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Conserved domains on  [gi|374532800|ref|NP_001243411|]
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bifunctional epoxide hydrolase 2 isoform 2 [Homo sapiens]

Protein Classification

HAD_sEH-N_like and Abhydrolase_1 domain-containing protein( domain architecture ID 11552356)

HAD_sEH-N_like and Abhydrolase_1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 206-478 1.39e-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: 1.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  206 PAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGG 285
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  286 MLVWYMALFYPERVRAVASLNTPfipanpnMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDesvLS 365
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGAL-------DPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLL---LR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  366 MHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRnmernwkwackslgrkilIPALMVTAEKDFV 445
Cdd:pfam00561 151 LRLLKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDPL 212

                         250       260       270
                  ....*....|....*....|....*....|...
gi 374532800  446 LVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKP 478
Cdd:pfam00561 213 VPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 1-161 1.95e-49

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: 168.29  E-value: 1.95e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800   1 MKGEITLSQwiplMEENCRKCSETAkvclpknfSIKEIFDKAISAR-KINRPMLQAALMLRKKGFTTAILTNTWLDDRae 79
Cdd:cd02603   49 ERGRITEEE----FWEELREELGRP--------LSAELFEELVLAAvDPNPEMLDLLEALRAKGYKVYLLSNTWPDHF-- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  80 rdgLAQLMCELKM--HFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTAL 157
Cdd:cd02603  115 ---KFQLELLPRRgdLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDAL 191


                 ....
gi 374532800 158 KELE 161
Cdd:cd02603  192 RELA 195
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 206-478 1.39e-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: 1.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  206 PAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGG 285
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  286 MLVWYMALFYPERVRAVASLNTPfipanpnMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDesvLS 365
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGAL-------DPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLL---LR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  366 MHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRnmernwkwackslgrkilIPALMVTAEKDFV 445
Cdd:pfam00561 151 LRLLKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDPL 212

                         250       260       270
                  ....*....|....*....|....*....|...
gi 374532800  446 LVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKP 478
Cdd:pfam00561 213 VPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 1-161 1.95e-49

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: 168.29  E-value: 1.95e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800   1 MKGEITLSQwiplMEENCRKCSETAkvclpknfSIKEIFDKAISAR-KINRPMLQAALMLRKKGFTTAILTNTWLDDRae 79
Cdd:cd02603   49 ERGRITEEE----FWEELREELGRP--------LSAELFEELVLAAvDPNPEMLDLLEALRAKGYKVYLLSNTWPDHF-- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  80 rdgLAQLMCELKM--HFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTAL 157
Cdd:cd02603  115 ---KFQLELLPRRgdLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDAL 191


                 ....
gi 374532800 158 KELE 161
Cdd:cd02603  192 RELA 195
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 184-491 6.12e-43

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: 151.69  E-value: 6.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 184 MSHGYVTVKPrVRLHFVELG-SGPAVCLCHGFPESWYSWRYQIPALAqAGYRVLAMDMKGYGESSAPPEieEYCMEVLCK 262
Cdd:COG0596    2 STPRFVTVDG-VRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAG--GYTLDDLAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 263 EMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNtpfipanpnmsplesikanpvfdyqlyfqepgvaea 342
Cdd:COG0596   78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------ 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 343 eleqnlsrtfkslfrasdesvlsmhkvceagglfvnspeepslsrmvteEEIQFYVQQFKKSGfRGPLNWYRNMERNWKW 422
Cdd:COG0596  122 -------------------------------------------------EVLAALAEPLRRPG-LAPEALAALLRALART 151

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374532800 423 ACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDS 491
Cdd:COG0596  152 DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
HAD-1A3-hyp TIGR02247
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
 2-166 4.44e-34

