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Conserved domains on  [gi|27597073|ref|NP_001970|]
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bifunctional epoxide hydrolase 2 isoform 1 [Homo sapiens]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11552356)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 3-214 2.79e-64

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: 208.35  E-value: 2.79e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   3 LRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLlndAFQKGGPEGATTRLMKGEITLSQwiplMEENCRKCSETAkvcl 82
Cdd:cd02603   1 IRAVLFDFGGVLIDPDPAAAVARFEALTGEPSEF---VLDTEGLAGAFLELERGRITEEE----FWEELREELGRP---- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  83 pknfSIKEIFDKAISAR-KINRPMLQAALMLRKKGFTTAILTNTWLDDRaerdgLAQLMCELKM--HFDFLIESCQVGMV 159
Cdd:cd02603  70 ----LSAELFEELVLAAvDPNPEMLDLLEALRAKGYKVYLLSNTWPDHF-----KFQLELLPRRgdLFDGVVESCRLGVR 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27597073 160 KPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELE 214
Cdd:cd02603 141 KPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALRELA 195
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 259-531 4.07e-55

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


:

Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 186.17  E-value: 4.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   259 PAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGG 338
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   339 MLVWYMALFYPERVRAVASLNTPfipanpnMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDesvLS 418
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGAL-------DPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLL---LR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   419 MHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRnmernwkwackslgrkilIPALMVTAEKDFV 498
Cdd:pfam00561 151 LRLLKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDPL 212

                         250       260       270
                  ....*....|....*....|....*....|...
gi 27597073   499 LVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKP 531
Cdd:pfam00561 213 VPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
 
Name Accession Description Interval E-value
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 3-214 2.79e-64

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: 208.35  E-value: 2.79e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   3 LRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLlndAFQKGGPEGATTRLMKGEITLSQwiplMEENCRKCSETAkvcl 82
Cdd:cd02603   1 IRAVLFDFGGVLIDPDPAAAVARFEALTGEPSEF---VLDTEGLAGAFLELERGRITEEE----FWEELREELGRP---- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  83 pknfSIKEIFDKAISAR-KINRPMLQAALMLRKKGFTTAILTNTWLDDRaerdgLAQLMCELKM--HFDFLIESCQVGMV 159
Cdd:cd02603  70 ----LSAELFEELVLAAvDPNPEMLDLLEALRAKGYKVYLLSNTWPDHF-----KFQLELLPRRgdLFDGVVESCRLGVR 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27597073 160 KPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELE 214
Cdd:cd02603 141 KPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALRELA 195
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 259-531 4.07e-55

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 186.17  E-value: 4.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   259 PAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGG 338
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   339 MLVWYMALFYPERVRAVASLNTPfipanpnMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDesvLS 418
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGAL-------DPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLL---LR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   419 MHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRnmernwkwackslgrkilIPALMVTAEKDFV 498
Cdd:pfam00561 151 LRLLKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDPL 212

                         250       260       270
                  ....*....|....*....|....*....|...
gi 27597073   499 LVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKP 531
Cdd:pfam00561 213 VPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 237-544 5.21e-42

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 150.15  E-value: 5.21e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 237 MSHGYVTVKPrVRLHFVELG-SGPAVCLCHGFPESWYSWRYQIPALAqAGYRVLAMDMKGYGESSAPPEieEYCMEVLCK 315
Cdd:COG0596   2 STPRFVTVDG-VRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAG--GYTLDDLAD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 316 EMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNtpfipanpnmsplesikanpvfdyqlyfqepgvaea 395
Cdd:COG0596  78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------ 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 396 eleqnlsrtfkslfrasdesvlsmhkvceagglfvnspeepslsrmvteEEIQFYVQQFKKSGfRGPLNWYRNMERNWKW 475
Cdd:COG0596 122 -------------------------------------------------EVLAALAEPLRRPG-LAPEALAALLRALART 151

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27597073 476 ACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDS 544
Cdd:COG0596 152 DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
HAD-1A3-hyp TIGR02247
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
 2-219 7.53e-38

epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of sequences including C. elegans and mammalian sequences as well as a small number of bacteria. In eukaryotes, this domain exists as an N-terminal fusion to the soluble epoxide hydrolase enzyme and has recently been shown to be an active phosphatase, although the nature of the biological substrate is unclear. These appear to be members of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases by general homology and the conservation of all of the recognized catalytic motifs (although the first motif is unusual in the replacement of the more common aspartate with glycine...). The variable domain is found in between motifs 1 and 2, indicating membership in subfamily I and phylogeny and prediction of the alpha helical nature of the variable domain (by PSI-PRED) indicate membership in subfamily IA.


Pssm-ID: 274054 [Multi-domain]  Cd Length: 211  Bit Score: 138.80  E-value: 7.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073     2 TLRAAVFDLDGVLaLPAVFGVLG-RTEEALALPRGLLNDAFQKGGPEGATTRLM-KGEITLSQWIPLMEencRKCSETAK 79
Cdd:TIGR02247   1 AIKAVIFDFGGVL-LPSPGVMRRwETERGLPGLKDFIVTVNITGPDFNPWARTFeRGELTAEAFDGLFR---HEYGLRLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073    80 vclpKNFSIKEIFDKAISARKINRPMLQAAL-MLRKKGFTTAILTNTWLDDRAErdGLAQLMCELKMHFDFLIESCQVGM 158
Cdd:TIGR02247  77 ----HDVRIAPVFPLLYGENTKLRPSMMAAIkTLRAKGFKTACITNNFPTDHSA--EEALLPGDIMALFDAVVESCLEGL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27597073   159 VKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGI 219
Cdd:TIGR02247 151 RKPDPRIYQLMLERLGVAPEECVFLDDLGSNLKPAAALGITTIKVSDEEQAIHDLEKATKL 211
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 241-551 3.78e-28

