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Conserved domains on  [gi|1034656382|ref|XP_016867956|]
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phosphoserine phosphatase isoform X1 [Homo sapiens]

Protein Classification

phosphoserine phosphatase( domain architecture ID 11560826)

phosphoserine phosphatase is a HAD (haloacid dehalogenase) family hydrolase that catalyzes the dephosphorylation of phosphoserine (P-Ser)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 15-216 2.72e-135

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. 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: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 377.78  E-value: 2.72e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  15 DAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIREL 94
Cdd:cd04309     1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHPPRLTPGVEEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  95 VSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKI 174
Cdd:cd04309    81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKHHYKRV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034656382 175 IMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDF 216
Cdd:cd04309   161 IMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202
 
Name Accession Description Interval E-value
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 15-216 2.72e-135

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. 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: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 377.78  E-value: 2.72e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  15 DAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIREL 94
Cdd:cd04309     1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHPPRLTPGVEEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  95 VSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKI 174
Cdd:cd04309    81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKHHYKRV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034656382 175 IMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDF 216
Cdd:cd04309   161 IMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202
PLN02954 PLN02954
phosphoserine phosphatase
 10-224 4.39e-103

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 297.37  E-value: 4.39e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  10 LFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTP 89
Cdd:PLN02954    8 LWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFEEALAARLSLFKPSLSQVEEFLEKRPPRLSP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  90 GIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKF 169
Cdd:PLN02954   88 GIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSGGKAEAVQHIKKKH 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034656382 170 HFKKIIMIGDGATDMEACPP--ADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELE 224
Cdd:PLN02954  168 GYKTMVMIGDGATDLEARKPggADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 1-220 5.39e-102

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 294.26  E-value: 5.39e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382   1 MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQvQRLI 80
Cdd:TIGR00338   1 DIAHSELSPLLRSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKGLPVE-LLKE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  81 AEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPAtnVFANRLKFYfNGEYAGFDETQPTAES-GGKG 159
Cdd:TIGR00338  80 VRENLPLTEGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEVE-DGKLTGLVEGPIVDASyKGKT 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034656382 160 KVIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNA--KWYITDFVELL 220
Cdd:TIGR00338 157 LLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKADICinKKDLTDILPLL 219
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 16-216 5.06e-37

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: 128.80  E-value: 5.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  16 AVCFDVDSTVIREEGIDELAKICG---------VEDAVSEMTRRAMGGAVPFKAALTERLALIQP-SREQVQRLIAE--- 82
Cdd:COG0560     5 LAVFDLDGTLIAGESIDELARFLGrrglvdrreVLEEVAAITERAMAGELDFEESLRFRVALLAGlPEEELEELAERlfe 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  83 QPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatNVFANRLKFYfNGEYAGfDETQPTAESGGKGKVI 162
Cdd:COG0560    85 EVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGID--HVIANELEVE-DGRLTG-EVVGPIVDGEGKAEAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382 163 KLLKEKF--HFKKIIMIGDGATD---MEAcppADAFIGFGGN-VIRQQVKDNAKWYITDF 216
Cdd:COG0560   161 RELAAELgiDLEQSYAYGDSANDlpmLEA---AGLPVAVNPDpALREAADRERGWPVLDL 217
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 15-186 3.34e-16

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: 73.77  E-value: 3.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  15 DAVCFDVDSTVIR-----EEGIDELA-----------KICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQ--- 75
Cdd:pfam00702   2 KAVVFDLDGTLTDgepvvTEAIAELAsehplakaivaAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEglt 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  76 ------VQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpatnvfanrlKFYFNGEYAGFDET 149
Cdd:pfam00702  82 vvlvelLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGL----------DDYFDVVISGDDVG 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034656382 150 QPTAESGGKGKVIKLLKEKFHfkKIIMIGDGATDMEA 186
Cdd:pfam00702 152 VGKPKPEIYLAALERLGVKPE--EVLMVGDGVNDIPA 186
 
Name Accession Description Interval E-value
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 15-216 2.72e-135

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. 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: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 377.78  E-value: 2.72e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  15 DAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIREL 94
Cdd:cd04309     1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHPPRLTPGVEEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  95 VSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKI 174
Cdd:cd04309    81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKHHYKRV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034656382 175 IMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDF 216
Cdd:cd04309   161 IMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202
PLN02954 PLN02954
phosphoserine phosphatase
 10-224 4.39e-103

