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Conserved domains on  [gi|568065194|ref|WP_024052855|]
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MULTISPECIES: HAD-IA family hydrolase [Streptococcus]

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 ...
 4-181 4.39e-64

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 cd07523:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 173  Bit Score: 195.67  E-value: 4.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   4 AFIWDLDGTLLDSYDAILAGIEETYTHYGLDFDREVIRAYILQHSVQKLLEKVAaekglDAEEMNRFRGQSLQEKNAHIQ 83
Cdd:cd07523    1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYA-----EVPDLEEEYKELEAEYLAKPI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  84 LMDGAKAILTWAQEADIQQFVYTHKGKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYYIGD 163
Cdd:cd07523   76 LFPGAKAVLRWIKEQGGKNFLMTHRDHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVMIGD 155

                        170
                 ....*....|....*...
gi 568065194 164 RTLDVDVAFNSGIQSINF 181
Cdd:cd07523  156 RELDIEAGHNAGISTILF 173
 
Name Accession Description Interval E-value
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 4-181 4.39e-64

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. 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: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 195.67  E-value: 4.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   4 AFIWDLDGTLLDSYDAILAGIEETYTHYGLDFDREVIRAYILQHSVQKLLEKVAaekglDAEEMNRFRGQSLQEKNAHIQ 83
Cdd:cd07523    1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYA-----EVPDLEEEYKELEAEYLAKPI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  84 LMDGAKAILTWAQEADIQQFVYTHKGKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYYIGD 163
Cdd:cd07523   76 LFPGAKAVLRWIKEQGGKNFLMTHRDHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVMIGD 155

                        170
                 ....*....|....*...
gi 568065194 164 RTLDVDVAFNSGIQSINF 181
Cdd:cd07523  156 RELDIEAGHNAGISTILF 173
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-179 4.76e-32

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 115.03  E-value: 4.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   3 KAFIWDLDGTLLDSYDAILAGIEETYTHYGLD-FDREVIRAYI---LQHSVQKLLEKVAAEkglDAEEMNRFRGQSLQEK 78
Cdd:COG0546    2 KLVLFDLDGTLVDSAPDIAAALNEALAELGLPpLDLEELRALIglgLRELLRRLLGEDPDE---ELEELLARFRELYEEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  79 NA-HIQLMDGAKAILTWAQEADIQQFVYTHK-GKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKI 156
Cdd:COG0546   79 LLdETRLFPGVRELLEALKARGIKLAVVTNKpREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPE 158

                        170       180
                 ....*....|....*....|...
gi 568065194 157 STYYIGDRTLDVDVAFNSGIQSI 179
Cdd:COG0546  159 EVLMVGDSPHDIEAARAAGVPFI 181
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-179 4.89e-23

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 90.72  E-value: 4.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194    6 IWDLDGTLLDSYDAILAGIEETYTHYGL-DFDREVIRAYIlQHSVQKLLEKVAAEKGLDA--EEMNRFRGQSLQEKnaHI 82
Cdd:pfam13419   2 IFDFDGTLLDTEELIIKSFNYLLEEFGYgELSEEEILKFI-GLPLREIFRYLGVSEDEEEkiEFYLRKYNEELHDK--LV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   83 QLMDGAKAILTWAQEADIQQFVYTHK-GKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYYI 161
Cdd:pfam13419  79 KPYPGIKELLEELKEQGYKLGIVTSKsRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYV 158

                         170
                  ....*....|....*...
gi 568065194  162 GDRTLDVDVAFNSGIQSI 179
Cdd:pfam13419 159 GDSPRDIEAAKNAGIKVI 176
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 4-175 8.01e-15

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: 68.96  E-value: 8.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194    4 AFIWDLDGTLLDSYDAILAGIEetYTHYGLDFDREVIRAYILQHSVQkllekvAAEKGLDAEEM-NRFRGQSLQEKNAHI 82
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFP--QTFEEFGLDPASFKALKQAGGLA------EEEWYRIATSAlEELQGRFWSEYDAEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   83 QLMDGAKAILTWAQEADIQQFVYTHKGKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKiSTYYIG 162
Cdd:TIGR01549  73 AYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGSKPEPEIFLAALESLGVPP-EVLHVG 151

                         170
                  ....*....|...
gi 568065194  163 DRTLDVDVAFNSG 175
Cdd:TIGR01549 152 DNLNDIEGARNAG 164
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
3-179 1.23e-14

