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Conserved domains on  [gi|1062061009|gb|AOL10821|]
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Phosphoglycolate phosphatase [Bifidobacterium longum]

Protein Classification

HAD family hydrolase( domain architecture ID 11425524)

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

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|7966317

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-216 2.67e-54

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


:

Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 173.19  E-value: 2.67e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   3 YRCLLWDFDGTLADTGSDVWNSLTYAARRAGGAIDDLyMRDDANLADPMDEIMRHVIPYPGEAYLETFDEDVRVHYRTLN 82
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDL-EELRALIGLGLRELLRRLLGEDPDEELEELLARFRELYEEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  83 DfSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGREaTKVEMIAEIVRRHGIAP 162
Cdd:COG0546    80 L-DETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAK-PKPEPLLEALERLGLDP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1062061009 163 RQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRNPAYVAHDIAELNDI 216
Cdd:COG0546   158 EEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGADYVIDSLAELLAL 211
 
Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-216 2.67e-54

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 173.19  E-value: 2.67e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   3 YRCLLWDFDGTLADTGSDVWNSLTYAARRAGGAIDDLyMRDDANLADPMDEIMRHVIPYPGEAYLETFDEDVRVHYRTLN 82
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDL-EELRALIGLGLRELLRRLLGEDPDEELEELLARFRELYEEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  83 DfSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGREaTKVEMIAEIVRRHGIAP 162
Cdd:COG0546    80 L-DETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAK-PKPEPLLEALERLGLDP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1062061009 163 RQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRNPAYVAHDIAELNDI 216
Cdd:COG0546   158 EEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGADYVIDSLAELLAL 211
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-222 6.87e-33

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 118.37  E-value: 6.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   1 MEYRCLLWDFDGTLADTGSDvwnsLTYAARRA------------------GGAIDDLYMRD-DANLADPMDEIMRHVipy 61
Cdd:PRK13222    4 MDIRAVAFDLDGTLVDSAPD----LAAAVNAAlaalglppageervrtwvGNGADVLVERAlTWAGREPDEELLEKL--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  62 pgeayLETFDEdvrvHYRTlNDFSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIP 141
Cdd:PRK13222   77 -----RELFDR----HYAE-NVAGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009 142 GReatK--VEMIAEIVRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYG--DGDEIALLsrNPAYVAHDIAELNDIM 217
Cdd:PRK13222  147 NK---KpdPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYGynYGEPIALS--EPDVVIDHFAELLPLL 221


                  ....*
gi 1062061009 218 TDTVI 222
Cdd:PRK13222  222 GLALS 226
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 5-216 1.55e-29

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: 109.22  E-value: 1.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   5 CLLWDFDGTLADTGSDVWNSLTYAARRAGGAIDDlymrdDANLAD----PMDEIMRHvipypgeaYLETFDEDVR---VH 77
Cdd:cd04302     1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPD-----ESELRRfigpPLEDSFRE--------LLPFDEEEAQravDA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  78 YRtlNDFSRT-----RLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDwICPDSIPGREATKVEMIA 152
Cdd:cd04302    68 YR--EYYKEKglfenEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDG-IAGASLDGSRVHKADVIR 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062061009 153 EIVRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRNPAYVAHDIAELNDI 216
Cdd:cd04302   145 YALDTLGIAPEQAVMIGDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATYIVETPAELLEL 208
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-188 6.51e-26

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 99.20  E-value: 6.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   6 LLWDFDGTLADTGSDVWNSLTYAARRAG-GAIDDLYMRDDANLadPMDEIMRHVIPYPGEAY-LETFDEDVRVHyrtLND 83
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIGL--PLREIFRYLGVSEDEEEkIEFYLRKYNEE---LHD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  84 FSrTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGReatKV--EMIAEIVRRHGIA 161
Cdd:pfam13419  76 KL-VKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGK---KPdpDPILKALEQLGLK 151

                         170       180
                  ....*....|....*....|....*..
gi 1062061009 162 PRQCLYVGDTFSDIEAARTNGISCIAV 188
Cdd:pfam13419 152 PEEVIYVGDSPRDIEAAKNAGIKVIAV 178
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 6-191 1.16e-19

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: 83.72  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   6 LLWDFDGTLADTGSDVW---NSLTYAARRAGGAIDDLYmrddANLADPMDEIMRHVIPYPGEA--------YLETFDEdv 74
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAaavNMALAALGLPPATLARVI----GFIGNGVPVLMERVLAWAGQEpdaqrvaeLRKLFDR-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  75 rvHYRTLNDfSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGREATKVEMIAeI 154
Cdd:TIGR01449  75 --HYEEVAG-ELTSVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQRKPHPDPLLL-A 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1062061009 155 VRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYG 191
Cdd:TIGR01449 151 AERLGVAPQQMVYVGDSRVDIQAARAAGCPSVLLTYG 187
 
Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-216 2.67e-54

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 173.19  E-value: 2.67e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   3 YRCLLWDFDGTLADTGSDVWNSLTYAARRAGGAIDDLyMRDDANLADPMDEIMRHVIPYPGEAYLETFDEDVRVHYRTLN 82
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDL-EELRALIGLGLRELLRRLLGEDPDEELEELLARFRELYEEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  83 DfSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGREaTKVEMIAEIVRRHGIAP 162
Cdd:COG0546    80 L-DETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAK-PKPEPLLEALERLGLDP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1062061009 163 RQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRNPAYVAHDIAELNDI 216
Cdd:COG0546   158 EEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGADYVIDSLAELLAL 211
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-222 6.87e-33

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 118.37  E-value: 6.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   1 MEYRCLLWDFDGTLADTGSDvwnsLTYAARRA------------------GGAIDDLYMRD-DANLADPMDEIMRHVipy 61
Cdd:PRK13222    4 MDIRAVAFDLDGTLVDSAPD----LAAAVNAAlaalglppageervrtwvGNGADVLVERAlTWAGREPDEELLEKL--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  62 pgeayLETFDEdvrvHYRTlNDFSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIP 141
Cdd:PRK13222   77 -----RELFDR----HYAE-NVAGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009 142 GReatK--VEMIAEIVRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYG--DGDEIALLsrNPAYVAHDIAELNDIM 217
Cdd:PRK13222  147 NK---KpdPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYGynYGEPIALS--EPDVVIDHFAELLPLL 221


                  ....*
gi 1062061009 218 TDTVI 222
Cdd:PRK13222  222 GLALS 226
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 5-216 1.55e-29

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: 109.22  E-value: 1.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   5 CLLWDFDGTLADTGSDVWNSLTYAARRAGGAIDDlymrdDANLAD----PMDEIMRHvipypgeaYLETFDEDVR---VH 77
Cdd:cd04302     1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPD-----ESELRRfigpPLEDSFRE--------LLPFDEEEAQravDA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  78 YRtlNDFSRT-----RLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDwICPDSIPGREATKVEMIA 152
Cdd:cd04302    68 YR--EYYKEKglfenEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDG-IAGASLDGSRVHKADVIR 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062061009 153 EIVRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRNPAYVAHDIAELNDI 216
Cdd:cd04302   145 YALDTLGIAPEQAVMIGDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATYIVETPAELLEL 208
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-188 6.51e-26

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 99.20  E-value: 6.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   6 LLWDFDGTLADTGSDVWNSLTYAARRAG-GAIDDLYMRDDANLadPMDEIMRHVIPYPGEAY-LETFDEDVRVHyrtLND 83
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIGL--PLREIFRYLGVSEDEEEkIEFYLRKYNEE---LHD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  84 FSrTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGReatKV--EMIAEIVRRHGIA 161
Cdd:pfam13419  76 KL-VKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGK---KPdpDPILKALEQLGLK 151

                         170       180
                  ....*....|....*....|....*..
gi 1062061009 162 PRQCLYVGDTFSDIEAARTNGISCIAV 188
Cdd:pfam13419 152 PEEVIYVGDSPRDIEAAKNAGIKVIAV 178
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 6-213 3.13e-24

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: 95.38  E-value: 3.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   6 LLWDFDGTLADTGSDvwnsLTYAARRaggaiddlyMRDDANLADPMDEIMRHVI--------------PYPGEAYLETFD 71
Cdd:cd16417     2 VAFDLDGTLVDSAPD----LAEAANA---------MLAALGLPPLPEETVRTWIgngadvlveraltgAREAEPDEELFK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  72 EDVRV---HYRTLNDfSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGRE--AT 146
Cdd:cd16417    69 EARALfdrHYAETLS-VHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKpdPA 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062061009 147 KVEMIAEivrRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYG--DGDEIALLsrNPAYVAHDIAEL 213
Cdd:cd16417   148 PLLHACE---KLGIAPAQMLMVGDSRNDILAARAAGCPSVGLTYGynYGEDIAAS--GPDAVIDSLAEL 211
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 9-213 3.68e-22

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/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: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 89.72  E-value: 3.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   9 DFDGTLADTGSDVWNSLTYAARRAG-GAIDDlymRDDANLAD-PMDEIMRH--VIPYPGEAYLETFdedVRVHYRTLNDF 84
Cdd:cd04303     5 DFDGTLADSFPWFLSILNQLAARHGfKTVDE---EEIEQLRQlSSREILKQlgVPLWKLPLIAKDF---RRLMAEAAPEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  85 SrtrLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDdWICPDSIPGreatKVEMIAEIVRRHGIAPRQ 164
Cdd:cd04303    79 A---LFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFA-VIEGSSLFG----KAKKIRRVLRRTKITAAQ 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1062061009 165 CLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRNPAYVAHDIAEL 213
Cdd:cd04303   151 VIYVGDETRDIEAARKVGLAFAAVSWGYAKPEVLKALAPDHMLEDPEDL 199
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
3-213 4.23e-22

