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Conserved domains on  [gi|17132640|dbj|BAB75206|]
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alr3507 [Nostoc sp. PCC 7120 = FACHB-418]

Protein Classification

YqeG family HAD IIIA-type phosphatase( domain architecture ID 11493037)

YqeG family HAD (haloacid dehalogenase) IIIA-type phosphatase similar to Bacillus subtilis YqeG, which may be involved in the hydrolysis of the phosphate group of 5'-nucleotides and is necessary for normal colony formation on solid medium

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 20-190 1.58e-84

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical 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. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.


:

Pssm-ID: 273744  Cd Length: 170  Bit Score: 246.93  E-value: 1.58e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640    20 PDKLPKQIL-TLAEVKIDWLKNAGIRGVILDLDNTIISEDDRYLAPWAEDWIAEAKLAGLKLFILSNGKRRYRVKYWSHR 98
Cdd:TIGR01668   1 KFCLPHAIVkTLNDLTIDLLKKVGIKGVVLDKDNTLVYPDHNEAYPALRDWIEELKAAGRKLLIVSNNAGEQRAKAVEKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640    99 LDINAISPAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVASLPHPLRWWEKLAGKWVQIPYPkg 178
Cdd:TIGR01668  81 LGIPVLPHAVKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDQWFIKRIWRRVERTVL-- 158

                         170
                  ....*....|..
gi 17132640   179 KELWDFEGAFGY 190
Cdd:TIGR01668 159 KFLVSRGGPAPE 170
 
Name Accession Description Interval E-value
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 20-190 1.58e-84

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical 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. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.


Pssm-ID: 273744  Cd Length: 170  Bit Score: 246.93  E-value: 1.58e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640    20 PDKLPKQIL-TLAEVKIDWLKNAGIRGVILDLDNTIISEDDRYLAPWAEDWIAEAKLAGLKLFILSNGKRRYRVKYWSHR 98
Cdd:TIGR01668   1 KFCLPHAIVkTLNDLTIDLLKKVGIKGVVLDKDNTLVYPDHNEAYPALRDWIEELKAAGRKLLIVSNNAGEQRAKAVEKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640    99 LDINAISPAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVASLPHPLRWWEKLAGKWVQIPYPkg 178
Cdd:TIGR01668  81 LGIPVLPHAVKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDQWFIKRIWRRVERTVL-- 158

                         170
                  ....*....|..
gi 17132640   179 KELWDFEGAFGY 190
Cdd:TIGR01668 159 KFLVSRGGPAPE 170
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
19-170 2.74e-54

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];


Pssm-ID: 441782  Cd Length: 164  Bit Score: 169.93  E-value: 2.74e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  19 QPDKLPKQILtlaEVKIDWLKNAGIRGVILDLDNTIISEDDRYLAPWAEDWIAEAKLAGLKLFILSNGKRRyRVKYWSHR 98
Cdd:COG2179   5 KPDEYVKSIY---DIDPEKLKEKGIKGLILDLDNTLVPWDEPEATPEVIEWLEELKEAGFKVCIVSNNSEK-RVKRFAEK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17132640  99 LDINAISPAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVASLPHP-------LRWWEKLAGKW 170
Cdd:COG2179  81 LGIPYIARAKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKPLVDKefwftriNRFLERRILKR 159
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 45-153 5.70e-29

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: 103.89  E-value: 5.70e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  45 GVILDLDNTIISEDDRYLAPWAEDWIAEAKLAGLKLFILSNGKRRyRVKYWSHRLDINAISPAKKPFPSAFRKAMTQMRL 124
Cdd:cd16416   1 GVITDLDNTLLAWDNPDLTPEVKAWLADLKEAGIKVVLVSNNNER-RVAKVIEKLDLPFVARAGKPRPRAFRRALKEMDL 79

                        90       100
                ....*....|....*....|....*....
gi 17132640 125 SSKNVLVIGDSLHTDVMGAKFSGCRCIQV 153
Cdd:cd16416  80 PPEQVAMVGDQLFTDILGGNRAGLYTILV 108
Hydrolase_like pfam13242
HAD-hyrolase-like;
109-155 3.05e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 54.16  E-value: 3.05e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 17132640   109 KPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVAS 155
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLT 50
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 70-151 1.22e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 41.62  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640   70 IAEAKLAGLKL------------FILSN--GKRRYRvkywshRLDINA--ISPAKKPFPSAFRKAMTQMRLSSKNVLVIG 133
Cdd:PLN02779 153 MDEALAAGIKVavcstsnekavsKIVNTllGPERAQ------GLDVFAgdDVPKKKPDPDIYNLAAETLGVDPSRCVVVE 226

                         90
                 ....*....|....*...
gi 17132640  134 DSlHTDVMGAKFSGCRCI 151
Cdd:PLN02779 227 DS-VIGLQAAKAAGMRCI 243
 
Name Accession Description Interval E-value
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 20-190 1.58e-84

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical 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. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.


