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Conserved domains on  [gi|500712646|ref|WP_011979083|]
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MULTISPECIES: HAD family hydrolase [Pseudomonas aeruginosa group]

Protein Classification

HAD family hydrolase( domain architecture ID 11560819)

HAD (Haloacid Dehalogenase) family hydrolase such as Pseudomonas aeruginosa 5'-nucleotidase, which specifically dephosphorylates nucleoside 5'-monophosphates to nucleosides and inorganic phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 10-218 7.62e-114

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: 323.77  E-value: 7.62e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  10 HILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPLLQCFMQTYGFDEARAWEAVNHYRERFRVTGLYEN 89
Cdd:cd04302    1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRELLPFDEEEAQRAVDAYREYYKEKGLFEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  90 RVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQCLMI 169
Cdd:cd04302   81 EVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGSRVHKADVIRYALDTLGIAPEQAVMI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 500712646 170 GDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAALRQVL 218
Cdd:cd04302  161 GDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATYIVETPAELLELL 209
 
Name Accession Description Interval E-value
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 10-218 7.62e-114

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: 323.77  E-value: 7.62e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  10 HILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPLLQCFMQTYGFDEARAWEAVNHYRERFRVTGLYEN 89
Cdd:cd04302    1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRELLPFDEEEAQRAVDAYREYYKEKGLFEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  90 RVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQCLMI 169
Cdd:cd04302   81 EVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGSRVHKADVIRYALDTLGIAPEQAVMI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 500712646 170 GDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAALRQVL 218
Cdd:cd04302  161 GDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATYIVETPAELLELL 209
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
8-220 1.05e-66

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 204.39  E-value: 1.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   8 YPHILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPLLQCFMQTYGFD-EARAWEAVNHYRERFRVTGL 86
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDpDEELEELLARFRELYEEELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  87 YENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQC 166
Cdd:COG0546   81 DETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500712646 167 LMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAALRQVLES 220
Cdd:COG0546  161 LMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGADYVIDSLAELLALLAE 214
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-189 6.19e-29

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 106.51  E-value: 6.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPLLQCFMQTygFDEARAWEAVNHYRERFRvTGLYENR 90
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYL--GVSEDEEEKIEFYLRKYN-EELHDKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   91 V--FDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQCLM 168
Cdd:pfam13419  78 VkpYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIY 157

                         170       180
                  ....*....|....*....|.
gi 500712646  169 IGDRMHDLLGASRNGVACIGV 189
Cdd:pfam13419 158 VGDSPRDIEAAKNAGIKVIAV 178
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
11-219 1.84e-25

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 98.73  E-value: 1.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIG---PPLLQ--CFMQTYGFDEARAWEAVNHYRERFRVTG 85
Cdd:PRK13222   9 VAFDLDGTLVDSAPDLAAAVNAALAALGLPPAGEERVRTWVGngaDVLVEraLTWAGREPDEELLEKLRELFDRHYAENV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  86 LYENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSeldgtrthkDEL---------IRHLL 156
Cdd:PRK13222  89 AGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGG---------DSLpnkkpdpapLLLAC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500712646 157 DSEGLAAEQCLMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAALRQVLE 219
Cdd:PRK13222 160 EKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYGYNYGEPIALSEPDVVIDHFAELLPLLG 222
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 11-202 3.37e-16

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: 74.09  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIG---PPLLQCFMQTYG--FDEARAWEAVNHYRERFRVTG 85
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAAAVNMALAALGLPPATLARVIGFIGngvPVLMERVLAWAGqePDAQRVAELRKLFDRHYEEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   86 LYENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQ 165
Cdd:TIGR01449  81 GELTSVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQRKPHPDPLLLAAERLGVAPQQ 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 500712646  166 CLMIGDRMHDLLGASRNGVACIGVGYGF---GSEDELRAH 202
Cdd:TIGR01449 161 MVYVGDSRVDIQAARAAGCPSVLLTYGYrygEAIDLLPPD 200
 
