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Conserved domains on  [gi|15596882|ref|NP_250376|]
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enolase-phosphatase [Pseudomonas aeruginosa PAO1]

Protein Classification

Utr4 family protein( domain architecture ID 10008373)

Utr4 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Utr4 COG4229
Enolase-phosphatase E1 involved in merthionine salvage [Amino acid transport and metabolism];
1-218 2.06e-144

Enolase-phosphatase E1 involved in merthionine salvage [Amino acid transport and metabolism];


:

Pssm-ID: 443373 [Multi-domain]  Cd Length: 227  Bit Score: 402.99  E-value: 2.06e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882   1 MTIKAILTDIEGTTSAVSFVFDVLFPYAARHLPDFVREHAGETEVAAQLAAVRAESGEADADVERVIAILLQWIAEDRKA 80
Cdd:COG4229   1 MMIRAILTDIEGTTSSISFVHDVLFPYARERLPAFLREHAEDPEVAAALAAVRAEAGEPDADLEELIAVLLRWIDEDRKA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882  81 TPLKALQGMVWAQGYRDGQLKGHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCSEAGDLGSLFSGYFDTTSGPK 160
Cdd:COG4229  81 TPLKALQGLIWEEGYEAGDLKGHVYPDVAPALRAWHAQGLRLYVYSSGSVAAQKLLFGHSDAGDLTPLFSGYFDTRIGPK 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596882 161 RESASYARIAGAIGLPAAEILFLSDVVQELDAARDAGMRTLGLAREGGSLD---GHPTVAS 218
Cdd:COG4229 161 REAASYRNIAEALGLPPEEILFLSDVVEELDAAREAGLQTCQLVRPGDPTDdpgGHPVVAS 221
 
Name Accession Description Interval E-value
Utr4 COG4229
Enolase-phosphatase E1 involved in merthionine salvage [Amino acid transport and metabolism];
1-218 2.06e-144

Enolase-phosphatase E1 involved in merthionine salvage [Amino acid transport and metabolism];


Pssm-ID: 443373 [Multi-domain]  Cd Length: 227  Bit Score: 402.99  E-value: 2.06e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882   1 MTIKAILTDIEGTTSAVSFVFDVLFPYAARHLPDFVREHAGETEVAAQLAAVRAESGEADADVERVIAILLQWIAEDRKA 80
Cdd:COG4229   1 MMIRAILTDIEGTTSSISFVHDVLFPYARERLPAFLREHAEDPEVAAALAAVRAEAGEPDADLEELIAVLLRWIDEDRKA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882  81 TPLKALQGMVWAQGYRDGQLKGHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCSEAGDLGSLFSGYFDTTSGPK 160
Cdd:COG4229  81 TPLKALQGLIWEEGYEAGDLKGHVYPDVAPALRAWHAQGLRLYVYSSGSVAAQKLLFGHSDAGDLTPLFSGYFDTRIGPK 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596882 161 RESASYARIAGAIGLPAAEILFLSDVVQELDAARDAGMRTLGLAREGGSLD---GHPTVAS 218
Cdd:COG4229 161 REAASYRNIAEALGLPPEEILFLSDVVEELDAAREAGLQTCQLVRPGDPTDdpgGHPVVAS 221
HAD_EP cd01629
Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. ...
5-207 1.61e-121

Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. Oryzae enolase-phosphatase Xep; Enolase-phosphatase E1 (also called MASA) is a bifunctional enolase- phosphatase which promotes the conversion of 2,3-diketo-5-methylthio-1-phosphopentane to 1,2-dihydroxy-3-keto-5-methylthiopentene anion (an aci-reductone) in the methionine salvage pathway. The catalytic reaction is carried out continuously by enolization and dephosphorylation, and the enolase activity cannot be classified as typical enzymatic enolization. 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: 319768 [Multi-domain]  Cd Length: 204  Bit Score: 344.14  E-value: 1.61e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882   5 AILTDIEGTTSAVSFVFDVLFPYAARHLPDFVREHAGETEVA-AQLAAVRAESGEADADVERVIAILLQWIAEDRKATPL 83
Cdd:cd01629   1 AILLDIEGTTTPISFVKDVLFPYARERLPDFLAEHWEDPEVKeDVLAAAAEAEGEAEASIEAVVANLLDWMDEDRKATPL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882  84 KALQGMVWAQGYRDGQLKGHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCSEAGDLGSLFSGYFDTTSGPKRES 163
Cdd:cd01629  81 KALQGLIWREGYESGELKGHLYPDVVPALRRWHAAGLRLYIYSSGSVAAQKLLFGHSDAGDLTPLFSGYFDTTIGPKREA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15596882 164 ASYARIAGAIGLPAAEILFLSDVVQELDAARDAGMRTLGLAREG 207
Cdd:cd01629 161 ASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLLVRPG 204
enolase-ppase TIGR01691
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This enzyme is the enolase-phosphatase ...
3-220 1.66e-88

2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This enzyme is the enolase-phosphatase of methionine salvage, a pathway that regenerates methionine from methylthioadenosine (MTA). Adenosylmethionine (AdoMet) is a donor of different moieties for various processes, including methylation reactions. Use of AdoMet for spermidine biosynthesis, which leads to polyamine biosynthesis, leaves MTA as a by-product that must be cleared. In Bacillus subtilis and related species, this single protein is replaced by separate enzymes with enolase and phosphatase activities. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273760 [Multi-domain]  Cd Length: 220  Bit Score: 261.32  E-value: 1.66e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882     3 IKAILTDIEGTTSAVSFVFDVLFPYAARHLPDFVREHAGETEVAAqlaavRAESGeADADVERVIAILLQWIAEDRKATP 82
Cdd:TIGR01691   1 IKNVLLDIEGTTGSISFVHDVLFPYAASRLESFVNDNYESTIVEN-----LRELG-KTPEELILLRKLHAEMDKDRKATP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882    83 LKALQGMVWAQGYRDGQLKGHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCSEAGDLGSLFSGYFDTTSGPKRE 162
Cdd:TIGR01691  75 LKTLQGLIWRQGYESGELTSHLYPDVPPALEAWLQLGLRLAVYSSGSVPAQKLLFGHSDAGNLTPYFSGYFDTTVGLKTE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15596882   163 SASYARIAGAIGLPAAEILFLSDVVQELDAARDAGMRTLGLAREGGSLDGHPTVASSP 220
Cdd:TIGR01691 155 AQSYVKIAGQLGSPPREILFLSDIINELDAARKAGLHTGQLVRPGNDPVVDPSFPVYP 212
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
3-197 1.11e-11

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: 61.83  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882     3 IKAILTDIEGTTSAVSFVFDVLFPYAARHLPDFVREHAGETEVAAQLAAVRAESGEADADverviaiLLQWIAEDRKATP 82
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRD-------WLEELDILRGLVE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882    83 LKALQGMVWAQGYRDGQLKGH----VYPDAVQALREWKARGLDLYVYSSGSIQ-AQKLIFGCSEAGDLGSLFSGYFDTTS 157
Cdd:pfam00702  74 TLEAEGLTVVLVELLGVIALAdelkLYPGAAEALKALKERGIKVAILTGDNPEaAEALLRLLGLDDYFDVVISGDDVGVG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 15596882   158 GPKRESasYARIAGAIGLPAAEILFLSDVVQELDAARDAG 197
Cdd:pfam00702 154 KPKPEI--YLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
 
Name Accession Description Interval E-value
Utr4 COG4229
Enolase-phosphatase E1 involved in merthionine salvage [Amino acid transport and metabolism];
1-218 2.06e-144

Enolase-phosphatase E1 involved in merthionine salvage [Amino acid transport and metabolism];


