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Conserved domains on  [gi|499266193|ref|WP_010963586|]
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MULTISPECIES: HAD-IB family hydrolase [Clostridium]

Protein Classification

HAD-IB family hydrolase( domain architecture ID 10019258)

HAD (haloacid dehalogenase)-IB family hydrolase similar to Caulobacter vibrioides protein CicA which may be involved in essential phosphotransferase reactions and may play a role in cell wall biosynthesis, morphogenesis, and cell division

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 5-207 2.54e-86

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: 254.96  E-value: 2.54e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193    5 AAFFDIDGTLYREGLISEVFKKLIKYEIIDEEKWYKEVRPEFEKWDNRkgdYDDYLLKMTEIYVDALNGLSKSQVEFIAS 84
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFLNR---GLDYMAYYRAFALDALAGLLEEDVRAIVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   85 QVVNQK-GERVYTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDYRGAEYLLDENDVYTGEVI-PMWDSKSKE 162
Cdd:TIGR01490  78 EFVNQKiESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEDGIYTGNIDgNNCKGEGKV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 499266193  163 RAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVGNPVCINPTKEL 207
Cdd:TIGR01490 158 HALAELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
 
Name Accession Description Interval E-value
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 5-207 2.54e-86

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: 254.96  E-value: 2.54e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193    5 AAFFDIDGTLYREGLISEVFKKLIKYEIIDEEKWYKEVRPEFEKWDNRkgdYDDYLLKMTEIYVDALNGLSKSQVEFIAS 84
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFLNR---GLDYMAYYRAFALDALAGLLEEDVRAIVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   85 QVVNQK-GERVYTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDYRGAEYLLDENDVYTGEVI-PMWDSKSKE 162
Cdd:TIGR01490  78 EFVNQKiESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEDGIYTGNIDgNNCKGEGKV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 499266193  163 RAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVGNPVCINPTKEL 207
Cdd:TIGR01490 158 HALAELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-230 1.26e-63

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: 197.75  E-value: 1.26e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   1 MKAKAAFFDIDGTLYREGLISEVFKKLIKYEIIDEEKWYKEVRPEFEKWDNRKGDYDDYLlkmtEIYVDALNGLSKSQVE 80
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESL----RFRVALLAGLPEEELE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193  81 FIASQVVNQKGeRVYTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDYRGAEyLLDENDVYTGEVI-PMWDSK 159
Cdd:COG0560   77 ELAERLFEEVP-RLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANE-LEVEDGRLTGEVVgPIVDGE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499266193 160 SKERAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVGNPVCINPTKELVKEILSdeevKNKIRIIVERKDM 230
Cdd:COG0560  155 GKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAADR----ERGWPVLDLLGDR 221
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 5-204 2.24e-58

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: 183.66  E-value: 2.24e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   5 AAFFDIDGTLYRegliSEVFKKLIKYEIIDEEKWYKEVRPEfekwdnrkgdyddyLLKMTEIYVDALNGLSKSQVEFIA- 83
Cdd:cd02612    1 LAFFDLDGTLIA----GDSFFAFLRFKGIAERRAPLEELLL--------------LRLMALYALGRLDGAGMEALLGFAt 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193  84 -----------SQVVNQKGERV-YTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDYRGAEYLLdENDVYTGE 151
Cdd:cd02612   63 aglagelaalvEEFVEEYILRVlYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLET-EDGRYTGR 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499266193 152 VI-PMWDSKSKERAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVGNPVCINPT 204
Cdd:cd02612  142 IIgPPCYGEGKVKRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
6-193 3.70e-22