Name Accession Description Interval E-value
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 10-218 7.62e-114

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: 323.77  E-value: 7.62e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  10 HILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPLLQCFMQTYGFDEARAWEAVNHYRERFRVTGLYEN 89
Cdd:cd04302    1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRELLPFDEEEAQRAVDAYREYYKEKGLFEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  90 RVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQCLMI 169
Cdd:cd04302   81 EVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGSRVHKADVIRYALDTLGIAPEQAVMI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 500712646 170 GDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAALRQVL 218
Cdd:cd04302  161 GDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATYIVETPAELLELL 209
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
8-220 1.05e-66

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 204.39  E-value: 1.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   8 YPHILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPLLQCFMQTYGFD-EARAWEAVNHYRERFRVTGL 86
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDpDEELEELLARFRELYEEELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  87 YENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQC 166
Cdd:COG0546   81 DETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500712646 167 LMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAALRQVLES 220
Cdd:COG0546  161 LMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGADYVIDSLAELLALLAE 214
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-189 6.19e-29

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 106.51  E-value: 6.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPLLQCFMQTygFDEARAWEAVNHYRERFRvTGLYENR 90
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYL--GVSEDEEEKIEFYLRKYN-EELHDKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   91 V--FDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQCLM 168
Cdd:pfam13419  78 VkpYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIY 157

                         170       180
                  ....*....|....*....|.
gi 500712646  169 IGDRMHDLLGASRNGVACIGV 189
Cdd:pfam13419 158 VGDSPRDIEAAKNAGIKVIAV 178
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 11-214 1.41e-28

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: 106.59  E-value: 1.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPL---LQCFMQTYGfdEARAWEAVNHYRERFRVtgly 87
Cdd:cd02616    4 ILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVLPFIGPPLretFEKIDPDKL--EDMVEEFRKYYREHNDD---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  88 ENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGseLDGTRTHKD--ELIRHLLDSEGLAAEQ 165
Cdd:cd02616   78 LTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVG--GDDVTHHKPdpEPVLKALELLGAEPEE 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 500712646 166 CLMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAAL 214
Cdd:cd02616  156 ALMVGDSPHDILAGKNAGVKTVGVTWGYKGREYLKAFNPDFIIDKMSDL 204
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 11-214 2.09e-26

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: 101.16  E-value: 2.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIG---PPLLQCFMqTYGFDEARAWEAVNHYRERF----RV 83
Cdd:cd16417    2 VAFDLDGTLVDSAPDLAEAANAMLAALGLPPLPEETVRTWIGngaDVLVERAL-TGAREAEPDEELFKEARALFdrhyAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  84 TGLYENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSE-LDGTRTHKDELiRHLLDSEGLA 162
Cdd:cd16417   81 TLSVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDsLPEKKPDPAPL-LHACEKLGIA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500712646 163 AEQCLMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAAL 214
Cdd:cd16417  160 PAQMLMVGDSRNDILAARAAGCPSVGLTYGYNYGEDIAASGPDAVIDSLAEL 211
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
11-219 1.84e-25

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 98.73  E-value: 1.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIG---PPLLQ--CFMQTYGFDEARAWEAVNHYRERFRVTG 85
Cdd:PRK13222   9 VAFDLDGTLVDSAPDLAAAVNAALAALGLPPAGEERVRTWVGngaDVLVEraLTWAGREPDEELLEKLRELFDRHYAENV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  86 LYENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSeldgtrthkDEL---------IRHLL 156
Cdd:PRK13222  89 AGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGG---------DSLpnkkpdpapLLLAC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500712646 157 DSEGLAAEQCLMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAALRQVLE 219
Cdd:PRK13222 160 EKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYGYNYGEPIALSEPDVVIDHFAELLPLLG 222
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 11-197 3.43e-24

