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Conserved domains on  [gi|705682853|ref|XP_010119330|]
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PREDICTED: phosphomannomutase 1, partial [Chlamydotis macqueenii]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 1-187 3.37e-118

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member pfam03332:

Pssm-ID: 473868  Cd Length: 220  Bit Score: 333.97  E-value: 3.37e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853    1 IDKFDYVFAENGTVQYKNGHLVSKQAIQDHLGEELLQDLINFCLNYMALLKLPKKRGTFIEFRNGMLNISPIGRSCTPEE 80
Cdd:pfam03332  34 LDEFDYVFSENGLVAYKGGKLLASQSIINHLGEEKLQKLINFCLRYIADLDLPIKRGTFIEFRNGMINVSPIGRNCSQEE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853   81 RIEFSELDKKERIREKFVAALQREFAGKGLRFSRGGMISFDVFPEGWDKRYCLNVLDDERFDTIHFFGNETTPGGNDYEI 160
Cdd:pfam03332 114 RNEFEEYDKKHKIRQKFVEALKEEFADYGLTFSIGGQISFDVFPKGWDKTYCLQHVEKDGFDTIHFFGDKTYPGGNDYEI 193

                         170       180
                  ....*....|....*....|....*..
gi 705682853  161 YDDPRTVGHSVQSPQDTVQRCRKIFFP 187
Cdd:pfam03332 194 FNDPRTIGHSVTSPDDTVRILEELLKL 220
 
Name Accession Description Interval E-value
PMM pfam03332
Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the ...
 1-187 3.37e-118

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: 333.97  E-value: 3.37e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853    1 IDKFDYVFAENGTVQYKNGHLVSKQAIQDHLGEELLQDLINFCLNYMALLKLPKKRGTFIEFRNGMLNISPIGRSCTPEE 80
Cdd:pfam03332  34 LDEFDYVFSENGLVAYKGGKLLASQSIINHLGEEKLQKLINFCLRYIADLDLPIKRGTFIEFRNGMINVSPIGRNCSQEE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853   81 RIEFSELDKKERIREKFVAALQREFAGKGLRFSRGGMISFDVFPEGWDKRYCLNVLDDERFDTIHFFGNETTPGGNDYEI 160
Cdd:pfam03332 114 RNEFEEYDKKHKIRQKFVEALKEEFADYGLTFSIGGQISFDVFPKGWDKTYCLQHVEKDGFDTIHFFGDKTYPGGNDYEI 193

                         170       180
                  ....*....|....*....|....*..
gi 705682853  161 YDDPRTVGHSVQSPQDTVQRCRKIFFP 187
Cdd:pfam03332 194 FNDPRTIGHSVTSPDDTVRILEELLKL 220
HAD_PMM cd02585
phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis ...
 1-184 1.98e-114

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: 325.00  E-value: 1.98e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853   1 IDKFDYVFAENGTVQYKNGHLVSKQAIQDHLGEELLQDLINFCLNYMALLKLPKKRGTFIEFRNGMLNISPIGRSCTPEE 80
Cdd:cd02585   55 LLDFDYVFPENGLVAYRDGELLSRQSIIRALGEEKLQALINFCLRYIADLDLPKKRGTFIEFRNGMINISPIGRNCSQEE 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853  81 RIEFSELDKKERIREKFVAALQREFAGKGLRFSRGGMISFDVFPEGWDKRYCLNVLDDERFDTIHFFGNETTPGGNDYEI 160
Cdd:cd02585  135 RIEFEELDKKHKIREKFVSALKEEFADKGLTFSIGGQISFDVFPKGWDKTYCLRHLEEDLYEEIHFFGDKTQPGGNDYEI 214

                        170       180
                 ....*....|....*....|....
gi 705682853 161 YDDPRTVGHSVQSPQDTVQRCRKI 184
Cdd:cd02585  215 YQDPRTIGHSVTSPKDTVRILEEL 238
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-187 7.73e-105