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 69.45  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   3 KAFIWDLDGTLLDSYDAILAGIEETYTHYGLD-FDREVIRAYIlQHSVQKLLEKV--AAEKGLDAEEMNRFRGQSLQ--E 77
Cdd:PRK13222   7 RAVAFDLDGTLVDSAPDLAAAVNAALAALGLPpAGEERVRTWV-GNGADVLVERAltWAGREPDEELLEKLRELFDRhyA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  78 KNAHI--QLMDGAKAILTWAQEADIQQFVYTHK-GKNAYQILADLEILDYFTEIV---TTANgfaRKPDPEGVNYLVEKY 151
Cdd:PRK13222  86 ENVAGgsRLYPGVKETLAALKAAGYPLAVVTNKpTPFVAPLLEALGIADYFSVVIggdSLPN---KKPDPAPLLLACEKL 162

                        170       180
                 ....*....|....*....|....*...
gi 568065194 152 QLDKISTYYIGDRTLDVDVAFNSGIQSI 179
Cdd:PRK13222 163 GLDPEEMLFVGDSRNDIQAARAAGCPSV 190
 
Name Accession Description Interval E-value
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 4-181 4.39e-64

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. 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: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 195.67  E-value: 4.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   4 AFIWDLDGTLLDSYDAILAGIEETYTHYGLDFDREVIRAYILQHSVQKLLEKVAaekglDAEEMNRFRGQSLQEKNAHIQ 83
Cdd:cd07523    1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYA-----EVPDLEEEYKELEAEYLAKPI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  84 LMDGAKAILTWAQEADIQQFVYTHKGKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYYIGD 163
Cdd:cd07523   76 LFPGAKAVLRWIKEQGGKNFLMTHRDHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVMIGD 155

                        170
                 ....*....|....*...
gi 568065194 164 RTLDVDVAFNSGIQSINF 181
Cdd:cd07523  156 RELDIEAGHNAGISTILF 173
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-179 4.76e-32

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 115.03  E-value: 4.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   3 KAFIWDLDGTLLDSYDAILAGIEETYTHYGLD-FDREVIRAYI---LQHSVQKLLEKVAAEkglDAEEMNRFRGQSLQEK 78
Cdd:COG0546    2 KLVLFDLDGTLVDSAPDIAAALNEALAELGLPpLDLEELRALIglgLRELLRRLLGEDPDE---ELEELLARFRELYEEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  79 NA-HIQLMDGAKAILTWAQEADIQQFVYTHK-GKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKI 156
Cdd:COG0546   79 LLdETRLFPGVRELLEALKARGIKLAVVTNKpREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPE 158

                        170       180
                 ....*....|....*....|...
gi 568065194 157 STYYIGDRTLDVDVAFNSGIQSI 179
Cdd:COG0546  159 EVLMVGDSPHDIEAARAAGVPFI 181
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-179 4.89e-23

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 90.72  E-value: 4.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194    6 IWDLDGTLLDSYDAILAGIEETYTHYGL-DFDREVIRAYIlQHSVQKLLEKVAAEKGLDA--EEMNRFRGQSLQEKnaHI 82
Cdd:pfam13419   2 IFDFDGTLLDTEELIIKSFNYLLEEFGYgELSEEEILKFI-GLPLREIFRYLGVSEDEEEkiEFYLRKYNEELHDK--LV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   83 QLMDGAKAILTWAQEADIQQFVYTHK-GKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYYI 161
Cdd:pfam13419  79 KPYPGIKELLEELKEQGYKLGIVTSKsRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYV 158

                         170
                  ....*....|....*...
gi 568065194  162 GDRTLDVDVAFNSGIQSI 179
Cdd:pfam13419 159 GDSPRDIEAAKNAGIKVI 176
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 3-202 1.20e-18