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 89.90  E-value: 3.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193    6 AFFDIDGTLYREGLISEVFKKLIKYEIIDEEKWYKEVRPEFEKWDNRKGDYDDYLlkmtEIYVDALNGLSKSQVEFIASQ 85
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGAR----ELLRALLAGLPEEDAAELERF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   86 VVNQKGERVYTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDYRGAEyLLDENDVYTGEVIPMWDSKSKERAV 165
Cdd:pfam12710  77 VAEVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATE-LEVDDGRFTGELRLIGPPCAGEGKV 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 499266193  166 HELEA-----KYNIDLGESYAYGDTSGDLTMLK 193
Cdd:pfam12710 156 RRLRAwlaarGLGLDLADSVAYGDSPSDLPMLR 188
serB PRK11133
phosphoserine phosphatase; Provisional
 149-196 2.34e-03

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 38.39  E-value: 2.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 499266193 149 TGEVI-PMWDSKSKERAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVG 196
Cdd:PRK11133 236 TGNVLgDIVDAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAG 284
 
Name Accession Description Interval E-value
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 5-207 2.54e-86

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: 254.96  E-value: 2.54e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193    5 AAFFDIDGTLYREGLISEVFKKLIKYEIIDEEKWYKEVRPEFEKWDNRkgdYDDYLLKMTEIYVDALNGLSKSQVEFIAS 84
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFLNR---GLDYMAYYRAFALDALAGLLEEDVRAIVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   85 QVVNQK-GERVYTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDYRGAEYLLDENDVYTGEVI-PMWDSKSKE 162
Cdd:TIGR01490  78 EFVNQKiESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEDGIYTGNIDgNNCKGEGKV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 499266193  163 RAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVGNPVCINPTKEL 207
Cdd:TIGR01490 158 HALAELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-230 1.26e-63

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: 197.75  E-value: 1.26e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   1 MKAKAAFFDIDGTLYREGLISEVFKKLIKYEIIDEEKWYKEVRPEFEKWDNRKGDYDDYLlkmtEIYVDALNGLSKSQVE 80
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESL----RFRVALLAGLPEEELE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193  81 FIASQVVNQKGeRVYTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDYRGAEyLLDENDVYTGEVI-PMWDSK 159
Cdd:COG0560   77 ELAERLFEEVP-RLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANE-LEVEDGRLTGEVVgPIVDGE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499266193 160 SKERAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVGNPVCINPTKELVKEILSdeevKNKIRIIVERKDM 230
Cdd:COG0560  155 GKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAADR----ERGWPVLDLLGDR 221
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 5-204 2.24e-58

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: 183.66  E-value: 2.24e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   5 AAFFDIDGTLYRegliSEVFKKLIKYEIIDEEKWYKEVRPEfekwdnrkgdyddyLLKMTEIYVDALNGLSKSQVEFIA- 83
Cdd:cd02612    1 LAFFDLDGTLIA----GDSFFAFLRFKGIAERRAPLEELLL--------------LRLMALYALGRLDGAGMEALLGFAt 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193  84 -----------SQVVNQKGERV-YTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDYRGAEYLLdENDVYTGE 151
Cdd:cd02612   63 aglagelaalvEEFVEEYILRVlYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLET-EDGRYTGR 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499266193 152 VI-PMWDSKSKERAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVGNPVCINPT 204
Cdd:cd02612  142 IIgPPCYGEGKVKRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 5-195 1.49e-44

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: 147.89  E-value: 1.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193    5 AAFFDIDGTLYREGLISEVFKKLIKY--EIIDEEKWYKEVRPEFEKWDNRKGDYDDYLLKmtEIYVDalnglsksqvEFI 82
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLAKLLGTndEVIELTRLAPSGRISFEDALGRRLALLHRSRS--EEVAK----------EFL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   83 ASQVVNQkgervyTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDYRGAEYLLDENDVYTG----EVIPMWDS 158
Cdd:TIGR01488  69 ARQVALR------PGARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDNGLLTGpiegQVNPEGEC 142

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 499266193  159 KSKERAVHELEAKynIDLGESYAYGDTSGDLTMLKMV 195
Cdd:TIGR01488 143 KGKVLKELLEESK--ITLKKIIAVGDSVNDLPMLKLA 177
HAD pfam12710
haloacid dehalogenase-like hydrolase;
6-193 3.70e-22