Pssm-ID: 443373 [Multi-domain]  Cd Length: 227  Bit Score: 402.99  E-value: 2.06e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882   1 MTIKAILTDIEGTTSAVSFVFDVLFPYAARHLPDFVREHAGETEVAAQLAAVRAESGEADADVERVIAILLQWIAEDRKA 80
Cdd:COG4229   1 MMIRAILTDIEGTTSSISFVHDVLFPYARERLPAFLREHAEDPEVAAALAAVRAEAGEPDADLEELIAVLLRWIDEDRKA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882  81 TPLKALQGMVWAQGYRDGQLKGHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCSEAGDLGSLFSGYFDTTSGPK 160
Cdd:COG4229  81 TPLKALQGLIWEEGYEAGDLKGHVYPDVAPALRAWHAQGLRLYVYSSGSVAAQKLLFGHSDAGDLTPLFSGYFDTRIGPK 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596882 161 RESASYARIAGAIGLPAAEILFLSDVVQELDAARDAGMRTLGLAREGGSLD---GHPTVAS 218
Cdd:COG4229 161 REAASYRNIAEALGLPPEEILFLSDVVEELDAAREAGLQTCQLVRPGDPTDdpgGHPVVAS 221
HAD_EP cd01629
Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. ...
5-207 1.61e-121

Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. Oryzae enolase-phosphatase Xep; Enolase-phosphatase E1 (also called MASA) is a bifunctional enolase- phosphatase which promotes the conversion of 2,3-diketo-5-methylthio-1-phosphopentane to 1,2-dihydroxy-3-keto-5-methylthiopentene anion (an aci-reductone) in the methionine salvage pathway. The catalytic reaction is carried out continuously by enolization and dephosphorylation, and the enolase activity cannot be classified as typical enzymatic enolization. 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: 319768 [Multi-domain]  Cd Length: 204  Bit Score: 344.14  E-value: 1.61e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882   5 AILTDIEGTTSAVSFVFDVLFPYAARHLPDFVREHAGETEVA-AQLAAVRAESGEADADVERVIAILLQWIAEDRKATPL 83
Cdd:cd01629   1 AILLDIEGTTTPISFVKDVLFPYARERLPDFLAEHWEDPEVKeDVLAAAAEAEGEAEASIEAVVANLLDWMDEDRKATPL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882  84 KALQGMVWAQGYRDGQLKGHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCSEAGDLGSLFSGYFDTTSGPKRES 163
Cdd:cd01629  81 KALQGLIWREGYESGELKGHLYPDVVPALRRWHAAGLRLYIYSSGSVAAQKLLFGHSDAGDLTPLFSGYFDTTIGPKREA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15596882 164 ASYARIAGAIGLPAAEILFLSDVVQELDAARDAGMRTLGLAREG 207
Cdd:cd01629 161 ASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLLVRPG 204
enolase-ppase TIGR01691
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This enzyme is the enolase-phosphatase ...
3-220 1.66e-88

2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This enzyme is the enolase-phosphatase of methionine salvage, a pathway that regenerates methionine from methylthioadenosine (MTA). Adenosylmethionine (AdoMet) is a donor of different moieties for various processes, including methylation reactions. Use of AdoMet for spermidine biosynthesis, which leads to polyamine biosynthesis, leaves MTA as a by-product that must be cleared. In Bacillus subtilis and related species, this single protein is replaced by separate enzymes with enolase and phosphatase activities. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273760 [Multi-domain]  Cd Length: 220  Bit Score: 261.32  E-value: 1.66e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882     3 IKAILTDIEGTTSAVSFVFDVLFPYAARHLPDFVREHAGETEVAAqlaavRAESGeADADVERVIAILLQWIAEDRKATP 82
Cdd:TIGR01691   1 IKNVLLDIEGTTGSISFVHDVLFPYAASRLESFVNDNYESTIVEN-----LRELG-KTPEELILLRKLHAEMDKDRKATP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882    83 LKALQGMVWAQGYRDGQLKGHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCSEAGDLGSLFSGYFDTTSGPKRE 162
Cdd:TIGR01691  75 LKTLQGLIWRQGYESGELTSHLYPDVPPALEAWLQLGLRLAVYSSGSVPAQKLLFGHSDAGNLTPYFSGYFDTTVGLKTE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15596882   163 SASYARIAGAIGLPAAEILFLSDVVQELDAARDAGMRTLGLAREGGSLDGHPTVASSP 220
Cdd:TIGR01691 155 AQSYVKIAGQLGSPPREILFLSDIINELDAARKAGLHTGQLVRPGNDPVVDPSFPVYP 212
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
5-197 1.39e-18