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 297.37  E-value: 4.39e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  10 LFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTP 89
Cdd:PLN02954    8 LWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFEEALAARLSLFKPSLSQVEEFLEKRPPRLSP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  90 GIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKF 169
Cdd:PLN02954   88 GIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSGGKAEAVQHIKKKH 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034656382 170 HFKKIIMIGDGATDMEACPP--ADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELE 224
Cdd:PLN02954  168 GYKTMVMIGDGATDLEARKPggADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 1-220 5.39e-102

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 294.26  E-value: 5.39e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382   1 MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQvQRLI 80
Cdd:TIGR00338   1 DIAHSELSPLLRSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKGLPVE-LLKE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  81 AEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPAtnVFANRLKFYfNGEYAGFDETQPTAES-GGKG 159
Cdd:TIGR00338  80 VRENLPLTEGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEVE-DGKLTGLVEGPIVDASyKGKT 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034656382 160 KVIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNA--KWYITDFVELL 220
Cdd:TIGR00338 157 LLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKADICinKKDLTDILPLL 219
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 16-190 1.18e-53

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 170.23  E-value: 1.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  16 AVCFDVDSTVIREEG-IDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSR-EQVQRLIAEQPPHLTPGIRE 93
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSlIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRSRsEEVAKEFLARQVALRPGARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  94 LVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKE--KFHF 171
Cdd:TIGR01488  81 LISWLKERGIDTVIVSGGFDFFVEPVAEKLGID--DVFANRLEFDDNGLLTGPIEGQVNPEGECKGKVLKELLEesKITL 158

                         170
                  ....*....|....*....
gi 1034656382 172 KKIIMIGDGATDMEACPPA 190
Cdd:TIGR01488 159 KKIIAVGDSVNDLPMLKLA 177
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 16-216 5.06e-37

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: 128.80  E-value: 5.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  16 AVCFDVDSTVIREEGIDELAKICG---------VEDAVSEMTRRAMGGAVPFKAALTERLALIQP-SREQVQRLIAE--- 82
Cdd:COG0560     5 LAVFDLDGTLIAGESIDELARFLGrrglvdrreVLEEVAAITERAMAGELDFEESLRFRVALLAGlPEEELEELAERlfe 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  83 QPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatNVFANRLKFYfNGEYAGfDETQPTAESGGKGKVI 162
Cdd:COG0560    85 EVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGID--HVIANELEVE-DGRLTG-EVVGPIVDGEGKAEAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382 163 KLLKEKF--HFKKIIMIGDGATD---MEAcppADAFIGFGGN-VIRQQVKDNAKWYITDF 216
Cdd:COG0560   161 RELAAELgiDLEQSYAYGDSANDlpmLEA---AGLPVAVNPDpALREAADRERGWPVLDL 217
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 17-183 3.98e-33

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 117.65  E-value: 3.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  17 VCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQpPHLTPGIRELVS 96
Cdd:cd07500     2 IVFDMDSTLIQQEVIDELAAEAGVGEEVAAITERAMRGELDFEESLRERVALLKGLPESVLDEVYER-LTLTPGAEELIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  97 RLQERNVQVFLISGGFRSIVEHVASKLNIPAtnVFANRLKF---YFNGEYAGfdetqPTAESGGKGKVIKLLKEKFHFKK 173
Cdd:cd07500    81 TLKAKGYKTAVVSGGFTYFTDRLAEELGLDY--AFANELEIkdgKLTGKVLG-----PIVDAQRKAETLQELAARLGIPL 153

                         170
                  ....*....|..
gi 1034656382 174 --IIMIGDGATD 183
Cdd:cd07500   154 eqTVAVGDGAND 165
serB PRK11133
phosphoserine phosphatase; Provisional
 19-184 1.25e-21

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 90.78  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  19 FDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPhLTPGIRELVSRL 98
Cdd:PRK11133  115 MDMDSTAIQIECIDEIAKLAGTGEEVAEVTERAMRGELDFEASLRQRVATLKGADANILQQVRENLP-LMPGLTELVLKL 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  99 QERNVQVFLISGGFRSIVEHVASKLNIPAtnVFANRLKFY---FNGEYAGfdetqPTAESGGKGKVIKLLKEKFHF--KK 173
Cdd:PRK11133  194 QALGWKVAIASGGFTYFADYLRDKLRLDA--AVANELEIMdgkLTGNVLG-----DIVDAQYKADTLTRLAQEYEIplAQ 266

                         170
                  ....*....|.
gi 1034656382 174 IIMIGDGATDM 184
Cdd:PRK11133  267 TVAIGDGANDL 277
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 15-186 3.34e-16

