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Conserved domains on  [gi|1756648666|gb|KAB1323846|]
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HAD-IIIA family hydrolase [Bacteroides ovatus]

Protein Classification

KdsC family phosphatase( domain architecture ID 10004505)

KdsC family phosphatase such as 3-deoxy-manno-octulosonate-8-phosphatase KdsC, a HAD (haloacid dehalogenase) superfamily hydrolase that catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate

CATH:  3.30.1240.10
EC:  3.1.3.-
Gene Ontology:  GO:0016788
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 4-166 2.74e-78

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


:

Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 230.32  E-value: 2.74e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666   4 INYDLSRIKALAFDVDGVLSSTTVPLHPSGEPMRTVNIKDGYAIQLAVKKGLHIAIITGGRTEAVRIRFEGLGVKDLYMG 83
Cdd:COG1778     1 LLERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAEELGITHVYQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  84 SAVKIHDYRAFRDKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYISYADGGRGCGRDVVEQVLKAHG 163
Cdd:COG1778    81 VKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQG 160


                  ...
gi 1756648666 164 LWM 166
Cdd:COG1778   161 KWD 163
 
Name Accession Description Interval E-value
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 4-166 2.74e-78

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 230.32  E-value: 2.74e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666   4 INYDLSRIKALAFDVDGVLSSTTVPLHPSGEPMRTVNIKDGYAIQLAVKKGLHIAIITGGRTEAVRIRFEGLGVKDLYMG 83
Cdd:COG1778     1 LLERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAEELGITHVYQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  84 SAVKIHDYRAFRDKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYISYADGGRGCGRDVVEQVLKAHG 163
Cdd:COG1778    81 VKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQG 160


                  ...
gi 1756648666 164 LWM 166
Cdd:COG1778   161 KWD 163
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 11-156 2.09e-65

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. 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: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 196.59  E-value: 2.09e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  11 IKALAFDVDGVLSSTTVPLHPSGEPMRTVNIKDGYAIQLAVKKGLHIAIITGGRTEAVRIRFEGLGVKDLYMGSAVKIHD 90
Cdd:cd01630     1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQSEAVRRRAKELGIEDLFQGVKDKLEA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1756648666  91 YRAFRDKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYISYADGGRGCGRDVVE 156
Cdd:cd01630    81 LEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 11-164 5.02e-36

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. One member of this family, the YrbI protein from H. influenzae has been cloned, expressed, purified and found to be an active 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase. Furthermore, its crystal structure has been determined. This family consists of sequences from beta, gamma and epsilon proteobacteria, Aquifex, Fusobacterium, Porphyromonas and Methanosarcina. The Methanosarcina sequence is distinctive in that it is linked to an N-terminal cytidylyltransferase domain (pfam02348) and is annotated as acylneuraminate cytidylyltransferase. This may give some clue as the function of these phosphatases. Several eukaryotic sequences scoring between trusted and noise are also closely related to this function such as the CMP-N-acetylneuraminic acid synthetase from mouse, but in these cases the phosphatase domain is clearly inactive as many of the active site residues are not conserved. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130731 [Multi-domain]  Cd Length: 154  Bit Score: 122.63  E-value: 5.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  11 IKALAFDVDGVLSSTTVPLHPSGEPMRTVNIKDGYAIQLAVKKGLHIAIITGGRTEAVRIRFEGLGVKDLYMGSAVKIHD 90
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKSGIEVAIITGRKAKLVEDRCKTLGITHLYQGQSNKLIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756648666  91 YRAFRDKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYISYADGGRGCGRDVVEQVLKAHGL 164
Cdd:TIGR01670  81 FSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLAQGK 154
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
9-163 2.73e-34

3-deoxy-manno-octulosonate-8-phosphatase KdsC;