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 113.94  E-value: 3.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  241 YVTVKPRvRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGyRVLAMDMKGYGESSAPPEieEYCMEVLCKEMVTF 320
Cdd:PRK03592  11 RVEVLGS-RMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDI--DYTFADHARYLDAW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  321 LDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLEsikANPVFdyQLyFQEPGVAEAE-LEQ 399
Cdd:PRK03592  87 FDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPA---VRELF--QA-LRSPGEGEEMvLEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  400 NlsrtfkslfrasdesvlsmhkvceaggLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGP-LNWYRNM--------- 469
Cdd:PRK03592 161 N---------------------------VFIERVLPGSILRPLSDEEMAVYRRPFPTPESRRPtLSWPRELpidgepadv 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  470 ----ERNWKWACKSlgrkiLIPALMVTAEKDFVLV-PQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDS 544
Cdd:PRK03592 214 valvEEYAQWLATS-----DVPKLLINAEPGAILTtGAIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAAWLRR 288


                 ....*..
gi 27597073  545 DARNPPV 551
Cdd:PRK03592 289 LRLAVSA 295
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 4-207 2.86e-25

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: 103.95  E-value: 2.86e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   4 RAAVFDLDGVL------------ALPAVFGVLGRTEEALALPRGLLNDAFQkggpegattRLMKGEITLSQWIPLMeenC 71
Cdd:COG1011   2 KAVLFDLDGTLldfdpviaealrALAERLGLLDEAEELAEAYRAIEYALWR---------RYERGEITFAELLRRL---L 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  72 RKCSETAKVCLPKNFsiKEIFDKAISARKINRPMLQAalmLRKKGFTTAILTNT---WLDDRAERDGLAQlmcelkmHFD 148
Cdd:COG1011  70 EELGLDLAEELAEAF--LAALPELVEPYPDALELLEA---LKARGYRLALLTNGsaeLQEAKLRRLGLDD-------LFD 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 149 FLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIG-ANLKPARDLGMVTILVQDTD 207
Cdd:COG1011 138 AVVSSEEVGVRKPDPEIFELALERLGVPPEEALFVGDSPeTDVAGARAAGMRTVWVNRSG 197
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-197 4.32e-20

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: 88.41  E-value: 4.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073     3 LRAAVFDLDGVLAL--PAVFGVLGRTEEALALPRGLLNDAFQKGGP-EGATTRLMKGEITLSQWIPLMEENCRKCSETAK 79
Cdd:pfam00702   1 IKAVVFDLDGTLTDgePVVTEAIAELASEHPLAKAIVAAAEDLPIPvEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073    80 VClpknFSIKEIFDKAISARKINRPMLQAAL-MLRKKGFTTAILTNtwlDDRAERDGLAQLmCELKMHFDFLIESCQVGM 158
Cdd:pfam00702  81 TV----VLVELLGVIALADELKLYPGAAEALkALKERGIKVAILTG---DNPEAAEALLRL-LGLDDYFDVVISGDDVGV 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 27597073   159 VKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLG 197
Cdd:pfam00702 153 GKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 252-543 7.14e-14

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 72.41  E-value: 7.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   252 FVELGSGPAVCLCHGFP----ESWYSWRYQipaLAQAGYRVLAMDMKGYGESSAPPEIEE--YCMEVLCKEMVTFLDKLG 325
Cdd:TIGR01250  19 TGGEGEKIKLLLLHGGPgmshEYLENLREL---LKEEGREVIMYDQLGCGYSDQPDDSDEelWTIDYFVDELEEVREKLG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   326 LSQAVFIGHDWGGMLVWYMALFYPERVRAVaslntpfIPANPNMS-PLESIKANPVFDYqlyfQEPGVAEAELEQNLSRT 404
Cdd:TIGR01250  96 LDKFYLLGHSWGGMLAQEYALKYGQHLKGL-------IISSMLDSaPEYVKELNRLRKE----LPPEVRAAIKRCEASGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   405 FKSLFRASDESVLSMHKVCeagglfVNSPEEPSLSRMVTEEEIQFYvqqfkkSGFRGPlNWYRNMERNWKWACKSLGRKI 484
Cdd:TIGR01250 165 YDNPEYQEAVEVFYHHLLC------RLRKWPEALKHLKSGGNTNVY------NIMQGP-NEFTITGNLKDWDITDKLSEI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 27597073   485 LIPALMVTAEKDFVlVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLD 543
Cdd:TIGR01250 232 KVPTLLTVGEFDTM-TPEAAREMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFIR 289
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 112-208 2.15e-12

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 66.22  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  112 LRKKGFTTAILTNTwldDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLK 191
Cdd:PRK09456  96 LREQGHRVVVLSNT---NRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNADNIE 172

                         90
                 ....*....|....*..
gi 27597073  192 PARDLGMVTILVQDTDT 208
Cdd:PRK09456 173 AANALGITSILVTDKQT 189
 
Name Accession Description Interval E-value
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 3-214 2.79e-64

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: 208.35  E-value: 2.79e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   3 LRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLlndAFQKGGPEGATTRLMKGEITLSQwiplMEENCRKCSETAkvcl 82
Cdd:cd02603   1 IRAVLFDFGGVLIDPDPAAAVARFEALTGEPSEF---VLDTEGLAGAFLELERGRITEEE----FWEELREELGRP---- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  83 pknfSIKEIFDKAISAR-KINRPMLQAALMLRKKGFTTAILTNTWLDDRaerdgLAQLMCELKM--HFDFLIESCQVGMV 159
Cdd:cd02603  70 ----LSAELFEELVLAAvDPNPEMLDLLEALRAKGYKVYLLSNTWPDHF-----KFQLELLPRRgdLFDGVVESCRLGVR 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27597073 160 KPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELE 214
Cdd:cd02603 141 KPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALRELA 195
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 259-531 4.07e-55

