NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490726596|ref|WP_004589089|]
View 

MULTISPECIES: 3-deoxy-manno-octulosonate-8-phosphatase KdsC [Pseudoalteromonas]

Protein Classification

3-deoxy-manno-octulosonate-8-phosphatase KdsC( domain architecture ID 10013251)

3-deoxy-manno-octulosonate-8-phosphatase KdsC is a HAD (haloacid dehalogenase) family 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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
1-182 2.85e-110

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


:

Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 312.25  E-value: 2.85e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596   1 MQFEDLYQPLSDDAKARAKKVKLLICDIDGVFSDGRIYLGNQGEELKAFNTKDGFGIKALINSGFEVAVITGRHSEIVQT 80
Cdd:PRK09484   1 ASLATCYGPVSDDVMAKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGRKSKLVED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  81 RMSSLTVQHIYQGQEDKLIAYQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTTQMPGGFGA 160
Cdd:PRK09484  81 RMTTLGITHLYQGQSNKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGA 160

                        170       180
                 ....*....|....*....|..
gi 490726596 161 VRELTDLLMLENGIALTTQGTS 182
Cdd:PRK09484 161 VREVCDLLLLAQGKLDEAKGQS 182
 
Name Accession Description Interval E-value
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
1-182 2.85e-110

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 312.25  E-value: 2.85e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596   1 MQFEDLYQPLSDDAKARAKKVKLLICDIDGVFSDGRIYLGNQGEELKAFNTKDGFGIKALINSGFEVAVITGRHSEIVQT 80
Cdd:PRK09484   1 ASLATCYGPVSDDVMAKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGRKSKLVED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  81 RMSSLTVQHIYQGQEDKLIAYQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTTQMPGGFGA 160
Cdd:PRK09484  81 RMTTLGITHLYQGQSNKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGA 160

                        170       180
                 ....*....|....*....|..
gi 490726596 161 VRELTDLLMLENGIALTTQGTS 182
Cdd:PRK09484 161 VREVCDLLLLAQGKLDEAKGQS 182
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 15-173 3.75e-89

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: 258.06  E-value: 3.75e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  15 KARAKKVKLLICDIDGVFSDGRIYLGNQGEELKAFNTKDGFGIKALINSGFEVAVITGRHSEIVQTRMSSLTVQHIYQGQ 94
Cdd:COG1778    2 LERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAEELGITHVYQGV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490726596  95 EDKLIAYQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTTQMPGGFGAVRELTDLLMLENG 173
Cdd:COG1778   82 KDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQG 160
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 21-166 2.11e-71

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: 212.38  E-value: 2.11e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  21 VKLLICDIDGVFSDGRIYLGNQGEELKAFNTKDGFGIKALINSGFEVAVITGRHSEIVQTRMSSLTVQHIYQGQEDKLIA 100
Cdd:cd01630    1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQSEAVRRRAKELGIEDLFQGVKDKLEA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490726596 101 YQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTTQMPGGFGAVRELTD 166
Cdd:cd01630   81 LEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 21-173 8.07e-61

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: 185.81  E-value: 8.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596   21 VKLLICDIDGVFSDGRIYLGNQGEELKAFNTKDGFGIKALINSGFEVAVITGRHSEIVQTRMSSLTVQHIYQGQEDKLIA 100
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKSGIEVAIITGRKAKLVEDRCKTLGITHLYQGQSNKLIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726596  101 YQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTTQMPGGFGAVRELTDLLMLENG 173
Cdd:TIGR01670  81 FSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLAQG 153
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 96-152 1.49e-06

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 46.85  E-value: 1.49e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 490726596   96 DKLIAYQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTT 152
Cdd:pfam08282 187 SKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYVT 243
 
Name Accession Description Interval E-value
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
1-182 2.85e-110

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 312.25  E-value: 2.85e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596   1 MQFEDLYQPLSDDAKARAKKVKLLICDIDGVFSDGRIYLGNQGEELKAFNTKDGFGIKALINSGFEVAVITGRHSEIVQT 80
Cdd:PRK09484   1 ASLATCYGPVSDDVMAKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGRKSKLVED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  81 RMSSLTVQHIYQGQEDKLIAYQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTTQMPGGFGA 160
Cdd:PRK09484  81 RMTTLGITHLYQGQSNKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGA 160

                        170       180
                 ....*....|....*....|..
gi 490726596 161 VRELTDLLMLENGIALTTQGTS 182
Cdd:PRK09484 161 VREVCDLLLLAQGKLDEAKGQS 182
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 15-173 3.75e-89

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: 258.06  E-value: 3.75e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  15 KARAKKVKLLICDIDGVFSDGRIYLGNQGEELKAFNTKDGFGIKALINSGFEVAVITGRHSEIVQTRMSSLTVQHIYQGQ 94
Cdd:COG1778    2 LERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAEELGITHVYQGV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490726596  95 EDKLIAYQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTTQMPGGFGAVRELTDLLMLENG 173
Cdd:COG1778   82 KDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQG 160
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 21-166 2.11e-71

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: 212.38  E-value: 2.11e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  21 VKLLICDIDGVFSDGRIYLGNQGEELKAFNTKDGFGIKALINSGFEVAVITGRHSEIVQTRMSSLTVQHIYQGQEDKLIA 100
Cdd:cd01630    1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQSEAVRRRAKELGIEDLFQGVKDKLEA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490726596 101 YQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTTQMPGGFGAVRELTD 166
Cdd:cd01630   81 LEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 21-173 8.07e-61