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 301.10  E-value: 7.73e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853   1 IDKFDYVFAENGTVQYKNGHLVSKQAIQDHLGEELLQDLINFCLNYMALLKLPKKRGTFIEFRNGMLNISPIGRSCTPEE 80
Cdd:PTZ00174  61 LEDFDYVFSENGLVAYKDGELFHSQSILKFLGEEKLKKFINFCLRYIADLDIPVKRGTFIEYRNGMINISPIGRNCSQEE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853  81 RIEFSELDKKERIREKFVAALQREFAGKGLRFSRGGMISFDVFPEGWDKRYCLNVLdDERFDTIHFFGNETTPGGNDYEI 160
Cdd:PTZ00174 141 RDEFEKYDKEHHIREKFIQDLKKEFSDLGLKFSIGGQISFDVFPKGWDKTYCLRHL-ENDFKEIHFFGDKTFEGGNDYEI 219

                        170       180
                 ....*....|....*....|....*..
gi 705682853 161 YDDPRTVGHSVQSPQDTVQRCRKIFFP 187
Cdd:PTZ00174 220 YNDPRTIGHSVKNPEDTIKILKELFLK 246
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 4-169 7.28e-09

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: 53.15  E-value: 7.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853    4 FDYVFAENGTVQYKNGHLVSKQAIQDhlGEELL---QDLINFCLNYMALLKLpkkrGTFIEFRNGMLNISPIGRSCtpee 80
Cdd:TIGR01484  57 PLPLIAENGALIFYPGEILYIEPSDV--FEEILgikFEEIGAELKSLSEHYV----GTFIEDKAIAVAIHYVGAEL---- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853   81 rieFSELDKKERIREKFVAALQREFagkGLRFSrgGMISFDVFPEGWDKRYCLNVLDDERF---DTIHFFGNettpGGND 157
Cdd:TIGR01484 127 ---GQELDSKMRERLEKIGRNDLEL---EAIYS--GKTDLEVLPAGVNKGSALQALLQELNgkkDEILAFGD----SGND 194

                         170
                  ....*....|..
gi 705682853  158 YEIYDDPRTVGH 169
Cdd:TIGR01484 195 EEMFEVAGLAVA 206
 
Name Accession Description Interval E-value
PMM pfam03332
Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the ...
 1-187 3.37e-118

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: 333.97  E-value: 3.37e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853    1 IDKFDYVFAENGTVQYKNGHLVSKQAIQDHLGEELLQDLINFCLNYMALLKLPKKRGTFIEFRNGMLNISPIGRSCTPEE 80
Cdd:pfam03332  34 LDEFDYVFSENGLVAYKGGKLLASQSIINHLGEEKLQKLINFCLRYIADLDLPIKRGTFIEFRNGMINVSPIGRNCSQEE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853   81 RIEFSELDKKERIREKFVAALQREFAGKGLRFSRGGMISFDVFPEGWDKRYCLNVLDDERFDTIHFFGNETTPGGNDYEI 160
Cdd:pfam03332 114 RNEFEEYDKKHKIRQKFVEALKEEFADYGLTFSIGGQISFDVFPKGWDKTYCLQHVEKDGFDTIHFFGDKTYPGGNDYEI 193

                         170       180
                  ....*....|....*....|....*..
gi 705682853  161 YDDPRTVGHSVQSPQDTVQRCRKIFFP 187
Cdd:pfam03332 194 FNDPRTIGHSVTSPDDTVRILEELLKL 220
HAD_PMM cd02585
phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis ...
 1-184 1.98e-114

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: 325.00  E-value: 1.98e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853   1 IDKFDYVFAENGTVQYKNGHLVSKQAIQDHLGEELLQDLINFCLNYMALLKLPKKRGTFIEFRNGMLNISPIGRSCTPEE 80
Cdd:cd02585   55 LLDFDYVFPENGLVAYRDGELLSRQSIIRALGEEKLQALINFCLRYIADLDLPKKRGTFIEFRNGMINISPIGRNCSQEE 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853  81 RIEFSELDKKERIREKFVAALQREFAGKGLRFSRGGMISFDVFPEGWDKRYCLNVLDDERFDTIHFFGNETTPGGNDYEI 160
Cdd:cd02585  135 RIEFEELDKKHKIREKFVSALKEEFADKGLTFSIGGQISFDVFPKGWDKTYCLRHLEEDLYEEIHFFGDKTQPGGNDYEI 214