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 186.17  E-value: 4.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   259 PAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGG 338
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   339 MLVWYMALFYPERVRAVASLNTPfipanpnMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDesvLS 418
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGAL-------DPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLL---LR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   419 MHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRnmernwkwackslgrkilIPALMVTAEKDFV 498
Cdd:pfam00561 151 LRLLKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDPL 212

                         250       260       270
                  ....*....|....*....|....*....|...
gi 27597073   499 LVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKP 531
Cdd:pfam00561 213 VPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 237-544 5.21e-42

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 150.15  E-value: 5.21e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 237 MSHGYVTVKPrVRLHFVELG-SGPAVCLCHGFPESWYSWRYQIPALAqAGYRVLAMDMKGYGESSAPPEieEYCMEVLCK 315
Cdd:COG0596   2 STPRFVTVDG-VRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAG--GYTLDDLAD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 316 EMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNtpfipanpnmsplesikanpvfdyqlyfqepgvaea 395
Cdd:COG0596  78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------ 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 396 eleqnlsrtfkslfrasdesvlsmhkvceagglfvnspeepslsrmvteEEIQFYVQQFKKSGfRGPLNWYRNMERNWKW 475
Cdd:COG0596 122 -------------------------------------------------EVLAALAEPLRRPG-LAPEALAALLRALART 151

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27597073 476 ACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDS 544
Cdd:COG0596 152 DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
HAD-1A3-hyp TIGR02247
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
 2-219 7.53e-38

epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of sequences including C. elegans and mammalian sequences as well as a small number of bacteria. In eukaryotes, this domain exists as an N-terminal fusion to the soluble epoxide hydrolase enzyme and has recently been shown to be an active phosphatase, although the nature of the biological substrate is unclear. These appear to be members of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases by general homology and the conservation of all of the recognized catalytic motifs (although the first motif is unusual in the replacement of the more common aspartate with glycine...). The variable domain is found in between motifs 1 and 2, indicating membership in subfamily I and phylogeny and prediction of the alpha helical nature of the variable domain (by PSI-PRED) indicate membership in subfamily IA.


Pssm-ID: 274054 [Multi-domain]  Cd Length: 211  Bit Score: 138.80  E-value: 7.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073     2 TLRAAVFDLDGVLaLPAVFGVLG-RTEEALALPRGLLNDAFQKGGPEGATTRLM-KGEITLSQWIPLMEencRKCSETAK 79
Cdd:TIGR02247   1 AIKAVIFDFGGVL-LPSPGVMRRwETERGLPGLKDFIVTVNITGPDFNPWARTFeRGELTAEAFDGLFR---HEYGLRLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073    80 vclpKNFSIKEIFDKAISARKINRPMLQAAL-MLRKKGFTTAILTNTWLDDRAErdGLAQLMCELKMHFDFLIESCQVGM 158
Cdd:TIGR02247  77 ----HDVRIAPVFPLLYGENTKLRPSMMAAIkTLRAKGFKTACITNNFPTDHSA--EEALLPGDIMALFDAVVESCLEGL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27597073   159 VKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGI 219
Cdd:TIGR02247 151 RKPDPRIYQLMLERLGVAPEECVFLDDLGSNLKPAAALGITTIKVSDEEQAIHDLEKATKL 211
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 5-203 6.02e-35

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: 129.46  E-value: 6.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073     5 AAVFDLDGVLALPAVFG-VLGRTEEALALPRGLLNDAFQKggPEGATTRLMKGEITLSQWIPLMeencrkcsetakvCLP 83
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIaKLINREELGLVPDELGVSAVGR--LELALRRFKAQYGRTISPEDAQ-------------LLY 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073    84 KNFSIKEIFDKAISarKINRPMLQAALMLRKKGFTTAILTNTWLDDRaerdgLAQLMCELKMHFDFLIESCQVGMVKPEP 163
Cdd:TIGR01509  66 KQLFYEQIEEEAKL--KPLPGVRALLEALRARGKKLALLTNSPRAHK-----LVLALLGLRDLFDVVIDSSDVGLGKPDP 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 27597073   164 QIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILV 203
Cdd:TIGR01509 139 DIYLQALKALGLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 241-551 3.78e-28

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 113.94  E-value: 3.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  241 YVTVKPRvRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGyRVLAMDMKGYGESSAPPEieEYCMEVLCKEMVTF 320
Cdd:PRK03592  11 RVEVLGS-RMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDI--DYTFADHARYLDAW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  321 LDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLEsikANPVFdyQLyFQEPGVAEAE-LEQ 399
Cdd:PRK03592  87 FDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPA---VRELF--QA-LRSPGEGEEMvLEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  400 NlsrtfkslfrasdesvlsmhkvceaggLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGP-LNWYRNM--------- 469
Cdd:PRK03592 161 N---------------------------VFIERVLPGSILRPLSDEEMAVYRRPFPTPESRRPtLSWPRELpidgepadv 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  470 ----ERNWKWACKSlgrkiLIPALMVTAEKDFVLV-PQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDS 544
Cdd:PRK03592 214 valvEEYAQWLATS-----DVPKLLINAEPGAILTtGAIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAAWLRR 288


                 ....*..
gi 27597073  545 DARNPPV 551
Cdd:PRK03592 289 LRLAVSA 295
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 4-207 2.86e-25

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: 103.95  E-value: 2.86e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   4 RAAVFDLDGVL------------ALPAVFGVLGRTEEALALPRGLLNDAFQkggpegattRLMKGEITLSQWIPLMeenC 71
Cdd:COG1011   2 KAVLFDLDGTLldfdpviaealrALAERLGLLDEAEELAEAYRAIEYALWR---------RYERGEITFAELLRRL---L 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  72 RKCSETAKVCLPKNFsiKEIFDKAISARKINRPMLQAalmLRKKGFTTAILTNT---WLDDRAERDGLAQlmcelkmHFD 148
Cdd:COG1011  70 EELGLDLAEELAEAF--LAALPELVEPYPDALELLEA---LKARGYRLALLTNGsaeLQEAKLRRLGLDD-------LFD 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 149 FLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIG-ANLKPARDLGMVTILVQDTD 207
Cdd:COG1011 138 AVVSSEEVGVRKPDPEIFELALERLGVPPEEALFVGDSPeTDVAGARAAGMRTVWVNRSG 197
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 241-365 2.66e-21