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: 127.63  E-value: 4.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800    2 KGEITLSQWIPLMEencRKCSETAKvclpKNFSIKEIFDKAISARKINRPMLQAAL-MLRKKGFTTAILTNTWLDDRAEr 80
Cdd:TIGR02247  55 RGELTAEAFDGLFR---HEYGLRLG----HDVRIAPVFPLLYGENTKLRPSMMAAIkTLRAKGFKTACITNNFPTDHSA- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800   81 dGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKEL 160
Cdd:TIGR02247 127 -EEALLPGDIMALFDAVVESCLEGLRKPDPRIYQLMLERLGVAPEECVFLDDLGSNLKPAAALGITTIKVSDEEQAIHDL 205


                  ....*.
gi 374532800  161 EKVTGI 166
Cdd:TIGR02247 206 EKATKL 211
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 188-498 1.24e-28

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 115.09  E-value: 1.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 188 YVTVKPRvRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGyRVLAMDMKGYGESSAPPEieEYCMEVLCKEMVTF 267
Cdd:PRK03592  11 RVEVLGS-RMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDI--DYTFADHARYLDAW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 268 LDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLEsikANPVFdyQLyFQEPGVAEAE-LEQ 346
Cdd:PRK03592  87 FDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPA---VRELF--QA-LRSPGEGEEMvLEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 347 NlsrtfkslfrasdesvlsmhkvceaggLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGP-LNWYRNM--------- 416
Cdd:PRK03592 161 N---------------------------VFIERVLPGSILRPLSDEEMAVYRRPFPTPESRRPtLSWPRELpidgepadv 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 417 ----ERNWKWACKSlgrkiLIPALMVTAEKDFVLV-PQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDS 491
Cdd:PRK03592 214 valvEEYAQWLATS-----DVPKLLINAEPGAILTtGAIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAAWLRR 288


                 ....*..
gi 374532800 492 DARNPPV 498
Cdd:PRK03592 289 LRLAVSA 295
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 50-154 2.35e-21

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: 92.40  E-value: 2.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  50 RPMLQAalmLRKKGFTTAILTNT---WLDDRAERDGLAQlmcelkmHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSE 126
Cdd:COG1011   99 LELLEA---LKARGYRLALLTNGsaeLQEAKLRRLGLDD-------LFDAVVSSEEVGVRKPDPEIFELALERLGVPPEE 168

                         90       100
                 ....*....|....*....|....*....
gi 374532800 127 VVFLDDIG-ANLKPARDLGMVTILVQDTD 154
Cdd:COG1011  169 ALFVGDSPeTDVAGARAAGMRTVWVNRSG 197
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 199-490 6.31e-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: 72.03  E-value: 6.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  199 FVELGSGPAVCLCHGFP----ESWYSWRYQipaLAQAGYRVLAMDMKGYGESSAPPEIEE--YCMEVLCKEMVTFLDKLG 272
Cdd:TIGR01250  19 TGGEGEKIKLLLLHGGPgmshEYLENLREL---LKEEGREVIMYDQLGCGYSDQPDDSDEelWTIDYFVDELEEVREKLG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  273 LSQAVFIGHDWGGMLVWYMALFYPERVRAVaslntpfIPANPNMS-PLESIKANPVFDYqlyfQEPGVAEAELEQNLSRT 351
Cdd:TIGR01250  96 LDKFYLLGHSWGGMLAQEYALKYGQHLKGL-------IISSMLDSaPEYVKELNRLRKE----LPPEVRAAIKRCEASGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  352 FKSLFRASDESVLSMHKVCeagglfVNSPEEPSLSRMVTEEEIQFYvqqfkkSGFRGPlNWYRNMERNWKWACKSLGRKI 431
Cdd:TIGR01250 165 YDNPEYQEAVEVFYHHLLC------RLRKWPEALKHLKSGGNTNVY------NIMQGP-NEFTITGNLKDWDITDKLSEI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 374532800  432 LIPALMVTAEKDFVlVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLD 490
Cdd:TIGR01250 232 KVPTLLTVGEFDTM-TPEAAREMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFIR 289
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 1-144 4.09e-13