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: 95.46  E-value: 3.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIG---PPLLQCFMQTYGF--DEARAWEAVNHYRERFRVTG 85
Cdd:cd07512    2 VIFDLDGTLIDSAPDLHAALNAVLAAEGLAPLSLAEVRSFVGhgaPALIRRAFAAAGEdlDGPLHDALLARFLDHYEADP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  86 LYENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQ 165
Cdd:cd07512   82 PGLTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGDVSR 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 500712646 166 CLMIGDRMHDLLGASRNGVACIGVGYGFGSED 197
Cdd:cd07512  162 ALMVGDSETDAATARAAGVPFVLVTFGYRHAP 193
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 8-218 2.14e-22

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: 90.86  E-value: 2.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   8 YPHILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPP----------------LLQCFMQTYGFDEARaw 71
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEyalwrryergeitfaeLLRRLLEELGLDLAE-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  72 EAVNHYRERFRvtglYENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRthK-DE 150
Cdd:COG1011   79 ELAEAFLAALP----ELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVR--KpDP 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646 151 LI-RHLLDSEGLAAEQCLMIGDRM-HDLLGASRNGVACIGVGYgfGSEDELRAHQPTHYCADLAALRQVL 218
Cdd:COG1011  153 EIfELALERLGVPPEEALFVGDSPeTDVAGARAAGMRTVWVNR--SGEPAPAEPRPDYVISDLAELLELL 220
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 11-219 2.32e-20

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 85.08  E-value: 2.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPLLQCFMqtyGFDEARAWEAVNHYRErFRVTGLYEN- 89
Cdd:PRK13288   6 VLFDLDGTLINTNELIISSFLHTLKTYYPNQYKREDVLPFIGPSLHDTFS---KIDESKVEEMITTYRE-FNHEHHDELv 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  90 RVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGseLDGTRTHK--DELIRHLLDSEGLAAEQCL 167
Cdd:PRK13288  82 TEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVIT--LDDVEHAKpdPEPVLKALELLGAKPEEAL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500712646 168 MIGDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAALRQVLE 219
Cdd:PRK13288 160 MVGDNHHDILAGKNAGTKTAGVAWTIKGREYLEQYKPDFMLDKMSDLLAIVG 211
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 11-201 1.62e-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: 82.83  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPLLQCFMQTYGFDEARAWEAVNHYRERFRVTGLY--- 87
Cdd:cd07533    2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAEVRSIIGLSLDEAIARLLPMATPALVAVAERYKEAFDILRLLpeh 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  88 ENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFkaiygselDGTRTHKD-------ELIRHLLDSEG 160
Cdd:cd07533   82 AEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYF--------DATRTADDtpskphpEMLREILAELG 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500712646 161 LAAEQCLMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRA 201
Cdd:cd07533  154 VDPSRAVMVGDTAYDMQMAANAGAHAVGVAWGYHSLEDLRS 194
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 11-183 4.30e-18

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: 78.78  E-value: 4.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPplLQCFMQTYGFDEARAWEAVNHYRER---------- 80
Cdd:pfam00702   4 VVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIP--VEDFTARLLLGKRDWLEELDILRGLvetleaeglt 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   81 ------FRVTGLYEN-RVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIR 153
Cdd:pfam00702  82 vvlvelLGVIALADElKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYL 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 500712646  154 HLLDSEGLAAEQCLMIGDRMHDLLGASRNG 183
Cdd:pfam00702 162 AALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 92-189 9.93e-18

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: 75.51  E-value: 9.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  92 FDG---IPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQCLM 168
Cdd:cd01427    6 LDGtllAVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLF 85

                         90       100
                 ....*....|....*....|.
gi 500712646 169 IGDRMHDLLGASRNGVACIGV 189
Cdd:cd01427   86 VGDSENDIEAARAAGGRTVAV 106
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
11-214 1.83e-17

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 77.17  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLGIDePDLARLEHFIGPPL---LQCFMQTYG--FDEARAWEAVN-HYRERFRVT 84
Cdd:COG0637    5 VIFDMDGTLVDSEPLHARAWREAFAELGID-LTEEEYRRLMGRSRediLRYLLEEYGldLPEEELAARKEeLYRELLAEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  85 GLyenRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSElDGTRtHKD--ELIRHLLDSEGLA 162
Cdd:COG0637   84 GL---PLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGD-DVAR-GKPdpDIYLLAAERLGVD 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500712646 163 AEQCLMIGDRMHDLLGASRNGVACIGVGYGFGSEDELraHQPTHYCADLAAL 214
Cdd:COG0637  159 PEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEEL--AGADLVVDDLAEL 208
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 11-216 1.72e-16

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: 74.70  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLG---IDEPDLARLEHFIGPPLLQCFmqtygfdEARAWEAVNHYRERFRvtgLY 87
Cdd:cd04303    2 IIFDFDGTLADSFPWFLSILNQLAARHGfktVDEEEIEQLRQLSSREILKQL-------GVPLWKLPLIAKDFRR---LM 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  88 ENRV-----FDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGtrthKDELIRHLLDSEGLA 162
Cdd:cd04303   72 AEAApelalFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFAVIEGSSLFG----KAKKIRRVLRRTKIT 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500712646 163 AEQCLMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAALRQ 216
Cdd:cd04303  148 AAQVIYVGDETRDIEAARKVGLAFAAVSWGYAKPEVLKALAPDHMLEDPEDLIQ 201
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 11-202 3.37e-16

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: 74.09  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIG---PPLLQCFMQTYG--FDEARAWEAVNHYRERFRVTG 85
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAAAVNMALAALGLPPATLARVIGFIGngvPVLMERVLAWAGqePDAQRVAELRKLFDRHYEEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   86 LYENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQ 165
Cdd:TIGR01449  81 GELTSVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQRKPHPDPLLLAAERLGVAPQQ 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 500712646  166 CLMIGDRMHDLLGASRNGVACIGVGYGF---GSEDELRAH 202
Cdd:TIGR01449 161 MVYVGDSRVDIQAARAAGCPSVLLTYGYrygEAIDLLPPD 200
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 10-183 1.02e-15

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


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 71.66  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   10 HILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEhfIGPPLLQCfmQTYGFDEARAWEAVNHYRERFRVTGLYen 89
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALK--QAGGLAEE--EWYRIATSALEELQGRFWSEYDAEEAY-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   90 rvFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKdELIRHLLDSEGLAAEqCLMI 169
Cdd:TIGR01549  75 --IRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGSKPEP-EIFLAALESLGVPPE-VLHV 150

                         170
                  ....*....|....
gi 500712646  170 GDRMHDLLGASRNG 183
Cdd:TIGR01549 151 GDNLNDIEGARNAG 164
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 11-202 2.77e-13

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: 66.40  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTdPREGITRSVQFALARLGIDEPDLARLEHFIgpplLQCFMQ-TYGFDEARAW----------EAVNHYRE 79
Cdd:COG0560    6 AVFDLDGTLI-AGESIDELARFLGRRGLVDRREVLEEVAAI----TERAMAgELDFEESLRFrvallaglpeEELEELAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  80 RFRVTglyENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRhfkaIYGSEL---DGT-----------R 145
Cdd:COG0560   81 RLFEE---VPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDH----VIANELeveDGRltgevvgpivdG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 500712646 146 THKDELIRHLLDSEGLAAEQCLMIGDRMHDL--LGASRNGVAcigvgygFGSEDELRAH 202
Cdd:COG0560  154 EGKAEALRELAAELGIDLEQSYAYGDSANDLpmLEAAGLPVA-------VNPDPALREA 205
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 11-214 3.98e-12