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 94.65  E-value: 2.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  241 YVTVKP----RVRLHFVELGS--GPAVCLCHGFPeSW-YSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVL 313
Cdd:PRK00870  23 YVDVDDgdggPLRMHYVDEGPadGPPVLLLHGEP-SWsYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPTRREDYTYARH 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 27597073  314 CKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTpFIPA 365
Cdd:PRK00870 102 VEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANT-GLPT 152
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-197 4.32e-20

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: 88.41  E-value: 4.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073     3 LRAAVFDLDGVLAL--PAVFGVLGRTEEALALPRGLLNDAFQKGGP-EGATTRLMKGEITLSQWIPLMEENCRKCSETAK 79
Cdd:pfam00702   1 IKAVVFDLDGTLTDgePVVTEAIAELASEHPLAKAIVAAAEDLPIPvEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073    80 VClpknFSIKEIFDKAISARKINRPMLQAAL-MLRKKGFTTAILTNtwlDDRAERDGLAQLmCELKMHFDFLIESCQVGM 158
Cdd:pfam00702  81 TV----VLVELLGVIALADELKLYPGAAEALkALKERGIKVAILTG---DNPEAAEALLRL-LGLDDYFDVVISGDDVGV 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 27597073   159 VKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLG 197
Cdd:pfam00702 153 GKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PLN02578 PLN02578
hydrolase
 249-375 2.68e-17

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 83.35  E-value: 2.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  249 RLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAgYRVLAMDMKGYGESSAPpeIEEYCMEVLCKEMVTFLDKLGLSQ 328
Cdd:PLN02578  77 KIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKK-YKVYALDLLGFGWSDKA--LIEYDAMVWRDQVADFVKEVVKEP 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 27597073  329 AVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESI 375
Cdd:PLN02578 154 AVLVGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESREKEEAI 200
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
247-367 7.66e-17

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 79.66  E-value: 7.66e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 247 RVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAP----PEIEEYCMEVlcKEMVTFLD 322
Cdd:COG2267  17 RGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPrghvDSFDDYVDDL--RAALDALR 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 27597073 323 KLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVAsLNTPFIPANP 367
Cdd:COG2267  95 ARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLV-LLAPAYRADP 138
PRK05855 PRK05855
SDR family oxidoreductase;
248-531 1.31e-14

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 76.56  E-value: 1.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  248 VRLHFVELG--SGPAVCLCHGFPESWYSWRYQIPALAqAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLG 325
Cdd:PRK05855  13 VRLAVYEWGdpDRPTVVLVHGYPDNHEVWDGVAPLLA-DRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  326 LSQAV-FIGHDWGGMLVWYmALFYPERVRAVASLNTpfipanpnMSplesikaNPVFDYQLYFQEPGVAeAELEQNLSRT 404
Cdd:PRK05855  92 PDRPVhLLAHDWGSIQGWE-AVTRPRAAGRIASFTS--------VS-------GPSLDHVGFWLRSGLR-RPTPRRLARA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  405 FKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVteEEI---QFYVQQFKKSGFRGpLNWYR-NMERnwkwackSL 480
Cdd:PRK05855 155 LGQLLRSWYIYLFHLPVLPELLWRLGLGRAWPRLLRRV--EGTpvdPIPTQTTLSDGAHG-VKLYRaNMIR-------SL 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 27597073  481 GRK----ILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIeDCGHWTQMDKP 531
Cdd:PRK05855 225 SRPreryTDVPVQLIVPTGDPYVRPALYDDLSRWVPRLWRREI-KAGHWLPMSHP 278
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 247-366 1.82e-14

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 74.12  E-value: 1.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  247 RVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALaQAGYRVLAMDMKGYGESSAPPEIEeYCMEVLCKEMVTFLDKLGL 326
Cdd:PRK03204  23 RGRIHYIDEGTGPPILLCHGNPTWSFLYRDIIVAL-RDRFRCVAPDYLGFGLSERPSGFG-YQIDEHARVIGEFVDHLGL 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 27597073  327 SQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPAN 366
Cdd:PRK03204 101 DRYLSMGQDWGGPISMAVAVERADRVRGVVLGNTWFWPAD 140
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
259-358 1.97e-14

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 72.74  E-value: 1.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 259 PAVCLCHGFPES-WYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEY--CMEVLcKEMVT--FLD--KLGLsqavf 331
Cdd:COG1506  24 PVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVddVLAAI-DYLAArpYVDpdRIGI----- 97

                        90       100
                ....*....|....*....|....*..
gi 27597073 332 IGHDWGGMLVWYMALFYPERVRAVASL 358
Cdd:COG1506  98 YGHSYGGYMALLAAARHPDRFKAAVAL 124
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 252-543 7.14e-14