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: 80.46  E-value: 1.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   3 KAFIWDLDGTLLDSYDAILAGIEETYTHYG-LDFDREVIRAYIL------------QHSVQKLLEKVAAEKGLD--AEEM 67
Cdd:COG1011    2 KAVLFDLDGTLLDFDPVIAEALRALAERLGlLDEAEELAEAYRAieyalwrryergEITFAELLRRLLEELGLDlaEELA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  68 NRFrgqsLQEKNAHIQLMDGAKAILTWAQEADIQQFVYThkgkNA-----YQILADLEILDYFTEIVTTANGFARKPDPE 142
Cdd:COG1011   82 EAF----LAALPELVEPYPDALELLEALKARGYRLALLT----NGsaelqEAKLRRLGLDDLFDAVVSSEEVGVRKPDPE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568065194 143 GVNYLVEKYQLDKISTYYIGDR-TLDVDVAFNSGIQSINFCDYRPNIN------HKINHLLEIKQII 202
Cdd:COG1011  154 IFELALERLGVPPEEALFVGDSpETDVAGARAAGMRTVWVNRSGEPAPaeprpdYVISDLAELLELL 220
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
3-147 1.00e-17

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 77.56  E-value: 1.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   3 KAFIWDLDGTLLDSYDAILAGIEETYTHYGLDFDREVIRAYI---LQHSVQKLLEKVAAEkgLDAEEMNRFRGQSLQE-- 77
Cdd:COG0637    3 KAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMgrsREDILRYLLEEYGLD--LPEEELAARKEELYREll 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568065194  78 KNAHIQLMDGAKAILTWAQEADIQQFVYT-HKGKNAYQILADLEILDYFTEIVtTANGFAR-KPDPEGvnYL 147
Cdd:COG0637   81 AEEGLPLIPGVVELLEALKEAGIKIAVATsSPRENAEAVLEAAGLLDYFDVIV-TGDDVARgKPDPDI--YL 149
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 3-178 2.42e-16

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. 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: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 73.85  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   3 KAFIWDLDGTLLDSYDAILAGIEETYTHYGLD-FDREVIRAYILQhSVQKLLEKVAAEKGLDAEEMnrFRGQSLQEKNAH 81
Cdd:cd02616    2 TTILFDLDGTLIDTNELIIKSFNHTLKEYGLEgYTREEVLPFIGP-PLRETFEKIDPDKLEDMVEE--FRKYYREHNDDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  82 IQLMDGAKAILTWAQEADIQQFVYTHKGKN-AYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYY 160
Cdd:cd02616   79 TKEYPGVYETLARLKSQGIKLGVVTTKLREtALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEEALM 158

                        170
                 ....*....|....*...
gi 568065194 161 IGDRTLDVDVAFNSGIQS 178
Cdd:cd02616  159 VGDSPHDILAGKNAGVKT 176
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 4-175 8.01e-15

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: 68.96  E-value: 8.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194    4 AFIWDLDGTLLDSYDAILAGIEetYTHYGLDFDREVIRAYILQHSVQkllekvAAEKGLDAEEM-NRFRGQSLQEKNAHI 82
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFP--QTFEEFGLDPASFKALKQAGGLA------EEEWYRIATSAlEELQGRFWSEYDAEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   83 QLMDGAKAILTWAQEADIQQFVYTHKGKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKiSTYYIG 162
Cdd:TIGR01549  73 AYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGSKPEPEIFLAALESLGVPP-EVLHVG 151

                         170
                  ....*....|...
gi 568065194  163 DRTLDVDVAFNSG 175
Cdd:TIGR01549 152 DNLNDIEGARNAG 164
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
3-179 1.23e-14

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 69.45  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   3 KAFIWDLDGTLLDSYDAILAGIEETYTHYGLD-FDREVIRAYIlQHSVQKLLEKV--AAEKGLDAEEMNRFRGQSLQ--E 77
Cdd:PRK13222   7 RAVAFDLDGTLVDSAPDLAAAVNAALAALGLPpAGEERVRTWV-GNGADVLVERAltWAGREPDEELLEKLRELFDRhyA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  78 KNAHI--QLMDGAKAILTWAQEADIQQFVYTHK-GKNAYQILADLEILDYFTEIV---TTANgfaRKPDPEGVNYLVEKY 151
Cdd:PRK13222  86 ENVAGgsRLYPGVKETLAALKAAGYPLAVVTNKpTPFVAPLLEALGIADYFSVVIggdSLPN---KKPDPAPLLLACEKL 162

                        170       180
                 ....*....|....*....|....*...
gi 568065194 152 QLDKISTYYIGDRTLDVDVAFNSGIQSI 179
Cdd:PRK13222 163 GLDPEEMLFVGDSRNDIQAARAAGCPSV 190
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-175 1.70e-13

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: 66.07  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194    3 KAFIWDLDGTLLDSYDAILAGIEETYTHY-----------GLDFDREVIRAyILQHSVQKLLEKVAAEKGLDAEEMNRFR 71
Cdd:pfam00702   2 KAVVFDLDGTLTDGEPVVTEAIAELASEHplakaivaaaeDLPIPVEDFTA-RLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   72 GQSLQEKNAHI------QLMDGAKAILTWAQEADIQQFVYTHKGKNAYQ-ILADLEILDYFTEIVTTANGFARKPDPEGV 144
Cdd:pfam00702  81 TVVLVELLGVIaladelKLYPGAAEALKALKERGIKVAILTGDNPEAAEaLLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568065194  145 NYLVEKYQLDKISTYYIGDRTLDVDVAFNSG 175
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 4-181 3.58e-13

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 65.41  E-value: 3.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   4 AFIWDLDGTLLDSYDAILAGIEETYTHYG---LDFDRevIRAYIlQHSVQKLLEKVAAEKGLDAEE------MNRFRGQS 74
Cdd:cd07512    1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGlapLSLAE--VRSFV-GHGAPALIRRAFAAAGEDLDGplhdalLARFLDHY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  75 LQEKNAHIQLMDGAKAILTWAQEADIQQFVYTHK-GKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQL 153
Cdd:cd07512   78 EADPPGLTRPYPGVIEALERLRAAGWRLAICTNKpEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGG 157

                        170       180
                 ....*....|....*....|....*...
gi 568065194 154 DKISTYYIGDRTLDVDVAFNSGIQSINF 181
Cdd:cd07512  158 DVSRALMVGDSETDAATARAAGVPFVLV 185
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 4-179 1.31e-12

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: 63.79  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   4 AFIWDLDGTLLDSYDAILAGIEETYTHYGLD-FDREVIRAYIlQHSVQKLLEKV-------AAEKGLDAEEMNRFrGQSL 75
Cdd:cd16417    1 LVAFDLDGTLVDSAPDLAEAANAMLAALGLPpLPEETVRTWI-GNGADVLVERAltgareaEPDEELFKEARALF-DRHY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  76 QEKNAHI-QLMDGAKAILTWAQEADIQQFVYTHK-GKNAYQILADLEILDYFTEIV---TTANgfaRKPDPEGVNYLVEK 150
Cdd:cd16417   79 AETLSVHsHLYPGVKEGLAALKAQGYPLACVTNKpERFVAPLLEALGISDYFSLVLggdSLPE---KKPDPAPLLHACEK 155

                        170       180
                 ....*....|....*....|....*....
gi 568065194 151 YQLDKISTYYIGDRTLDVDVAFNSGIQSI 179
Cdd:cd16417  156 LGIAPAQMLMVGDSRNDILAARAAGCPSV 184
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 6-179 2.18e-11

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 60.49  E-value: 2.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   6 IWDLDGTLLDSYDAILAGIEETYTHYGL-DFDREVIRAYI---LQHSVQKLLEKV--AAEKGLDAEEMNRFRGQSLQEKN 79
Cdd:cd07533    3 IFDWDGTLADSQHNIVAAMTAAFADLGLpVPSAAEVRSIIglsLDEAIARLLPMAtpALVAVAERYKEAFDILRLLPEHA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  80 AhiQLMDGAKAILTWAQEADIQQFVYTHKGKNAY-QILADLEILDYFtEIVTTANGFARKPDPEGVNYLVEKYQLDKIST 158
Cdd:cd07533   83 E--PLFPGVREALDALAAQGVLLAVATGKSRRGLdRVLEQHGLGGYF-DATRTADDTPSKPHPEMLREILAELGVDPSRA 159

                        170       180
                 ....*....|....*....|.
gi 568065194 159 YYIGDRTLDVDVAFNSGIQSI 179
Cdd:cd07533  160 VMVGDTAYDMQMAANAGAHAV 180
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 1-178 2.64e-09

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 54.65  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   1 MRKAFIWDLDGTLLDSYDAILAGIEETY-THYGLDFDREVIRAYIlQHSVQKLLEKVAAEKgldAEEM-NRFRGQSLQEK 78
Cdd:PRK13288   2 KINTVLFDLDGTLINTNELIISSFLHTLkTYYPNQYKREDVLPFI-GPSLHDTFSKIDESK---VEEMiTTYREFNHEHH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  79 NAHIQLMDGAKAILTWAQEADIQQFVYTHKGKNAYQILADLEILDYFTEIVTTANGFAR-KPDPEGVNYLVEKYQLDKIS 157
Cdd:PRK13288  78 DELVTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHaKPDPEPVLKALELLGAKPEE 157

                        170       180
                 ....*....|....*....|.
gi 568065194 158 TYYIGDRTLDVDVAFNSGIQS 178
Cdd:PRK13288 158 ALMVGDNHHDILAGKNAGTKT 178
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 8-179 8.90e-09

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. 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: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 53.36  E-value: 8.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   8 DLDGTLLDSYDAILAGIEETYTHYGLD-FDREVIRAYI---LQHSVQKLL--EKVAAEKGLDAEEmNRFRGQSLQEKnah 81
Cdd:cd04302    5 DLDGTLTDSAEGITASVQYALEELGIPvPDESELRRFIgppLEDSFRELLpfDEEEAQRAVDAYR-EYYKEKGLFEN--- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  82 iQLMDGAKAILTWAQEADIQQFVYTHKGKN-AYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYY 160
Cdd:cd04302   81 -EVYPGIPELLEKLKAAGYRLYVATSKPEVfARRILEHFGLDEYFDGIAGASLDGSRVHKADVIRYALDTLGIAPEQAVM 159

                        170
                 ....*....|....*....
gi 568065194 161 IGDRTLDVDVAFNSGIQSI 179
Cdd:cd04302  160 IGDRKHDIIGARANGIDSI 178
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 85-179 1.82e-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: 50.47  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  85 MDG---AKAILTWAQEADIQQFVYTHKGKN-AYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYY 160
Cdd:cd01427    6 LDGtllAVELLKRLRAAGIKLAIVTNRSREaLRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLF 85

                         90
                 ....*....|....*....
gi 568065194 161 IGDRTLDVDVAFNSGIQSI 179
Cdd:cd01427   86 VGDSENDIEAARAAGGRTV 104
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 4-179 1.06e-07

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; 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, (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 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the 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 related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 49.73  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194    4 AFIWDLDGTLLDSYDAILAGIEETYTHY-GLDFDREVIRAYI--LQHSVQKLLEKVAAEKGLDAEEmNRFRGQSLQEKNA 80
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINREELGLvPDELGVSAVGRLElaLRRFKAQYGRTISPEDAQLLYK-QLFYEQIEEEAKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   81 HIqlMDGAKAILTWAQEADIQQFVYTHKGKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYY 160
Cdd:TIGR01509  80 KP--LPGVRALLEALRARGKKLALLTNSPRAHKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPSECVF 157

                         170
                  ....*....|....*....
gi 568065194  161 IGDRTLDVDVAFNSGIQSI 179
Cdd:TIGR01509 158 VDDSPAGIEAAKAAGMHTV 176
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 6-181 1.50e-07

2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In Ralstonia (Alcaligenes) eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO. The only other pertinent experimental evidence concerns the gene from E. coli. The in vitro activity of the Ralstonia and Escherichia enzymes was determined with crude cell extracts of strains containing PGP on expression plasmids and compared to controls. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes). The E. coli enzyme is not expressed under normal laboratory conditions; the pathway to which it belongs has not been determined. In fact, the possibility exists, although unlikely, that the E. coli enzyme and others within this equivalog have as their physiological substrate another, closely related molecule. The other seed chosen for this model, from Xylella fastidiosa has no experimental evidence, but is a plant pathogen and thus may obtain phosphoglycolate from its host. This model has been restricted to encompass only proteobacteria as no related PGP has been verified outside of this clade. Sequences from Aquifex aeolicus and Treponema pallidum fall between the trusted and noise cutoffs. Just below the noise cutoff is a gene which is part of the operon for the biosynthesis of the blue pigment, indigoidine, from Erwinia (Pectobacterium) chrysanthemi, a plant pathogen. It does not seem likely, considering the proposed biosynthetic mechanism, that the dephosphorylation of phosphoglycolate or a closely related compound is required. Possibly, this gene is fortuitously located in this operon, or has an indirect relationship to the necessity for the biosynthesis of this compound. Sequences from 11 species have been annotated as PGP or putative PGP but fall below the noise cutoff. None of these have experimental validation. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes (pfam00702). [Energy metabolism, Sugars]