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 63.73  E-value: 3.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIG---PPL----LQCFMQTYGFDEARAWEAV----NHYRE 79
Cdd:PRK13223  16 VMFDLDGTLVDSVPDLAAAVDRMLLELGRPPAGLEAVRHWVGngaPVLvrraLAGSIDHDGVDDELAEQALalfmEAYAD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  80 RFRVTglyenRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSE 159
Cdd:PRK13223  96 SHELT-----VVYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVMKMA 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 500712646 160 GLAAEQCLMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAAL 214
Cdd:PRK13223 171 GVPPSQSLFVGDSRSDVLAAKAAGVQCVALSYGYNHGRPIAEESPALVIDDLRAL 225
Hydrolase_like pfam13242
HAD-hyrolase-like;
150-214 2.34e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 54.93  E-value: 2.34e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500712646  150 ELIRHLLDSEGLAAEQCLMIGDRM-HDLLGASRNGVACIGVGYGFGSEDELR--AHQPTHYCADLAAL 214
Cdd:pfam13242   8 GMLERALARLGLDPERTVMIGDRLdTDILGAREAGARTILVLTGVTRPADLEkaPIRPDYVVDDLAEA 75
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 4-210 6.13e-10

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 57.17  E-value: 6.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   4 AALRYPH-ILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPLLQCFMQTYGFDEARAWEA-VNHYRERF 81
Cdd:PRK13226   7 AAVRFPRaVLFDLDGTLLDSAPDMLATVNAMLAARGRAPITLAQLRPVVSKGARAMLAVAFPELDAAARDAlIPEFLQRY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  82 RVTGLYENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGL 161
Cdd:PRK13226  87 EALIGTQSQLFDGVEGMLQRLECAGCVWGIVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPHPLPLLVAAERIGV 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 500712646 162 AAEQCLMIGDRMHDLLGASRNGVACIGVGYGFGSEDElrahQPTHYCAD 210
Cdd:PRK13226 167 APTDCVYVGDDERDILAARAAGMPSVAALWGYRLHDD----DPLAWQAD 211
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
150-214 8.49e-09

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 53.96  E-value: 8.49e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500712646 150 ELIRHLLDSEGLAAEQCLMIGDRMH-DLLGASRNGVACIGVGYGFGSEDELRAH--QPTHYCADLAAL 214
Cdd:COG0647  190 PIYELALERLGVDPERVLMVGDRLDtDILGANAAGLDTLLVLTGVTTAEDLEAApiRPDYVLDSLAEL 257
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 10-189 1.42e-08

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: 52.42  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   10 HILFDLDGTLTDPREGITRSVQFALARLgidEPDLARLEHFIGPPLLQCFMQT--YGFDEARAWEAVNHYRERFRVTGLY 87
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINREELGL---VPDELGVSAVGRLELALRRFKAqyGRTISPEDAQLLYKQLFYEQIEEEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   88 ENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIArHFAFDRHFKAIYGSElDGTRTHKDELI-RHLLDSEGLAAEQC 166
Cdd:TIGR01509  78 KLKPLPGVRALLEALRARGKKLALLTNSPRAHKLVLA-LLGLRDLFDVVIDSS-DVGLGKPDPDIyLQALKALGLEPSEC 155

                         170       180
                  ....*....|....*....|...
gi 500712646  167 LMIGDRMHDLLGASRNGVACIGV 189
Cdd:TIGR01509 156 VFVDDSPAGIEAAKAAGMHTVGV 178
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 11-187 1.02e-07

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: 50.07  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLGIdEPDLARLEHFIGPPLLQCFMQTYGfdearAWEAVNHYRERFRVTGLYENR 90
Cdd:cd07523    2 FIWDLDGTLLDSYPAMTKALSETLADFGI-PQDLETVYKIIKESSVQFAIQYYA-----EVPDLEEEYKELEAEYLAKPI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  91 VFDGIPELLEALVGRGHTLYVATSKpGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQCLMIG 170
Cdd:cd07523   76 LFPGAKAVLRWIKEQGGKNFLMTHR-DHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVMIG 154

                        170
                 ....*....|....*..
gi 500712646 171 DRMHDLLGASRNGVACI 187
Cdd:cd07523  155 DRELDIEAGHNAGISTI 171
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 95-189 3.67e-07

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: 47.07  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  95 IPELLEALVGRGHTLYVATSKPGVFAREIARHFaFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQCLMIGDRMH 174
Cdd:cd16421   12 ILELLKALRQKGIKLAVLSNKPNEAVQVLVEEL-FPGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSGV 90

