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Conserved domains on  [gi|489189468|ref|WP_003098849|]
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MULTISPECIES: HAD family hydrolase [Pseudomonas]

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 ...
 13-179 9.74e-85

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: 246.89  E-value: 9.74e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  13 RASRIRLAIFDVDGVLTDGKLYFLVDGSEFKTFNTLDGHGIKMLIASGVRTAIITGRDTPVVERRARNLGIQHLYQGRED 92
Cdd:COG1778    4 RAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAEELGITHVYQGVKD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  93 KLAVLDELLGELGLGYEQVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAAREFCELIMRAQGTLE 172
Cdd:COG1778   84 KLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQGKWD 163


                 ....*..
gi 489189468 173 AAQGAYL 179
Cdd:COG1778  164 ALLAAYL 170
 
Name Accession Description Interval E-value
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 13-179 9.74e-85

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: 246.89  E-value: 9.74e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  13 RASRIRLAIFDVDGVLTDGKLYFLVDGSEFKTFNTLDGHGIKMLIASGVRTAIITGRDTPVVERRARNLGIQHLYQGRED 92
Cdd:COG1778    4 RAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAEELGITHVYQGVKD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  93 KLAVLDELLGELGLGYEQVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAAREFCELIMRAQGTLE 172
Cdd:COG1778   84 KLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQGKWD 163


                 ....*..
gi 489189468 173 AAQGAYL 179
Cdd:COG1778  164 ALLAAYL 170
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 17-162 2.85e-66

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: 199.29  E-value: 2.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  17 IRLAIFDVDGVLTDGKLYFLVDGSEFKTFNTLDGHGIKMLIASGVRTAIITGRDTPVVERRARNLGIQHLYQGREDKLAV 96
Cdd:cd01630    1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQSEAVRRRAKELGIEDLFQGVKDKLEA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489189468  97 LDELLGELGLGYEQVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAAREFCE 162
Cdd:cd01630   81 LEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
13-177 5.82e-66

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 199.77  E-value: 5.82e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  13 RASRIRLAIFDVDGVLTDGKLYFLVDGSEFKTFNTLDGHGIKMLIASGVRTAIITGRDTPVVERRARNLGIQHLYQGRED 92
Cdd:PRK09484  17 KAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGRKSKLVEDRMTTLGITHLYQGQSN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  93 KLAVLDELLGELGLGYEQVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAAREFCELIMRAQGTLE 172
Cdd:PRK09484  97 KLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLLLLAQGKLD 176


                 ....*
gi 489189468 173 AAQGA 177
Cdd:PRK09484 177 EAKGQ 181
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 17-169 4.40e-50

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: 158.46  E-value: 4.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468   17 IRLAIFDVDGVLTDGKLYFLVDGSEFKTFNTLDGHGIKMLIASGVRTAIITGRDTPVVERRARNLGIQHLYQGREDKLAV 96
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKSGIEVAIITGRKAKLVEDRCKTLGITHLYQGQSNKLIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489189468   97 LDELLGELGLGYEQVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAAREFCELIMRAQG 169
Cdd:TIGR01670  81 FSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLAQG 153
 
Name Accession Description Interval E-value
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 13-179 9.74e-85

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: 246.89  E-value: 9.74e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  13 RASRIRLAIFDVDGVLTDGKLYFLVDGSEFKTFNTLDGHGIKMLIASGVRTAIITGRDTPVVERRARNLGIQHLYQGRED 92
Cdd:COG1778    4 RAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAEELGITHVYQGVKD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  93 KLAVLDELLGELGLGYEQVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAAREFCELIMRAQGTLE 172
Cdd:COG1778   84 KLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQGKWD 163


                 ....*..
gi 489189468 173 AAQGAYL 179
Cdd:COG1778  164 ALLAAYL 170
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 17-162 2.85e-66

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: 199.29  E-value: 2.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  17 IRLAIFDVDGVLTDGKLYFLVDGSEFKTFNTLDGHGIKMLIASGVRTAIITGRDTPVVERRARNLGIQHLYQGREDKLAV 96
Cdd:cd01630    1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQSEAVRRRAKELGIEDLFQGVKDKLEA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489189468  97 LDELLGELGLGYEQVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAAREFCE 162
Cdd:cd01630   81 LEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
13-177 5.82e-66

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 199.77  E-value: 5.82e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  13 RASRIRLAIFDVDGVLTDGKLYFLVDGSEFKTFNTLDGHGIKMLIASGVRTAIITGRDTPVVERRARNLGIQHLYQGRED 92
Cdd:PRK09484  17 KAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGRKSKLVEDRMTTLGITHLYQGQSN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  93 KLAVLDELLGELGLGYEQVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAAREFCELIMRAQGTLE 172
Cdd:PRK09484  97 KLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLLLLAQGKLD 176


