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Conserved domains on  [gi|256013056|gb|EAS66964|]
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phosphomannomutase B [Dictyostelium discoideum AX4]

Protein Classification

phosphomannomutase( domain architecture ID 10015262)

phosphomannomutase is involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 2-249 2.63e-159

phosphomannomutase; Provisional


:

Pssm-ID: 240305  Cd Length: 247  Bit Score: 441.31  E-value: 2.63e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   2 SQNKNTICLFDVDDTLTKPRNAITNEMKELLASLRTK-IKIGVVGGSNFNKIKEQLGENFINDFDYVFAENGLIAYKDGS 80
Cdd:PTZ00174   1 MEMKKTILLFDVDGTLTKPRNPITQEMKDTLAKLKSKgFKIGVVGGSDYPKIKEQLGEDVLEDFDYVFSENGLVAYKDGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  81 LLEIQDIKKYLGEENIKKFINFVLHYVADLDIPIKRGTFVEFRNGMLNISPIGRNCSQQEREEFEKYDLEHKIRSTMVSI 160
Cdd:PTZ00174  81 LFHSQSILKFLGEEKLKKFINFCLRYIADLDIPVKRGTFIEYRNGMINISPIGRNCSQEERDEFEKYDKEHHIREKFIQD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056 161 LKEEFKSFGLQYSIGGQISFDVFPIGWDKTYCLRHLPEDeFKTLYFFGDKTFLGGNDYEIANHPRiTQSFTVKSPANTLA 240
Cdd:PTZ00174 161 LKKEFSDLGLKFSIGGQISFDVFPKGWDKTYCLRHLEND-FKEIHFFGDKTFEGGNDYEIYNDPR-TIGHSVKNPEDTIK 238


                 ....*....
gi 256013056 241 ILNDFFFKK 249
Cdd:PTZ00174 239 ILKELFLKK 247
 
Name Accession Description Interval E-value
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 2-249 2.63e-159

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 441.31  E-value: 2.63e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   2 SQNKNTICLFDVDDTLTKPRNAITNEMKELLASLRTK-IKIGVVGGSNFNKIKEQLGENFINDFDYVFAENGLIAYKDGS 80
Cdd:PTZ00174   1 MEMKKTILLFDVDGTLTKPRNPITQEMKDTLAKLKSKgFKIGVVGGSDYPKIKEQLGEDVLEDFDYVFSENGLVAYKDGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  81 LLEIQDIKKYLGEENIKKFINFVLHYVADLDIPIKRGTFVEFRNGMLNISPIGRNCSQQEREEFEKYDLEHKIRSTMVSI 160
Cdd:PTZ00174  81 LFHSQSILKFLGEEKLKKFINFCLRYIADLDIPVKRGTFIEYRNGMINISPIGRNCSQEERDEFEKYDKEHHIREKFIQD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056 161 LKEEFKSFGLQYSIGGQISFDVFPIGWDKTYCLRHLPEDeFKTLYFFGDKTFLGGNDYEIANHPRiTQSFTVKSPANTLA 240
Cdd:PTZ00174 161 LKKEFSDLGLKFSIGGQISFDVFPKGWDKTYCLRHLEND-FKEIHFFGDKTFEGGNDYEIYNDPR-TIGHSVKNPEDTIK 238


                 ....*....
gi 256013056 241 ILNDFFFKK 249
Cdd:PTZ00174 239 ILKELFLKK 247
HAD_PMM cd02585
phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis ...
 8-242 5.32e-135

phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis thaliana PMM; PMM catalyzes the interconversion of mannose-6-phosphate (M6P) to mannose-1-phosphate (M1P); the conversion of M6P to M1P is an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes. M1P is the substrate for the synthesis of GDP-mannose, which is an intermediate for protein glycosylation, protein sorting and secretion, and maintaining a functional endomembrane system in eukaryotic cells. Proteins in this family contains a conserved phosphorylated motif DxDx(T/V) shared with some other phosphotransferases. This family contains two human homologs, PMM1 and PMM2; PMM2 deficiency causes congenital disorder of glycosylation type I-a, also known as Jaeken syndrome. PMM1 can also act as glucose-1,6-bisphosphatase in the brain after stimulation with inosine monophosphate; PMM2 on the other hand, is insensitive to IMP and demonstrates low glucose-1,6-bisphosphatase activity. Arabidopsis thaliana PMM converted M1P into M6P and glucose-1-phosphate into glucose-6-phosphate, with the latter reaction being less efficient. Arabidopsis thaliana and Nicotiana benthamian PPMs are involved in ascorbic acid 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: 319784  Cd Length: 238  Bit Score: 379.70  E-value: 5.32e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   8 ICLFDVDDTLTKPRNAITNEMKELLASLRTKIKIGVVGGSNFNKIKEQLGENF-INDFDYVFAENGLIAYKDGSLLEIQD 86
Cdd:cd02585    1 LLLFDVDGTLTPPRQPITPEMAEFLAELRQKVKIGVVGGSDYDKIKEQLGDNVpLLDFDYVFPENGLVAYRDGELLSRQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  87 IKKYLGEENIKKFINFVLHYVADLDIPIKRGTFVEFRNGMLNISPIGRNCSQQEREEFEKYDLEHKIRSTMVSILKEEFK 166
Cdd:cd02585   81 IIRALGEEKLQALINFCLRYIADLDLPKKRGTFIEFRNGMINISPIGRNCSQEERIEFEELDKKHKIREKFVSALKEEFA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256013056 167 SFGLQYSIGGQISFDVFPIGWDKTYCLRHLPEDEFKTLYFFGDKTFLGGNDYEIANHPRiTQSFTVKSPANTLAIL 242
Cdd:cd02585  161 DKGLTFSIGGQISFDVFPKGWDKTYCLRHLEEDLYEEIHFFGDKTQPGGNDYEIYQDPR-TIGHSVTSPKDTVRIL 235
PMM pfam03332
Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the ...
 28-247 3.11e-121

Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.


Pssm-ID: 397425  Cd Length: 220  Bit Score: 343.98  E-value: 3.11e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   28 MKELLASLRTKIKIGVVGGSNFNKIKEQLGENFINDFDYVFAENGLIAYKDGSLLEIQDIKKYLGEENIKKFINFVLHYV 107
Cdd:pfam03332   1 VKDFLQKLRKRVTIGVVGGSDLSKIQEQLGDNVLDEFDYVFSENGLVAYKGGKLLASQSIINHLGEEKLQKLINFCLRYI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  108 ADLDIPIKRGTFVEFRNGMLNISPIGRNCSQQEREEFEKYDLEHKIRSTMVSILKEEFKSFGLQYSIGGQISFDVFPIGW 187
Cdd:pfam03332  81 ADLDLPIKRGTFIEFRNGMINVSPIGRNCSQEERNEFEEYDKKHKIRQKFVEALKEEFADYGLTFSIGGQISFDVFPKGW 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  188 DKTYCLRHLPEDEFKTLYFFGDKTFLGGNDYEIANHPRiTQSFTVKSPANTLAILNDFFF 247
Cdd:pfam03332 161 DKTYCLQHVEKDGFDTIHFFGDKTYPGGNDYEIFNDPR-TIGHSVTSPDDTVRILEELLK 219
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 10-220 2.95e-18

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 80.12  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   10 LFDVDDTLTKPRNA-ITNEMKELLASLRTK-IKIGVVGGSNFNKIKEQLGEnfINDFDYVFAENG-LIAYKDGSLL--EI 84
Cdd:TIGR01484   3 FFDLDGTLLDPNAHeLSPETIEALERLREAgVKVVIVTGRSLAEIKELLKQ--LNLPLPLIAENGaLIFYPGEILYiePS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   85 QDIKKYLGEenIKKFINFVLHYVADldipIKRGTFVEFRNGMLNISPIGRNCSQqereefeKYDLEHKIRSTMVSILKEE 164
Cdd:TIGR01484  81 DVFEEILGI--KFEEIGAELKSLSE----HYVGTFIEDKAIAVAIHYVGAELGQ-------ELDSKMRERLEKIGRNDLE 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 256013056  165 FKsfgLQYSigGQISFDVFPIGWDKTYCLRHLPEDEF---KTLYFFGDktflGGNDYEI 220
Cdd:TIGR01484 148 LE---AIYS--GKTDLEVLPAGVNKGSALQALLQELNgkkDEILAFGD----SGNDEEM 197
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 11-133 2.89e-04

