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Conserved domains on  [gi|518675523|ref|WP_019837216|]
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MULTISPECIES: HAD-IA family hydrolase [Acinetobacter]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
4-202 1.02e-89

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


The actual alignment was detected with superfamily member cd04302:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 209  Bit Score: 262.53  E-value: 1.02e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   4 NLLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLLHVDvhDVLAEQALAGYRERFAATGLF 83
Cdd:cd04302    1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRELLPFD--EEEAQRAVDAYREYYKEKGLF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  84 ENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQCL 163
Cdd:cd04302   79 ENEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGSRVHKADVIRYALDTLGIAPEQAV 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 518675523 164 MIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAPKH 202
Cdd:cd04302  159 MIGDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATY 197
 
Name Accession Description Interval E-value
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
4-202 1.02e-89

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: 262.53  E-value: 1.02e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   4 NLLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLLHVDvhDVLAEQALAGYRERFAATGLF 83
Cdd:cd04302    1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRELLPFD--EEEAQRAVDAYREYYKEKGLF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  84 ENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQCL 163
Cdd:cd04302   79 ENEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGSRVHKADVIRYALDTLGIAPEQAV 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 518675523 164 MIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAPKH 202
Cdd:cd04302  159 MIGDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATY 197
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
2-216 1.27e-58

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 183.98  E-value: 1.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   2 IKNLLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLLHVDVHDvLAEQALAGYRERFAATG 81
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDPDE-ELEELLARFRELYEEEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  82 LFENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQ 161
Cdd:COG0546   80 LDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518675523 162 CLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAPKHRIQCFAQILSVLEQ 216
Cdd:COG0546  160 VLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGADYVIDSLAELLALLAE 214
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-218 9.93e-27

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 102.19  E-value: 9.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   1 MIKNLLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENI-DWI-------IGPPLKASLAkllhvDVHDVLAEQALAG 72
Cdd:PRK13222   5 DIRAVAFDLDGTLVDSAPDLAAAVNAALAALGLPPAGEERVrTWVgngadvlVERALTWAGR-----EPDEELLEKLREL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  73 YRERFAATGLFENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYIL 152
Cdd:PRK13222  80 FDRHYAENVAGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAPLLLAC 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518675523 153 QQEQLQPEQCLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAPKHRIQCFAQILSVLEQLS 218
Cdd:PRK13222 160 EKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYGYNYGEPIALSEPDVVIDHFAELLPLLGLAL 225
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
5-185 2.21e-25

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 97.27  E-value: 2.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523    5 LLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLLH-VDVHDVLAEqalagYRERFAAtGLF 83
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVsEDEEEKIEF-----YLRKYNE-ELH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   84 ENHV--FEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQ 161
Cdd:pfam13419  75 DKLVkpYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEE 154
                         170       180
                  ....*....|....*....|....
gi 518675523  162 CLMIGDREHDILGARANGVDCVAV 185
Cdd:pfam13419 155 VIYVGDSPRDIEAAKNAGIKVIAV 178
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
5-200 6.64e-20

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: 84.10  E-value: 6.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523    5 LLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLLHV-----DVHDVLAEQALagYRERFAA 79
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAAAVNMALAALGLPPATLARVIGFIGNGVPVLMERVLAWagqepDAQRVAELRKL--FDRHYEE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   80 TGLFENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQP 159
Cdd:TIGR01449  79 VAGELTSVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQRKPHPDPLLLAAERLGVAP 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 518675523  160 EQCLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAP 200
Cdd:TIGR01449 159 QQMVYVGDSRVDIQAARAAGCPSVLLTYGYRYGEAIDLLPP 199
 
Name Accession Description Interval E-value
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
4-202 1.02e-89