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 89.90  E-value: 3.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193    6 AFFDIDGTLYREGLISEVFKKLIKYEIIDEEKWYKEVRPEFEKWDNRKGDYDDYLlkmtEIYVDALNGLSKSQVEFIASQ 85
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGAR----ELLRALLAGLPEEDAAELERF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   86 VVNQKGERVYTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDYRGAEyLLDENDVYTGEVIPMWDSKSKERAV 165
Cdd:pfam12710  77 VAEVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATE-LEVDDGRFTGELRLIGPPCAGEGKV 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 499266193  166 HELEA-----KYNIDLGESYAYGDTSGDLTMLK 193
Cdd:pfam12710 156 RRLRAwlaarGLGLDLADSVAYGDSPSDLPMLR 188
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 106-196 4.41e-10

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: 57.17  E-value: 4.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193 106 KERGHKIITISGSPIELVRNMAEKYGFDDYRgAEYLLDENDVYTGEVI-PMWDSKSKERAVHELEAKYNIDLGESYAYGD 184
Cdd:cd07500   83 KAKGYKTAVVSGGFTYFTDRLAEELGLDYAF-ANELEIKDGKLTGKVLgPIVDAQRKAETLQELAARLGIPLEQTVAVGD 161

                         90
                 ....*....|..
gi 499266193 185 TSGDLTMLKMVG 196
Cdd:cd07500  162 GANDLPMLKAAG 173
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 4-196 1.29e-09

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: 56.06  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193    4 KAAFFDIDGTLYR-EGLISEVFKKLIKYEIIDEE--KWYKEVRPEFEKWDNRKGDYDDYLLK---MTEIYVDALNGLSKS 77
Cdd:pfam00702   2 KAVVFDLDGTLTDgEPVVTEAIAELASEHPLAKAivAAAEDLPIPVEDFTARLLLGKRDWLEeldILRGLVETLEAEGLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   78 QV-EFIASQVVNQKGERVYTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDYRGAEYLLDENDVytgevipmw 156
Cdd:pfam00702  82 VVlVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGV--------- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 499266193  157 dSKSKERAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVG 196
Cdd:pfam00702 153 -GKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-211 3.19e-07

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. 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: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 49.53  E-value: 3.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   4 KAAFFDIDGTLYREGL-----ISEVFKKLIKYEIIdeekwykeV-----RPEFEKWDNRKG-DYDDYLlkmteiyvdALN 72
Cdd:cd07517    1 KIVFFDIDGTLLDEDTtipesTKEAIAALKEKGIL--------VviatgRAPFEIQPIVKAlGIDSYV---------SYN 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193  73 G-LSKSQVEFIASQVVNQkgERVytytRDRIKWHKERGHKIITisGSPIELVRNMAEKYGFDDYRGAEYLLDENDVYTgE 151
Cdd:cd07517   64 GqYVFFEGEVIYKNPLPQ--ELV----ERLTEFAKEQGHPVSF--YGQLLLFEDEEEEQKYEELRPELRFVRWHPLST-D 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193 152 VIPMWDSKSKerAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVGNPVCINPTKELVKEI 211
Cdd:cd07517  135 VIPKGGSKAK--GIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEI 192
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 97-200 4.15e-07

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: 48.98  E-value: 4.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193  97 YTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDY---------------------------RGAEYLLDENDVYT 149
Cdd:COG0561   23 RTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPlitsngaliydpdgevlyerpldpedvREILELLREHGLHL 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193 150 gEVIPMWDSK---------SKERAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVGNPVC 200
Cdd:COG0561  103 -QVVVRSGPGfleilpkgvSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVA 161
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 4-135 2.05e-06