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: 68.00  E-value: 4.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800    1 MKGEITLSQWIPLMEENCRKCSETAKVClpknFSIKEIFDKAISARKINRPMLQAAL-MLRKKGFTTAILTNtwlDDRAE 79
Cdd:pfam00702  55 LLGKRDWLEELDILRGLVETLEAEGLTV----VLVELLGVIALADELKLYPGAAEALkALKERGIKVAILTG---DNPEA 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374532800   80 RDGLAQLmCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLG 144
Cdd:pfam00702 128 AEALLRL-LGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 59-155 1.88e-12

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 66.22  E-value: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  59 LRKKGFTTAILTNTwldDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLK 138
Cdd:PRK09456  96 LREQGHRVVVLSNT---NRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNADNIE 172

                         90
                 ....*....|....*..
gi 374532800 139 PARDLGMVTILVQDTDT 155
Cdd:PRK09456 173 AANALGITSILVTDKQT 189
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 206-478 1.39e-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: 1.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  206 PAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGG 285
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  286 MLVWYMALFYPERVRAVASLNTPfipanpnMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDesvLS 365
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGAL-------DPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLL---LR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  366 MHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRnmernwkwackslgrkilIPALMVTAEKDFV 445
Cdd:pfam00561 151 LRLLKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDPL 212

                         250       260       270
                  ....*....|....*....|....*....|...
gi 374532800  446 LVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKP 478
Cdd:pfam00561 213 VPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 1-161 1.95e-49

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: 168.29  E-value: 1.95e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800   1 MKGEITLSQwiplMEENCRKCSETAkvclpknfSIKEIFDKAISAR-KINRPMLQAALMLRKKGFTTAILTNTWLDDRae 79
Cdd:cd02603   49 ERGRITEEE----FWEELREELGRP--------LSAELFEELVLAAvDPNPEMLDLLEALRAKGYKVYLLSNTWPDHF-- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  80 rdgLAQLMCELKM--HFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTAL 157
Cdd:cd02603  115 ---KFQLELLPRRgdLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDAL 191


                 ....
gi 374532800 158 KELE 161
Cdd:cd02603  192 RELA 195
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 184-491 6.12e-43

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: 151.69  E-value: 6.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 184 MSHGYVTVKPrVRLHFVELG-SGPAVCLCHGFPESWYSWRYQIPALAqAGYRVLAMDMKGYGESSAPPEieEYCMEVLCK 262
Cdd:COG0596    2 STPRFVTVDG-VRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAG--GYTLDDLAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 263 EMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNtpfipanpnmsplesikanpvfdyqlyfqepgvaea 342
Cdd:COG0596   78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------ 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 343 eleqnlsrtfkslfrasdesvlsmhkvceagglfvnspeepslsrmvteEEIQFYVQQFKKSGfRGPLNWYRNMERNWKW 422
Cdd:COG0596  122 -------------------------------------------------EVLAALAEPLRRPG-LAPEALAALLRALART 151

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374532800 423 ACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDS 491
Cdd:COG0596  152 DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
HAD-1A3-hyp TIGR02247
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
 2-166 4.44e-34

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: 127.63  E-value: 4.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800    2 KGEITLSQWIPLMEencRKCSETAKvclpKNFSIKEIFDKAISARKINRPMLQAAL-MLRKKGFTTAILTNTWLDDRAEr 80
Cdd:TIGR02247  55 RGELTAEAFDGLFR---HEYGLRLG----HDVRIAPVFPLLYGENTKLRPSMMAAIkTLRAKGFKTACITNNFPTDHSA- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800   81 dGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKEL 160
Cdd:TIGR02247 127 -EEALLPGDIMALFDAVVESCLEGLRKPDPRIYQLMLERLGVAPEECVFLDDLGSNLKPAAALGITTIKVSDEEQAIHDL 205


                  ....*.
gi 374532800  161 EKVTGI 166
Cdd:TIGR02247 206 EKATKL 211
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 188-498 1.24e-28