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: 262.53  E-value: 1.02e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   4 NLLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLLHVDvhDVLAEQALAGYRERFAATGLF 83
Cdd:cd04302    1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRELLPFD--EEEAQRAVDAYREYYKEKGLF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  84 ENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQCL 163
Cdd:cd04302   79 ENEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGSRVHKADVIRYALDTLGIAPEQAV 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 518675523 164 MIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAPKH 202
Cdd:cd04302  159 MIGDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATY 197
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
2-216 1.27e-58

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 183.98  E-value: 1.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   2 IKNLLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLLHVDVHDvLAEQALAGYRERFAATG 81
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDPDE-ELEELLARFRELYEEEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  82 LFENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQ 161
Cdd:COG0546   80 LDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518675523 162 CLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAPKHRIQCFAQILSVLEQ 216
Cdd:COG0546  160 VLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGADYVIDSLAELLALLAE 214
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
5-211 2.85e-29

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: 108.48  E-value: 2.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   5 LLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENI-DWI---IGPPLKASLAKLLHVDVHDVLAEQALAGYRERFAAT 80
Cdd:cd16417    2 VAFDLDGTLVDSAPDLAEAANAMLAALGLPPLPEETVrTWIgngADVLVERALTGAREAEPDEELFKEARALFDRHYAET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  81 GLFENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPE 160
Cdd:cd16417   82 LSVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPLLHACEKLGIAPA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518675523 161 QCLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAPKHRIQCFAQIL 211
Cdd:cd16417  162 QMLMVGDSRNDILAARAAGCPSVGLTYGYNYGEDIAASGPDAVIDSLAELL 212
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
2-213 7.16e-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: 104.67  E-value: 7.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   2 IKNLLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLLHVDVHDVLAEqalagYRERFAATG 81
Cdd:cd02616    1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVLPFIGPPLRETFEKIDPDKLEDMVEE-----FRKYYREHN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  82 LFENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQ 161
Cdd:cd02616   76 DDLTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEE 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518675523 162 CLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAPKHRIQCFAQILSV 213
Cdd:cd02616  156 ALMVGDSPHDILAGKNAGVKTVGVTWGYKGREYLKAFNPDFIIDKMSDLLTI 207
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-218 9.93e-27

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 102.19  E-value: 9.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   1 MIKNLLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENI-DWI-------IGPPLKASLAkllhvDVHDVLAEQALAG 72
Cdd:PRK13222   5 DIRAVAFDLDGTLVDSAPDLAAAVNAALAALGLPPAGEERVrTWVgngadvlVERALTWAGR-----EPDEELLEKLREL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  73 YRERFAATGLFENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYIL 152
Cdd:PRK13222  80 FDRHYAENVAGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAPLLLAC 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518675523 153 QQEQLQPEQCLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAPKHRIQCFAQILSVLEQLS 218
Cdd:PRK13222 160 EKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYGYNYGEPIALSEPDVVIDHFAELLPLLGLAL 225
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
5-185 2.21e-25

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 97.27  E-value: 2.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523    5 LLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLLH-VDVHDVLAEqalagYRERFAAtGLF 83
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVsEDEEEKIEF-----YLRKYNE-ELH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   84 ENHV--FEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQ 161
Cdd:pfam13419  75 DKLVkpYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEE 154
                         170       180
                  ....*....|....*....|....
gi 518675523  162 CLMIGDREHDILGARANGVDCVAV 185
Cdd:pfam13419 155 VIYVGDSPRDIEAAKNAGIKVIAV 178
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
5-200 2.94e-22

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 91.46  E-value: 2.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   5 LLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENI-DWI-IGPPL---KASLAKLLHVDVHDVLAEQALAGYRERFAA 79
Cdd:PRK13223  16 VMFDLDGTLVDSVPDLAAAVDRMLLELGRPPAGLEAVrHWVgNGAPVlvrRALAGSIDHDGVDDELAEQALALFMEAYAD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  80 TGLFeNHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSE-LNGERTNKADLIaYILQQEQLQ 158
Cdd:PRK13223  96 SHEL-TVVYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDtLPQKKPDPAALL-FVMKMAGVP 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 518675523 159 PEQCLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAP 200
Cdd:PRK13223 174 PSQSLFVGDSRSDVLAAKAAGVQCVALSYGYNHGRPIAEESP 215
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
5-200 6.64e-20