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 89.88  E-value: 4.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   3 YRCLLWDFDGTLADTgSDVWN-SLTYAARRAGGAIDDLYMRddANLADPMDEIMRHVIPYPGEAY-LETFDEDVRVHYRT 80
Cdd:COG0637     2 IKAVIFDMDGTLVDS-EPLHArAWREAFAELGIDLTEEEYR--RLMGRSREDILRYLLEEYGLDLpEEELAARKEELYRE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  81 LNDFSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIP-GREATkvEMIAEIVRRHG 159
Cdd:COG0637    79 LLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVArGKPDP--DIYLLAAERLG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1062061009 160 IAPRQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALlsRNPAYVAHDIAEL 213
Cdd:COG0637   157 VDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEEL--AGADLVVDDLAEL 208
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 3-216 2.20e-21

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: 88.11  E-value: 2.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   3 YRCLLWDFDGTLADTGSDVWNSLTYAARRAGGaidDLYMRDD--ANLADPMDEIMRHVIPYPGEAYLETFDEdvrvHYRT 80
Cdd:cd02616     1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGL---EGYTREEvlPFIGPPLRETFEKIDPDKLEDMVEEFRK----YYRE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  81 LNDfSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGR--EATKVEMIAEIVrrh 158
Cdd:cd02616    74 HND-DLTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHkpDPEPVLKALELL--- 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1062061009 159 GIAPRQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRNPAYVAHDIAELNDI 216
Cdd:cd02616   150 GAEPEEALMVGDSPHDILAGKNAGVKTVGVTWGYKGREYLKAFNPDFIIDKMSDLLTI 207
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 3-216 1.95e-20

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: 85.85  E-value: 1.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   3 YRCLLWDFDGTLADTGSDVWNSLTYAARRAGG------------AIDDLYMRDDANLADPMDEIMRHVIPYPGEAYLETF 70
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLldeaeelaeayrAIEYALWRRYERGEITFAELLRRLLEELGLDLAEEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  71 DEDVRVHYRTLndfsrTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIpGREATKVEM 150
Cdd:COG1011    81 AEAFLAALPEL-----VEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEV-GVRKPDPEI 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062061009 151 IAEIVRRHGIAPRQCLYVGDT-FSDIEAARTNGISCIAVTygDGDEIALLSRNPAYVAHDIAELNDI 216
Cdd:COG1011   155 FELALERLGVPPEEALFVGDSpETDVAGARAAGMRTVWVN--RSGEPAPAEPRPDYVISDLAELLEL 219
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 5-217 4.26e-20

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: 84.67  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   5 CLLWDFDGTLADTGSDVWNSLTYAARRAGGA-IDDLYMRDDANLADPMdeIMRHVIPYPGEayletfDEDVRVHYRTLND 83
Cdd:cd07512     1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLApLSLAEVRSFVGHGAPA--LIRRAFAAAGE------DLDGPLHDALLAR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  84 F---------SRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGREATKvEMIAEI 154
Cdd:cd07512    73 FldhyeadppGLTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDP-APLRAA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062061009 155 VRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIaLLSRNPAYVAHDIAELNDIM 217
Cdd:cd07512   152 IRRLGGDVSRALMVGDSETDAATARAAGVPFVLVTFGYRHAP-VAELPHDAVFSDFDALPDLL 213
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 6-191 1.16e-19

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: 83.72  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   6 LLWDFDGTLADTGSDVW---NSLTYAARRAGGAIDDLYmrddANLADPMDEIMRHVIPYPGEA--------YLETFDEdv 74
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAaavNMALAALGLPPATLARVI----GFIGNGVPVLMERVLAWAGQEpdaqrvaeLRKLFDR-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  75 rvHYRTLNDfSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGREATKVEMIAeI 154
Cdd:TIGR01449  75 --HYEEVAG-ELTSVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQRKPHPDPLLL-A 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1062061009 155 VRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYG 191
Cdd:TIGR01449 151 AERLGVAPQQMVYVGDSRVDIQAARAAGCPSVLLTYG 187
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 6-223 1.24e-19