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: 185.81  E-value: 8.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596   21 VKLLICDIDGVFSDGRIYLGNQGEELKAFNTKDGFGIKALINSGFEVAVITGRHSEIVQTRMSSLTVQHIYQGQEDKLIA 100
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKSGIEVAIITGRKAKLVEDRCKTLGITHLYQGQSNKLIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726596  101 YQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTTQMPGGFGAVRELTDLLMLENG 173
Cdd:TIGR01670  81 FSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLAQG 153
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 24-161 3.22e-09

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 54.21  E-value: 3.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  24 LICDIDGVFSDG----RIYLGNQGEELKAFNT-KDGFGIKALinsGFEVAVITGRHSEIVQTR-MSSLTVQ--------- 88
Cdd:PRK01158  63 VIAENGGVISVGfdgkRIFLGDIEECEKAYSElKKRFPEAST---SLTKLDPDYRKTEVALRRtVPVEEVRelleelgld 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  89 ----------HIYQGQEDKLIAYQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTTQMPGGF 158
Cdd:PRK01158 140 leivdsgfaiHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVTEKSYGE 219


                 ...
gi 490726596 159 GAV 161
Cdd:PRK01158 220 GVA 222
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 23-161 5.43e-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: 52.21  E-value: 5.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  23 LLICDIDGVFSDGRIYLgnqgeELKAFNTkdgfgIKALINSGFEVAVITGRHSEIVQTRMSSL-TVQHIY--QGQEDKLI 99
Cdd:cd07514    1 LIAVDIDGTLTDRRRSI-----DLRAIEA-----IRKLEKAGIPVVLVTGNSLPVARALAKYLgLSGPVVaeNGGVDKGT 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726596 100 AYQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTTQMPGGFGAV 161
Cdd:cd07514   71 GLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVL 132
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 20-152 2.06e-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: 48.59  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  20 KVKLLICDIDGVFsdgriyLGNQGEELKAfnTKDGfgIKALINSGFEVAVITGRH------------------------- 74
Cdd:COG0561    1 MIKLIALDLDGTL------LNDDGEISPR--TKEA--LRRLREKGIKVVIATGRPlrsalplleelglddplitsngali 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  75 -----SEIVQTRMSSLTVQHIYQGQEDKLIAYQ------------------------ELKNTLKLTDEQIAYIGDDGPDM 125
Cdd:COG0561   71 ydpdgEVLYERPLDPEDVREILELLREHGLHLQvvvrsgpgfleilpkgvskgsalkKLAERLGIPPEEVIAFGDSGNDL 150

                        170       180
                 ....*....|....*....|....*..
gi 490726596 126 PVMERVGFAVAVNDAHPLIKRLSHYTT 152
Cdd:COG0561  151 EMLEAAGLGVAMGNAPPEVKAAADYVT 177
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 22-136 3.44e-07

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 47.40  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596   22 KLLICDIDGVFSDGRIYLGNQGEELKAFNTKDGFgiKALINSGFEVAVITG-----------RHSEIVQTRMSSLTVQHi 90
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVPYVSDEDERILYPEVPDAL--AELKEAGYKVVIVTNqsgigrgyfsrSFSGRVARRLEELGVPI- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490726596   91 yqgqeDKLIAYQE------------LKNTLKLTDEQIAYIGD-DGPDMPVMERVGFAVA 136
Cdd:TIGR01662  78 -----DILYACPGcrkpkpgmfleaLKRFNEIDPEESVYVGDqDLTDLQAAKRVGLATI 131
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 96-152 1.49e-06

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 46.85  E-value: 1.49e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 490726596   96 DKLIAYQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTT 152
Cdd:pfam08282 187 SKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYVT 243
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 4-137 3.38e-03

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: 36.97  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596    4 EDLYQPLSDDAKARAKKVKLLICDIDGVFSDGRIYLGNQGEEL-KAFNTKDGFGIKALINSGFEVAVITGRHSEIVQTRM 82
Cdd:TIGR01484  73 EILYIEPSDVFEEILGIKFEEIGAELKSLSEHYVGTFIEDKAIaVAIHYVGAELGQELDSKMRERLEKIGRNDLELEAIY 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490726596   83 SSLTVQHIYQGQEDKLIAYQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAV 137
Cdd:TIGR01484 153 SGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 55-138 3.56e-03

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: 36.74  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  55 FGIKALINSGFEVA--VITGRHSEIVqtrmssltvqhIYQgqEDKLIAYQELKNTLKLTDEQIAYIGDDGPDMPVMERVG 132
Cdd:COG0560  125 LGIDHVIANELEVEdgRLTGEVVGPI-----------VDG--EGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAG 191


                 ....*.
gi 490726596 133 FAVAVN 138
Cdd:COG0560  192 LPVAVN 197
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 57-137 3.96e-03

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: 35.45  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726596  57 IKALINSGFEVAVITGRHSEIVQTRMSSLTVQHI---YQGQEDKLI------AYQELKNTLKLTDEQIAYIGDDGPDMPV 127
Cdd:cd01427   16 LKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLfdgIIGSDGGGTpkpkpkPLLLLLLKLGVDPEEVLFVGDSENDIEA 95

                         90
                 ....*....|.
gi 490726596 128 MERVG-FAVAV 137
Cdd:cd01427   96 ARAAGgRTVAV 106
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 97-152 5.64e-03

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: 36.05  E-value: 5.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490726596  97 KLIAYQELKNTLKLTDEQIAYIGDDGPDMPVMERVGFAVAVNDAHPLIKRLSHYTT 152
Cdd:cd07517  142 KAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYVT 197
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH