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Conserved domains on  [gi|490585696|ref|WP_004450716|]
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HAD family hydrolase [Leptospira noguchii]

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 ...
 12-173 1.41e-67

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: 203.74  E-value: 1.41e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  12 KEKLKNVELLIIDVDGVLTDGKLYYTEDGEVQKVFDVKDGLGIKLANKE-IILAIMSGNSSAIIKRRAQDLGIKYCFVGI 90
Cdd:COG1778    2 LERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAgIKVAIITGRDSPAVRRRAEELGITHVYQGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  91 VDKAECLRNLMKELNLAKEKVAYIGDDLNDLVVRPLVNCFVCPSDAHRIIIQQSDIVLSSKGGNGAVREFTDRVLIAKGI 170
Cdd:COG1778   82 KDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQGK 161


                 ...
gi 490585696 171 LND 173
Cdd:COG1778  162 WDA 164
 
Name Accession Description Interval E-value
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 12-173 1.41e-67

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: 203.74  E-value: 1.41e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  12 KEKLKNVELLIIDVDGVLTDGKLYYTEDGEVQKVFDVKDGLGIKLANKE-IILAIMSGNSSAIIKRRAQDLGIKYCFVGI 90
Cdd:COG1778    2 LERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAgIKVAIITGRDSPAVRRRAEELGITHVYQGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  91 VDKAECLRNLMKELNLAKEKVAYIGDDLNDLVVRPLVNCFVCPSDAHRIIIQQSDIVLSSKGGNGAVREFTDRVLIAKGI 170
Cdd:COG1778   82 KDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQGK 161


                 ...
gi 490585696 171 LND 173
Cdd:COG1778  162 WDA 164
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 18-162 7.34e-55

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: 170.40  E-value: 7.34e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  18 VELLIIDVDGVLTDGKLYYTEDGEVQKVFDVKDGLGIKLANKE-IILAIMSGNSSAIIKRRAQDLGIKYCFVGIVDKAEC 96
Cdd:cd01630    1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSgIEVAIITGRQSEAVRRRAKELGIEDLFQGVKDKLEA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490585696  97 LRNLMKELNLAKEKVAYIGDDLNDLVVRPLVNCFVCPSDAHRIIIQQSDIVLSSKGGNGAVREFTD 162
Cdd:cd01630   81 LEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
13-173 1.18e-43

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 143.15  E-value: 1.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  13 EKLKNVELLIIDVDGVLTDGKLYYTEDGEVQKVFDVKDGLGIK-LANKEIILAIMSGNSSAIIKRRAQDLGIKYCFVGIV 91
Cdd:PRK09484  16 AKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRcLLTSGIEVAIITGRKSKLVEDRMTTLGITHLYQGQS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  92 DKAECLRNLMKELNLAKEKVAYIGDDLNDLVVRPLVNCFVCPSDAHRIIIQQSDIVLSSKGGNGAVREFTDRVLIAKGIL 171
Cdd:PRK09484  96 NKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLLLLAQGKL 175


                 ..
gi 490585696 172 ND 173
Cdd:PRK09484 176 DE 177
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 18-169 3.33e-43

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: 141.12  E-value: 3.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696   18 VELLIIDVDGVLTDGKLYYTEDGEVQKVFDVKDGLGIKLANK-EIILAIMSGNSSAIIKRRAQDLGIKYCFVGIVDKAEC 96
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKsGIEVAIITGRKAKLVEDRCKTLGITHLYQGQSNKLIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490585696   97 LRNLMKELNLAKEKVAYIGDDLNDLVVRPLVNCFVCPSDAHRIIIQQSDIVLSSKGGNGAVREFTDRVLIAKG 169
Cdd:TIGR01670  81 FSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLAQG 153
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 55-121 3.83e-07

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: 47.97  E-value: 3.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490585696   55 KLANKEIILAIMSGNSSAIIKRRAQDLGIKYCFVGIVD---------KAECLRNLMKELNLAKEKVAYIGDDLNDL 121
Cdd:pfam00702 109 ALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISgddvgvgkpKPEIYLAALERLGVKPEEVLMVGDGVNDI 184
 
Name Accession Description Interval E-value
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 12-173 1.41e-67