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: 83.22  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   6 LLWDFDGTLADTGSDVWNSLTYAARRAG-GAIDDLYMRDDANLAdpMDEIMRHVIPYPGEA---YLETFDEDVRVHyRTL 81
Cdd:cd07533     2 VIFDWDGTLADSQHNIVAAMTAAFADLGlPVPSAAEVRSIIGLS--LDEAIARLLPMATPAlvaVAERYKEAFDIL-RLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  82 NDFSrTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGREATkvEMIAEIVRRHGIA 161
Cdd:cd07533    79 PEHA-EPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADDTPSKPHP--EMLREILAELGVD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1062061009 162 PRQCLYVGDTFSDIEAARTNGISCIAVTYGdgdeiallsrnpayvAHDIAELNDIMTDTVIH 223
Cdd:cd07533   156 PSRAVMVGDTAYDMQMAANAGAHAVGVAWG---------------YHSLEDLRSAGADAVVD 202
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 96-188 3.79e-15

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: 68.58  E-value: 3.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  96 MLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIpGREATKVEMIAEIVRRHGIAPRQCLYVGDTFSDI 175
Cdd:cd01427    15 LLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGG-GTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDI 93

                          90
                  ....*....|...
gi 1062061009 176 EAARTNGISCIAV 188
Cdd:cd01427    94 EAARAAGGRTVAV 106
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-179 1.29e-14

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: 69.54  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   3 YRCLLWDFDGTLADTGS---DVWN---SLTYAARRAGGAIDDLYMRDDANLADPM------DEIMRHVIPYPGEAYLETF 70
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPvvtEAIAelaSEHPLAKAIVAAAEDLPIPVEDFTARLLlgkrdwLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  71 DEDVRVHYRTLNDFSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDsIPGREATKVEM 150
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGD-DVGVGKPKPEI 159

                         170       180
                  ....*....|....*....|....*....
gi 1062061009 151 IAEIVRRHGIAPRQCLYVGDTFSDIEAAR 179
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVNDIPAAK 188
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 5-188 2.24e-14

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: 68.60  E-value: 2.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   5 CLLWDFDGTLADTGSDVWNSLTyaARRAGGAIDDL----YMRDDANLADPMDEIMRHVIPYPGEAYLETFDEDVRVHYRT 80
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLIN--REELGLVPDELgvsaVGRLELALRRFKAQYGRTISPEDAQLLYKQLFYEQIEEEAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  81 LndfsrtRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGsKGWANLFDDWICPDSIPgreATK--VEMIAEIVRRH 158
Cdd:TIGR01509  79 L------KPLPGVRALLEALRARGKKLALLTNSPRAHKLVLAL-LGLRDLFDVVIDSSDVG---LGKpdPDIYLQALKAL 148

                         170       180       190
                  ....*....|....*....|....*....|
gi 1062061009 159 GIAPRQCLYVGDTFSDIEAARTNGISCIAV 188
Cdd:TIGR01509 149 GLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 4-191 3.71e-13

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 66.41  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   4 RCLLWDFDGTLADTGSDVwnsltYAARRAggaiddlyMRDDANLADPMDEIMRHVIPYPGEAYLET----FDEDVRV--- 76
Cdd:PRK13226   13 RAVLFDLDGTLLDSAPDM-----LATVNA--------MLAARGRAPITLAQLRPVVSKGARAMLAVafpeLDAAARDali 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  77 -----HYRTLNDfSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGREATKVEMI 151
Cdd:PRK13226   80 peflqRYEALIG-TQSQLFDGVEGMLQRLECAGCVWGIVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPHPLPLL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1062061009 152 AEiVRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYG 191
Cdd:PRK13226  159 VA-AERIGVAPTDCVYVGDDERDILAARAAGMPSVAALWG 197
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 87-213 1.21e-12

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 65.27  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  87 TRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGREATKVEMIAeIVRRHGIAPRQCL 166
Cdd:PRK13223  100 TVVYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLF-VMKMAGVPPSQSL 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1062061009 167 YVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRNPAYVAHDIAEL 213
Cdd:PRK13223  179 FVGDSRSDVLAAKAAGVQCVALSYGYNHGRPIAEESPALVIDDLRAL 225
Hydrolase_like pfam13242
HAD-hyrolase-like;
149-213 1.03e-11

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 58.78  E-value: 1.03e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062061009 149 EMIAEIVRRHGIAPRQCLYVGDTF-SDIEAARTNGISCIAVTYG--DGDEIALLSRNPAYVAHDIAEL 213
Cdd:pfam13242   8 GMLERALARLGLDPERTVMIGDRLdTDILGAREAGARTILVLTGvtRPADLEKAPIRPDYVVDDLAEA 75
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 1-219 1.71e-11

