTCMVGDRLDTDILFGQNCGLKTL 246
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 101-230 5.49e-03

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: 36.61  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195 101 LSGAHEFLDSLIERDYDLYAATN--GITaiqTGRLAQSDLAA--------------YFNQVFI-----SEQLQTQKPdal 159
Cdd:COG0241    30 LPGVLEALARLNEAGYRLVVVTNqsGIG---RGLFTEEDLNAvhakmlellaaeggRIDAIYYcphhpDDNCDCRKP--- 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002545195 160 fyeKIG--QQIA---GFSKEKTLMIGDSLTaDIQGGNNADIDTIWYNPHHLENHTQAQPTYEVHSyqDLLDCLDKL 230
Cdd:COG0241   104 ---KPGmlLQAAerlGIDLSNSYMIGDRLS-DLQAAKAAGCKGILVLTGKGAEELAEALPDTVAD--DLAEAVDYL 173
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-135 6.47e-03

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: 36.74  E-value: 6.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   1 MPYKFLLFDLDHTLLDFDAaeDVALTQLLKEEGVADIQAYKDyyvpMNKTLWKDLEQKKISKQELVNTRFSRLfayfgQG 80
Cdd:COG0560     1 RKMRLAVFDLDGTLIAGES--IDELARFLGRRGLVDRREVLE----EVAAITERAMAGELDFEESLRFRVALL-----AG 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002545195  81 KDGRLLAQRYQFYLAQQGQTLSGAHEFLDSLIERDYDLYAATNGITAIqTGRLAQ 135
Cdd:COG0560    70 LPEEELEELAERLFEEVPRLYPGARELIAEHRAAGHKVAIVSGGFTFF-VEPIAE 123
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 7-198 7.49e-03

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: 36.20  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195   7 LFDLDHTLLDFDAAEDVALTQLLKEEGVaDIQAYKDYyvpmnktlwkdleqkKISKQELVntrfSRLFAYFGQGKDgrlL 86
Cdd:cd07523     3 IWDLDGTLLDSYPAMTKALSETLADFGI-PQDLETVY---------------KIIKESSV----QFAIQYYAEVPD---L 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002545195  87 AQRYQFYLAQQGQTL---SGAHEFLDSLIE---RDYDLYAATNGITAIqtgrLAQSDLAAYFNQVFISEQLQTQKPD--A 158
Cdd:cd07523    60 EEEYKELEAEYLAKPilfPGAKAVLRWIKEqggKNFLMTHRDHSALTI----LKKDGIASYFTEIVTSDNGFPRKPNpeA 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1002545195 159 LFY--EKIGQQIagfskEKTLMIGDSlTADIQGGNNADIDTI 198
Cdd:cd07523   136 INYllNKYQLNP-----EETVMIGDR-ELDIEAGHNAGISTI 171
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 155-202 8.12e-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: 35.46  E-value: 8.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1002545195 155 KPDALFYEKIGQQIAGFSKEKTLMIGDSLTADIQGGNNADIDTIWYNP 202
Cdd:TIGR01662  88 KPKPGMFLEALKRFNEIDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135
 
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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