                         90
                 ....*....|....*
gi 500712646 175 DLLGASRNGVACIGV 189
Cdd:cd16421   91 DMQTARNAGMDEIGV 105
HAD pfam12710
haloacid dehalogenase-like hydrolase;
11-176 5.51e-07

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 48.30  E-value: 5.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   11 ILFDLDGTLTDPREGItrsvQFALARLGIDEPDLARLEHFIGPPLLQCFMQTYGFDEARA---------WEAVNHYRERF 81
Cdd:pfam12710   1 ALFDLDGTLLDGDSLF----LLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGAREllrallaglPEEDAAELERF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   82 rVTGLYENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDrhfkAIYGSELDGTRTH-------------- 147
Cdd:pfam12710  77 -VAEVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFD----EVLATELEVDDGRftgelrligppcag 151

                         170       180       190
                  ....*....|....*....|....*....|...
gi 500712646  148 --KDELIRHLLD--SEGLAAEQCLMIGDRMHDL 176
Cdd:pfam12710 152 egKVRRLRAWLAarGLGLDLADSVAYGDSPSDL 184
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 10-172 1.46e-06

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. 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: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 46.95  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  10 HILFDLDGTLTDPreGITRSVQfALARLGIDEPDLARLEHFIGPPLLQcfMQTYGFDEARAWEAVNHYRERFRVTGLYE- 88
Cdd:cd02603    3 AVLFDFGGVLIDP--DPAAAVA-RFEALTGEPSEFVLDTEGLAGAFLE--LERGRITEEEFWEELREELGRPLSAELFEe 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  89 -----NRVFDGIPELLEALVGRGHTLYVAT-SKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLA 162
Cdd:cd02603   78 lvlaaVDPNPEMLDLLEALRAKGYKVYLLSnTWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIYQLALERLGVK 157

                        170
                 ....*....|
gi 500712646 163 AEQCLMIGDR 172
Cdd:cd02603  158 PEEVLFIDDR 167
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 12-176 3.28e-06

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 46.18  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   12 LFDLDGTLTDpREGITRSVQFALARLGIDE-----PDLARLEHFIG---PPLLQCFMQTYGFDEARAWEAVNHYRERFrV 83
Cdd:TIGR01490   3 FFDFDGTLTA-KDTLFIFLKFLASKNILFEelrlpKVLARFEFFLNrglDYMAYYRAFALDALAGLLEEDVRAIVEEF-V 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   84 TGLYENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKA--------IYGSELDGTRTH---KDELI 152
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTrleesedgIYTGNIDGNNCKgegKVHAL 160

                         170       180
                  ....*....|....*....|....
gi 500712646  153 RHLLDSEGLAAEQCLMIGDRMHDL 176
Cdd:TIGR01490 161 AELLAEEQIDLKDSYAYGDSISDL 184
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 11-220 3.49e-06

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 46.93  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  11 ILFDLDGTL--TDpregitrsvqfALARLGIDEP--DLARLEHFIGPPLLQCFMQTYGFDEARAWEAV--NHYRERFRVT 84
Cdd:PRK06698 244 LIFDMDGTLfqTD-----------KILELSLDDTfdHLRSLQLWDTVTPIDKYREIMGVPLPKVWEALlpDHSLEIREQT 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  85 GLY------EN------RVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTrTHKDELI 152
Cdd:PRK06698 313 DAYflerliENiksgkgALYPNVKEIFTYIKENNCSIYIASNGLTEYLRAIVSYYDLDQWVTETFSIEQINS-LNKSDLV 391

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500712646 153 RHLLDSEGLaaEQCLMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRahQPTHYCADLAALRQVLES 220
Cdd:PRK06698 392 KSILNKYDI--KEAAVVGDRLSDINAAKDNGLIAIGCNFDFAQEDELA--QADIVIDDLLELKGILST 455
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 11-176 7.06e-06