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 61.20  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   1 MEYRCLLWDFDGTLADTGSDVWNSL-----TYAarraggaiDDLYMRDDanladpmdeimrhVIPYPGEAYLETFD---- 71
Cdd:PRK13288    1 MKINTVLFDLDGTLINTNELIISSFlhtlkTYY--------PNQYKRED-------------VLPFIGPSLHDTFSkide 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  72 ---EDVRVHYRTLN----DfSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPgRE 144
Cdd:PRK13288   60 skvEEMITTYREFNhehhD-ELVTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVE-HA 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062061009 145 ATKVEMIAEIVRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRNPAYVAHDIAELNDIMTD 219
Cdd:PRK13288  138 KPDPEPVLKALELLGAKPEEALMVGDNHHDILAGKNAGTKTAGVAWTIKGREYLEQYKPDFMLDKMSDLLAIVGD 212
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 4-218 1.99e-10

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 58.96  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   4 RCLLWDFDGTLADTGSDVWNSLTYAARRAGgaIDDLYMRDDANLADPMDeimRHVIPYPGEAYLETFDEDVRVHYRTLND 83
Cdd:PRK13225   63 QAIIFDFDGTLVDSLPTVVAIANAHAPDFG--YDPIDERDYAQLRQWSS---RTIVRRAGLSPWQQARLLQRVQRQLGDC 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  84 FSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDdwICPDSIPgrEATKVEMIAEIVRRHGIAPR 163
Cdd:PRK13225  138 LPALQLFPGVADLLAQLRSRSLCLGILSSNSRQNIEAFLQRQGLRSLFS--VVQAGTP--ILSKRRALSQLVAREGWQPA 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1062061009 164 QCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRNPAYVAHDIAELNDIMT 218
Cdd:PRK13225  214 AVMYVGDETRDVEAARQVGLIAVAVTWGFNDRQSLVAACPDWLLETPSDLLQAVT 268
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 7-186 3.30e-10

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: 57.00  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   7 LWDFDGTLADTGSDVWNSLTYAARRAGGAIDDlymrdDANLADPMDEIMRHVIPYPGEayLETFDEDVRVHYRTLNDfsR 86
Cdd:cd07523     3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDL-----ETVYKIIKESSVQFAIQYYAE--VPDLEEEYKELEAEYLA--K 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  87 TRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRrILGSKGWANLFDDWICPDS----IPGREAtkvemIAEIVRRHGIAP 162
Cdd:cd07523    74 PILFPGAKAVLRWIKEQGGKNFLMTHRDHSALT-ILKKDGIASYFTEIVTSDNgfprKPNPEA-----INYLLNKYQLNP 147

                         170       180
                  ....*....|....*....|....
gi 1062061009 163 RQCLYVGDTFSDIEAARTNGISCI 186
Cdd:cd07523   148 EETVMIGDRELDIEAGHNAGISTI 171
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 6-179 8.46e-10

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: 55.86  E-value: 8.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   6 LLWDFDGTLADTGSDVWNSLTYAARRaggaIDDLYMRDDANLADPmdEIMRHVIPYPGEAYLETFDEDVRVHYRTLNDFs 85
Cdd:TIGR01549   2 ILFDIDGTLVDIKFAIRRAFPQTFEE----FGLDPASFKALKQAG--GLAEEEWYRIATSALEELQGRFWSEYDAEEAY- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  86 rtrlYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDwICPDSIPGREATKvEMIAEIVRRHGIAPRqC 165
Cdd:TIGR01549  75 ----IRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFEL-ILVSDEPGSKPEP-EIFLAALESLGVPPE-V 147

                         170
                  ....*....|....
gi 1062061009 166 LYVGDTFSDIEAAR 179
Cdd:TIGR01549 148 LHVGDNLNDIEGAR 161
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 88-212 1.28e-08

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: 52.79  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  88 RLYPGIQSMLNELKGHSVRNIIVTN---------------KPEGALRRILGSKGwaNLFDDW-ICPDSI----------P 141
Cdd:COG0241    28 EFLPGVLEALARLNEAGYRLVVVTNqsgigrglfteedlnAVHAKMLELLAAEG--GRIDAIyYCPHHPddncdcrkpkP 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062061009 142 GreatkveMIAEIVRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEiALLSRNPAYVAHDIAE 212
Cdd:COG0241   106 G-------MLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKGAE-ELAEALPDTVADDLAE 168
HAD pfam12710
haloacid dehalogenase-like hydrolase;
6-179 4.10e-08

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 51.38  E-value: 4.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   6 LLWDFDGTLADTGSD-------VWNSLTYAARRAGGAIDDLYMRDDANLADPMDEIMRhvipypgEAYLETF-DEDVRVH 77
Cdd:pfam12710   1 ALFDLDGTLLDGDSLflliralLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELL-------RALLAGLpEEDAAEL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  78 YRTLNDFSRTRLYPGIQSMLNELKGHSVRNIIVTnkpeGALRRILGSKGWANLFDDWIC---------------PDSIPG 142
Cdd:pfam12710  74 ERFVAEVALPRLHPGALELLAAHRAAGDRVVVVT----GGLRPLVEPVLAELGFDEVLAtelevddgrftgelrLIGPPC 149