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 115.09  E-value: 1.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 188 YVTVKPRvRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGyRVLAMDMKGYGESSAPPEieEYCMEVLCKEMVTF 267
Cdd:PRK03592  11 RVEVLGS-RMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDI--DYTFADHARYLDAW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 268 LDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLEsikANPVFdyQLyFQEPGVAEAE-LEQ 346
Cdd:PRK03592  87 FDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPA---VRELF--QA-LRSPGEGEEMvLEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 347 NlsrtfkslfrasdesvlsmhkvceaggLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGP-LNWYRNM--------- 416
Cdd:PRK03592 161 N---------------------------VFIERVLPGSILRPLSDEEMAVYRRPFPTPESRRPtLSWPRELpidgepadv 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 417 ----ERNWKWACKSlgrkiLIPALMVTAEKDFVLV-PQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDS 491
Cdd:PRK03592 214 valvEEYAQWLATS-----DVPKLLINAEPGAILTtGAIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAAWLRR 288


                 ....*..
gi 374532800 492 DARNPPV 498
Cdd:PRK03592 289 LRLAVSA 295
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 28-150 2.54e-28

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: 110.59  E-value: 2.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800   28 CLPKNFSIKEIFDKAISarKINRPMLQAALMLRKKGFTTAILTNTWLDDRaerdgLAQLMCELKMHFDFLIESCQVGMVK 107
Cdd:TIGR01509  63 LLYKQLFYEQIEEEAKL--KPLPGVRALLEALRARGKKLALLTNSPRAHK-----LVLALLGLRDLFDVVIDSSDVGLGK 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 374532800  108 PEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILV 150
Cdd:TIGR01509 136 PDPDIYLQALKALGLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 188-312 1.36e-21

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 95.03  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 188 YVTVKP----RVRLHFVELGS--GPAVCLCHGFPeSW-YSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVL 260
Cdd:PRK00870  23 YVDVDDgdggPLRMHYVDEGPadGPPVLLLHGEP-SWsYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPTRREDYTYARH 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 374532800 261 CKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTpFIPA 312
Cdd:PRK00870 102 VEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANT-GLPT 152
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 50-154 2.35e-21

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: 92.40  E-value: 2.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  50 RPMLQAalmLRKKGFTTAILTNT---WLDDRAERDGLAQlmcelkmHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSE 126
Cdd:COG1011   99 LELLEA---LKARGYRLALLTNGsaeLQEAKLRRLGLDD-------LFDAVVSSEEVGVRKPDPEIFELALERLGVPPEE 168

                         90       100
                 ....*....|....*....|....*....
gi 374532800 127 VVFLDDIG-ANLKPARDLGMVTILVQDTD 154
Cdd:COG1011  169 ALFVGDSPeTDVAGARAAGMRTVWVNRSG 197
PLN02578 PLN02578
hydrolase
 196-322 2.19e-17

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 83.35  E-value: 2.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 196 RLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAgYRVLAMDMKGYGESSAPpeIEEYCMEVLCKEMVTFLDKLGLSQ 275
Cdd:PLN02578  77 KIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKK-YKVYALDLLGFGWSDKA--LIEYDAMVWRDQVADFVKEVVKEP 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 374532800 276 AVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESI 322
Cdd:PLN02578 154 AVLVGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESREKEEAI 200
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
184-314 4.08e-17

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 80.05  E-value: 4.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 184 MSH--GYVTVKPRVRLHFVEL----GSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAP----PEIE 253
Cdd:COG2267    1 MTRrlVTLPTRDGLRLRGRRWrpagSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPrghvDSFD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374532800 254 EYCMEVlcKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVAsLNTPFIPANP 314
Cdd:COG2267   81 DYVDDL--RAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLV-LLAPAYRADP 138
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 194-313 9.88e-15