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: 40.50  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  11 FDVDDTLTKPRNAITNEMKELLASLRTK-IKIGVVGGSNFNKIKEQLGEnfINDFDYVFAENG-LIAYKDGSLLEIQDIK 88
Cdd:COG0561    7 LDLDGTLLNDDGEISPRTKEALRRLREKgIKVVIATGRPLRSALPLLEE--LGLDDPLITSNGaLIYDPDGEVLYERPLD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 256013056  89 kylgeeniKKFINFVLHYVADLDIPIkrGTFVEFRNGMLNISPIG 133
Cdd:COG0561   85 --------PEDVREILELLREHGLHL--QVVVRSGPGFLEILPKG 119
 
Name Accession Description Interval E-value
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 2-249 2.63e-159

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 441.31  E-value: 2.63e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   2 SQNKNTICLFDVDDTLTKPRNAITNEMKELLASLRTK-IKIGVVGGSNFNKIKEQLGENFINDFDYVFAENGLIAYKDGS 80
Cdd:PTZ00174   1 MEMKKTILLFDVDGTLTKPRNPITQEMKDTLAKLKSKgFKIGVVGGSDYPKIKEQLGEDVLEDFDYVFSENGLVAYKDGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  81 LLEIQDIKKYLGEENIKKFINFVLHYVADLDIPIKRGTFVEFRNGMLNISPIGRNCSQQEREEFEKYDLEHKIRSTMVSI 160
Cdd:PTZ00174  81 LFHSQSILKFLGEEKLKKFINFCLRYIADLDIPVKRGTFIEYRNGMINISPIGRNCSQEERDEFEKYDKEHHIREKFIQD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056 161 LKEEFKSFGLQYSIGGQISFDVFPIGWDKTYCLRHLPEDeFKTLYFFGDKTFLGGNDYEIANHPRiTQSFTVKSPANTLA 240
Cdd:PTZ00174 161 LKKEFSDLGLKFSIGGQISFDVFPKGWDKTYCLRHLEND-FKEIHFFGDKTFEGGNDYEIYNDPR-TIGHSVKNPEDTIK 238


                 ....*....
gi 256013056 241 ILNDFFFKK 249
Cdd:PTZ00174 239 ILKELFLKK 247
HAD_PMM cd02585
phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis ...
 8-242 5.32e-135

phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis thaliana PMM; PMM catalyzes the interconversion of mannose-6-phosphate (M6P) to mannose-1-phosphate (M1P); the conversion of M6P to M1P is an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes. M1P is the substrate for the synthesis of GDP-mannose, which is an intermediate for protein glycosylation, protein sorting and secretion, and maintaining a functional endomembrane system in eukaryotic cells. Proteins in this family contains a conserved phosphorylated motif DxDx(T/V) shared with some other phosphotransferases. This family contains two human homologs, PMM1 and PMM2; PMM2 deficiency causes congenital disorder of glycosylation type I-a, also known as Jaeken syndrome. PMM1 can also act as glucose-1,6-bisphosphatase in the brain after stimulation with inosine monophosphate; PMM2 on the other hand, is insensitive to IMP and demonstrates low glucose-1,6-bisphosphatase activity. Arabidopsis thaliana PMM converted M1P into M6P and glucose-1-phosphate into glucose-6-phosphate, with the latter reaction being less efficient. Arabidopsis thaliana and Nicotiana benthamian PPMs are involved in ascorbic acid 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: 319784  Cd Length: 238  Bit Score: 379.70  E-value: 5.32e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   8 ICLFDVDDTLTKPRNAITNEMKELLASLRTKIKIGVVGGSNFNKIKEQLGENF-INDFDYVFAENGLIAYKDGSLLEIQD 86
Cdd:cd02585    1 LLLFDVDGTLTPPRQPITPEMAEFLAELRQKVKIGVVGGSDYDKIKEQLGDNVpLLDFDYVFPENGLVAYRDGELLSRQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  87 IKKYLGEENIKKFINFVLHYVADLDIPIKRGTFVEFRNGMLNISPIGRNCSQQEREEFEKYDLEHKIRSTMVSILKEEFK 166
Cdd:cd02585   81 IIRALGEEKLQALINFCLRYIADLDLPKKRGTFIEFRNGMINISPIGRNCSQEERIEFEELDKKHKIREKFVSALKEEFA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256013056 167 SFGLQYSIGGQISFDVFPIGWDKTYCLRHLPEDEFKTLYFFGDKTFLGGNDYEIANHPRiTQSFTVKSPANTLAIL 242
Cdd:cd02585  161 DKGLTFSIGGQISFDVFPKGWDKTYCLRHLEEDLYEEIHFFGDKTQPGGNDYEIYQDPR-TIGHSVTSPKDTVRIL 235
PLN02423 PLN02423
phosphomannomutase
 1-238 2.18e-130