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: 84.10  E-value: 6.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523    5 LLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLLHV-----DVHDVLAEQALagYRERFAA 79
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAAAVNMALAALGLPPATLARVIGFIGNGVPVLMERVLAWagqepDAQRVAELRKL--FDRHYEE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   80 TGLFENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQP 159
Cdd:TIGR01449  79 VAGELTSVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQRKPHPDPLLLAAERLGVAP 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 518675523  160 EQCLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAP 200
Cdd:TIGR01449 159 QQMVYVGDSRVDIQAARAAGCPSVLLTYGYRYGEAIDLLPP 199
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
5-210 4.66e-18

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: 78.98  E-value: 4.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   5 LLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLL---HVDVHDVlAEQALAGYRERFAATG 81
Cdd:cd07533    2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAEVRSIIGLSLDEAIARLLpmaTPALVAV-AERYKEAFDILRLLPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  82 LFENhVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEypyGSELNGERTNKAD--LIAYILQQEQLQP 159
Cdd:cd07533   81 HAEP-LFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFD---ATRTADDTPSKPHpeMLREILAELGVDP 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518675523 160 EQCLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAPKHRIQCFAQI 210
Cdd:cd07533  157 SRAVMVGDTAYDMQMAANAGAHAVGVAWGYHSLEDLRSAGADAVVDHFSEL 207
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
8-199 9.57e-17

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: 75.43  E-value: 9.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   8 DLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIG---PPLKASLAKLLHVDVHDVLAEQALAGYRERFAATGLFE 84
Cdd:cd07512    5 DLDGTLIDSAPDLHAALNAVLAAEGLAPLSLAEVRSFVGhgaPALIRRAFAAAGEDLDGPLHDALLARFLDHYEADPPGL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  85 NHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQCLM 164
Cdd:cd07512   85 TRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGDVSRALM 164
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 518675523 165 IGDREHDILGARANGVDCVAVEYGYGSAQELDLAA 199
Cdd:cd07512  165 VGDSETDAATARAAGVPFVLVTFGYRHAPVAELPH 199
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
91-185 5.77e-16

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: 70.89  E-value: 5.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  91 VAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQCLMIGDREH 170
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91
                         90
                 ....*....|....*
gi 518675523 171 DILGARANGVDCVAV 185
Cdd:cd01427   92 DIEAARAAGGRTVAV 106
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
2-214 3.57e-15

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: 71.21  E-value: 3.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   2 IKNLLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKAS----------------LAKLLHVDVHDVL 65
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWrryergeitfaellrrLLEELGLDLAEEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  66 AEQALAGYRERFaatglfenHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKA 145
Cdd:COG1011   81 AEAFLAALPELV--------EPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDP 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523 146 DLIAYILQQEQLQPEQCLMIGDR-EHDILGARANGVDCVAVEygYGSAQELDLAAPKHRIQCFAQILSVL 214
Cdd:COG1011  153 EIFELALERLGVPPEEALFVGDSpETDVAGARAAGMRTVWVN--RSGEPAPAEPRPDYVISDLAELLELL 220
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
2-179 4.27e-15

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: 70.69  E-value: 4.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523    2 IKNLLIDLDGTLTDPKEGITASARYglAKVGHPIADT-----ENIDW---------IIGPPLKASLAKLLHVDVHDVLAE 67
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAE--LASEHPLAKAivaaaEDLPIpvedftarlLLGKRDWLEELDILRGLVETLEAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   68 QALAGYRERFAATGLFENH-VFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKAD 146
Cdd:pfam00702  79 GLTVVLVELLGVIALADELkLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPE 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 518675523  147 LIAYILQQEQLQPEQCLMIGDREHDILGARANG 179
Cdd:pfam00702 159 IYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
5-179 1.70e-14