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 74.51  E-value: 9.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 194 RVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALaQAGYRVLAMDMKGYGESSAPPEIEeYCMEVLCKEMVTFLDKLGL 273
Cdd:PRK03204  23 RGRIHYIDEGTGPPILLCHGNPTWSFLYRDIIVAL-RDRFRCVAPDYLGFGLSERPSGFG-YQIDEHARVIGEFVDHLGL 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 374532800 274 SQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPAN 313
Cdd:PRK03204 101 DRYLSMGQDWGGPISMAVAVERADRVRGVVLGNTWFWPAD 140
PRK05855 PRK05855
SDR family oxidoreductase;
195-478 1.03e-14

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 76.56  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 195 VRLHFVELG--SGPAVCLCHGFPESWYSWRYQIPALAqAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLG 272
Cdd:PRK05855  13 VRLAVYEWGdpDRPTVVLVHGYPDNHEVWDGVAPLLA-DRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 273 LSQAV-FIGHDWGGMLVWYmALFYPERVRAVASLNTpfipanpnMSplesikaNPVFDYQLYFQEPGVAeAELEQNLSRT 351
Cdd:PRK05855  92 PDRPVhLLAHDWGSIQGWE-AVTRPRAAGRIASFTS--------VS-------GPSLDHVGFWLRSGLR-RPTPRRLARA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 352 FKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVteEEI---QFYVQQFKKSGFRGpLNWYR-NMERnwkwackSL 427
Cdd:PRK05855 155 LGQLLRSWYIYLFHLPVLPELLWRLGLGRAWPRLLRRV--EGTpvdPIPTQTTLSDGAHG-VKLYRaNMIR-------SL 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 374532800 428 GRK----ILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIeDCGHWTQMDKP 478
Cdd:PRK05855 225 SRPreryTDVPVQLIVPTGDPYVRPALYDDLSRWVPRLWRREI-KAGHWLPMSHP 278
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
206-305 1.70e-14

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 72.74  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 206 PAVCLCHGFPES-WYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEY--CMEVLcKEMVT--FLD--KLGLsqavf 278
Cdd:COG1506   24 PVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVddVLAAI-DYLAArpYVDpdRIGI----- 97

                         90       100
                 ....*....|....*....|....*..
gi 374532800 279 IGHDWGGMLVWYMALFYPERVRAVASL 305
Cdd:COG1506   98 YGHSYGGYMALLAAARHPDRFKAAVAL 124
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 199-490 6.31e-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: 72.03  E-value: 6.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  199 FVELGSGPAVCLCHGFP----ESWYSWRYQipaLAQAGYRVLAMDMKGYGESSAPPEIEE--YCMEVLCKEMVTFLDKLG 272
Cdd:TIGR01250  19 TGGEGEKIKLLLLHGGPgmshEYLENLREL---LKEEGREVIMYDQLGCGYSDQPDDSDEelWTIDYFVDELEEVREKLG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  273 LSQAVFIGHDWGGMLVWYMALFYPERVRAVaslntpfIPANPNMS-PLESIKANPVFDYqlyfQEPGVAEAELEQNLSRT 351
Cdd:TIGR01250  96 LDKFYLLGHSWGGMLAQEYALKYGQHLKGL-------IISSMLDSaPEYVKELNRLRKE----LPPEVRAAIKRCEASGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  352 FKSLFRASDESVLSMHKVCeagglfVNSPEEPSLSRMVTEEEIQFYvqqfkkSGFRGPlNWYRNMERNWKWACKSLGRKI 431
Cdd:TIGR01250 165 YDNPEYQEAVEVFYHHLLC------RLRKWPEALKHLKSGGNTNVY------NIMQGP-NEFTITGNLKDWDITDKLSEI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 374532800  432 LIPALMVTAEKDFVlVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLD 490
Cdd:TIGR01250 232 KVPTLLTVGEFDTM-TPEAAREMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFIR 289
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 1-144 4.09e-13

