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Conserved domains on  [gi|1085344508|gb|OGV17213|]
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MAG: hypothetical protein A2237_19205 [Stygiobacter sp. RIFOXYA2_FULL_38_8]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 12-146 2.76e-19

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


The actual alignment was detected with superfamily member cd01630:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 146  Bit Score: 78.72  E-value: 2.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  12 IKLFLFDLDGVLIS--------KNSIKTtesesqFLLQLRMACEEFLQHDAKLGIVTASnDSLIVKI--KENSKCVMLSD 81
Cdd:cd01630     1 IKLLVLDVDGVLTDgriyydsnGEELKS------FNVRDGLGIKLLQKSGIEVAIITGR-QSEAVRRraKELGIEDLFQG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085344508  82 SINKVKMVDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSSGE 146
Cdd:cd01630    74 VKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGR 138
 
Name Accession Description Interval E-value
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 12-146 2.76e-19

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: 78.72  E-value: 2.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  12 IKLFLFDLDGVLIS--------KNSIKTtesesqFLLQLRMACEEFLQHDAKLGIVTASnDSLIVKI--KENSKCVMLSD 81
Cdd:cd01630     1 IKLLVLDVDGVLTDgriyydsnGEELKS------FNVRDGLGIKLLQKSGIEVAIITGR-QSEAVRRraKELGIEDLFQG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085344508  82 SINKVKMVDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSSGE 146
Cdd:cd01630    74 VKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGR 138
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 5-155 4.42e-19

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: 78.94  E-value: 4.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508   5 FLNKLKEIKLFLFDLDGVLiSKNSIKTTESESQFL-------LQLRMAceefLQHDAKLGIVTASnDSLIV-------KI 70
Cdd:COG1778     1 LLERAKKIKLLIFDVDGVL-TDGRIYYDEDGEELKrfnvrdgLGIKLL----RKAGIKVAIITGR-DSPAVrrraeelGI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  71 KEnskcVMLsDSINKVKMVDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSSGE-VLP 149
Cdd:COG1778    75 TH----VYQ-GVKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRgAVR 149


                  ....*.
gi 1085344508 150 EIIDYL 155
Cdd:COG1778   150 EVCELI 155
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 12-155 3.19e-13

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: 63.31  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  12 IKLFLFDLDGVLISKNSIKTTESES--QFLLQLRMACEEFLQHDAKLGIVTASNDSLIVK-IKENSKCVMLSDSINKVKM 88
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEikAFNVRDGYGIRCALKSGIEVAIITGRKAKLVEDrCKTLGITHLYQGQSNKLIA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344508  89 VDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSSGE-VLPEIIDYL 155
Cdd:TIGR01670  81 FSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRgAVREVCELL 148
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
84-145 1.13e-05

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 43.38  E-value: 1.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085344508  84 NKVKMVDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSSG 145
Cdd:PRK09484   96 NKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGG 157
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 10-142 1.86e-04

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 40.30  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  10 KEIKLFLFDLDGVLISKNSIKTTESESQFLLQlrmaceEFLQHDAKLGIVTASNDSLIVkikenskcvMLSDSINKVKMV 89
Cdd:pfam08282 128 VPEIDDFELLEDEDINKILILLDEEDLDELEK------ELKELFGSLITITSSGPGYLE---------IMPKGVSKGTAL 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1085344508  90 DDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKS 142
Cdd:pfam08282 193 KALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYVTDS 245
 
Name Accession Description Interval E-value
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 12-146 2.76e-19

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: 78.72  E-value: 2.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  12 IKLFLFDLDGVLIS--------KNSIKTtesesqFLLQLRMACEEFLQHDAKLGIVTASnDSLIVKI--KENSKCVMLSD 81
Cdd:cd01630     1 IKLLVLDVDGVLTDgriyydsnGEELKS------FNVRDGLGIKLLQKSGIEVAIITGR-QSEAVRRraKELGIEDLFQG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085344508  82 SINKVKMVDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSSGE 146
Cdd:cd01630    74 VKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGR 138
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 5-155 4.42e-19

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: 78.94  E-value: 4.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508   5 FLNKLKEIKLFLFDLDGVLiSKNSIKTTESESQFL-------LQLRMAceefLQHDAKLGIVTASnDSLIV-------KI 70
Cdd:COG1778     1 LLERAKKIKLLIFDVDGVL-TDGRIYYDEDGEELKrfnvrdgLGIKLL----RKAGIKVAIITGR-DSPAVrrraeelGI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  71 KEnskcVMLsDSINKVKMVDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSSGE-VLP 149
Cdd:COG1778    75 TH----VYQ-GVKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRgAVR 149


                  ....*.
gi 1085344508 150 EIIDYL 155
Cdd:COG1778   150 EVCELI 155
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 12-155 3.19e-13