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: 73.77  E-value: 3.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  15 DAVCFDVDSTVIR-----EEGIDELA-----------KICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQ--- 75
Cdd:pfam00702   2 KAVVFDLDGTLTDgepvvTEAIAELAsehplakaivaAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEglt 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  76 ------VQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpatnvfanrlKFYFNGEYAGFDET 149
Cdd:pfam00702  82 vvlvelLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGL----------DDYFDVVISGDDVG 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034656382 150 QPTAESGGKGKVIKLLKEKFHfkKIIMIGDGATDMEA 186
Cdd:pfam00702 152 VGKPKPEIYLAALERLGVKPE--EVLMVGDGVNDIPA 186
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 20-191 1.02e-11

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. 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: 319826 [Multi-domain]  Cd Length: 211  Bit Score: 61.96  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  20 DVDSTVIREEGIDELAKICGV-EDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRL 98
Cdd:cd07524     5 DFDGTITENDNIIYLMDEFAPpLEEWEALKEGVLSQTLSFREGVGQMFELLPSSLKDEIIEFLEKTAKIRPGFKEFVAFC 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  99 QERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKfyFNGEYAGFDETQPTAESGG----KGKVIKLLKEKFHFkkI 174
Cdd:cd07524    85 QEHGIPFIIVSGGMDFFIEPLLEGLVIEKIAIYCNGSD--FSGEQIHIDWPHECDCTNGcgccKSSIIRKYSKPRPF--I 160

                         170
                  ....*....|....*..
gi 1034656382 175 IMIGDGATDMEACPPAD 191
Cdd:cd07524   161 IVIGDSVTDLEAAKEAD 177
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
15-225 1.52e-11

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 61.48  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  15 DAVCFD-----VDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVP--FKAALTERL-ALIQPSREQVQRLIAE---Q 83
Cdd:COG0546     2 KLVLFDldgtlVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRelLRRLLGEDPdEELEELLARFRELYEEellD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  84 PPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNipatnvfanrLKFYFNGEYAGFDetqpTAESGGKGKVIK 163
Cdd:COG0546    82 ETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALG----------LDDYFDAIVGGDD----VPPAKPKPEPLL 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034656382 164 LLKEKFHFKK--IIMIGDGATDMEACPPADA-FIG--FGGNVIRQQVKDNAKWYITDFVELLGELEE 225
Cdd:COG0546   148 EALERLGLDPeeVLMVGDSPHDIEAARAAGVpFIGvtWGYGSAEELEAAGADYVIDSLAELLALLAE 214
HAD pfam12710
haloacid dehalogenase-like hydrolase;
17-186 2.29e-11

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 60.62  E-value: 2.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  17 VCFDVDSTVIREEGIDELAKI---CGVEDAVSEMTRRAMGGAVPFKAALTER------LALIQPSREQVQRLIAE----- 82
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRAllrRGGPDLWRALLVLLLLALLRLLGRLSRAgarellRALLAGLPEEDAAELERfvaev 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  83 QPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatNVFANRLKF---YFNGEYAGFDEtqptaESGGKG 159
Cdd:pfam12710  81 ALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFD--EVLATELEVddgRFTGELRLIGP-----PCAGEG 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034656382 160 KVIKL------LKEKFHFKKIIMIGDGATDMEA 186
Cdd:pfam12710 154 KVRRLrawlaaRGLGLDLADSVAYGDSPSDLPM 186
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 16-185 5.64e-09

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 53.85  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  16 AVCFDVDSTVI---------REEGIDELAKICGVEDAVSEMTRRAMGGAVpfkAALTERL--ALIQPSREQVQRLIAEQ- 83
Cdd:cd02612     1 LAFFDLDGTLIagdsffaflRFKGIAERRAPLEELLLLRLMALYALGRLD---GAGMEALlgFATAGLAGELAALVEEFv 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  84 ----PPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpaTNVFANRLKfYFNGEYAGfdETQPTAeSGGKG 159
Cdd:cd02612    78 eeyiLRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGI--DNVLGTQLE-TEDGRYTG--RIIGPP-CYGEG 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034656382 160 KVIKLL----KEKFHFKKIIMIGDGATDME 185
Cdd:cd02612   152 KVKRLRewlaEEGIDLKDSYAYSDSINDLP 181
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 91-196 6.13e-09

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: 52.01  E-value: 6.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  91 IRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatnvfanrlkFYFNGEYAGFDETQPTAEsgGKGKVIKLLKEKFH 170
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLG----------DLFDGIIGSDGGGTPKPK--PKPLLLLLLKLGVD 79

                          90       100
                  ....*....|....*....|....*..
gi 1034656382 171 FKKIIMIGDGATDMEACPPA-DAFIGF 196
Cdd:cd01427    80 PEEVLFVGDSENDIEAARAAgGRTVAV 106
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 15-125 5.11e-07

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: 48.87  E-value: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  15 DAVCFDVDSTVI-----REEGIDELAKICGVEDAVSE-----------MTRRAMGGAVPFKAALTERLAL--IQPSREQV 76
Cdd:COG1011     2 KAVLFDLDGTLLdfdpvIAEALRALAERLGLLDEAEElaeayraieyaLWRRYERGEITFAELLRRLLEElgLDLAEELA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034656382  77 QRLIAEQPPHLT--PGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNI 125
Cdd:COG1011    82 EAFLAALPELVEpyPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGL 132
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
15-125 5.09e-06

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 45.59  E-value: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  15 DAVCFDVDSTVI--------------REEGI----DELAKICGV-EDAVSEMTRRAMGGAVPfKAALTERLaliqpsREQ 75
Cdd:COG0637     3 KAVIFDMDGTLVdseplharawreafAELGIdlteEEYRRLMGRsREDILRYLLEEYGLDLP-EEELAARK------EEL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034656382  76 VQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNI 125
Cdd:COG0637    76 YRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGL 125
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
89-180 1.73e-05

Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 45.13  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  89 PGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpaTNVFANRLkfyfngeyagfdetqPtaesGGKGKVIKLLKEK 168
Cdd:COG2217   544 PEAAEAIAALKALGIRVVMLTGDNERTAEAVARELGI--DEVRAEVL---------------P----EDKAAAVRELQAQ 602

                          90
                  ....*....|..
gi 1034656382 169 FHfkKIIMIGDG 180
Cdd:COG2217   603 GK--KVAMVGDG 612
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
89-186 3.24e-05

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 42.96  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  89 PGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpatnvfanrlKFYFNGEYAGFDETQ--PTAEsggkgkVIKLLK 166
Cdd:pfam13419  82 PGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGL----------EDYFDVIVGGDDVEGkkPDPD------PILKAL 145

                          90       100
                  ....*....|....*....|..
gi 1034656382 167 EKFHFKK--IIMIGDGATDMEA 186
Cdd:pfam13419 146 EQLGLKPeeVIYVGDSPRDIEA 167
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
 89-183 3.33e-05

P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B; The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319783 [Multi-domain]  Cd Length: 647  Bit Score: 44.01  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  89 PGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpaTNVFANRLkfyfngeyagfdetqPtaesGGKGKVIKLLKEK 168
Cdd:cd02094   471 PDAAEAIEALKKMGIKVVMLTGDNRRTARAIAKELGI--DEVIAEVL---------------P----EDKAEKVKKLQAQ 529

                          90
                  ....*....|....*
gi 1034656382 169 FHfkKIIMIGDGATD 183
Cdd:cd02094   530 GK--KVAMVGDGIND 542
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
 89-219 3.43e-05

P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+)-ATPase; Archaeoglobus fulgidus CopB transports Cu(2+) from the cytoplasm to the exterior of the cell using ATP as energy source, it transports preferentially Cu(2+) over Cu(+), it is activated by Cu(2+) with high affinity and partially by Cu(+) and Ag(+). This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319850 [Multi-domain]  Cd Length: 632  Bit Score: 44.22  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  89 PGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpaTNVFANRLKfyfngeyagfDEtqptaesggKGKVIKLLKEK 168
Cdd:cd07552   458 PESKEAIRALKAQGITPVMLTGDNEEVAQAVAEELGI--DEYFAEVLP----------ED---------KAKKVKELQAE 516

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034656382 169 fhFKKIIMIGDGATDMEACPPADA--FIGFGGNV---------IRQQVKDnakwyITDFVEL 219
Cdd:cd07552   517 --GKKVAMVGDGVNDAPALAQADVgiAIGAGTDVaiesadvvlVKSDPRD-----IVDFLEL 571
P-type_ATPase_HM cd07553
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
 54-200 9.06e-05

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319851 [Multi-domain]  Cd Length: 610  Bit Score: 42.89  E-value: 9.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  54 GAVPFKAALTERLALIQPSREQVQRLIAEQPPHltPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFAN 133
Cdd:cd07553   404 GSAPDACGIQESGVVIARDGRQLLDLSFNDLLR--PDSNREIEELKKGGLSIAILSGDNEEKVRLVGDSLGLDPRQLFGN 481