                 ....*
gi 489189468 173 AAQGA 177
Cdd:PRK09484 177 EAKGQ 181
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 17-169 4.40e-50

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: 158.46  E-value: 4.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468   17 IRLAIFDVDGVLTDGKLYFLVDGSEFKTFNTLDGHGIKMLIASGVRTAIITGRDTPVVERRARNLGIQHLYQGREDKLAV 96
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKSGIEVAIITGRKAKLVEDRCKTLGITHLYQGQSNKLIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489189468   97 LDELLGELGLGYEQVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAAREFCELIMRAQG 169
Cdd:TIGR01670  81 FSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLAQG 153
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 19-157 2.65e-06

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: 44.89  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  19 LAIFDVDGVLTDGKLyfLVDGSEFKTFNTLDGHGIKMLIASG------VRTAIITGRDTPVVerrARNLGIqhlyqgreD 92
Cdd:cd07514    1 LIAVDIDGTLTDRRR--SIDLRAIEAIRKLEKAGIPVVLVTGnslpvaRALAKYLGLSGPVV---AENGGV--------D 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489189468  93 KLAVLDELLGELGLGYEQVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAA 157
Cdd:cd07514   68 KGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVL 132
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 110-157 5.21e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 42.27  E-value: 5.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489189468 110 QVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAA 157
Cdd:PRK01158 175 EVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVTEKSYGEGVA 222
P-type_ATPase-Cd_Zn_Co_like cd07548
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to ...
 53-133 1.95e-04

P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to transport cadmium, zinc and cobalt but not copper out of the cell; Bacillus subtilis CadA/YvgW appears to transport cadmium, zinc and cobalt but not copper, out of the cell. Functions in metal ion resistance and cellular metal ion homeostasis. CadA/YvgW is also important for sporulation in B. subtilis, the significant specific expression of the cadA/yvgW gene during the late stage of sporulation, is controlled by forespore-specific sigma factor, sigma G, and mother cell-specific sigma factor, sigma E. This subfamily also includes Helicobacter pylori CadA an essential resistance pump with ion specificity towards Cd(2+), Zn(2+) and Co(2+), and Zn-transporting ATPase, ZiaA(N) in Synechocystis PCC 6803. Transcription of ziaA is induced by Zn under the control of the Zn responsive repressor ZiaR. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319847 [Multi-domain]  Cd Length: 604  Bit Score: 41.07  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  53 IKMLIASGV-RTAIITGRDTPVVERRARNLGIQHLYQG--REDKLAVLDELLGELGLgyeQVAYLGDDLPDLPVIRRVGL 129
Cdd:cd07548  438 IKGLKELGIkNLVMLTGDRKSVAEKVAKKLGIDEVYAEllPEDKVEKVEELKAESKG---KVAFVGDGINDAPVLARADV 514


                 ....
gi 489189468 130 GMAV 133
Cdd:cd07548  515 GIAM 518
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 53-145 2.21e-04

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: 40.21  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189468  53 IKMLIASGVRTAIITGRDTPVVERRARNLGIQHLY-------QGR------------EDKLAVLDELLGELGLGYEQVAY 113
Cdd:COG0560   97 IAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIaneleveDGRltgevvgpivdgEGKAEALRELAAELGIDLEQSYA 176

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489189468 114 LGDDLPDLPVIRRVGLGMAVaSADPFVRQHAH 145
Cdd:COG0560  177 YGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 18-85 7.56e-04

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: 37.77  E-value: 7.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489189468   18 RLAIFDVDGVLTDGKLYFLVDGSEFKTFNTLDghGIKMLIASGVRTAIITG-----------RDTPVVERRARNLGIQH 85
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVPYVSDEDERILYPEVPD--ALAELKEAGYKVVIVTNqsgigrgyfsrSFSGRVARRLEELGVPI 77
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 110-155 1.52e-03

phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases.


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 37.80  E-value: 1.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 489189468  110 QVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEG 155
Cdd:TIGR01487 165 EVAAIGDSENDIDLFRVVGFKVAVANADDQLKEIADYVTSNPYGEG 210
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 110-158 2.02e-03

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: 37.42  E-value: 2.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489189468 110 QVAYLGDDLPDLPVIRRVGLGMAVASADPFVRQHAHGVTAARGGEGAAR 158
Cdd:COG0561  139 EVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAE 187
 
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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