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Conserved domains on  [gi|1081189395|gb|OFT34532|]
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phosphoserine phosphatase [Corynebacterium sp. HMSC08A12]

Protein Classification

HAD family hydrolase( domain architecture ID 10001729)

haloacid dehalogenase (HAD) family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 141-356 1.45e-65

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: 207.77  E-value: 1.45e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 141 AFFDVDNTLIKGASILLFARGLAKRRFFTARQLLGFIWVQMKFRVLGKEsadDISSGREQALALVKGRKESEVIDMAQEI 220
Cdd:COG0560     6 AVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGEL---DFEESLRFRVALLAGLPEEELEELAERL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 221 WAAtiAERIFPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGTVAEVKDGRFTGRMVGHMLHGEEKKHAV 300
Cdd:COG0560    83 FEE--VPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEAL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1081189395 301 IALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAINPDSKLRKAA-LERGWEIRDY 356
Cdd:COG0560   161 RELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDL 217
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 141-356 1.45e-65

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: 207.77  E-value: 1.45e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 141 AFFDVDNTLIKGASILLFARGLAKRRFFTARQLLGFIWVQMKFRVLGKEsadDISSGREQALALVKGRKESEVIDMAQEI 220
Cdd:COG0560     6 AVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGEL---DFEESLRFRVALLAGLPEEELEELAERL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 221 WAAtiAERIFPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGTVAEVKDGRFTGRMVGHMLHGEEKKHAV 300
Cdd:COG0560    83 FEE--VPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEAL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1081189395 301 IALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAINPDSKLRKAA-LERGWEIRDY 356
Cdd:COG0560   161 RELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDL 217
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 140-342 1.14e-64

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 204.88  E-value: 1.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 140 GAFFDVDNTLIKGASILLFARGLAKRRFFTARQLLGFIWVQMKFrvLGKESADDISSGREQALALVKGRKESEVIDMAQE 219
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEF--FLNRGLDYMAYYRAFALDALAGLLEEDVRAIVEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 220 IWAATIAERIFPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGT-VAEVKDGRFTGRMVGHMLHGEEKKH 298
Cdd:TIGR01490  79 FVNQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTrLEESEDGIYTGNIDGNNCKGEGKVH 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1081189395 299 AVIALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAINPDSKL 342
Cdd:TIGR01490 159 ALAELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 141-339 6.21e-48

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: 161.32  E-value: 6.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 141 AFFDVDNTLIKGASILLFAR--GLAKRRFFTARQLLgfiWVQMKFRVLGKESADdissGREQALALVKGRKESEVIDMAQ 218
Cdd:cd02612     2 AFFDLDGTLIAGDSFFAFLRfkGIAERRAPLEELLL---LRLMALYALGRLDGA----GMEALLGFATAGLAGELAALVE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 219 EIWAATIAERIFPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGTVAEVKDGRFTGRMVGHMLHGEEKKH 298
Cdd:cd02612    75 EFVEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVK 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1081189395 299 AVIALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAINPD 339
Cdd:cd02612   155 RLREWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
141-328 4.09e-31

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 117.25  E-value: 4.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 141 AFFDVDNTLIKGASILLFARGLAKRRFFTARQLLGFIWVQMKFRVLGKESADDIssgREQALALVKGRKEsEVIDMAQEI 220
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGA---RELLRALLAGLPE-EDAAELERF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 221 WAATIAERIFPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGTVAEVKDGRFTGR--MVGHMLHGEEKKH 298
Cdd:pfam12710  77 VAEVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGElrLIGPPCAGEGKVR 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1081189395 299 AV--IALANYEGLDLQRCTAYSDSVNDLPMLS 328
Cdd:pfam12710 157 RLraWLAARGLGLDLADSVAYGDSPSDLPMLR 188
serB PRK11133
phosphoserine phosphatase; Provisional
 264-335 2.59e-05

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 45.71  E-value: 2.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081189395 264 ELGFTGALGTVAEVKDGRFTGRMVGHMLHGEEKKHAVIALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVA 335
Cdd:PRK11133  217 KLRLDAAVANELEIMDGKLTGNVLGDIVDAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 141-356 1.45e-65

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: 207.77  E-value: 1.45e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 141 AFFDVDNTLIKGASILLFARGLAKRRFFTARQLLGFIWVQMKFRVLGKEsadDISSGREQALALVKGRKESEVIDMAQEI 220
Cdd:COG0560     6 AVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGEL---DFEESLRFRVALLAGLPEEELEELAERL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 221 WAAtiAERIFPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGTVAEVKDGRFTGRMVGHMLHGEEKKHAV 300
Cdd:COG0560    83 FEE--VPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEAL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1081189395 301 IALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAINPDSKLRKAA-LERGWEIRDY 356
Cdd:COG0560   161 RELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDL 217
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 140-342 1.14e-64