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: 68.00  E-value: 4.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800    1 MKGEITLSQWIPLMEENCRKCSETAKVClpknFSIKEIFDKAISARKINRPMLQAAL-MLRKKGFTTAILTNtwlDDRAE 79
Cdd:pfam00702  55 LLGKRDWLEELDILRGLVETLEAEGLTV----VLVELLGVIALADELKLYPGAAEALkALKERGIKVAILTG---DNPEA 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374532800   80 RDGLAQLmCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLG 144
Cdd:pfam00702 128 AEALLRL-LGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 196-485 4.10e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 70.74  E-value: 4.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 196 RLHFVELG--SGPAVCLCHGFPESWYSWRYQIPALAqAGYRVLAMDMKGYGESSapPEIEEYCMEVLCKEMVTFLDKLGL 273
Cdd:PRK14875 120 TVRYLRLGegDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASS--KAVGAGSLDELAAAVLAFLDALGI 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 274 SQAVFIGHDWGGMLVWYMALFYPERVRAVASL---------NTPFI------PANPNMSP-LESIKANP-------VFDY 330
Cdd:PRK14875 197 ERAHLVGHSMGGAVALRLAARAPQRVASLTLIapaglgpeiNGDYIdgfvaaESRRELKPvLELLFADPalvtrqmVEDL 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 331 QLYFQEPGVAEAeleqnLSRTFKSLFRASdesvlsmhkvceagglfvnspeepslsrmvteeeiqfyVQQFkksGFRGPL 410
Cdd:PRK14875 277 LKYKRLDGVDDA-----LRALADALFAGG--------------------------------------RQRV---DLRDRL 310

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374532800 411 nwyrnmernwkwacKSLGrkilIPALMVTAEKDFVLVPQMSQHMEDWIP-HLkrghIEDCGHWTQMDKPTEVNQIL 485
Cdd:PRK14875 311 --------------ASLA----IPVLVIWGEQDRIIPAAHAQGLPDGVAvHV----LPGAGHMPQMEAAADVNRLL 364
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 59-155 1.88e-12

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 66.22  E-value: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  59 LRKKGFTTAILTNTwldDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLK 138
Cdd:PRK09456  96 LREQGHRVVVLSNT---NRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNADNIE 172

                         90
                 ....*....|....*..
gi 374532800 139 PARDLGMVTILVQDTDT 155
Cdd:PRK09456 173 AANALGITSILVTDKQT 189
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 203-306 1.95e-11

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 64.76  E-value: 1.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 203 GSGPAVCLCHGFPESWYSWRYQIPALAQAGyRVLAMDMKGYGESSAP-----PEIEEYCMEVLCKEMVTFLDKLGLSQAV 277
Cdd:PLN02824  27 TSGPALVLVHGFGGNADHWRKNTPVLAKSH-RVYAIDLLGYGYSDKPnprsaPPNSFYTFETWGEQLNDFCSDVVGDPAF 105

                         90       100
                 ....*....|....*....|....*....
gi 374532800 278 FIGHDWGGMLVWYMALFYPERVRAVASLN 306
Cdd:PLN02824 106 VICNSVGGVVGLQAAVDAPELVRGVMLIN 134
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 207-319 5.52e-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: 5.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  207 AVCLCHGFPEswYSWRYQ--IPALAQAGYRVLAMDMKGYGESSAP----PEIEEYCMEVlcKEMVTFLDKLGLSQAVFI- 279
Cdd:pfam12146   6 VVVLVHGLGE--HSGRYAhlADALAAQGFAVYAYDHRGHGRSDGKrghvPSFDDYVDDL--DTFVDKIREEHPGLPLFLl 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 374532800  280 GHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPL 319
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPI 121
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 210-309 4.20e-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: 4.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 210 LCHGFPESWYSWRYQIPALAQAGYRVLAMDmkgYGESSAPpeieeycMEVLCKEMVTFLDKL----GLSQAVFIGHDWGG 285
Cdd:COG1075   10 LVHGLGGSAASWAPLAPRLRAAGYPVYALN---YPSTNGS-------IEDSAEQLAAFVDAVlaatGAEKVDLVGHSMGG 79