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: 63.31  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  12 IKLFLFDLDGVLISKNSIKTTESES--QFLLQLRMACEEFLQHDAKLGIVTASNDSLIVK-IKENSKCVMLSDSINKVKM 88
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEikAFNVRDGYGIRCALKSGIEVAIITGRKAKLVEDrCKTLGITHLYQGQSNKLIA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344508  89 VDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSSGE-VLPEIIDYL 155
Cdd:TIGR01670  81 FSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRgAVREVCELL 148
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 14-124 2.16e-08

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: 49.32  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  14 LFLFDLDGVLISKnsikttesesQFLLQLRmaceeflQHDAKLGIVTASNDSLIVKIKENSKCVMLSDSI---------- 83
Cdd:cd01427     1 AVLFDLDGTLLAV----------ELLKRLR-------AAGIKLAIVTNRSREALRALLEKLGLGDLFDGIigsdgggtpk 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1085344508  84 NKVKMVDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGV 124
Cdd:cd01427    64 PKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGRTV 104
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 98-155 3.16e-08

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: 49.51  E-value: 3.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344508  98 ISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSSGEVLPEIIDYL 155
Cdd:cd07514    81 IDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKL 138
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 15-142 3.12e-06

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: 44.74  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  15 FLFDLDGVLISKNSIKTTesesqfllQLRMACEEFLQHDAKLGIVTASNDSLIvkikEnskcvMLSDSINKVKMVDDYLK 94
Cdd:COG0561    69 LIYDPDGEVLYERPLDPE--------DVREILELLREHGLHLQVVVRSGPGFL----E-----ILPKGVSKGSALKKLAE 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1085344508  95 HDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKS 142
Cdd:COG0561   132 RLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYVTGS 179
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
84-145 1.13e-05

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 43.38  E-value: 1.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085344508  84 NKVKMVDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSSG 145
Cdd:PRK09484   96 NKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGG 157
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 98-155 5.45e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 41.50  E-value: 5.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344508  98 ISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSSGEVLPEIIDYL 155
Cdd:PRK01158  171 IDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVTEKSYGEGVAEAIEHL 228
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 10-142 1.86e-04

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 40.30  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  10 KEIKLFLFDLDGVLISKNSIKTTESESQFLLQlrmaceEFLQHDAKLGIVTASNDSLIVkikenskcvMLSDSINKVKMV 89
Cdd:pfam08282 128 VPEIDDFELLEDEDINKILILLDEEDLDELEK------ELKELFGSLITITSSGPGYLE---------IMPKGVSKGTAL 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1085344508  90 DDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKS 142
Cdd:pfam08282 193 KALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYVTDS 245
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 85-142 2.47e-04

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 39.51  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344508  85 KVKMVDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKS 142
Cdd:cd07517   142 KAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYVTKD 199
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 47-132 7.15e-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: 38.28  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  47 EEFLQHDAKLGIVTASNDSLIVKIKE---------------NSKCV-----MLSDSINKVKMVDDYLKHDTISYKQVMYI 106
Cdd:COG0560    98 AEHRAAGHKVAIVSGGFTFFVEPIAErlgidhvianeleveDGRLTgevvgPIVDGEGKAEALRELAAELGIDLEQSYAY 177

                          90       100
                  ....*....|....*....|....*....
gi 1085344508 107 GDDILDIPLLQKVGIsGV---PKDGRREV 132
Cdd:COG0560   178 GDSANDLPMLEAAGL-PVavnPDPALREA 205
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 78-144 2.28e-03

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 36.98  E-value: 2.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  78 MLSDSINK---VKMVDDYLKhdtISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKSSS 144
Cdd:PRK10513  190 ILDKRVNKgtgVKSLAEHLG---IKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNL 256
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 79-142 3.55e-03

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 36.48  E-value: 3.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085344508  79 LSDSINKVKMVDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKS 142
Cdd:TIGR00099 183 TAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALADYVTDS 246
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 83-142 3.64e-03

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 36.42  E-value: 3.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  83 INKVKMVDDYLKHDTISYKQVMYIGDDILDIPLLQKVGISGVPKDGRREVKRVVNFITKS 142
Cdd:cd07516   182 VSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEAADYVTLT 241
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 13-120 7.79e-03

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: 34.69  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344508  13 KLFLFDLDGVLISKNSIKTTESESQFLLQLRMACEEFLQHDAKLGIVTASNDSLIVKIKENSKCVMLSDSI--------- 83
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVPYVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRSFSGRVARRLEelgvpidil 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1085344508  84 --------NKVKMVDDYLKH-DTISYKQVMYIGDDIL-DIPLLQKVG 120
Cdd:TIGR01662  81 yacpgcrkPKPGMFLEALKRfNEIDPEESVYVGDQDLtDLQAAKRVG 127
 
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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