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


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 68.19  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523    5 LLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDwiIGPPLKASLAKLLHVDVHDVLAEQALAGYRERFAAtglfe 84
Cdd:TIGR01549   2 ILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALK--QAGGLAEEEWYRIATSALEELQGRFWSEYDAEEAY----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   85 nhvFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKAdlIAYILQQEQLQPEQCLM 164
Cdd:TIGR01549  75 ---IRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGSKPEPE--IFLAALESLGVPPEVLH 149
                         170
                  ....*....|....*
gi 518675523  165 IGDREHDILGARANG 179
Cdd:TIGR01549 150 VGDNLNDIEGARNAG 164
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
1-218 2.37e-12

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 63.51  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   1 MIKNLLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKLlhvdvHDVLAEQALAGYRErfaat 80
Cdd:PRK13288   2 KINTVLFDLDGTLINTNELIISSFLHTLKTYYPNQYKREDVLPFIGPSLHDTFSKI-----DESKVEEMITTYRE----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  81 glF--ENH-----VFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSEL------NGERTNKAdl 147
Cdd:PRK13288  72 --FnhEHHdelvtEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDvehakpDPEPVLKA-- 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518675523 148 iayiLQQEQLQPEQCLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAAPKHRIQCFAQILSVLEQLS 218
Cdd:PRK13288 148 ----LELLGAKPEEALMVGDNHHDILAGKNAGTKTAGVAWTIKGREYLEQYKPDFMLDKMSDLLAIVGDMN 214
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
8-202 4.80e-11

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: 59.68  E-value: 4.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   8 DLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKaSLAKLLHVDVHDVlaeQALAGYRERFAATGLFENHV 87
Cdd:cd04303    5 DFDGTLADSFPWFLSILNQLAARHGFKTVDEEEIEQLRQLSSR-EILKQLGVPLWKL---PLIAKDFRRLMAEAAPELAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  88 FEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGertnKADLIAYILQQEQLQPEQCLMIGD 167
Cdd:cd04303   81 FPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFAVIEGSSLFG----KAKKIRRVLRRTKITAAQVIYVGD 156
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 518675523 168 REHDILGARANGVDCVAVEYGYGSAQELDLAAPKH 202
Cdd:cd04303  157 ETRDIEAARKVGLAFAAVSWGYAKPEVLKALAPDH 191
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-210 9.60e-10

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 55.99  E-value: 9.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   1 MIKNLLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDwIIGPPLKASLAKLLH-----VDVHDvLAEQALAGYRE 75
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRR-LMGRSREDILRYLLEeygldLPEEE-LAARKEELYRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  76 RFAATGLfenHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEY---------------PYgsELNGE 140
Cdd:COG0637   79 LLAEEGL---PLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVivtgddvargkpdpdIY--LLAAE 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523 141 RTNKADliayilqqeqlqpEQCLMIGDREHDILGARANGVDCVAVEYGYGSAQELDLAApkHRIQCFAQI 210
Cdd:COG0637  154 RLGVDP-------------EECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGAD--LVVDDLAEL 208
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
5-189 3.83e-08