Pssm-ID: 273744  Cd Length: 170  Bit Score: 246.93  E-value: 1.58e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640    20 PDKLPKQIL-TLAEVKIDWLKNAGIRGVILDLDNTIISEDDRYLAPWAEDWIAEAKLAGLKLFILSNGKRRYRVKYWSHR 98
Cdd:TIGR01668   1 KFCLPHAIVkTLNDLTIDLLKKVGIKGVVLDKDNTLVYPDHNEAYPALRDWIEELKAAGRKLLIVSNNAGEQRAKAVEKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640    99 LDINAISPAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVASLPHPLRWWEKLAGKWVQIPYPkg 178
Cdd:TIGR01668  81 LGIPVLPHAVKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDQWFIKRIWRRVERTVL-- 158

                         170
                  ....*....|..
gi 17132640   179 KELWDFEGAFGY 190
Cdd:TIGR01668 159 KFLVSRGGPAPE 170
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
19-170 2.74e-54

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];


Pssm-ID: 441782  Cd Length: 164  Bit Score: 169.93  E-value: 2.74e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  19 QPDKLPKQILtlaEVKIDWLKNAGIRGVILDLDNTIISEDDRYLAPWAEDWIAEAKLAGLKLFILSNGKRRyRVKYWSHR 98
Cdd:COG2179   5 KPDEYVKSIY---DIDPEKLKEKGIKGLILDLDNTLVPWDEPEATPEVIEWLEELKEAGFKVCIVSNNSEK-RVKRFAEK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17132640  99 LDINAISPAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVASLPHP-------LRWWEKLAGKW 170
Cdd:COG2179  81 LGIPYIARAKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKPLVDKefwftriNRFLERRILKR 159
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 45-153 5.70e-29

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: 103.89  E-value: 5.70e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  45 GVILDLDNTIISEDDRYLAPWAEDWIAEAKLAGLKLFILSNGKRRyRVKYWSHRLDINAISPAKKPFPSAFRKAMTQMRL 124
Cdd:cd16416   1 GVITDLDNTLLAWDNPDLTPEVKAWLADLKEAGIKVVLVSNNNER-RVAKVIEKLDLPFVARAGKPRPRAFRRALKEMDL 79

                        90       100
                ....*....|....*....|....*....
gi 17132640 125 SSKNVLVIGDSLHTDVMGAKFSGCRCIQV 153
Cdd:cd16416  80 PPEQVAMVGDQLFTDILGGNRAGLYTILV 108
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 44-155 2.15e-25

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: 95.55  E-value: 2.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640    44 RGVILDLDNTII-------SEDDRYLAPWAEDWIAEAKLAGLKLFILSNGK---RRY-------RVKYWSHRLDIN---- 102
Cdd:TIGR01662   1 KAVVLDLDGTLTddvpyvsDEDERILYPEVPDALAELKEAGYKVVIVTNQSgigRGYfsrsfsgRVARRLEELGVPidil 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17132640   103 -AISPAKKPFPSAFRKAMTQM-RLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVAS 155
Cdd:TIGR01662  81 yACPGCRKPKPGMFLEALKRFnEIDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
109-155 4.97e-11

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 59.74  E-value: 4.97e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 17132640 109 KPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVAS 155
Cdd:COG0647 186 KPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLT 232
Hydrolase_like pfam13242
HAD-hyrolase-like;
109-155 3.05e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 54.16  E-value: 3.05e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 17132640   109 KPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVAS 155
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLT 50
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 21-153 3.23e-10