                        170       180
                 ....*....|....*....|....
gi 705682853 161 YDDPRTVGHSVQSPQDTVQRCRKI 184
Cdd:cd02585  215 YQDPRTIGHSVTSPKDTVRILEEL 238
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-187 7.73e-105

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 301.10  E-value: 7.73e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853   1 IDKFDYVFAENGTVQYKNGHLVSKQAIQDHLGEELLQDLINFCLNYMALLKLPKKRGTFIEFRNGMLNISPIGRSCTPEE 80
Cdd:PTZ00174  61 LEDFDYVFSENGLVAYKDGELFHSQSILKFLGEEKLKKFINFCLRYIADLDIPVKRGTFIEYRNGMINISPIGRNCSQEE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853  81 RIEFSELDKKERIREKFVAALQREFAGKGLRFSRGGMISFDVFPEGWDKRYCLNVLdDERFDTIHFFGNETTPGGNDYEI 160
Cdd:PTZ00174 141 RDEFEKYDKEHHIREKFIQDLKKEFSDLGLKFSIGGQISFDVFPKGWDKTYCLRHL-ENDFKEIHFFGDKTFEGGNDYEI 219

                        170       180
                 ....*....|....*....|....*..
gi 705682853 161 YDDPRTVGHSVQSPQDTVQRCRKIFFP 187
Cdd:PTZ00174 220 YNDPRTIGHSVKNPEDTIKILKELFLK 246
PLN02423 PLN02423
phosphomannomutase
 1-186 1.03e-91

phosphomannomutase


Pssm-ID: 178043 [Multi-domain]  Cd Length: 245  Bit Score: 268.12  E-value: 1.03e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853   1 IDKFDYVFAENGTVQYKNGHLVSKQAIQDHLGEELLQDLINFCLNYMALLKLPKKRGTFIEFRNGMLNISPIGRSCTPEE 80
Cdd:PLN02423  62 INDYDYVFSENGLVAHKDGKLIGTQSLKSFLGEDKLKEFINFTLHYIADLDIPIKRGTFIEFRSGMLNVSPIGRNCSQEE 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853  81 RIEFSELDKKERIREKFVAALQREFAGKGLRFSRGGMISFDVFPEGWDKRYCLNVLDDerFDTIHFFGNETTPGGNDYEI 160
Cdd:PLN02423 142 RDEFEKYDKVHNIRPKMVSVLREKFAHLNLTYSIGGQISFDVFPQGWDKTYCLQFLED--FDEIHFFGDKTYEGGNDHEI 219

                        170       180
                 ....*....|....*....|....*.
gi 705682853 161 YDDPRTVGHSVQSPQDTVQRCRKIFF 186
Cdd:PLN02423 220 FESERTIGHTVTSPDDTREQCTALFL 245
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 4-169 7.28e-09

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: 53.15  E-value: 7.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853    4 FDYVFAENGTVQYKNGHLVSKQAIQDhlGEELL---QDLINFCLNYMALLKLpkkrGTFIEFRNGMLNISPIGRSCtpee 80
Cdd:TIGR01484  57 PLPLIAENGALIFYPGEILYIEPSDV--FEEILgikFEEIGAELKSLSEHYV----GTFIEDKAIAVAIHYVGAEL---- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705682853   81 rieFSELDKKERIREKFVAALQREFagkGLRFSrgGMISFDVFPEGWDKRYCLNVLDDERF---DTIHFFGNettpGGND 157
Cdd:TIGR01484 127 ---GQELDSKMRERLEKIGRNDLEL---EAIYS--GKTDLEVLPAGVNKGSALQALLQELNgkkDEILAFGD----SGND 194

                         170
                  ....*....|..
gi 705682853  158 YEIYDDPRTVGH 169
Cdd:TIGR01484 195 EEMFEVAGLAVA 206
 
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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