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1062061009 143 REATKVEMIAE--IVRRHGIAPRQCLYVGDTFSDIEAAR 179
Cdd:pfam12710 150 AGEGKVRRLRAwlAARGLGLDLADSVAYGDSPSDLPMLR 188
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-176 3.15e-07

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 49.45  E-value: 3.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   1 MEYRCLLWDFDGTLadTGSDVWNSLTYAARRAGG-----------AIDDLYMRDDANladpMDEIMRHVIpypgeAYLET 69
Cdd:COG0560     1 RKMRLAVFDLDGTL--IAGESIDELARFLGRRGLvdrrevleevaAITERAMAGELD----FEESLRFRV-----ALLAG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  70 FDEDV--RVHYRTLNDfsRTRLYPGIQSMLNELKGHSVRNIIVTNKPE---GALRRILGskgwanlFDDWIC-------- 136
Cdd:COG0560    70 LPEEEleELAERLFEE--VPRLYPGARELIAEHRAAGHKVAIVSGGFTffvEPIAERLG-------IDHVIAnelevedg 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1062061009 137 ------PDSIPGREAtKVEMIAEIVRRHGIAPRQCLYVGDTFSDIE 176
Cdd:COG0560   141 rltgevVGPIVDGEG-KAEALRELAAELGIDLEQSYAYGDSANDLP 185
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 88-188 4.73e-07

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 49.26  E-value: 4.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  88 RLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPgREATKVEMIAEIVRRHGIAPRQCLY 167
Cdd:PLN03243  109 RLRPGSREFVQALKKHEIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVY-RGKPDPEMFMYAAERLGFIPERCIV 187

                          90       100
                  ....*....|....*....|.
gi 1062061009 168 VGDTFSDIEAARTNGISCIAV 188
Cdd:PLN03243  188 FGNSNSSVEAAHDGCMKCVAV 208
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 6-191 6.62e-07

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: 48.14  E-value: 6.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   6 LLWDFDGTLADTGSD---VWNSLTYAARRAGGAID-DLYmRDDANLADPMDEIMRHV-IPYPGEAYLETFDEDVR----- 75
Cdd:cd07528     2 LIFDVDGTLAETEELhrrAFNNAFFAERGLDWYWDrELY-GELLRVGGGKERIAAYFeKVGWPESAPKDLKELIAdlhka 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  76 --VHYRTLNDFSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGA----LRRILGsKGWANLFDDWICPDSIPGRE-ATKV 148
Cdd:cd07528    81 ktERYAELIAAGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANvdalLSALLG-PERRAIFDAIAAGDDVAEKKpDPDI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1062061009 149 EMIAeiVRRHGIAPRQCLYVGDTFSDIEAARTNGISCIaVTYG 191
Cdd:cd07528   160 YLLA--LERLGVSPSDCLAIEDSAIGLQAAKAAGLPCI-VTPS 199
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 88-183 1.61e-06

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. 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: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 45.99  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  88 RLYPGIQSMLNELKGHSVRNIIVTN---------------KPEGALRRILGSKGwaNLFDDW-ICPDSiPGREAT----K 147
Cdd:cd07503    25 EFLPGVIEALKKLKDAGYLVVVVTNqsgiargyfseadfeALHDKMRELLASQG--VEIDDIyYCPHH-PDDGCPcrkpK 101

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1062061009 148 VEMIAEIVRRHGIAPRQCLYVGDTFSDIEAARTNGI 183
Cdd:cd07503   102 PGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGC 137
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 6-189 2.22e-06

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: 45.68  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   6 LLWDFDGTLADTGSDVWNSLTYAARRaggaiddlymrddanladpmDEIMRHVIPypgeayletfdedvrvhyrtlndFS 85
Cdd:cd07505     2 VIFDMDGVLIDTEPLHRQAWQLLERK--------------------NALLLELIA-----------------------SE 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  86 RTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGS-KGWANLFDDWICPDSIpgrEATK--VEMIAEIVRRHGIAP 162
Cdd:cd07505    39 GLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLElGLLRGYFDVIVSGDDV---ERGKpaPDIYLLAAERLGVDP 115

                         170       180
                  ....*....|....*....|....*..
gi 1062061009 163 RQCLYVGDTFSDIEAARTNGISCIAVT 189
Cdd:cd07505   116 ERCLVFEDSLAGIEAAKAAGMTVVAVP 142
PLN02940 PLN02940
riboflavin kinase
 5-203 1.70e-05