Pssm-ID: 130516 [Multi-domain]  Cd Length: 213  Bit Score: 49.82  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194    6 IWDLDGTLLDSYDAILAGIEETYTHYGLD-FDREVIRAYIlQHSVQKLLEKVAAEKG--LDAEEMNRFRGQSLQEKNAHI 82
Cdd:TIGR01449   2 LFDLDGTLVDSAPDIAAAVNMALAALGLPpATLARVIGFI-GNGVPVLMERVLAWAGqePDAQRVAELRKLFDRHYEEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   83 ----QLMDGAKAILTWAQEADIQQFVYTHKGKN-AYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKIS 157
Cdd:TIGR01449  81 geltSVFPGVEATLGALRAKGLRLGLVTNKPTPlARPLLELLGLAKYFSVLIGGDSLAQRKPHPDPLLLAAERLGVAPQQ 160

                         170       180
                  ....*....|....*....|....
gi 568065194  158 TYYIGDRTLDVDVAFNSGIQSINF 181
Cdd:TIGR01449 161 MVYVGDSRVDIQAARAAGCPSVLL 184
HAD pfam12710
haloacid dehalogenase-like hydrolase;
5-171 2.61e-07

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 48.68  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194    5 FIWDLDGTLL--DSYDAIL-----AGIEETYTHYGLDFDREVIRAYILQHSVQKLLEKVAAEKGLDAEEMNRFRgqSLQE 77
Cdd:pfam12710   1 ALFDLDGTLLdgDSLFLLIrallrRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAELE--RFVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   78 KNAHIQLMDGAKAILTWAQEADIQQFVYTHKGK-NAYQILADL---EILDyfTEIVTTANGFARKPDPEGVN-------- 145
Cdd:pfam12710  79 EVALPRLHPGALELLAAHRAAGDRVVVVTGGLRpLVEPVLAELgfdEVLA--TELEVDDGRFTGELRLIGPPcagegkvr 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568065194  146 -----YLVEKYQLDKISTYYIGDRTLDVDVA 171
Cdd:pfam12710 157 rlrawLAARGLGLDLADSVAYGDSPSDLPML 187
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 85-179 5.77e-06

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; 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: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 43.60  E-value: 5.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  85 MDGAKAI---LTWAQEADIQQFVYTHKGKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYYI 161
Cdd:cd16421    6 LDGTLLIlelLKALRQKGIKLAVLSNKPNEAVQVLVEELFPGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYV 85

                         90
                 ....*....|....*...
gi 568065194 162 GDRTLDVDVAFNSGIQSI 179
Cdd:cd16421   86 GDSGVDMQTARNAGMDEI 103
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 4-147 3.89e-05

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong 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), 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: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 42.72  E-value: 3.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   4 AFIWDLDGTLLDSYDAilagIEETYTH----YGLDFDrEVIRAyilQHSVQ--KLLEKVAAEKGlDAEEMNRFRGQSLQE 77
Cdd:cd07527    1 ALLFDMDGTLVDSTPA----VERAWHKwakeHGVDPE-EVLKV---SHGRRaiDVIRKLAPDDA-DIELVLALETEEPES 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  78 KNAHIQLMDGAKAIL--------TWAqeadiqqfVYThKGKNAYqILADLEILDYF-TEIVTTANGFAR-KPDPEGvnYL 147
Cdd:cd07527   72 YPEGVIAIPGAVDLLaslpaagdRWA--------IVT-SGTRAL-AEARLEAAGLPhPEVLVTADDVKNgKPDPEP--YL 139
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 84-179 1.05e-04

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: 40.22  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  84 LMDGAKAILTWAQE-----------ADIQQfvytHKgknayqiLADLEILDYFTEIVTT-ANGFArKPDPEGVNYLVEKY 151
Cdd:cd04305   10 LLPGAKELLEELKKgyklgiitngpTEVQW----EK-------LEQLGIHKYFDHIVISeEVGVQ-KPNPEIFDYALNQL 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 568065194 152 QLDKISTYYIGDRtLDVDV--AFNSGIQSI 179
Cdd:cd04305   78 GVKPEETLMVGDS-LESDIlgAKNAGIKTV 106
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 125-179 1.08e-04

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: 41.97  E-value: 1.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568065194 125 FTEIVTTANG----FARKPDPEGVNYLVEKYQLDKISTYYIGDRtLDVDVAF--NSGIQSI 179
Cdd:cd07508  180 FAAAVEAATGrqplVLGKPSPWLGELALEKFGIDPERVLFVGDR-LATDVLFgkACGFQTL 239
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 4-143 1.76e-04

