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Conserved domains on  [gi|2017528049|emb|CAG0941697|]
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partial Mannosylfructose-phosphate phosphatase, partial [Candidatus Brocadiaceae bacterium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sucr_syn_bact_C super family cl30870
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate ...
 1-100 1.49e-46

sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate synthase (SPS) and sucrose phosphate phosphatase (SPP) are the last two enzymes of sucrose biosynthesis. In cyanobacteria and plants, the C-terminal region of most or all versions of SPS has a domain homologous to the known SPP. This domain may serve a binding or regulatory rather than catalytic function. Sequences in this family are bacterial C-terminal regions found in all but two of the putative bacterial sucrose phosphate synthases described by TIGR02472.


The actual alignment was detected with superfamily member TIGR02471:

Pssm-ID: 131524  Cd Length: 236  Bit Score: 149.15  E-value: 1.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049   1 ELSVNTTLSFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANrHSEELVALSETERV 80
Cdd:TIGR02471 138 SQAAKVILSCGWFLDVLPLRASKGLALRYLSYRWGLPLEQILVAGDSGNDEEMLRGLTLGVVVGN-HDPELEGLRHQQRI 216

                          90       100
                  ....*....|....*....|
gi 2017528049  81 YFAQGSHAWGILEAVEHYDF 100
Cdd:TIGR02471 217 YFANNPHAFGILEGINHYDF 236
 
Name Accession Description Interval E-value
sucr_syn_bact_C TIGR02471
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate ...
 1-100 1.49e-46

sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate synthase (SPS) and sucrose phosphate phosphatase (SPP) are the last two enzymes of sucrose biosynthesis. In cyanobacteria and plants, the C-terminal region of most or all versions of SPS has a domain homologous to the known SPP. This domain may serve a binding or regulatory rather than catalytic function. Sequences in this family are bacterial C-terminal regions found in all but two of the putative bacterial sucrose phosphate synthases described by TIGR02472.


Pssm-ID: 131524  Cd Length: 236  Bit Score: 149.15  E-value: 1.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049   1 ELSVNTTLSFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANrHSEELVALSETERV 80
Cdd:TIGR02471 138 SQAAKVILSCGWFLDVLPLRASKGLALRYLSYRWGLPLEQILVAGDSGNDEEMLRGLTLGVVVGN-HDPELEGLRHQQRI 216

                          90       100
                  ....*....|....*....|
gi 2017528049  81 YFAQGSHAWGILEAVEHYDF 100
Cdd:TIGR02471 217 YFANNPHAFGILEGINHYDF 236
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 1-100 1.09e-40

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 134.31  E-value: 1.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049   1 ELSVNTTLSFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANrHSEELVA-----LS 75
Cdd:pfam05116 143 GLDVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGN-AQPELLQwylenAR 221

                          90       100
                  ....*....|....*....|....*
gi 2017528049  76 ETERVYFAQGSHAWGILEAVEHYDF 100
Cdd:pfam05116 222 DNPRIYFASGRCAGGILEGIRHFGL 246
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 12-98 1.38e-27

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. 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: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 100.50  E-value: 1.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049  12 QFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANRHSEELVALSETERVYFAQGSHAWGI 91
Cdd:cd02605   159 YDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLAKGPYAGGI 238


                  ....*..
gi 2017528049  92 LEAVEHY 98
Cdd:cd02605   239 LEGLAHF 245
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 7-98 5.83e-22

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 84.80  E-value: 5.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049   7 TLSFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANrHSEELVALseteRVYFAQGS 86
Cdd:COG0561   106 VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGN-APPEVKAA----ADYVTGSN 180

                          90
                  ....*....|..
gi 2017528049  87 HAWGILEAVEHY 98
Cdd:COG0561   181 DEDGVAEALEKL 192
PLN02382 PLN02382
probable sucrose-phosphatase
 9-99 1.55e-10