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 118.88  E-value: 2.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666   9 SRIKALAFDVDGVLSSTTVPLHPSGEPMRTVNIKDGYAIQLAVKKGLHIAIITGGRTEAVRIRFEGLGVKDLYMGSAVKI 88
Cdd:PRK09484   19 ENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGRKSKLVEDRMTTLGITHLYQGQSNKL 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1756648666  89 HDYRAFRDKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYISYADGGRGCGRDVVEQVLKAHG 163
Cdd:PRK09484   99 IAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLLLLAQG 173
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 98-147 5.41e-04

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 39.14  E-value: 5.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1756648666  98 YGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYI--SYADGG 147
Cdd:pfam08282 199 LNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYVtdSNNEDG 250
 
Name Accession Description Interval E-value
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 4-166 2.74e-78

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 230.32  E-value: 2.74e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666   4 INYDLSRIKALAFDVDGVLSSTTVPLHPSGEPMRTVNIKDGYAIQLAVKKGLHIAIITGGRTEAVRIRFEGLGVKDLYMG 83
Cdd:COG1778     1 LLERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAEELGITHVYQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  84 SAVKIHDYRAFRDKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYISYADGGRGCGRDVVEQVLKAHG 163
Cdd:COG1778    81 VKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQG 160


                  ...
gi 1756648666 164 LWM 166
Cdd:COG1778   161 KWD 163
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 11-156 2.09e-65

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. 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: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 196.59  E-value: 2.09e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  11 IKALAFDVDGVLSSTTVPLHPSGEPMRTVNIKDGYAIQLAVKKGLHIAIITGGRTEAVRIRFEGLGVKDLYMGSAVKIHD 90
Cdd:cd01630     1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQSEAVRRRAKELGIEDLFQGVKDKLEA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1756648666  91 YRAFRDKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYISYADGGRGCGRDVVE 156
Cdd:cd01630    81 LEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 11-164 5.02e-36

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. One member of this family, the YrbI protein from H. influenzae has been cloned, expressed, purified and found to be an active 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase. Furthermore, its crystal structure has been determined. This family consists of sequences from beta, gamma and epsilon proteobacteria, Aquifex, Fusobacterium, Porphyromonas and Methanosarcina. The Methanosarcina sequence is distinctive in that it is linked to an N-terminal cytidylyltransferase domain (pfam02348) and is annotated as acylneuraminate cytidylyltransferase. This may give some clue as the function of these phosphatases. Several eukaryotic sequences scoring between trusted and noise are also closely related to this function such as the CMP-N-acetylneuraminic acid synthetase from mouse, but in these cases the phosphatase domain is clearly inactive as many of the active site residues are not conserved. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130731 [Multi-domain]  Cd Length: 154  Bit Score: 122.63  E-value: 5.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  11 IKALAFDVDGVLSSTTVPLHPSGEPMRTVNIKDGYAIQLAVKKGLHIAIITGGRTEAVRIRFEGLGVKDLYMGSAVKIHD 90
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKSGIEVAIITGRKAKLVEDRCKTLGITHLYQGQSNKLIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756648666  91 YRAFRDKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYISYADGGRGCGRDVVEQVLKAHGL 164
Cdd:TIGR01670  81 FSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLAQGK 154
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
9-163 2.73e-34

3-deoxy-manno-octulosonate-8-phosphatase KdsC;


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 118.88  E-value: 2.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666   9 SRIKALAFDVDGVLSSTTVPLHPSGEPMRTVNIKDGYAIQLAVKKGLHIAIITGGRTEAVRIRFEGLGVKDLYMGSAVKI 88
Cdd:PRK09484   19 ENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGRKSKLVEDRMTTLGITHLYQGQSNKL 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1756648666  89 HDYRAFRDKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYISYADGGRGCGRDVVEQVLKAHG 163
Cdd:PRK09484   99 IAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLLLLAQG 173
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 13-149 2.35e-09