phosphomannomutase


Pssm-ID: 178043 [Multi-domain]  Cd Length: 245  Bit Score: 368.28  E-value: 2.18e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   1 MSQNKNTICLFDVDDTLTKPRNAITNEMKELLASLRTKIKIGVVGGSNFNKIKEQLGENFINDFDYVFAENGLIAYKDGS 80
Cdd:PLN02423   2 AARKPGVIALFDVDGTLTAPRKEATPEMLEFMKELRKVVTVGVVGGSDLSKISEQLGKTVINDYDYVFSENGLVAHKDGK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  81 LLEIQDIKKYLGEENIKKFINFVLHYVADLDIPIKRGTFVEFRNGMLNISPIGRNCSQQEREEFEKYDLEHKIRSTMVSI 160
Cdd:PLN02423  82 LIGTQSLKSFLGEDKLKEFINFTLHYIADLDIPIKRGTFIEFRSGMLNVSPIGRNCSQEERDEFEKYDKVHNIRPKMVSV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256013056 161 LKEEFKSFGLQYSIGGQISFDVFPIGWDKTYCLRHLpeDEFKTLYFFGDKTFLGGNDYEIANHPRiTQSFTVKSPANT 238
Cdd:PLN02423 162 LREKFAHLNLTYSIGGQISFDVFPQGWDKTYCLQFL--EDFDEIHFFGDKTYEGGNDHEIFESER-TIGHTVTSPDDT 236
PMM pfam03332
Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the ...
 28-247 3.11e-121

Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.


Pssm-ID: 397425  Cd Length: 220  Bit Score: 343.98  E-value: 3.11e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   28 MKELLASLRTKIKIGVVGGSNFNKIKEQLGENFINDFDYVFAENGLIAYKDGSLLEIQDIKKYLGEENIKKFINFVLHYV 107
Cdd:pfam03332   1 VKDFLQKLRKRVTIGVVGGSDLSKIQEQLGDNVLDEFDYVFSENGLVAYKGGKLLASQSIINHLGEEKLQKLINFCLRYI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  108 ADLDIPIKRGTFVEFRNGMLNISPIGRNCSQQEREEFEKYDLEHKIRSTMVSILKEEFKSFGLQYSIGGQISFDVFPIGW 187
Cdd:pfam03332  81 ADLDLPIKRGTFIEFRNGMINVSPIGRNCSQEERNEFEEYDKKHKIRQKFVEALKEEFADYGLTFSIGGQISFDVFPKGW 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  188 DKTYCLRHLPEDEFKTLYFFGDKTFLGGNDYEIANHPRiTQSFTVKSPANTLAILNDFFF 247
Cdd:pfam03332 161 DKTYCLQHVEKDGFDTIHFFGDKTYPGGNDYEIFNDPR-TIGHSVTSPDDTVRILEELLK 219
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 10-220 2.95e-18