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 72.41  E-value: 7.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   252 FVELGSGPAVCLCHGFP----ESWYSWRYQipaLAQAGYRVLAMDMKGYGESSAPPEIEE--YCMEVLCKEMVTFLDKLG 325
Cdd:TIGR01250  19 TGGEGEKIKLLLLHGGPgmshEYLENLREL---LKEEGREVIMYDQLGCGYSDQPDDSDEelWTIDYFVDELEEVREKLG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   326 LSQAVFIGHDWGGMLVWYMALFYPERVRAVaslntpfIPANPNMS-PLESIKANPVFDYqlyfQEPGVAEAELEQNLSRT 404
Cdd:TIGR01250  96 LDKFYLLGHSWGGMLAQEYALKYGQHLKGL-------IISSMLDSaPEYVKELNRLRKE----LPPEVRAAIKRCEASGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   405 FKSLFRASDESVLSMHKVCeagglfVNSPEEPSLSRMVTEEEIQFYvqqfkkSGFRGPlNWYRNMERNWKWACKSLGRKI 484
Cdd:TIGR01250 165 YDNPEYQEAVEVFYHHLLC------RLRKWPEALKHLKSGGNTNVY------NIMQGP-NEFTITGNLKDWDITDKLSEI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 27597073   485 LIPALMVTAEKDFVlVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLD 543
Cdd:TIGR01250 232 KVPTLLTVGEFDTM-TPEAAREMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFIR 289
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 249-538 4.92e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 70.74  E-value: 4.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  249 RLHFVELG--SGPAVCLCHGFPESWYSWRYQIPALAqAGYRVLAMDMKGYGESSapPEIEEYCMEVLCKEMVTFLDKLGL 326
Cdd:PRK14875 120 TVRYLRLGegDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASS--KAVGAGSLDELAAAVLAFLDALGI 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  327 SQAVFIGHDWGGMLVWYMALFYPERVRAVASL---------NTPFI------PANPNMSP-LESIKANP-------VFDY 383
Cdd:PRK14875 197 ERAHLVGHSMGGAVALRLAARAPQRVASLTLIapaglgpeiNGDYIdgfvaaESRRELKPvLELLFADPalvtrqmVEDL 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  384 QLYFQEPGVAEAeleqnLSRTFKSLFRASdesvlsmhkvceagglfvnspeepslsrmvteeeiqfyVQQFkksGFRGPL 463
Cdd:PRK14875 277 LKYKRLDGVDDA-----LRALADALFAGG--------------------------------------RQRV---DLRDRL 310

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27597073  464 nwyrnmernwkwacKSLGrkilIPALMVTAEKDFVLVPQMSQHMEDWIP-HLkrghIEDCGHWTQMDKPTEVNQIL 538
Cdd:PRK14875 311 --------------ASLA----IPVLVIWGEQDRIIPAAHAQGLPDGVAvHV----LPGAGHMPQMEAAADVNRLL 364
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 112-208 2.15e-12

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 66.22  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  112 LRKKGFTTAILTNTwldDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLK 191
Cdd:PRK09456  96 LREQGHRVVVLSNT---NRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNADNIE 172

                         90
                 ....*....|....*..
gi 27597073  192 PARDLGMVTILVQDTDT 208
Cdd:PRK09456 173 AANALGITSILVTDKQT 189
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 256-359 2.38e-11

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 64.76  E-value: 2.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  256 GSGPAVCLCHGFPESWYSWRYQIPALAQAGyRVLAMDMKGYGESSAP-----PEIEEYCMEVLCKEMVTFLDKLGLSQAV 330
Cdd:PLN02824  27 TSGPALVLVHGFGGNADHWRKNTPVLAKSH-RVYAIDLLGYGYSDKPnprsaPPNSFYTFETWGEQLNDFCSDVVGDPAF 105

                         90       100
                 ....*....|....*....|....*....
gi 27597073  331 FIGHDWGGMLVWYMALFYPERVRAVASLN 359
Cdd:PLN02824 106 VICNSVGGVVGLQAAVDAPELVRGVMLIN 134
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 260-372 6.35e-11

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 62.62  E-value: 6.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   260 AVCLCHGFPEswYSWRYQ--IPALAQAGYRVLAMDMKGYGESSAP----PEIEEYCMEVlcKEMVTFLDKLGLSQAVFI- 332
Cdd:pfam12146   6 VVVLVHGLGE--HSGRYAhlADALAAQGFAVYAYDHRGHGRSDGKrghvPSFDDYVDDL--DTFVDKIREEHPGLPLFLl 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 27597073   333 GHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPL 372
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPI 121
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 263-362 4.69e-10

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 56.76  E-value: 4.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 263 LCHGFPESWYSWRYQIPALAQAGYRVLAMDmkgYGESSAPpeieeycMEVLCKEMVTFLDKL----GLSQAVFIGHDWGG 338
Cdd:COG1075  10 LVHGLGGSAASWAPLAPRLRAAGYPVYALN---YPSTNGS-------IEDSAEQLAAFVDAVlaatGAEKVDLVGHSMGG 79

                        90       100
                ....*....|....*....|....*.
gi 27597073 339 MLVWYMA--LFYPERVRAVASLNTPF 362
Cdd:COG1075  80 LVARYYLkrLGGAAKVARVVTLGTPH 105
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 101-203 6.02e-10

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: 56.64  E-value: 6.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 101 INRPMLQAalmLRKKGFTTAILTNT---WLDDRAERDGLAQlmcelkmHFDFLIESCQVGMVKPEPQIYKFLLDTLKASP 177
Cdd:cd01427  11 LAVELLKR---LRAAGIKLAIVTNRsreALRALLEKLGLGD-------LFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDP 80

                        90       100
                ....*....|....*....|....*.
gi 27597073 178 SEVVFLDDIGANLKPARDLGMVTILV 203
Cdd:cd01427  81 EEVLFVGDSENDIEAARAAGGRTVAV 106
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 101-223 1.31e-09

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 56.15  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 101 INRPMLQAalmLRKKGFTTAILTNTwldDRAERDGLAQlmCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEV 180
Cdd:cd16415  11 LAVETLKD---LKEKGLKLAVVSNF---DRRLRELLEA--LGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEA 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 27597073 181 VFL-DDIGANLKPARDLGMVTILVqDTDTALKELEKVTGIQLLN 223
Cdd:cd16415  83 LHVgDDLKNDYLGARAVGWHALLV-DREGALHELPSLANLLERL 125
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 240-339 5.48e-09