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049   9 SFGQFLDFVPARASKGQALRYIARQWNI---PLERILVTGDSGGDDDMLR-GNTLGVVVANRHSEELVALSETER----V 80
Cdd:PLN02382  162 SGGIDLDVLPQGAGKGQALAYLLKKLKAegkAPVNTLVCGDSGNDAELFSvPDVYGVMVSNAQEELLQWYAENAKdnpkI 241

                          90
                  ....*....|....*....
gi 2017528049  81 YFAQGSHAWGILEAVEHYD 99
Cdd:PLN02382  242 IHATERCAAGIIQAIGHFN 260
 
Name Accession Description Interval E-value
sucr_syn_bact_C TIGR02471
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate ...
 1-100 1.49e-46

sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate synthase (SPS) and sucrose phosphate phosphatase (SPP) are the last two enzymes of sucrose biosynthesis. In cyanobacteria and plants, the C-terminal region of most or all versions of SPS has a domain homologous to the known SPP. This domain may serve a binding or regulatory rather than catalytic function. Sequences in this family are bacterial C-terminal regions found in all but two of the putative bacterial sucrose phosphate synthases described by TIGR02472.


Pssm-ID: 131524  Cd Length: 236  Bit Score: 149.15  E-value: 1.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049   1 ELSVNTTLSFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANrHSEELVALSETERV 80
Cdd:TIGR02471 138 SQAAKVILSCGWFLDVLPLRASKGLALRYLSYRWGLPLEQILVAGDSGNDEEMLRGLTLGVVVGN-HDPELEGLRHQQRI 216

                          90       100
                  ....*....|....*....|
gi 2017528049  81 YFAQGSHAWGILEAVEHYDF 100
Cdd:TIGR02471 217 YFANNPHAFGILEGINHYDF 236
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 1-100 1.09e-40

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 134.31  E-value: 1.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049   1 ELSVNTTLSFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANrHSEELVA-----LS 75
Cdd:pfam05116 143 GLDVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGN-AQPELLQwylenAR 221

                          90       100
                  ....*....|....*....|....*
gi 2017528049  76 ETERVYFAQGSHAWGILEAVEHYDF 100
Cdd:pfam05116 222 DNPRIYFASGRCAGGILEGIRHFGL 246
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 12-98 1.38e-27

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. 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: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 100.50  E-value: 1.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049  12 QFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANRHSEELVALSETERVYFAQGSHAWGI 91
Cdd:cd02605   159 YDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLAKGPYAGGI 238


                  ....*..
gi 2017528049  92 LEAVEHY 98
Cdd:cd02605   239 LEGLAHF 245
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 7-98 5.83e-22

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 84.80  E-value: 5.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049   7 TLSFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANrHSEELVALseteRVYFAQGS 86
Cdd:COG0561   106 VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGN-APPEVKAA----ADYVTGSN 180

                          90
                  ....*....|..
gi 2017528049  87 HAWGILEAVEHY 98
Cdd:COG0561   181 DEDGVAEALEKL 192
PLN02382 PLN02382
probable sucrose-phosphatase
 9-99 1.55e-10

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049   9 SFGQFLDFVPARASKGQALRYIARQWNI---PLERILVTGDSGGDDDMLR-GNTLGVVVANRHSEELVALSETER----V 80
Cdd:PLN02382  162 SGGIDLDVLPQGAGKGQALAYLLKKLKAegkAPVNTLVCGDSGNDAELFSvPDVYGVMVSNAQEELLQWYAENAKdnpkI 241

                          90
                  ....*....|....*....
gi 2017528049  81 YFAQGSHAWGILEAVEHYD 99
Cdd:PLN02382  242 IHATERCAAGIIQAIGHFN 260
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 4-65 2.29e-10

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 54.94  E-value: 2.29e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017528049   4 VNTTLSFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVAN 65
Cdd:pfam08282 169 ITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGN 230
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 9-95 8.52e-10

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 53.24  E-value: 8.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049   9 SFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVAN-----RHSEELVALSeteRVYFA 83
Cdd:TIGR01482 136 DSGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANaqpelKEWADYVTES---PYGEG 212