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 44.65  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   11 ILFDLDGTLTDpREGITRSVQFALARLGIDEpDLARLEHFIGPPLLQCFMQTYGFDEARAWEAVNHYRERFRVTglyenr 90
Cdd:TIGR01488   2 AIFDFDGTLTR-QDSLIDLLAKLLGTNDEVI-ELTRLAPSGRISFEDALGRRLALLHRSRSEEVAKEFLARQVA------ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   91 VFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRhfkaIYGSEL----DGTRT------------HKDELIRH 154
Cdd:TIGR01488  74 LRPGARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDD----VFANRLefddNGLLTgpiegqvnpegeCKGKVLKE 149

                         170       180
                  ....*....|....*....|..
gi 500712646  155 LLDSEGLAAEQCLMIGDRMHDL 176
Cdd:TIGR01488 150 LLEESKITLKKIIAVGDSVNDL 171
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 93-189 8.97e-06

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: 44.55  E-value: 8.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  93 DGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSElDGTRTHKD-ELIRHLLDSEGLAAEQCLMIGD 171
Cdd:cd16423   47 EGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGD-DVEKSKPDpDLYLEAAERLGVNPEECVVIED 125

                         90
                 ....*....|....*...
gi 500712646 172 RMHDLLGASRNGVACIGV 189
Cdd:cd16423  126 SRNGVLAAKAAGMKCVGV 143
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 92-189 1.88e-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: 42.78  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   92 FDGIPELLEALVGRGHTLYVATSKPGVFAREIARHF-AFDRHFKAIYGSELDGTRTHKD------ELIRHLLDS-EGLAA 163
Cdd:TIGR01662  27 YPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRSFsGRVARRLEELGVPIDILYACPGcrkpkpGMFLEALKRfNEIDP 106

                          90       100
                  ....*....|....*....|....*..
gi 500712646  164 EQCLMIGDR-MHDLLGASRNGVACIGV 189
Cdd:TIGR01662 107 EESVYVGDQdLTDLQAAKRVGLATILV 133
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 89-187 2.49e-05

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: 42.14  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  89 NRVFDGIPELLEALVGrGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKDELIRHLLDSEGLAAEQCLM 168
Cdd:cd04305    8 DTLLPGAKELLEELKK-GYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLM 86

                         90       100
                 ....*....|....*....|
gi 500712646 169 IGDRMH-DLLGASRNGVACI 187
Cdd:cd04305   87 VGDSLEsDILGAKNAGIKTV 106
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 11-59 2.86e-05

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 43.79  E-value: 2.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARLG--------IDEPDLARLEHFIGPPLLQCF 59
Cdd:PTZ00174   8 LLFDVDGTLTKPRNPITQEMKDTLAKLKskgfkigvVGGSDYPKIKEQLGEDVLEDF 64
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 10-176 5.66e-05

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 42.37  E-value: 5.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   10 HILFDLDGTLTDPREG-ITRSVQFALARL---GID-----EPDLARLEHFIGPPLLQCFMQTYGFDEARAWE--AVNHYR 78
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHeLSPETIEALERLreaGVKvvivtGRSLAEIKELLKQLNLPLPLIAENGALIFYPGeiLYIEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   79 ERFRVtglYENRVFDGIPELLEALVGRG----------HTLYVATSKPG--VFAREI--------ARHFAFDRHFKAIYG 138
Cdd:TIGR01484  81 DVFEE---ILGIKFEEIGAELKSLSEHYvgtfiedkaiAVAIHYVGAELgqELDSKMrerlekigRNDLELEAIYSGKTD 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 500712646  139 SELDGTRTHKDELIRHLLDSEGLAAEQCLMIGDRMHDL 176
Cdd:TIGR01484 158 LEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDE 195
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 8-204 3.11e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 40.85  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646   8 YPH----ILFDLDGTLTDPREGITRSVQFALARLG---IDEPDLARLEHFIGppllQCFMQTYGFDearAWEAVNHYRER 80
Cdd:PRK13225  58 YPQtlqaIIFDFDGTLVDSLPTVVAIANAHAPDFGydpIDERDYAQLRQWSS----RTIVRRAGLS---PWQQARLLQRV 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  81 FRVTG--LYENRVFDGIPELLEALVGRGHTLYVATSKpgvfAREIARHFAFDRHFKAIYGSELDGTRT-HKDELIRHLLD 157
Cdd:PRK13225 131 QRQLGdcLPALQLFPGVADLLAQLRSRSLCLGILSSN----SRQNIEAFLQRQGLRSLFSVVQAGTPIlSKRRALSQLVA 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 500712646 158 SEGLAAEQCLMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQP 204
Cdd:PRK13225 207 REGWQPAAVMYVGDETRDVEAARQVGLIAVAVTWGFNDRQSLVAACP 253
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 151-212 8.68e-04