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 57.93  E-value: 5.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  240 GYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAgYRVLAMDMKGYGESSAPPEIeEYCMEVLCKEMVT 319
Cdd:PLN02679  70 GEYSINYLVKGSPEVTSSGPPVLLVHGFGASIPHWRRNIGVLAKN-YTVYAIDLLGFGASDKPPGF-SYTMETWAELILD 147

                         90       100
                 ....*....|....*....|
gi 27597073  320 FLDKLGLSQAVFIGHDWGGM 339
Cdd:PLN02679 148 FLEEVVQKPTVLIGNSVGSL 167
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 263-373 8.30e-09

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 55.94  E-value: 8.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   263 LCHGFpesWYSWRyQIPALAQAGYRVLAMDMKGYGESSAPP-EIEEYcmevlcKEMVTFLDKLG-LSQAVFIGHDWGGML 340
Cdd:pfam12697   3 LVHGA---GLSAA-PLAALLAAGVAVLAPDLPGHGSSSPPPlDLADL------ADLAALLDELGaARPVVLVGHSLGGAV 72

                          90       100       110
                  ....*....|....*....|....*....|...
gi 27597073   341 VWYMALFYPERVRAVASLNTPFIPANPNMSPLE 373
Cdd:pfam12697  73 ALAAAAAALVVGVLVAPLAAPPGLLAALLALLA 105
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-203 1.14e-08

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 55.71  E-value: 1.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   3 LRAAVFDLDGVLA--LPAVFGVLGRTEEALALP----------RGL-LNDAFQKGGPEGATTRLmkgEITLSQWIPLMEE 69
Cdd:COG0546   1 IKLVLFDLDGTLVdsAPDIAAALNEALAELGLPpldleelralIGLgLRELLRRLLGEDPDEEL---EELLARFRELYEE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  70 NCRKCSEtakvclpknfsikeIFDKAisarkinRPMLQAalmLRKKGFTTAILTNtwlddrAERDGLAQLMCELKM--HF 147
Cdd:COG0546  78 ELLDETR--------------LFPGV-------RELLEA---LKARGIKLAVVTN------KPREFAERLLEALGLddYF 127

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 148 DFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVF----LDDIGAnlkpARDLGMVTILV 203
Cdd:COG0546 128 DAIVGGDDVPPAKPKPEPLLEALERLGLDPEEVLMvgdsPHDIEA----ARAAGVPFIGV 183
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
252-414 1.43e-08

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 55.72  E-value: 1.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 252 FVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESsaPPEIEEYCMEVLCKEMVTFLDKL-GLSQAV 330
Cdd:COG1647   9 FFLEGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTS--PEDLLKTTWEDWLEDVEEAYEILkAGYDKV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 331 F-IGHDWGGMLVWYMALFYPErVRAVASLNTPFIPANPNMS--PLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKS 407
Cdd:COG1647  87 IvIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPllPLLKYLARSLRGIGSDIEDPEVAEYAYDRTPLRALAE 165


                ....*..
gi 27597073 408 LFRASDE 414
Cdd:COG1647 166 LQRLIRE 172
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 103-203 1.51e-08

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: 55.35  E-value: 1.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 103 RPMLQAalmLRKKGFTTAILTN---TWLDDRAERDGLAQLmcelkmhFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSE 179
Cdd:cd02588  97 VAGLRR---LREAGYRLAILSNgspDLIEDVVANAGLRDL-------FDAVLSAEDVRAYKPAPAVYELAAERLGVPPDE 166

                        90       100
                ....*....|....*....|....*..
gi 27597073 180 VVFlddIGAN---LKPARDLGMVTILV 203
Cdd:cd02588 167 ILH---VASHawdLAGARALGLRTAWI 190
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
2-216 1.75e-08

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 54.83  E-value: 1.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   2 TLRAAVFDLDGVLAlpavfgvlgRTEEalaLPRGLLNDAFQKGGPE--GATTRLMKGeITLSQWIPLMEENCRKCSETAK 79
Cdd:COG0637   1 MIKAVIFDMDGTLV---------DSEP---LHARAWREAFAELGIDltEEEYRRLMG-RSREDILRYLLEEYGLDLPEEE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  80 VCLPKNfsikEIFDKAISARKIN-RPMLQAAL-MLRKKGFTTAILTNT---WLDDRAERDGLAQlmcelkmHFDFLIESC 154
Cdd:COG0637  68 LAARKE----ELYRELLAEEGLPlIPGVVELLeALKEAGIKIAVATSSpreNAEAVLEAAGLLD-------YFDVIVTGD 136

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27597073 155 QVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKV 216
Cdd:COG0637 137 DVARGKPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGA 198
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
256-380 2.27e-07

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 51.89  E-value: 2.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 256 GSGPAVCLCHGfpesWYSWRYQIPA----LAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVT--------FL-- 321
Cdd:COG0412  27 GPRPGVVVLHE----IFGLNPHIRDvarrLAAAGYVVLAPDLYGRGGPGDDPDEARALMGALDPELLAadlraaldWLka 102

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27597073 322 ------DKLGLsqavfIGHDWGGMLVWYMALFYPeRVRAVASLNtPFIPANPNMSPLESIKAnPV 380
Cdd:COG0412 103 qpevdaGRVGV-----VGFCFGGGLALLAAARGP-DLAAAVSFY-GGLPADDLLDLAARIKA-PV 159
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 249-418 1.52e-06

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 50.65  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  249 RLHFVELGS--GPAVCLCHGFPESWYSWRYQIPALAQaGYRVLAMDMKGYGESSAPP-------EIEEY--CMEVLCKEM 317
Cdd:PLN03084 116 RWFCVESGSnnNPPVLLIHGFPSQAYSYRKVLPVLSK-NYHAIAFDWLGFGFSDKPQpgygfnyTLDEYvsSLESLIDEL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  318 VTflDKLGLsqaVFIGHdWGGMLVWYmALFYPERVRAVASLNTPFIPANPNMSPLESIKANpVFDYQLYFQEPgvaeael 397
Cdd:PLN03084 195 KS--DKVSL---VVQGY-FSPPVVKY-ASAHPDKIKKLILLNPPLTKEHAKLPSTLSEFSN-FLLGEIFSQDP------- 259