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 204.88  E-value: 1.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 140 GAFFDVDNTLIKGASILLFARGLAKRRFFTARQLLGFIWVQMKFrvLGKESADDISSGREQALALVKGRKESEVIDMAQE 219
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEF--FLNRGLDYMAYYRAFALDALAGLLEEDVRAIVEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 220 IWAATIAERIFPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGT-VAEVKDGRFTGRMVGHMLHGEEKKH 298
Cdd:TIGR01490  79 FVNQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTrLEESEDGIYTGNIDGNNCKGEGKVH 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1081189395 299 AVIALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAINPDSKL 342
Cdd:TIGR01490 159 ALAELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 141-339 6.21e-48

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: 161.32  E-value: 6.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 141 AFFDVDNTLIKGASILLFAR--GLAKRRFFTARQLLgfiWVQMKFRVLGKESADdissGREQALALVKGRKESEVIDMAQ 218
Cdd:cd02612     2 AFFDLDGTLIAGDSFFAFLRfkGIAERRAPLEELLL---LRLMALYALGRLDGA----GMEALLGFATAGLAGELAALVE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 219 EIWAATIAERIFPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGTVAEVKDGRFTGRMVGHMLHGEEKKH 298
Cdd:cd02612    75 EFVEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVK 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1081189395 299 AVIALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAINPD 339
Cdd:cd02612   155 RLREWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
141-328 4.09e-31

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 117.25  E-value: 4.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 141 AFFDVDNTLIKGASILLFARGLAKRRFFTARQLLGFIWVQMKFRVLGKESADDIssgREQALALVKGRKEsEVIDMAQEI 220
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGA---RELLRALLAGLPE-EDAAELERF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 221 WAATIAERIFPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGTVAEVKDGRFTGR--MVGHMLHGEEKKH 298
Cdd:pfam12710  77 VAEVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGElrLIGPPCAGEGKVR 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1081189395 299 AV--IALANYEGLDLQRCTAYSDSVNDLPMLS 328
Cdd:pfam12710 157 RLraWLAARGLGLDLADSVAYGDSPSDLPMLR 188
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 141-330 4.62e-14

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: 69.69  E-value: 4.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 141 AFFDVDNTLIKGASILLFARGLAKRRFFtarqllgfiWVQMKFRVLGKESADDISSGREQALAlvkGRKESEVIdmAQEI 220
Cdd:TIGR01488   2 AIFDFDGTLTRQDSLIDLLAKLLGTNDE---------VIELTRLAPSGRISFEDALGRRLALL---HRSRSEEV--AKEF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 221 WAATIAERifPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGTVAEVKD-GRFTGRMVGHMLH-GEEKKH 298
Cdd:TIGR01488  68 LARQVALR--PGARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDnGLLTGPIEGQVNPeGECKGK 145

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1081189395 299 AVIALANYEGLDLQRCTAYSDSVNDLPMLSTV 330
Cdd:TIGR01488 146 VLKELLEESKITLKKIIAVGDSVNDLPMLKLA 177
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 143-337 3.50e-13

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: 67.19  E-value: 3.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 143 FDVDNTLIKGASILLFARGLAKRR---FFTARQLLGfiwvQMKFrvlgkesaddissgrEQAL----ALVKGRKESEVid 215
Cdd:cd07500     4 FDMDSTLIQQEVIDELAAEAGVGEevaAITERAMRG----ELDF---------------EESLrervALLKGLPESVL-- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 216 maQEIWAATiaeRIFPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGTVAEVKDGRFTGRMVGHMLHGEE 295
Cdd:cd07500    63 --DEVYERL---TLTPGAEELIQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVLGPIVDAQR 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1081189395 296 KKHAVIALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAIN 337
Cdd:cd07500   138 KAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIAFH 179
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 142-331 4.72e-10

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: 58.75  E-value: 4.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 142 FFDVDNTLIKGASILLFARGLAKRRFFTARQLL----GFIWVQMKFRV---LGKESADDISSGREQALALVKGRKESEVI 214
Cdd:pfam00702   5 VFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVaaaeDLPIPVEDFTArllLGKRDWLEELDILRGLVETLEAEGLTVVL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 215 DMAQEIWAATIAERIFPDTKELADMHIQAGQQVWLVTASPVQLAQIIAKELGFTGALGTVAEVKDGRFTGrmvghmLHGE 294
Cdd:pfam00702  85 VELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGK------PKPE 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1081189395 295 EKKHAVIALanyeGLDLQRCTAYSDSVNDLPMLSTVG 331
Cdd:pfam00702 159 IYLAALERL----GVKPEEVLMVGDGVNDIPAAKAAG 191
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 296-346 1.02e-06