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: 52.98  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  13 ALAFDVDGVLSsttvplhpsgEPMRTVNIKDGYAIQLAVKKGLHIAIITGG-----RTEAVRIRFEGLGV-------Kdl 80
Cdd:cd07514     1 LIAVDIDGTLT----------DRRRSIDLRAIEAIRKLEKAGIPVVLVTGNslpvaRALAKYLGLSGPVVaenggvdK-- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1756648666  81 ymGSAVKIhdyraFRDKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYISYADGGRG 149
Cdd:cd07514    69 --GTGLEK-----LAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDG 130
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 10-146 3.97e-09

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: 53.22  E-value: 3.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  10 RIKALAFDVDGVLssttvpLHPSGE-PMRTVNikdgyAIQLAVKKGLHIAIITGGRTEAVRIRFEGLGVKDLYMGS--AV 86
Cdd:COG0561     1 MIKLIALDLDGTL------LNDDGEiSPRTKE-----ALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSngAL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  87 kIHDY-----------------------------------------------------RAFRDKYGLTDDEILYMGDDVP 113
Cdd:COG0561    70 -IYDPdgevlyerpldpedvreilellrehglhlqvvvrsgpgfleilpkgvskgsalKKLAERLGIPPEEVIAFGDSGN 148

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1756648666 114 DIEVMCECGLPCCPKDAVPEVKSVAKYI---SYADG 146
Cdd:COG0561   149 DLEMLEAAGLGVAMGNAPPEVKAAADYVtgsNDEDG 184
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 98-147 5.41e-04

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 39.14  E-value: 5.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1756648666  98 YGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYI--SYADGG 147
Cdd:pfam08282 199 LNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYVtdSNNEDG 250
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 96-142 8.75e-04

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: 38.36  E-value: 8.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1756648666  96 DKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYIS 142
Cdd:cd07517   151 EHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYVT 197
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 96-147 1.07e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 38.03  E-value: 1.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1756648666  96 DKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYI---SYADGG 147
Cdd:PRK01158  167 ELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVtekSYGEGV 221
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 96-141 1.92e-03

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: 37.57  E-value: 1.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1756648666  96 DKYGLTDDEILYMGDDVPDIEvMCEC-GLPCCPKDAVPEVKSVAKYI 141
Cdd:cd07516   193 EYLGISLEEVIAFGDNENDLS-MLEYaGLGVAMGNAIDEVKEAADYV 238
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 14-123 2.08e-03

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 35.90  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  14 LAFDVDGVLSSTTVPLHPSGEpmrtvnikdgyAIQLAVKKGLHIAIIT--GGRTEAVRI-RFEGLGV---KDLYMGSAVK 87
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAE-----------ALRALRAAGKPVVFVTnnSSRSREEYAeKLRKLGFdidEDEIITSGTA 69

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1756648666  88 IHDYRAFRDKYGLtddeILYMGDDvPDIEVMCECGL 123
Cdd:pfam13344  70 AADYLKERKFGKK----VLVIGSE-GLREELEEAGF 100
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 83-147 2.12e-03

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: 37.25  E-value: 2.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1756648666  83 GSAVkihdyRAFRDKYGLTDDEILYMGDDVPDIEVMCECGLPCCPKDAVPEVKSVAKYI--SYADGG 147
Cdd:TIGR00099 190 GSAL-----QSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALADYVtdSNNEDG 251
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 46-116 6.25e-03

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: 35.64  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756648666  46 AIQLAVKKGLHIAIITGGRTEAVRIRFEGLGVKDLYMGSAVKI---------HDYRAFRDKYGLTDDEILYMGDDVPDIE 116
Cdd:pfam00702 106 ALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDdvgvgkpkpEIYLAALERLGVKPEEVLMVGDGVNDIP 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
52-116 9.03e-03

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 35.25  E-value: 9.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756648666  52 KKGLHIAIITGGRTEAVRIRFEGLGVKDL----YMGSAVKIHD-----YRAFRDKYGLTDDEILYMGDDVPDIE 116
Cdd:pfam13419  93 EQGYKLGIVTSKSRENVEEFLKQLGLEDYfdviVGGDDVEGKKpdpdpILKALEQLGLKPEEVIYVGDSPRDIE 166
 
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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