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: 80.13  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882     5 AILTDIEGTTSAVSFVFDVLFPYAARHlpdfvrehageteVAAQLAAVRAESGEADadverVIAILLQWIAEDRkatpLK 84
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEE-------------FGLDPASFKALKQAGG-----LAEEEWYRIATSA----LE 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882    85 ALQGMVWAqGYRDGQLKghvYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCSEAGDLGSLFSGYFDTtsGPKRESA 164
Cdd:TIGR01549  59 ELQGRFWS-EYDAEEAY---IRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEP--GSKPEPE 132
                         170       180       190
                  ....*....|....*....|....*....|...
gi 15596882   165 SYARIAGAIGLPaAEILFLSDVVQELDAARDAG 197
Cdd:TIGR01549 133 IFLAALESLGVP-PEVLHVGDNLNDIEGARNAG 164
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
16-215 9.21e-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: 70.83  E-value: 9.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882  16 AVSF-VFDVLF---PYAARHLPDFVREHAGETEVAAQLAAVRAESGEADADVERV---IAILLQWIAEDRKATPLKALqg 88
Cdd:COG1011   3 AVLFdLDGTLLdfdPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYERGeitFAELLRRLLEELGLDLAEEL-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882  89 mvwAQGYRDG-QLKGHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFgcsEAGDLGSLFSGYFdtTSG----PKRES 163
Cdd:COG1011  81 ---AEAFLAAlPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKL---RRLGLDDLFDAVV--SSEevgvRKPDP 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15596882 164 ASYARIAGAIGLPAAEILFLSDVVQE-LDAARDAGMRTLGLAREGGSLDGHPT 215
Cdd:COG1011 153 EIFELALERLGVPPEEALFVGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPR 205
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
3-197 1.11e-11

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: 61.83  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882     3 IKAILTDIEGTTSAVSFVFDVLFPYAARHLPDFVREHAGETEVAAQLAAVRAESGEADADverviaiLLQWIAEDRKATP 82
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRD-------WLEELDILRGLVE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882    83 LKALQGMVWAQGYRDGQLKGH----VYPDAVQALREWKARGLDLYVYSSGSIQ-AQKLIFGCSEAGDLGSLFSGYFDTTS 157
Cdd:pfam00702  74 TLEAEGLTVVLVELLGVIALAdelkLYPGAAEALKALKERGIKVAILTGDNPEaAEALLRLLGLDDYFDVVISGDDVGVG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 15596882   158 GPKRESasYARIAGAIGLPAAEILFLSDVVQELDAARDAG 197
Cdd:pfam00702 154 KPKPEI--YLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-204 1.09e-07

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 50.70  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882   3 IKAILTDIEGTTSAVSFVFDVLFPYAARHL------PDFVREHAGETevaAQLAAVRAESGEADADVERVIAILLQWIAE 76
Cdd:COG0546   1 IKLVLFDLDGTLVDSAPDIAAALNEALAELglppldLEELRALIGLG---LRELLRRLLGEDPDEELEELLARFRELYEE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882  77 DRKAtplkalqgmvwaqgyrdgqlKGHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFgcsEAGDLGSLFSGYF--D 154
Cdd:COG0546  78 ELLD--------------------ETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLL---EALGLDDYFDAIVggD 134
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15596882 155 TTSGPKRESASYARIAGAIGLPAAEILFLSDVVQELDAARDAGMRTLGLA 204
Cdd:COG0546 135 DVPPAKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVT 184
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
108-203 2.24e-07

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: 48.16  E-value: 2.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882 108 AVQALREWKARGLDLYVYSSGSIQAQKLIFgcsEAGDLGSLFSGYF--DTTSGPKRESASYARIAGAIGLPAAEILFLSD 185
Cdd:cd01427  12 AVELLKRLRAAGIKLAIVTNRSREALRALL---EKLGLGDLFDGIIgsDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGD 88
                        90
                ....*....|....*...
gi 15596882 186 VVQELDAARDAGMRTLGL 203
Cdd:cd01427  89 SENDIEAARAAGGRTVAV 106
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
103-211 5.90e-07