                        170       180
                 ....*....|....*....|.
gi 27597073  398 eqnlsrtfkslFRASDESVLS 418
Cdd:PLN03084 260 -----------LRASDKALTS 269
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
7-203 2.06e-06

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 48.35  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073     7 VFDLDGVLAlpavfgvlgRTEEALAlprGLLNDAFQKGGPegattrlmkGEITLSQWIPLMEENCRKCSETAKVCLPKNF 86
Cdd:pfam13419   2 IFDFDGTLL---------DTEELII---KSFNYLLEEFGY---------GELSEEEILKFIGLPLREIFRYLGVSEDEEE 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073    87 SIKEIFDK--AISARKINRP------MLQAalmLRKKGFTTAILTNTwldDRAE-RDGLAQLmcELKMHFDFLIESCQVG 157
Cdd:pfam13419  61 KIEFYLRKynEELHDKLVKPypgikeLLEE---LKEQGYKLGIVTSK---SRENvEEFLKQL--GLEDYFDVIVGGDDVE 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 27597073   158 MVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILV 203
Cdd:pfam13419 133 GKKPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
PRK10673 PRK10673
esterase;
283-545 2.74e-05

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 45.88  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  283 QAGYRVLAMDMKGYGESSAPPEIEEYCMevlCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERV-RAVAslntp 361
Cdd:PRK10673  40 VNDHDIIQVDMRNHGLSPRDPVMNYPAM---AQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIdKLVA----- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  362 fipanpnmsplesIKANPVfDYQLyfqepgvaeaeleqnlsrtfkslfRASDESVLSMHKVCEAGglfVNSPEEPS-LSR 440
Cdd:PRK10673 112 -------------IDIAPV-DYHV------------------------RRHDEIFAAINAVSEAG---ATTRQQAAaIMR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  441 MVTEEE--IQFYVQQFKKSgfrgplNWYRNMERNWKWACKSLGRKILI----PALMVTAEkdfvLVPQMSQHMEDWI--- 511
Cdd:PRK10673 151 QHLNEEgvIQFLLKSFVDG------EWRFNVPVLWDQYPHIVGWEKIPawphPALFIRGG----NSPYVTEAYRDDLlaq 220

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 27597073  512 -PHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSD 545
Cdd:PRK10673 221 fPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLNDK 255
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 91-203 4.55e-05

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 43.55  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073    91 IFDKAISARKINRPMLQAALMLRKKGFTTAILTN-----TWLDDRAERDGLAQLMCELKMHFDFLIeSCQvGMVKPEPQI 165
Cdd:TIGR01662  16 PYVSDEDERILYPEVPDALAELKEAGYKVVIVTNqsgigRGYFSRSFSGRVARRLEELGVPIDILY-ACP-GCRKPKPGM 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 27597073   166 YKFLLDTL-KASPSEVVFL-DDIGANLKPARDLGMVTILV 203
Cdd:TIGR01662  94 FLEALKRFnEIDPEESVYVgDQDLTDLQAAKRVGLATILV 133
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 103-203 5.39e-05

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: 44.58  E-value: 5.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 103 RPMLQAalmLRKKGFTTAILTNTwLDDRAERdGLAqlMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVF 182
Cdd:cd02616  86 YETLAR---LKSQGIKLGVVTTK-LRETALK-GLK--LLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEEALM 158

                        90       100
                ....*....|....*....|.
gi 27597073 183 LDDIGANLKPARDLGMVTILV 203
Cdd:cd02616 159 VGDSPHDILAGKNAGVKTVGV 179
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 259-353 6.96e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 45.29  E-value: 6.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073  259 PAVCLCHGFPESWYSWRYQIPALAqAGYRVLAMDMKGYGESSAPP-------EIEEYcmevlckemvtFLDKL------- 324
Cdd:PLN02894 106 PTLVMVHGYGASQGFFFRNFDALA-SRFRVIAIDQLGWGGSSRPDftcksteETEAW-----------FIDSFeewrkak 173

                         90       100
                 ....*....|....*....|....*....
gi 27597073  325 GLSQAVFIGHDWGGMLVWYMALFYPERVR 353
Cdd:PLN02894 174 NLSNFILLGHSFGGYVAAKYALKHPEHVQ 202
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 256-362 8.71e-05

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 44.52  E-value: 8.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 256 GSGPAVCLCHGFPES-WYSWRYqIPALAQAGYRVLAMDMKGYGESS------APPEIEEYcmevlcKEMVTFLDKLGL-- 326
Cdd:COG1073  35 KKYPAVVVAHGNGGVkEQRALY-AQRLAELGFNVLAFDYRGYGESEgepreeGSPERRDA------RAAVDYLRTLPGvd 107

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 27597073 327 -SQAVFIGHDWGGMLVWYMALFYPeRVRAVASLnTPF 362
Cdd:COG1073 108 pERIGLLGISLGGGYALNAAATDP-RVKAVILD-SPF 142
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 114-201 1.62e-04

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 40.99  E-value: 1.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 114 KKGFTTAILTNtwlddraerdGLAQLM------CELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFL-DDI 186
Cdd:cd04305  22 KKGYKLGIITN----------GPTEVQwekleqLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVgDSL 91

                        90
                ....*....|....*
gi 27597073 187 GANLKPARDLGMVTI 201
Cdd:cd04305  92 ESDILGAKNAGIKTV 106
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 104-203 3.48e-04