                          90
                  ....*....|..
gi 2017528049  84 QGSHAWGILEAV 95
Cdd:TIGR01482 213 GAEAIGEILQAI 224
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-65 5.51e-09

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-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, 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 51.44  E-value: 5.51e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017528049   4 VNTTLSFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLR--GntLGVVVAN 65
Cdd:cd07516   165 LSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEyaG--LGVAMGN 226
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 1-75 1.11e-08

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 50.34  E-value: 1.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017528049   1 ELSVNTTLSFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANrHSEELVALS 75
Cdd:TIGR00099 167 EENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGN-ADEELKALA 240
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 4-63 1.20e-08

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: 50.07  E-value: 1.20e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049   4 VNTTLSFGQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVV 63
Cdd:TIGR01484 148 LEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 22-98 3.02e-07

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 45.27  E-value: 3.02e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017528049  22 SKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANRHSEelvALSETERVyfAQGSHAWGILEAVEHY 98
Cdd:cd07514    67 DKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEE---LKEAADYV--TDASYGDGVLEAIDKL 138
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 13-69 4.53e-07

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. 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: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 45.65  E-value: 4.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2017528049  13 FLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANRHSE 69
Cdd:cd07518   106 SIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEE 162
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 22-100 1.10e-06

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 44.96  E-value: 1.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017528049  22 SKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANRhSEELVALSEtervYFAQGSHAWGILEAVEHYDF 100
Cdd:PRK01158  157 NKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANA-DEELKEAAD----YVTEKSYGEGVAEAIEHLLL 230
HAD_SPS cd16419
sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily; ...
 14-51 2.11e-06

sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily; Sucrose phosphate synthase (SPS; EC 2.4.1.14) also known as UDP-glucose-fructose-phosphate glucosyltransferase, catalyzes the transfer of a hexosyl group from UDP-glucose to D-fructose 6-phosphate to form UDP and D-sucrose-6-phosphate, this is the rate limiting step of sucrose synthesis. 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: 319856  Cd Length: 174  Bit Score: 43.77  E-value: 2.11e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2017528049  14 LDFVPARASKGQALRYIARQWNIPLER-ILVTGDSGGDD 51
Cdd:cd16419   119 LHVLPLLASRSQALRYLFVRWGIDLSNmVVFVGESGDTD 157
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 21-97 2.80e-05

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 41.08  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049  21 ASKGQALRYIARQWNIPLERILVT-GDSGGDDDMLRGNTLGVVVANRHSEELVALSETE--RVYFAQGSHAWGILEAVEH 97
Cdd:PRK00192  189 GDKGKAVRWLKELYRRQDGVETIAlGDSPNDLPMLEAADIAVVVPGPDGPNPPLLPGIAdgEFILASAPGPEGWAEAINK 268
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 14-73 4.42e-05

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 40.53  E-value: 4.42e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017528049   14 LDFVPARASKGQALRYIARQWNIPLERILV-TGDSGGDD--DMLRGNTLGVV---VANRHSEELVA 73
Cdd:TIGR02468  948 LNVIPLLASRSQALRYLFVRWGIELANMAVfVGESGDTDyeGLLGGLHKTVIlkgVVSRGSEQLHA 1013
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 20-61 4.57e-04

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 37.14  E-value: 4.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2017528049  20 RASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGV 61
Cdd:cd07500   135 AQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGI 176
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 12-99 6.56e-04

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. 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: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 36.82  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017528049  12 QFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVVANRHsEEL--VALSETERVyfaqgSHAw 89
Cdd:cd07517   131 LSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAH-EELkeIADYVTKDV-----DED- 203

                          90
                  ....*....|
gi 2017528049  90 GILEAVEHYD 99
Cdd:cd07517   204 GILKALKHFG 213
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 11-63 1.81e-03

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: 35.58  E-value: 1.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2017528049  11 GQFLDFVPARASKGQALRYIARQWNIPLERILVTGDSGGDDDMLRGNTLGVVV 63
Cdd:COG0560   144 GEVVGPIVDGEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV 196
 
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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