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 48.80  E-value: 5.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882 103 HVYPDAVQALREWKARGLDLYVYSSGSIQaqkLIFGCSEAGDLGSLFSGYF--DTTSGPKRESASYARIAGAIGLPAAEI 180
Cdd:cd02588  91 PPFPDVVAGLRRLREAGYRLAILSNGSPD---LIEDVVANAGLRDLFDAVLsaEDVRAYKPAPAVYELAAERLGVPPDEI 167
                        90       100       110
                ....*....|....*....|....*....|.
gi 15596882 181 LFLSDVVQELDAARDAGMRTLGLAREGGSLD 211
Cdd:cd02588 168 LHVASHAWDLAGARALGLRTAWINRPGEVPD 198
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
3-208 1.16e-06

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 47.72  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882     3 IKAILTDIEGTTSAVSFVFDVlfpyAARHLPDFVrEHAGETEVAAQLAAVRA-ESGEADADVERVIAILLQWIAEDRKAT 81
Cdd:TIGR01428   1 IKALVFDVYGTLFDVHSVAER----AAELYGGRG-EALSQLWRQKQLEYSWLrTLMGPYKDFWDLTREALRYLLGRLGLE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882    82 PLKALQGMVwAQGYRDgqLKghVYPDAVQALREWKARGLDLYVYSSGSIQAqkLIFGCSEAGdlgslFSGYFD---TTSG 158
Cdd:TIGR01428  76 DDESAADRL-AEAYLR--LP--PHPDVPAGLRALKERGYRLAILSNGSPAM--LKSLVKHAG-----LDDPFDavlSADA 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15596882   159 PKR---ESASYARIAGAIGLPAAEILFLSDVVQELDAARDAGMRTLGLAREGG 208
Cdd:TIGR01428 144 VRAykpAPQVYQLALEALGVPPDEVLFVASNPWDLGGAKKFGFKTAWINRPGE 196
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
103-203 3.18e-06

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: 46.26  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882   103 HVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCseagDLGSLFSG--YFDTTSGPKRESASYARIAGAIGLPAAEI 180
Cdd:TIGR01509  80 KPLPGVRALLEALRARGKKLALLTNSPRAHKLVLALL----GLRDLFDVviDSSDVGLGKPDPDIYLQALKALGLEPSEC 155
                          90       100
                  ....*....|....*....|...
gi 15596882   181 LFLSDVVQELDAARDAGMRTLGL 203
Cdd:TIGR01509 156 VFVDDSPAGIEAAKAAGMHTVGV 178
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
102-200 4.96e-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: 45.80  E-value: 4.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882 102 GHVYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFGCSEagdlgsLFSGYFD--TTSGP----KRESASYARIAGAIGL 175
Cdd:cd02603  83 VDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLP------RRGDLFDgvVESCRlgvrKPDPEIYQLALERLGV 156
                        90       100
                ....*....|....*....|....*
gi 15596882 176 PAAEILFLSDVVQELDAARDAGMRT 200
Cdd:cd02603 157 KPEEVLFIDDREENVEAARALGIHA 181
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
104-204 8.67e-03

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


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 35.67  E-value: 8.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596882 104 VYPDAVQALREWKARGLDLYVYSSGSIQAQKLIFgcSEAGDLGSLFSGYF--DTTSGPKRESASYARIAGAIGLPAAEIL 181
Cdd:cd07505  42 LKPGVVELLDALKAAGIPVAVATSSSRRNVELLL--LELGLLRGYFDVIVsgDDVERGKPAPDIYLLAAERLGVDPERCL 119
                        90       100
                ....*....|....*....|...
gi 15596882 182 FLSDVVQELDAARDAGMRTLGLA 204
Cdd:cd07505 120 VFEDSLAGIEAAKAAGMTVVAVP 142
 
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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