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 40.13  E-value: 3.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 104 PMLQAalmLRKKGFTTAILTNTWldDRAERdglaqlMCE---LKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEV 180
Cdd:cd16421  14 ELLKA---LRQKGIKLAVLSNKP--NEAVQ------VLVeelFPGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEV 82

                        90       100
                ....*....|....*....|...
gi 27597073 181 VFLDDIGANLKPARDLGMVTILV 203
Cdd:cd16421  83 LYVGDSGVDMQTARNAGMDEIGV 105
Hydrolase_like pfam13242
HAD-hyrolase-like;
160-203 3.75e-04

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 39.14  E-value: 3.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 27597073   160 KPEPQIYKFLLDTLKASPSEVVF-----LDDIGAnlkpARDLGMVTILV 203
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMigdrlDTDILG----AREAGARTILV 48
PHA_depoly_arom TIGR02240
poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid ...
 288-547 4.95e-04

poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid (PHA) depolymerase of Pseudomonas oleovorans, Pseudomonas putida BM01, and related species. This enzyme is part of polyester storage and mobilization system as in many bacteria. However, species containing this enzyme are unusual in their capacity to produce aromatic polyesters when grown on carbon sources such as benzoic acid or phenylacetic acid. [Energy metabolism, Other]


Pssm-ID: 131294  Cd Length: 276  Bit Score: 42.29  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   288 VLAMDMKGYGESSAPPEieEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVR----AVASLNTPFI 363
Cdd:TIGR02240  54 VIAFDVPGVGGSSTPRH--PYRFPGLAKLAARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERCKklilAATAAGAVMV 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   364 PANPNMSpleSIKANPvfdyQLYFQEPGVAeaeleqnlsRTFKSLFrasdesvlsmhkvceaGGLFVNSPEepslsrmvt 443
Cdd:TIGR02240 132 PGKPKVL---MMMASP----RRYIQPSHGI---------HIAPDIY----------------GGAFRRDPE--------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073   444 eeeiqFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDfVLVPQMSQHMEDW-IPHLKRgHIEDC 522
Cdd:TIGR02240 171 -----LAMAHASKVRSGGKLGYYWQLFAGLGWTSIHWLHKIQQPTLVLAGDDD-PIIPLINMRLLAWrIPNAEL-HIIDD 243

                         250       260
                  ....*....|....*....|....*
gi 27597073   523 GHWTQMDKPTEVNQILIKWLDSDAR 547
Cdd:TIGR02240 244 GHLFLITRAEAVAPIIMKFLAEERQ 268
HAD_EP cd01629
Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. ...
 160-203 1.25e-03

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: 40.22  E-value: 1.25e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 27597073 160 KPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILV 203
Cdd:cd01629 157 KREAASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLL 200
HAD-SF-IA-v2 TIGR01493
Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid ...
 19-188 1.70e-03

Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid dehalogenase; 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 2 (this model) is distinctive of the type II haloacid dehalogenases, and nearly all of the sequences are also part of the HAD, type II equivalog model (TIGR01428). 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.


Pssm-ID: 130557 [Multi-domain]  Cd Length: 175  Bit Score: 39.43  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073    19 VFGVLGrteeALALPRGLLNDAFQKGGPEG-ATTRLMKGEITLSQWIPLMEENCRKCSETAKVclpknfSIKEIFDKAIS 97
Cdd:TIGR01493   3 VFDVYG----TLVDVHGGVRACLAAIAPEGgAFSDLWRAKQQEYSWRRSLMGDRRAFPEDTVR------ALRYIADRLGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073    98 A--RKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKM--HFDFLIESCQVGMVKPEPQIYKFLLDTL 173
Cdd:TIGR01493  73 DaePKYGERLRDAYKNLPPWPDSAAALARVAILSNASHWAFDQFAQQAGLpwYFDRAFSVDTVRAYKPDPVVYELVFDTV 152

                         170       180
                  ....*....|....*....|
gi 27597073   174 KASPSEVVFL-----DDIGA 188
Cdd:TIGR01493 153 GLPPDRVLMVaahqwDLIGA 172
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 103-203 1.74e-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: 39.14  E-value: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 103 RPMLQAALM-LRKKGFTTAILTNTWLDDRAERDGLAQLmceLKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVV 181
Cdd:cd07505  43 KPGVVELLDaLKAAGIPVAVATSSSRRNVELLLLELGL---LRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCL 119

                        90       100
                ....*....|....*....|..
gi 27597073 182 FLDDIGANLKPARDLGMVTILV 203
Cdd:cd07505 120 VFEDSLAGIEAAKAAGMTVVAV 141
homoserO_Ac_trn TIGR01392
homoserine O-acetyltransferase; This family describes homoserine-O-acetyltransferase, an ...
 320-361 3.77e-03

homoserine O-acetyltransferase; This family describes homoserine-O-acetyltransferase, an enzyme of methionine biosynthesis. This model has been rebuilt to identify sequences more broadly, including a number of sequences suggested to be homoserine O-acetyltransferase based on proximity to other Met biosynthesis genes. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273596 [Multi-domain]  Cd Length: 351  Bit Score: 39.60  E-value: 3.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 27597073   320 FLDKLGLSQ-AVFIGHDWGGMLVWYMALFYPERVRAVASLNTP 361
Cdd:TIGR01392 119 LLDHLGIEQiAAVVGGSMGGMQALEWAIDYPERVRAIVVLATS 161
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 119-202 5.29e-03

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 38.51  E-value: 5.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27597073 119 TAILTNTWLDDRAERdglaqlmcelkmhFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGM 198
Cdd:cd07528 126 DALLSALLGPERRAI-------------FDAIAAGDDVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGL 192


                ....
gi 27597073 199 VTIL 202
Cdd:cd07528 193 PCIV 196
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 160-203 6.03e-03

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 38.00  E-value: 6.03e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 27597073 160 KPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILV 203
Cdd:cd02604 137 KPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLV 180
 
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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