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: 203.74  E-value: 1.41e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  12 KEKLKNVELLIIDVDGVLTDGKLYYTEDGEVQKVFDVKDGLGIKLANKE-IILAIMSGNSSAIIKRRAQDLGIKYCFVGI 90
Cdd:COG1778    2 LERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAgIKVAIITGRDSPAVRRRAEELGITHVYQGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  91 VDKAECLRNLMKELNLAKEKVAYIGDDLNDLVVRPLVNCFVCPSDAHRIIIQQSDIVLSSKGGNGAVREFTDRVLIAKGI 170
Cdd:COG1778   82 KDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQGK 161


                 ...
gi 490585696 171 LND 173
Cdd:COG1778  162 WDA 164
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 18-162 7.34e-55

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: 170.40  E-value: 7.34e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  18 VELLIIDVDGVLTDGKLYYTEDGEVQKVFDVKDGLGIKLANKE-IILAIMSGNSSAIIKRRAQDLGIKYCFVGIVDKAEC 96
Cdd:cd01630    1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSgIEVAIITGRQSEAVRRRAKELGIEDLFQGVKDKLEA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490585696  97 LRNLMKELNLAKEKVAYIGDDLNDLVVRPLVNCFVCPSDAHRIIIQQSDIVLSSKGGNGAVREFTD 162
Cdd:cd01630   81 LEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
13-173 1.18e-43

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 143.15  E-value: 1.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  13 EKLKNVELLIIDVDGVLTDGKLYYTEDGEVQKVFDVKDGLGIK-LANKEIILAIMSGNSSAIIKRRAQDLGIKYCFVGIV 91
Cdd:PRK09484  16 AKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRcLLTSGIEVAIITGRKSKLVEDRMTTLGITHLYQGQS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  92 DKAECLRNLMKELNLAKEKVAYIGDDLNDLVVRPLVNCFVCPSDAHRIIIQQSDIVLSSKGGNGAVREFTDRVLIAKGIL 171
Cdd:PRK09484  96 NKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLLLLAQGKL 175


                 ..
gi 490585696 172 ND 173
Cdd:PRK09484 176 DE 177
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 18-169 3.33e-43

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: 141.12  E-value: 3.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696   18 VELLIIDVDGVLTDGKLYYTEDGEVQKVFDVKDGLGIKLANK-EIILAIMSGNSSAIIKRRAQDLGIKYCFVGIVDKAEC 96
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKsGIEVAIITGRKAKLVEDRCKTLGITHLYQGQSNKLIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490585696   97 LRNLMKELNLAKEKVAYIGDDLNDLVVRPLVNCFVCPSDAHRIIIQQSDIVLSSKGGNGAVREFTDRVLIAKG 169
Cdd:TIGR01670  81 FSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLAQG 153
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 20-165 8.08e-12

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: 59.91  E-value: 8.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  20 LLIIDVDGVLTDGKlyYTEDGEVQKVFDvkdglgiKLANKEIILAIMSGNSSAIIKRRAQDLGIKYCFV---GIVDKAEC 96
Cdd:cd07514    1 LIAVDIDGTLTDRR--RSIDLRAIEAIR-------KLEKAGIPVVLVTGNSLPVARALAKYLGLSGPVVaenGGVDKGTG 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490585696  97 LRNLMKELNLAKEKVAYIGDDLNDLVVRPLVNCFVCPSDAHRIIIQQSDIVLSSKGGNGaVREFTDRVL 165
Cdd:cd07514   72 LEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDG-VLEAIDKLL 139
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 20-121 1.26e-08

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: 51.25  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696   20 LLIIDVDGVLTDGKLYYTEDGEVQKVFDVKDGL------GIKLA----NKEIILAIMSGNSSAIIKRRAQDLGIKYCFVG 89
Cdd:TIGR01662   2 AVVLDLDGTLTDDVPYVSDEDERILYPEVPDALaelkeaGYKVVivtnQSGIGRGYFSRSFSGRVARRLEELGVPIDILY 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 490585696   90 IVD-----KAECLRNLMKELN-LAKEKVAYIGD-DLNDL 121
Cdd:TIGR01662  82 ACPgcrkpKPGMFLEALKRFNeIDPEESVYVGDqDLTDL 120
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
35-121 6.99e-08