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include 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: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 40.35  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   4 AFIWDLDGTLLDSydailagieeTYTHYgldfdreviRAYilqhsvQKLLEKVAAekgldAEEMNRFRGQSLQE-KNAHI 82
Cdd:cd02598    1 GVIFDLDGVITDT----------AEYHY---------RAW------KKLADKEEL-----AARKNRIYVELIEElTPVDV 50

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568065194  83 qlMDGAKAILTWAQEADIQQFVYTHKgKNAYQILADLEILDYFTEIVTTANGFARKPDPEG 143
Cdd:cd02598   51 --LPGIASLLVDLKAKGIKIALASAS-KNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDI 108
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 4-142 1.94e-04

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: 40.32  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   4 AFIWDLDGTLLDsydailagieeTYTHYgLDFDREVIRAYIlqhsvQKLLEKVAAEKGLdaeemnrfrgqslqeknahIQ 83
Cdd:cd16423    1 AVIFDFDGVIVD-----------TEPLW-YEAWQELLNERR-----NELIKRQFSEKTD-------------------LP 44

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568065194  84 LMDGAKAILTWAQEADIQQFVYTHKG-KNAYQILADLEILDYFTEIVtTANGFAR-KPDPE 142
Cdd:cd16423   45 PIEGVKELLEFLKEKGIKLAVASSSPrRWIEPHLERLGLLDYFEVIV-TGDDVEKsKPDPD 104
DREG-2 TIGR02252
REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes ...
 83-179 1.16e-03

REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes uncharacterized sequences from eukaryotes, cyanobacteria and Leptospira as well as the DREG-2 protein from Drosophila melanogaster which has been identified as a rhythmically (diurnally) regulated gene. This family is a member 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. This family is a member of subfamily 1A in which the cap domain consists of a predicted alpha helical bundle found in between the first and second catalytic motifs. A distinctive feature of this family is a conserved tandem pair of tryptophan residues in the cap domain. The most divergent sequences included within the scope of this model are from plants and have "FW" at this position instead. Most likely, these sequences, like the vast majority of HAD sequences, represent phosphatase enzymes.


Pssm-ID: 274056 [Multi-domain]  Cd Length: 203  Bit Score: 38.42  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   83 QLMDGAKAILTWAQEADIQQFVYTHKGKNAYQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYYIG 162
Cdd:TIGR02252 105 QVYPDAIKLLKDLRERGLILGVISNFDSRLRGLLEALGLLEYFDFVVTSYEVGAEKPDPKIFQEALERAGISPEEALHIG 184

                          90
                  ....*....|....*...
gi 568065194  163 D-RTLDVDVAFNSGIQSI 179
Cdd:TIGR02252 185 DsLRNDYQGARAAGWRAL 202
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 1-179 1.75e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 38.31  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194   1 MRKAFIWDLDGTLLDSYDAILAGIEETYTHYGldfdR-----EVIRAYI---LQHSVQKLLEKVAAEKGLDAEEMNR--- 69
Cdd:PRK13223  12 LPRLVMFDLDGTLVDSVPDLAAAVDRMLLELG----RppaglEAVRHWVgngAPVLVRRALAGSIDHDGVDDELAEQala 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194  70 FRGQSLQEKNAHIQLMDGAKAILTWAQEADIQQFVYTHKGKNAYQILAD-LEILDYFTEIVTTANGFARKPDPEGVNYLV 148
Cdd:PRK13223  88 LFMEAYADSHELTVVYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDqMKIGRYFRWIIGGDTLPQKKPDPAALLFVM 167

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568065194 149 EKYQLDKISTYYIGDRTLDVDVAFNSGIQSI 179
Cdd:PRK13223 168 KMAGVPPSQSLFVGDSRSDVLAAKAAGVQCV 198
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 113-202 8.09e-03

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: 34.96  E-value: 8.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065194 113 YQILADLEILDYFTEIVTTANGFARKPDPEGVNYLVEKYQLDKISTYYIGD-RTLDVDVAFNSGIQSInFCDyRPNINHK 191
Cdd:cd16415   37 RELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDdLKNDYLGARAVGWHAL-LVD-REGALHE 114

                         90
                 ....*....|.
gi 568065194 192 INHLLEIKQII 202
Cdd:cd16415  115 LPSLANLLERL 125
 
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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