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 80.12  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   10 LFDVDDTLTKPRNA-ITNEMKELLASLRTK-IKIGVVGGSNFNKIKEQLGEnfINDFDYVFAENG-LIAYKDGSLL--EI 84
Cdd:TIGR01484   3 FFDLDGTLLDPNAHeLSPETIEALERLREAgVKVVIVTGRSLAEIKELLKQ--LNLPLPLIAENGaLIFYPGEILYiePS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   85 QDIKKYLGEenIKKFINFVLHYVADldipIKRGTFVEFRNGMLNISPIGRNCSQqereefeKYDLEHKIRSTMVSILKEE 164
Cdd:TIGR01484  81 DVFEEILGI--KFEEIGAELKSLSE----HYVGTFIEDKAIAVAIHYVGAELGQ-------ELDSKMRERLEKIGRNDLE 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 256013056  165 FKsfgLQYSigGQISFDVFPIGWDKTYCLRHLPEDEF---KTLYFFGDktflGGNDYEI 220
Cdd:TIGR01484 148 LE---AIYS--GKTDLEVLPAGVNKGSALQALLQELNgkkDEILAFGD----SGNDEEM 197
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 10-217 1.98e-06

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. 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: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 47.34  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  10 LFDVDDTLTK--PRNAITNEMKELLASLRTK--IKIGVVGGSNFNKIKEQLGENFINDFDYVFAENGLIAYKDGSLLEIQ 85
Cdd:cd02605    3 VSDLDETLVGhdTNLQALERLQDLLEQLTADndVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYGESGYLEP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  86 DikkylgeenikkfinfvLHYVADLDIPIKRGTFVEFRNGMLNISPIgrncSQQEREEF-EKYDLEHKIRSTMVSILKEE 164
Cdd:cd02605   83 D-----------------TYWNEVLSEGWERFLFEAIADLFKQLKPQ----SELEQNPHkISFYLDPQNDAAVIEQLEEM 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056 165 FKSFGLQ----YSIGGQISFDVFPIGWDKTYCLRHLPED---EFKTLYFFGDKtflgGND 217
Cdd:cd02605  142 LLKAGLTvriiYSSGLAYDLDILPLGAGKGEALRYLQEKwnfPPERTLVCGDS----GND 197
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 10-78 1.84e-04

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: 39.69  E-value: 1.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256013056  10 LFDVDDTLTkprnaitneMKELLASLRTK-IKIGVVGGSNFNKIKEQLGE-NFINDFDYVFAENGLIAYKD 78
Cdd:cd01427    3 LFDLDGTLL---------AVELLKRLRAAgIKLAIVTNRSREALRALLEKlGLGDLFDGIIGSDGGGTPKP 64
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 11-133 2.89e-04

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: 40.50  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056  11 FDVDDTLTKPRNAITNEMKELLASLRTK-IKIGVVGGSNFNKIKEQLGEnfINDFDYVFAENG-LIAYKDGSLLEIQDIK 88
Cdd:COG0561    7 LDLDGTLLNDDGEISPRTKEALRRLREKgIKVVIATGRPLRSALPLLEE--LGLDDPLITSNGaLIYDPDGEVLYERPLD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 256013056  89 kylgeeniKKFINFVLHYVADLDIPIkrGTFVEFRNGMLNISPIG 133
Cdd:COG0561   85 --------PEDVREILELLREHGLHL--QVVVRSGPGFLEILPKG 119
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 11-219 3.42e-04

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 40.68  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   11 FDVDDTLTKPRNAITNEMKELLASLRTK-IKIGVVGGSNFNKIK---EQLGENfindfDYVFAENG-LIAYKDGSLLEIQ 85
Cdd:pfam08282   3 SDLDGTLLNSDKKISEKTKEAIKKLKEKgIKFVIATGRPYRAILpviKELGLD-----DPVICYNGaLIYDENGKILYSN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013056   86 DIKKylgeENIKKFINfvlhYVADLDIPIkrgtFVEFRNGMLNISPIGRNCSQQEREEFEKYDLE-------HKIRSTMV 158
Cdd:pfam08282  78 PISK----EAVKEIIE----YLKENNLEI----LLYTDDGVYILNDNELEKILKELNYTKSFVPEiddfellEDEDINKI 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256013056  159 SI---------LKEEFKS-FGLQYSI--GGQISFDVFPIGWDKTYCLRHLPED---EFKTLYFFGDktflGGNDYE 219
Cdd:pfam08282 146 LIlldeedldeLEKELKElFGSLITItsSGPGYLEIMPKGVSKGTALKALAKHlniSLEEVIAFGD----GENDIE 217
 
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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