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 57.35  E-value: 3.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  21 DKLPKQILTLAEVKIDWLKNAGIrGVILDLDNTIISEDDRYLAPW--AEDWIAEAKLAGLKLFILSNGKRRYrVKYWSHR 98
Cdd:COG1011  52 RRYERGEITFAELLRRLLEELGL-DLAEELAEAFLAALPELVEPYpdALELLEALKARGYRLALLTNGSAEL-QEAKLRR 129

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17132640  99 LDINA------IS---PAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQV 153
Cdd:COG1011 130 LGLDDlfdavvSSeevGVRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWV 193
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 45-153 3.29e-10

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: 55.09  E-value: 3.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  45 GVILDLDNTIiseddrylapWAEDWIAEAKLAGLKLFILSNGKRRYrVKYWSHRLDINAI---------SPAKKPFPSAF 115
Cdd:cd01427   1 AVLFDLDGTL----------LAVELLKRLRAAGIKLAIVTNRSREA-LRALLEKLGLGDLfdgiigsdgGGTPKPKPKPL 69

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17132640 116 RKAMTQMRLSSKNVLVIGDSlHTDVMGAKFSGCRCIQV 153
Cdd:cd01427  70 LLLLLKLGVDPEEVLFVGDS-ENDIEAARAAGGRTVAV 106
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 26-147 7.07e-09

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: 52.97  E-value: 7.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640    26 QILTLAEVKIDWLKNAGIRGVILDLDNTIISEDDRYLAPWAEDWIAEAKLAGLKLFILSNGKRRyRVKYWSHRLDINA-- 103
Cdd:pfam00702  63 EELDILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPE-AAEALLRLLGLDDyf 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17132640   104 -------ISPAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLhTDVMGAKFSG 147
Cdd:pfam00702 142 dvvisgdDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGV-NDIPAAKAAG 191
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
62-154 9.06e-09

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 53.01  E-value: 9.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  62 LAPWAEDWIAEAKLAGLKLFILSNgKRRYRVKYWSHRLDIN----AI-----SPAKKPFPSAFRKAMTQMRLSSKNVLVI 132
Cdd:COG0546  85 LFPGVRELLEALKARGIKLAVVTN-KPREFAERLLEALGLDdyfdAIvggddVPPAKPKPEPLLEALERLGLDPEEVLMV 163

                        90       100
                ....*....|....*....|..
gi 17132640 133 GDSLHtDVMGAKFSGCRCIQVA 154
Cdd:COG0546 164 GDSPH-DIEAARAAGVPFIGVT 184
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 46-144 4.25e-08

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 49.08  E-value: 4.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  46 VILDLDNTIIseddrylaPWAEDWIAEAKlAGLKLFILSNGkrrYRVKYWS--HRLDINA------IS---PAKKPFPSA 114
Cdd:cd04305   2 IIFDLDDTLL--------PGAKELLEELK-KGYKLGIITNG---PTEVQWEklEQLGIHKyfdhivISeevGVQKPNPEI 69

                        90       100       110
                ....*....|....*....|....*....|
gi 17132640 115 FRKAMTQMRLSSKNVLVIGDSLHTDVMGAK 144
Cdd:cd04305  70 FDYALNQLGVKPEETLMVGDSLESDILGAK 99
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 46-151 2.54e-07

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; 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: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 47.67  E-value: 2.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  46 VILDLDNTIIseddrylapwAEDWIAEAKLAGLKLFILSNGKRRYRV--------KYWSHRLdINAISPAKKPFPSAFRK 117
Cdd:cd16415   2 ITFDVTGTLL----------AVETLKDLKEKGLKLAVVSNFDRRLREllealgldDYFDFVV-FSYEVGYEKPDPRIFQK 70

                        90       100       110
                ....*....|....*....|....*....|....
gi 17132640 118 AMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCI 151
Cdd:cd16415  71 ALERLGVSPEEALHVGDDLKNDYLGARAVGWHAL 104
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 45-155 3.03e-07

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It 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: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 47.61  E-value: 3.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  45 GVILDLDNTII-SED---------DRY--------------LAPWAEDWIAEAKLAGLKLFILSNGKRRyRVKYWSHRLD 100
Cdd:cd07505   1 AVIFDMDGVLIdTEPlhrqawqllERKnallleliaseglkLKPGVVELLDALKAAGIPVAVATSSSRR-NVELLLLELG 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17132640 101 IN-----AIS-----PAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLHTdVMGAKFSGCRCIQVAS 155
Cdd:cd07505  80 LLrgyfdVIVsgddvERGKPAPDIYLLAAERLGVDPERCLVFEDSLAG-IEAAKAAGMTVVAVPD 143
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
66-159 8.08e-07