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 51.78  E-value: 3.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   5 LLIDLDGTLTDPKEGITASARYGLAKVGHPIADTENIDWIIGPPLKASLAKL---LHVDVHDVLAEQALagyrERFAATG 81
Cdd:PRK13226  15 VLFDLDGTLLDSAPDMLATVNAMLAARGRAPITLAQLRPVVSKGARAMLAVAfpeLDAAARDALIPEFL----QRYEALI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  82 LFENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQ 161
Cdd:PRK13226  91 GTQSQLFDGVEGMLQRLECAGCVWGIVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPHPLPLLVAAERIGVAPTD 170
                        170       180
                 ....*....|....*....|....*...
gi 518675523 162 CLMIGDREHDILGARANGVDCVAVEYGY 189
Cdd:PRK13226 171 CVYVGDDERDILAARAAGMPSVAALWGY 198
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
4-181 9.21e-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: 47.37  E-value: 9.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   4 NLLIDLDGTLTDPKEGITASARYGLAKVGHPIaDTENIDWIIGPPLKASLAKLLHvDVHDVLAEqalagyRERFAATGLF 83
Cdd:cd07523    1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQ-DLETVYKIIKESSVQFAIQYYA-EVPDLEEE------YKELEAEYLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  84 ENHVFEDVAATLADLKQQGYRLFLATAKPEiYARQILDHFDLLQYFEYPYGSELNGERTNKADLIAYILQQEQLQPEQCL 163
Cdd:cd07523   73 KPILFPGAKAVLRWIKEQGGKNFLMTHRDH-SALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETV 151
                        170
                 ....*....|....*...
gi 518675523 164 MIGDREHDILGARANGVD 181
Cdd:cd07523  152 MIGDRELDIEAGHNAGIS 169
HAD pfam12710
haloacid dehalogenase-like hydrolase;
8-137 7.90e-06

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 44.83  E-value: 7.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523    8 DLDGTLTDpKEGITASARYGLAKVGHPIADTENIDWIIgpPLKASLAKLLHVDVhDVLAEQALAGYRERFAA------TG 81
Cdd:pfam12710   4 DLDGTLLD-GDSLFLLIRALLRRGGPDLWRALLVLLLL--ALLRLLGRLSRAGA-RELLRALLAGLPEEDAAelerfvAE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 518675523   82 LFENHVFEDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDllqyFEYPYGSEL 137
Cdd:pfam12710  80 VALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELG----FDEVLATEL 131
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
162-211 4.34e-05

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 43.17  E-value: 4.34e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 518675523 162 CLMIGDR-EHDILGARANGVDCVAVEYGYGSAQELDLAA--PKHRIQCFAQIL 211
Cdd:COG0647  206 VLMVGDRlDTDILGANAAGLDTLLVLTGVTTAEDLEAAPirPDYVLDSLAELL 258
Hydrolase_like pfam13242
HAD-hyrolase-like;
162-203 6.78e-05

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 39.91  E-value: 6.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 518675523  162 CLMIGDR-EHDILGARANGVDCVAVeyGYGSAQELDLAAPKHR 203
Cdd:pfam13242  24 TVMIGDRlDTDILGAREAGARTILV--LTGVTRPADLEKAPIR 64
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
89-185 9.73e-04

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 38.39  E-value: 9.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523  89 EDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLLQYFEYPygseLNGERTNKA----DLIAYILQQEQLQPEQCLM 164
Cdd:cd16423   47 EGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVI----VTGDDVEKSkpdpDLYLEAAERLGVNPEECVV 122
                         90       100
                 ....*....|....*....|.
gi 518675523 165 IGDREHDILGARANGVDCVAV 185
Cdd:cd16423  123 IEDSRNGVLAAKAAGMKCVGV 143
PRK08238 PRK08238
UbiA family prenyltransferase;
5-149 1.58e-03

UbiA family prenyltransferase;


Pssm-ID: 236195 [Multi-domain]  Cd Length: 479  Bit Score: 39.09  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518675523   5 LLIDLDGTL--TDP-KEGITASARYGLAKVGHPIAdtenidWIIG--PPLKASLAKLLHVDVhdvlaeqALAGYRErfaa 79
Cdd:PRK08238  13 LVVDLDGTLirTDLlHESIFALLRRNPLALLRLPL------WLLRgkAALKRRLARRVDLDV-------ATLPYNE---- 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518675523  80 tglfenhvfeDVAATLADLKQQGYRLFLATAKPEIYARQILDHFDLlqyFEYPYGSE--LNGERTNKADLIA 149
Cdd:PRK08238  76 ----------EVLDYLRAERAAGRKLVLATASDERLAQAVAAHLGL---FDGVFASDgtTNLKGAAKAAALV 134
 
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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