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 50.31  E-value: 6.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  35 YYTEDGEVQ-KVFD-VKDGLGiKLANKEIILAIMSGNSSAIIKRRAQDLGIKYCFVGIV---------DKAECLRNLMKE 103
Cdd:COG0546   74 LYEEELLDEtRLFPgVRELLE-ALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVggddvppakPKPEPLLEALER 152

                         90
                 ....*....|....*...
gi 490585696 104 LNLAKEKVAYIGDDLNDL 121
Cdd:COG0546  153 LGLDPEEVLMVGDSPHDI 170
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 55-121 3.83e-07

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: 47.97  E-value: 3.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490585696   55 KLANKEIILAIMSGNSSAIIKRRAQDLGIKYCFVGIVD---------KAECLRNLMKELNLAKEKVAYIGDDLNDL 121
Cdd:pfam00702 109 ALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISgddvgvgkpKPEIYLAALERLGVKPEEVLMVGDGVNDI 184
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 20-121 2.79e-06

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: 44.31  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  20 LLIIDVDGVLTdgklyytedgevqkvfdVKDGLGiKLANKEIILAIMSGNSSAIIKRRAQDLGIKYCFVGIV-------- 91
Cdd:cd01427    1 AVLFDLDGTLL-----------------AVELLK-RLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIgsdgggtp 62

                         90       100       110
                 ....*....|....*....|....*....|.
gi 490585696  92 -DKAECLRNLMKELNLAKEKVAYIGDDLNDL 121
Cdd:cd01427   63 kPKPKPLLLLLLKLGVDPEEVLFVGDSENDI 93
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
47-121 4.71e-05

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 41.80  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696   47 DVKDGLgIKLANKEIILAIMSGNSSAIIKRRAQDLGIKYCF---VGIVDK------AECLRNLMKELNLAKEKVAYIGDD 117
Cdd:pfam13419  83 GIKELL-EELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFdviVGGDDVegkkpdPDPILKALEQLGLKPEEVIYVGDS 161


                  ....
gi 490585696  118 LNDL 121
Cdd:pfam13419 162 PRDI 165
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 73-121 2.30e-04

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: 40.06  E-value: 2.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 490585696   73 IIKRRAQDLGIKYCFVGI-------VDKAECLRNLMKELNLAKEKVAYIGDDLNDL 121
Cdd:TIGR01484 140 KIGRNDLELEAIYSGKTDlevlpagVNKGSALQALLQELNGKKDEILAFGDSGNDE 195
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 21-118 4.98e-04

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; The haloacid dehalogenase-like (HAD) hydrolases are 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 include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members 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: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 38.02  E-value: 4.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  21 LIIDVDGVLTDgklYYTEDG--EVQKVFDvkdglgiKLANKEIILAIMSGNSSAIIKRRAQDLGIKYCFVGIVDKAECLR 98
Cdd:cd16416    2 VITDLDNTLLA---WDNPDLtpEVKAWLA-------DLKEAGIKVVLVSNNNERRVAKVIEKLDLPFVARAGKPRPRAFR 71

                         90       100
                 ....*....|....*....|
gi 490585696  99 NLMKELNLAKEKVAYIGDDL 118
Cdd:cd16416   72 RALKEMDLPPEQVAMVGDQL 91
P-type_ATPase-Cd_Zn_Co_like cd07548
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to ...
 63-120 1.15e-03

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: 38.76  E-value: 1.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490585696  63 LAIMSGNSSAIIKRRAQDLGIKYCFVGIV--DKAECLRNLMKELnlaKEKVAYIGDDLND 120
Cdd:cd07548  449 LVMLTGDRKSVAEKVAKKLGIDEVYAELLpeDKVEKVEELKAES---KGKVAFVGDGIND 505
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 91-121 5.57e-03

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 36.45  E-value: 5.57e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 490585696   91 VDKAECLRNLMKELNLAKEKVAYIGDDLNDL 121
Cdd:pfam08282 186 VSKGTALKALAKHLNISLEEVIAFGDGENDI 216
 
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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