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 47.51  E-value: 8.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  66 AEDWIAEAKLAGLKLFILSNGKRRyRVKywsHRLDINAISP------------AKKPFPSAFRKAMTQMRLSSKNVLVIG 133
Cdd:COG0637  91 VVELLEALKEAGIKIAVATSSPRE-NAE---AVLEAAGLLDyfdvivtgddvaRGKPDPDIYLLAAERLGVDPEECVVFE 166

                        90       100
                ....*....|....*....|....*.
gi 17132640 134 DSLhTDVMGAKFSGCRCIQVASLPHP 159
Cdd:COG0637 167 DSP-AGIRAAKAAGMRVVGVPDGGTA 191
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
70-153 1.51e-06

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 46.42  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640    70 IAEAKLAGLKLFILSNGKRRYRVKYWSHrldINAIS-----------PAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLHt 138
Cdd:pfam13419  88 LEELKEQGYKLGIVTSKSRENVEEFLKQ---LGLEDyfdvivggddvEGKKPDPDPILKALEQLGLKPEEVIYVGDSPR- 163

                          90
                  ....*....|....*
gi 17132640   139 DVMGAKFSGCRCIQV 153
Cdd:pfam13419 164 DIEAAKNAGIKVIAV 178
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 57-144 4.75e-06

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 44.69  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640    57 EDDRYLAPWAEDWIAEAKLAGLKLFILSNGKRRYRVKYWSHRLDINAIS-------PAKKPFPSAFRKAMTQMRLSSKnV 129
Cdd:TIGR01549  69 DAEEAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFElilvsdePGSKPEPEIFLAALESLGVPPE-V 147

                          90
                  ....*....|....*
gi 17132640   130 LVIGDSLHtDVMGAK 144
Cdd:TIGR01549 148 LHVGDNLN-DIEGAR 161
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 70-155 5.26e-05

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 41.86  E-value: 5.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  70 IAEAKLAGLKLFILSNGKRRyRVKYWSHRLDI----NAISPAK-----KPFPSAFRKAMTQMRLSSKNVLVIGDSLHtDV 140
Cdd:cd16423  53 LEFLKEKGIKLAVASSSPRR-WIEPHLERLGLldyfEVIVTGDdveksKPDPDLYLEAAERLGVNPEECVVIEDSRN-GV 130

                        90
                ....*....|....*
gi 17132640 141 MGAKFSGCRCIQVAS 155
Cdd:cd16423 131 LAAKAAGMKCVGVPN 145
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 109-155 5.56e-05

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; 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: 319827 [Multi-domain]  Cd Length: 253  Bit Score: 42.31  E-value: 5.56e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17132640 109 KPFPSAFRKAMTQMRLSSKN-VLVIGDSLHTDVMGAKFSGCRCIQVAS 155
Cdd:cd07525 183 KPHPPIYDLALARLGRPAKArILAVGDGLHTDILGANAAGLDSLFVTG 230
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 46-171 7.68e-05

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 41.62  E-value: 7.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  46 VILDLDNTIIsEDDRYLA--------PWAEDWIAEAKLAGLKLFILSN----GKRRY------RVKYWSHRL------DI 101
Cdd:COG0241   6 VFLDRDGTIN-EDVGYVKspeefeflPGVLEALARLNEAGYRLVVVTNqsgiGRGLFteedlnAVHAKMLELlaaeggRI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640 102 NAI----------SPAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLhTDVMGAKFSGCRCIQVASlPHPLRWWEKLAGKWV 171
Cdd:COG0241  85 DAIyycphhpddnCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRL-SDLQAAKAAGCKGILVLT-GKGAEELAEALPDTV 162
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 106-153 8.08e-05

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and 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 (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. 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: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 41.84  E-value: 8.08e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17132640 106 PAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLhTDVMGAKFSGCRCIQV 153
Cdd:cd16417 140 PEKKPDPAPLLHACEKLGIAPAQMLMVGDSR-NDILAARAAGCPSVGL 186
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 109-155 1.09e-04