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: 47.33  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   4 KAAFFDIDGTLY-----REGLISEVFKKLIKYEIIDE--EKWYKEVRPEFEKWDNRKGDYDDYLLKMTEIY-VDALNGLS 75
Cdd:COG1011    2 KAVLFDLDGTLLdfdpvIAEALRALAERLGLLDEAEElaEAYRAIEYALWRRYERGEITFAELLRRLLEELgLDLAEELA 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193  76 KSQVEFIASQVvnqkgeRVYTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDY 135
Cdd:COG1011   82 EAFLAALPELV------EPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDL 135
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 102-196 2.73e-06

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: 45.08  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193 102 IKWHKERGHKIITISGSPIELVRNMAEKYGFDDYrgAEYLLDENDVYTGevipmwdsKSKERAVHELEAKYNIDLGESYA 181
Cdd:cd01427   16 LKRLRAAGIKLAIVTNRSREALRALLEKLGLGDL--FDGIIGSDGGGTP--------KPKPKPLLLLLLKLGVDPEEVLF 85

                         90
                 ....*....|....*
gi 499266193 182 YGDTSGDLTMLKMVG 196
Cdd:cd01427   86 VGDSENDIEAARAAG 100
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 7-211 3.86e-05

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 43.77  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193    7 FFDIDGTLYRE-GLISEVFKKLIKYeIIDEEKW--------YKEVRPEFEKwdnrkgdyddylLKMTEIYVdALNG---- 73
Cdd:pfam08282   2 ASDLDGTLLNSdKKISEKTKEAIKK-LKEKGIKfviatgrpYRAILPVIKE------------LGLDDPVI-CYNGaliy 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   74 -----------LSKSQVEFIAsQVVNQKGERVYTYTRDRIKWHKERGHKIITIS----GSPIELVRNMAEKYGFD----- 133
Cdd:pfam08282  68 dengkilysnpISKEAVKEII-EYLKENNLEILLYTDDGVYILNDNELEKILKElnytKSFVPEIDDFELLEDEDinkil 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193  134 ---DYRGAEYLLDENDVYTGEVIPMWDSK-----------SKERAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVGNPV 199
Cdd:pfam08282 147 illDEEDLDELEKELKELFGSLITITSSGpgyleimpkgvSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGV 226

                         250
                  ....*....|..
gi 499266193  200 CINPTKELVKEI 211
Cdd:pfam08282 227 AMGNASPEVKAA 238
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-135 2.11e-03

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 38.27  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193   4 KAAFFDIDGTLYR-EGLISEVFKKLIK---YEIIDEE------KWYKEVRPEFEKWDNRKGDYDDYLLKMTEIYVDALng 73
Cdd:COG0637    3 KAVIFDMDGTLVDsEPLHARAWREAFAelgIDLTEEEyrrlmgRSREDILRYLLEEYGLDLPEEELAARKEELYRELL-- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499266193  74 lsksqvefiasqvvNQKGERVYTYTRDRIKWHKERGHKIITISGSPIELVRNMAEKYGFDDY 135
Cdd:COG0637   81 --------------AEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDY 128
serB PRK11133
phosphoserine phosphatase; Provisional
 149-196 2.34e-03

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 38.39  E-value: 2.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 499266193 149 TGEVI-PMWDSKSKERAVHELEAKYNIDLGESYAYGDTSGDLTMLKMVG 196
Cdd:PRK11133 236 TGNVLgDIVDAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAG 284
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 107-211 3.87e-03

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: 36.41  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499266193 107 ERGHKIITISGSPIELVRNMAEKYGFDDYRGAEylldendvyTGEVipmwdskSKERAVHELEAKYNIDLGESYAYGDTS 186
Cdd:cd07514   30 KAGIPVVLVTGNSLPVARALAKYLGLSGPVVAE---------NGGV-------DKGTGLEKLAERLGIDPEEVLAIGDSE 93

                         90       100
                 ....*....|....*....|....*
gi 499266193 187 GDLTMLKMVGNPVCINPTKELVKEI 211
Cdd:cd07514   94 NDIEMFKVAGFKVAVANADEELKEA 118
 
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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