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 39.11  E-value: 8.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500712646 151 LIRHLLDSEGLAAEQCLMIGDRMH-DLLGASRNGVACIGVGYGFGSEDELR--AHQPTHYCADLA 212
Cdd:cd07530  182 MMRAALEKLGLKSEETLMVGDRLDtDIAAGIAAGIDTLLVLTGVTTREDLAkpPYRPTYIVPSLR 246
PLN02645 PLN02645
phosphoglycolate phosphatase
 151-220 2.48e-03

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 38.15  E-value: 2.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500712646 151 LIRHLLDSEGLAAEQCLMIGDRMH-DLLGASRNGVACIGVGYGFGSEDELRAH----QPTHYCADLAALRQVLES 220
Cdd:PLN02645 235 MMDYLANKFGIEKSQICMVGDRLDtDILFGQNGGCKTLLVLSGVTSESMLLSPenkiQPDFYTSKISDFLTLKAA 309
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 78-189 4.35e-03

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: 36.36  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500712646  78 RERFRVTGLYENRVFDGIPELLEALVGRGHTLYVATSKPGVfAREI---ARHFAFDRHFKAI---YGSELDGTR--THKD 149
Cdd:cd07503   13 VDVPYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGI-ARGYfseADFEALHDKMRELlasQGVEIDDIYycPHHP 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500712646 150 E-----------LIRHLLDSEGLAAEQCLMIGDRMHDLLGASRNGVACIGV 189
Cdd:cd07503   92 DdgcpcrkpkpgMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
HAD_PMM cd02585
phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis ...
 11-37 4.86e-03

phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis thaliana PMM; PMM catalyzes the interconversion of mannose-6-phosphate (M6P) to mannose-1-phosphate (M1P); the conversion of M6P to M1P is an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes. M1P is the substrate for the synthesis of GDP-mannose, which is an intermediate for protein glycosylation, protein sorting and secretion, and maintaining a functional endomembrane system in eukaryotic cells. Proteins in this family contains a conserved phosphorylated motif DxDx(T/V) shared with some other phosphotransferases. This family contains two human homologs, PMM1 and PMM2; PMM2 deficiency causes congenital disorder of glycosylation type I-a, also known as Jaeken syndrome. PMM1 can also act as glucose-1,6-bisphosphatase in the brain after stimulation with inosine monophosphate; PMM2 on the other hand, is insensitive to IMP and demonstrates low glucose-1,6-bisphosphatase activity. Arabidopsis thaliana PMM converted M1P into M6P and glucose-1-phosphate into glucose-6-phosphate, with the latter reaction being less efficient. Arabidopsis thaliana and Nicotiana benthamian PPMs are involved in ascorbic acid 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: 319784  Cd Length: 238  Bit Score: 36.87  E-value: 4.86e-03
                         10        20
                 ....*....|....*....|....*..
gi 500712646  11 ILFDLDGTLTDPREGITRSVQFALARL 37
Cdd:cd02585    2 LLFDVDGTLTPPRQPITPEMAEFLAEL 28
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 152-189 8.81e-03

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 34.94  E-value: 8.81e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 500712646 152 IRHLLDSEGLAAEQCLMIGDR-MHDLLGASRNGVACIGV 189
Cdd:cd16416   70 FRRALKEMDLPPEQVAMVGDQlFTDILGGNRAGLYTILV 108
 
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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