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 41.42  E-value: 1.09e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 17132640 109 KPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVAS 155
Cdd:cd07530 177 KPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLT 223
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 70-151 1.22e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 41.62  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640   70 IAEAKLAGLKL------------FILSN--GKRRYRvkywshRLDINA--ISPAKKPFPSAFRKAMTQMRLSSKNVLVIG 133
Cdd:PLN02779 153 MDEALAAGIKVavcstsnekavsKIVNTllGPERAQ------GLDVFAgdDVPKKKPDPDIYNLAAETLGVDPSRCVVVE 226

                         90
                 ....*....|....*...
gi 17132640  134 DSlHTDVMGAKFSGCRCI 151
Cdd:PLN02779 227 DS-VIGLQAAKAAGMRCI 243
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 109-153 2.84e-04

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 40.34  E-value: 2.84e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17132640 109 KPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQV 153
Cdd:cd07509 172 KPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILV 216
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 62-151 3.13e-04

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 40.06  E-value: 3.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132640  62 LAPWAEDWIAEAKLAGLKLFILSNGK--------RRYRVKYWSHRLDINA---ISPAKKPFPSAFRKAMTQMRLSSKNVL 130
Cdd:cd07528  96 LRPGVARLIDEAKAAGVRLAIATTTSpanvdallSALLGPERRAIFDAIAagdDVAEKKPDPDIYLLALERLGVSPSDCL 175

                        90       100
                ....*....|....*....|.
gi 17132640 131 VIGDSLHtDVMGAKFSGCRCI 151
Cdd:cd07528 176 AIEDSAI-GLQAAKAAGLPCI 195
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
 109-143 8.53e-04

HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram negative and primarily alpha proteobacteria. Only one sequence hase been annotated as other than "hypothetical." That one, from Brucella, is annotated as related to NagD, but only by sequence similarity and should be treated with some skepticism. (See comments for Class IIA subfamily model)


Pssm-ID: 130526 [Multi-domain]  Cd Length: 242  Bit Score: 39.11  E-value: 8.53e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 17132640   109 KPFPSAFRKAMTQMRLSSKN-VLVIGDSLHTDVMGA 143
Cdd:TIGR01459 195 KPYPAIFHKALKECSNIPKNrMLMVGDSFYTDILGA 230
PLN02940 PLN02940
riboflavin kinase
 109-157 8.92e-04

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 39.05  E-value: 8.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 17132640  109 KPFPSAFRKAMTQMRLSSKNVLVIGDSLhTDVMGAKFSGCRCIQVASLP 157
Cdd:PLN02940 150 KPSPDIFLEAAKRLNVEPSNCLVIEDSL-PGVMAGKAAGMEVIAVPSIP 197
GH25_AtlA-like cd06522
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell ...
 38-79 2.36e-03

AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.


Pssm-ID: 119382  Cd Length: 192  Bit Score: 37.35  E-value: 2.36e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17132640  38 LKNAGIRGVILDLdntiiSEDDRYLAPWAEDWIAEAKLAGLK 79
Cdd:cd06522  21 LKNYGVKAVIVKL-----TEGTTYRNPYAASQIANAKAAGLK 57
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 109-144 3.28e-03

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 37.31  E-value: 3.28e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 17132640   109 KPFPSAFRKAMTQMRLSSKN-VLVIGDSLHTDVMGAK 144
Cdd:TIGR01460 188 KPSPAIYRAALNLLQARPERrDVMVGDNLRTDILGAK 224
PRK10444 PRK10444
HAD-IIA family hydrolase;
101-155 3.37e-03

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 37.08  E-value: 3.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17132640  101 INAISpAKKPF----PSAF--RKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVAS 155
Cdd:PRK10444 161 IEKIS-GRKPFyvgkPSPWiiRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLS 220
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 109-155 7.81e-03

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. 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: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 36.19  E-value: 7.81e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 17132640 109 KPFPSAFRKAMTQMRLSSKNVLVIGDSLHTDVMGAKFSGCRCIQVAS 155
Cdd:cd07508 197 KPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQTLLVLT 243
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
106-151 8.18e-03

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 35.94  E-value: 8.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 17132640  106 PAKKPFPSAFRKAMTQMRLSSKNVLVIGDSLhTDVMGAKFSGCRCI 151
Cdd:PRK13222 146 PNKKPDPAPLLLACEKLGLDPEEMLFVGDSR-NDIQAARAAGCPSV 190
 
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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