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 44.82  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   5 CLLWDFDGTLADTGSDVWNSLTYAARRAGGAIDDlymRDDANLA--DPMDE----IMRHVIPYPGEAYLETFdedvrvhY 78
Cdd:PLN02940   13 HVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDG---REAQKIVgkTPLEAaatvVEDYGLPCSTDEFNSEI-------T 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  79 RTLND-FSRTRLYPGIQSMLNELKGHSVRNIIVTNKPEGALR-RILGSKGWANLFDDWICPDSI-PGREATkvEMIAEIV 155
Cdd:PLN02940   83 PLLSEqWCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEaKISCHQGWKESFSVIVGGDEVeKGKPSP--DIFLEAA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1062061009 156 RRHGIAPRQCLYVGDTFSDIEAARTNGISCIAV--------TYGDGDEI--ALLSRNP 203
Cdd:PLN02940  161 KRLNVEPSNCLVIEDSLPGVMAGKAAGMEVIAVpsipkqthLYSSADEVinSLLDLQP 218
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 89-189 5.84e-05

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: 41.62  E-value: 5.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  89 LYPGIQSMLNELKGHSVRNIIVTNK-----------PEGALRRILGSKGwANLFDDWICpdsiPGREATKVEMIAEIVRR 157
Cdd:TIGR01662  26 LYPEVPDALAELKEAGYKVVIVTNQsgigrgyfsrsFSGRVARRLEELG-VPIDILYAC----PGCRKPKPGMFLEALKR 100

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1062061009 158 H-GIAPRQCLYVGDT-FSDIEAARTNGISCIAVT 189
Cdd:TIGR01662 101 FnEIDPEESVYVGDQdLTDLQAAKRVGLATILVA 134
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 159-218 9.98e-05

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 42.92  E-value: 9.98e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1062061009  159 GIAPRQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIaLLSRNPAYVAHDIAE--LNDIMT 218
Cdd:PLN02919   232 GVPTSECVVIEDALAGVQAARAAGMRCIAVTTTLSEEI-LKDAGPSLIRKDIGNisLSDILT 292
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 89-183 1.66e-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: 39.83  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  89 LYPGIQSMLNELKGHsVRNIIVTNKP-EGALRRILGSkGWANLFDDWICPDSIpGREATKVEMIAEIVRRHGIAPRQCLY 167
Cdd:cd04305    10 LLPGAKELLEELKKG-YKLGIITNGPtEVQWEKLEQL-GIHKYFDHIVISEEV-GVQKPNPEIFDYALNQLGVKPEETLM 86

                          90
                  ....*....|....*..
gi 1062061009 168 VGDTF-SDIEAARTNGI 183
Cdd:cd04305    87 VGDSLeSDILGAKNAGI 103
PRK06769 PRK06769
HAD-IIIA family hydrolase;
73-212 2.00e-04

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 40.87  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  73 DVRVHYRtlNDFSrtrLYPGIQSMLNELKGHSVRNIIVTNKPEGAlrrilgsKGWANL-----------FDD-WICPDSI 140
Cdd:PRK06769   18 DTTIHYP--GSFT---LFPFTKASLQKLKANHIKIFSFTNQPGIA-------DGIATIadfvqelkgfgFDDiYLCPHKH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009 141 -PGREATKVE--MIAEIVRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRN------PAYVAHDIA 211
Cdd:PRK06769   86 gDGCECRKPStgMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVNATTILVRTGAGYDALHTYRDkwahiePNYIAENFE 165


                  .
gi 1062061009 212 E 212
Cdd:PRK06769  166 D 166
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 93-188 2.40e-04

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: 39.36  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  93 IQSMLNELKGHSVRNIIVTNKPEGALRRIL-----GSKGWANLFDDWICPDSIPgreatkvEMIAEIVRRHGIAPRQCLY 167
Cdd:cd16421    12 ILELLKALRQKGIKLAVLSNKPNEAVQVLVeelfpGSFDFVLGEKEGIRRKPDP-------T*ALECAKVLGVPPDEVLY 84

                          90       100
                  ....*....|....*....|.
gi 1062061009 168 VGDTFSDIEAARTNGISCIAV 188
Cdd:cd16421    85 VGDSGVDMQTARNAGMDEIGV 105
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 4-218 3.57e-04

bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 41.15  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009   4 RCLLWDFDGTLADTGSDVWNSL--TYAARRAggaiddLYMRDDANLADPMDEIMRHVIPYPGEAYLETFDEDVRVHY--- 78
Cdd:PRK06698  242 QALIFDMDGTLFQTDKILELSLddTFDHLRS------LQLWDTVTPIDKYREIMGVPLPKVWEALLPDHSLEIREQTday 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  79 ---RTLNDFSRTR--LYPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGwanlFDDWICPD-SIPGREA-TKVEMI 151
Cdd:PRK06698  316 fleRLIENIKSGKgaLYPNVKEIFTYIKENNCSIYIASNGLTEYLRAIVSYYD----LDQWVTETfSIEQINSlNKSDLV 391