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034656382 134 RLkfyfngeyagfdetqPTAesggKGKVIKLLKEKfhfkKIIMIGDGATDMEACPPADAFIGFGGNV 200
Cdd:cd07553   482 LS---------------PEE----KLAWIESHSPE----NTLMVGDGANDALALASAFVGIAVAGEV 525
mtnX PRK09552
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed
 86-191 2.52e-04

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed


Pssm-ID: 236562  Cd Length: 219  Bit Score: 40.73  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  86 HLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLnIPATNVFANRLKFyfNGEYAGFD-----ETQPTAESG-GKG 159
Cdd:PRK09552   74 EIREGFHEFVQFVKENNIPFYVVSGGMDFFVYPLLQGL-IPKEQIYCNGSDF--SGEYITITwphpcDEHCQNHCGcCKP 150

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034656382 160 KVIKLLKEKFHFkkIIMIGDGATDMEACPPAD 191
Cdd:PRK09552  151 SLIRKLSDTNDF--HIVIGDSITDLEAAKQAD 180
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
 89-198 3.76e-04

P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319774 [Multi-domain]  Cd Length: 617  Bit Score: 41.05  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  89 PGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIpaTNVFAnrlkfyfngeyagfdETQPtAEsggKGKVIKLLKEK 168
Cdd:cd02079   451 PEAKEVIAELKSGGIKVVMLTGDNEAAAQAVAKELGI--DEVHA---------------GLLP-ED---KLAIVKALQAE 509

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034656382 169 FHfkKIIMIGDGATDMEACPPADAFIGFGG 198
Cdd:cd02079   510 GG--PVAMVGDGINDAPALAQADVGIAMGS 537
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
 87-207 1.36e-03

ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily.


Pssm-ID: 273656 [Multi-domain]  Cd Length: 545  Bit Score: 39.22  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  87 LTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPatnVFAnrlkfyfngeyagfdETQPTaesgGKGKVIKLLK 166
Cdd:TIGR01494 388 LRPDAKETIEALRKAGIKVVMLTGDNVLTAKAIAKELGID---VFA---------------RVKPE----EKAAIVEALQ 445

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1034656382 167 EKFHfkKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKD 207
Cdd:TIGR01494 446 EKGR--TVAMTGDGVNDAPALKKADVGIAMGSGDVAKAAAD 484
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
 74-198 1.86e-03

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319848 [Multi-domain]  Cd Length: 592  Bit Score: 38.79  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  74 EQVQRLIAEQPPhLTPGIRELVSRLQERNV-QVFLISGGFRSIVEHVASKLNIpaTNVFANRLkfyfngeyagfdetqPT 152
Cdd:cd07550   410 GRLIGVIGLSDP-LRPEAAEVIARLRALGGkRIIMLTGDHEQRARALAEQLGI--DRYHAEAL---------------PE 471

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1034656382 153 aesgGKGKVIKLLKEKFHfkKIIMIGDGATDMEACPPADAFIGFGG 198
Cdd:cd07550   472 ----DKAEIVEKLQAEGR--TVAFVGDGINDSPALSYADVGISMRG 511
HAD-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
 72-194 5.72e-03

haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a small group of metazoan sequences. The sequences from mouse are annotated as Pyrimidine 5'-nucleotidases, aparrently in reference to HSPC233, the human homolog. However, no such annotation can currently be found for this gene. This group of sequences was found during searches for members of the haloacid dehalogenase (HAD) superfamily. All of the conserved catalytic motifs are found. The placement of the variable domain between motifs 1 and 2 indicates membership in subfamily I of the superfamily, but these sequences are sufficiently different from any of the branches (IA, TIGR01493, TIGR01509, TIGR01549; IB, TIGR01488; IC, TIGR01494; ID, TIGR01658; IF TIGR01545) of that subfamily as to constitute a separate branch to now be called IE. Considering that the closest identifiable hit outside of the noise range is to a phosphoserine phosphatase, this group may be considered to be most closely allied to subfamily IB.


Pssm-ID: 273683 [Multi-domain]  Cd Length: 283  Bit Score: 37.14  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656382  72 SREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNI--PATNVFANRLKFYFNGEYAGFdeT 149
Cdd:TIGR01544 113 DKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVESVLRQANVlhPNVKVVSNFLQFDEDGLLDGF--Q 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034656382 150 QPTAESGGKGK-VIKLLKEKFHFKK----IIMIGD--GATDMEACPPADAFI 194
Cdd:TIGR01544 191 QPLIHTFNKNEtVLNETTEYFDLVHtrdnIILLGDsiGDADMASGVPASSHI 242
 
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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