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 49.57  E-value: 1.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1081189395 296 KKHAVIALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAI-NPDSKLRKAA 346
Cdd:TIGR00099 189 KGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMgNADEELKALA 240
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 296-346 6.02e-06

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 47.23  E-value: 6.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1081189395 296 KKHAVIALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAI-NPDSKLRKAA 346
Cdd:pfam08282 188 KGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMgNASPEVKAAA 239
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 296-346 2.27e-05

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 44.74  E-value: 2.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1081189395 296 KKHAVIALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAI-NPDSKLRKAA 346
Cdd:COG0561   122 KGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMgNAPPEVKAAA 173
serB PRK11133
phosphoserine phosphatase; Provisional
 264-335 2.59e-05

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 45.71  E-value: 2.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081189395 264 ELGFTGALGTVAEVKDGRFTGRMVGHMLHGEEKKHAVIALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVA 335
Cdd:PRK11133  217 KLRLDAAVANELEIMDGKLTGNVLGDIVDAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 296-346 1.57e-04

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-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, 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 42.97  E-value: 1.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1081189395 296 KKHAVIALANYEGLDLQRCTAYSDSVNDLPMLSTVGTAVAI-NPDSKLRKAA 346
Cdd:cd07516   184 KGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMgNAIDEVKEAA 235
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 243-346 1.63e-04

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 41.42  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 243 AGQQVWLVTASPVQLAQIIAKELGFTGalGTVAEvkDGrftgrmvghmlhGEEKKHAVIALANYEGLDLQRCTAYSDSVN 322
Cdd:cd07514    31 AGIPVVLVTGNSLPVARALAKYLGLSG--PVVAE--NG------------GVDKGTGLEKLAERLGIDPEEVLAIGDSEN 94

                          90       100
                  ....*....|....*....|....*
gi 1081189395 323 DLPMLSTVGTAVAI-NPDSKLRKAA 346
Cdd:cd07514    95 DIEMFKVAGFKVAVaNADEELKEAA 119
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 284-341 1.87e-04

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 42.62  E-value: 1.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 284 GRMvGHMLHGEEKKHAVIALAN-YEGLDLQRCTAYSDSVNDLPMLSTVGTAVAI-NPDSK 341
Cdd:PRK00192  180 GRF-LHLLGGGDKGKAVRWLKElYRRQDGVETIALGDSPNDLPMLEAADIAVVVpGPDGP 238
PRK08238 PRK08238
UbiA family prenyltransferase;
242-346 2.80e-04

UbiA family prenyltransferase;


Pssm-ID: 236195 [Multi-domain]  Cd Length: 479  Bit Score: 42.94  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 242 QAGQQVWLVTASPVQLAQIIAKELG-FTGALGTvaevkDGRFTgrmvghmLHGEEKKHAVIALANyegldlQRCTAYS-D 319
Cdd:PRK08238   86 AAGRKLVLATASDERLAQAVAAHLGlFDGVFAS-----DGTTN-------LKGAAKAAALVEAFG------ERGFDYAgN 147

                          90       100
                  ....*....|....*....|....*..
gi 1081189395 320 SVNDLPMLSTVGTAVAINPDSKLRKAA 346
Cdd:PRK08238  148 SAADLPVWAAARRAIVVGASPGVARAA 174
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 254-346 6.19e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 40.73  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081189395 254 PVQLAQIIAKELGFTgalgtvAEVKDGRFTgrmvghmLH----GEEKKHAVIALANYEGLDLQRCTAYSDSVNDLPMLST 329
Cdd:PRK01158  125 PVEEVRELLEELGLD------LEIVDSGFA-------IHikspGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEV 191

                          90
                  ....*....|....*...
gi 1081189395 330 VGTAVAI-NPDSKLRKAA 346
Cdd:PRK01158  192 AGFGVAVaNADEELKEAA 209
PRK10976 PRK10976
putative hydrolase; Provisional
 290-331 3.94e-03

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 38.88  E-value: 3.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1081189395 290 MLHGEEKKHAVIALANYEGLDLQRCTAYSDSVNDLPMLSTVG 331
Cdd:PRK10976  185 MAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAG 226
PRK15126 PRK15126
HMP-PP phosphatase;
293-331 7.24e-03

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 37.75  E-value: 7.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1081189395 293 GEEKKHAVIALANYEGLDLQRCTAYSDSVNDLPMLSTVG 331
Cdd:PRK15126  186 GCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVG 224
 
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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