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062061009 152 AEIVRRHGIapRQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIALLSRNpaYVAHDIAELNDIMT 218
Cdd:PRK06698  392 KSILNKYDI--KEAAVVGDRLSDINAAKDNGLIAIGCNFDFAQEDELAQAD--IVIDDLLELKGILS 454
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 75-189 4.26e-04

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. 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. 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: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 39.22  E-value: 4.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  75 RVHYRTLNDFSRTRLY---------PGIQSMLNELkghSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGREA 145
Cdd:cd07526    20 RVLVEVLAELGARVLAafeaelqpiPGAAAALSAL---TLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASDVGRGK 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1062061009 146 TKVEMIAEIVRRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVT 189
Cdd:cd07526    97 PAPDLFLHAAAQMGVAPERCLVIEDSPTGVRAALAAGMTVFGFT 140
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 96-182 8.63e-04

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 38.77  E-value: 8.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  96 MLNELKGhsvRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIPGREATKVEMIAEIVRRHGIAPRQCLYVGDTFSDI 175
Cdd:cd02604    91 LLLALPG---RKIIFTNASKNHAIRVLKRLGLADLFDGIFDIEYAGPDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNL 167


                  ....*..
gi 1062061009 176 EAARTNG 182
Cdd:cd02604   168 LAAKALG 174
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 91-189 2.86e-03

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: 37.23  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  91 PGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSIpgrEATKV--EMIAEIVRRHGIAPRQCLYV 168
Cdd:cd16423    47 EGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDV---EKSKPdpDLYLEAAERLGVNPEECVVI 123

                          90       100
                  ....*....|....*....|.
gi 1062061009 169 GDTFSDIEAARTNGISCIAVT 189
Cdd:cd16423   124 EDSRNGVLAAKAAGMKCVGVP 144
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 10-215 2.93e-03

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 37.63  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  10 FD--GTLADtgsdvWNSLTYAARRA----GGAIDDLYMRDDANLADpMDEIMRHVIPYPgEAYLETFDEDVRVHYRTLND 83
Cdd:cd02588     5 FDvyGTLID-----WHSGLAAAERAfpgrGEELSRLWRQKQLEYTW-LVTLMGPYVDFD-ELTRDALRATAAELGLELDE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  84 FSRTRL---------YPGIQSMLNELKGHSVRNIIVTNKPEGALRRILGSKGWANLFDDWICPDSI----PGREAtkVEM 150
Cdd:cd02588    78 SDLDELgdaylrlppFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVraykPAPAV--YEL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062061009 151 IAEivrRHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYGDGDEIAlLSRNPAYVAHDIAELND 215
Cdd:cd02588   156 AAE---RLGVPPDEILHVASHAWDLAGARALGLRTAWINRPGEVPDP-LGPAPDFVVPDLGELAD 216
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
 86-188 3.74e-03

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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: 319804 [Multi-domain]  Cd Length: 129  Bit Score: 36.17  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062061009  86 RTRLYPGIQSMLNELKGhsvRNIIV-----TNKPEGAlRRILGSKGWANLFDDW-ICPDSipgreatKVEMIAEIVRRHG 159
Cdd:cd07501    32 EVSLYPDAQEILKELKE---RGILLavasrNNEFDHA-NEVLEKLDLKELFDAFeIYPGS-------KSSHFRKIAKELG 100

                          90       100
                  ....*....|....*....|....*....
gi 1062061009 160 IAPRQCLYVGDTFSDIEAARTNGISCIAV 188
Cdd:cd07501   101 IGFDSMVFFDDEPRNREEVSEGGVTCILV 129
HAD_like cd07506
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 157-191 3.76e-03

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: 319809  Cd Length: 115  Bit Score: 36.20  E-value: 3.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1062061009 157 RHGIAPRQCLYVGDTFSDIEAARTNGISCIAVTYG 191
Cdd:cd07506    81 GYAFDPHQVVVIGDTPNDVACARALGARSVAVATG 115
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 132-198 9.27e-03

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 36.12  E-value: 9.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062061009 132 DDWICPDSIP-GREATkvEMIAEIVRRHGIAP-RQCLYVGDTFSDIEAARTNGISCIAVTYGdGDEIAL 198
Cdd:cd02586   143 DSLVTPDDVPaGRPYP--WMCYKNAIELGVYDvAAVVKVGDTVPDIKEGLNAGMWTVGVILS-GNELGL 208
 
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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