                         90       100
                 ....*....|....*....|....*.
gi 374532800 286 MLVWYMA--LFYPERVRAVASLNTPF 309
Cdd:COG1075   80 LVARYYLkrLGGAAKVARVVTLGTPH 105
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 48-150 5.38e-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: 5.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  48 INRPMLQAalmLRKKGFTTAILTNT---WLDDRAERDGLAQlmcelkmHFDFLIESCQVGMVKPEPQIYKFLLDTLKASP 124
Cdd:cd01427   11 LAVELLKR---LRAAGIKLAIVTNRsreALRALLEKLGLGD-------LFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDP 80

                         90       100
                 ....*....|....*....|....*.
gi 374532800 125 SEVVFLDDIGANLKPARDLGMVTILV 150
Cdd:cd01427   81 EEVLFVGDSENDIEAARAAGGRTVAV 106
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 48-170 1.16e-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: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  48 INRPMLQAalmLRKKGFTTAILTNTwldDRAERDGLAQlmCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEV 127
Cdd:cd16415   11 LAVETLKD---LKEKGLKLAVVSNF---DRRLRELLEA--LGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 374532800 128 VFL-DDIGANLKPARDLGMVTILVqDTDTALKELEKVTGIQLLN 170
Cdd:cd16415   83 LHVgDDLKNDYLGARAVGWHALLV-DREGALHELPSLANLLERL 125
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 187-286 3.80e-09

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 58.31  E-value: 3.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 187 GYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAgYRVLAMDMKGYGESSAPPEIeEYCMEVLCKEMVT 266
Cdd:PLN02679  70 GEYSINYLVKGSPEVTSSGPPVLLVHGFGASIPHWRRNIGVLAKN-YTVYAIDLLGFGASDKPPGF-SYTMETWAELILD 147

                         90       100
                 ....*....|....*....|
gi 374532800 267 FLDKLGLSQAVFIGHDWGGM 286
Cdd:PLN02679 148 FLEEVVQKPTVLIGNSVGSL 167
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 210-320 5.59e-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: 56.33  E-value: 5.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  210 LCHGFpesWYSWRyQIPALAQAGYRVLAMDMKGYGESSAPP-EIEEYcmevlcKEMVTFLDKLG-LSQAVFIGHDWGGML 287
Cdd:pfam12697   3 LVHGA---GLSAA-PLAALLAAGVAVLAPDLPGHGSSSPPPlDLADL------ADLAALLDELGaARPVVLVGHSLGGAV 72

                          90       100       110
                  ....*....|....*....|....*....|...
gi 374532800  288 VWYMALFYPERVRAVASLNTPFIPANPNMSPLE 320
Cdd:pfam12697  73 ALAAAAAALVVGVLVAPLAAPPGLLAALLALLA 105
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
199-361 9.19e-09

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 56.10  E-value: 9.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 199 FVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESsaPPEIEEYCMEVLCKEMVTFLDKL-GLSQAV 277
Cdd:COG1647    9 FFLEGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTS--PEDLLKTTWEDWLEDVEEAYEILkAGYDKV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 278 F-IGHDWGGMLVWYMALFYPErVRAVASLNTPFIPANPNMS--PLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKS 354
Cdd:COG1647   87 IvIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPllPLLKYLARSLRGIGSDIEDPEVAEYAYDRTPLRALAE 165


                 ....*..
gi 374532800 355 LFRASDE 361
Cdd:COG1647  166 LQRLIRE 172
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 50-150 1.18e-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: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  50 RPMLQAalmLRKKGFTTAILTN---TWLDDRAERDGLAQLmcelkmhFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSE 126
Cdd:cd02588   97 VAGLRR---LREAGYRLAILSNgspDLIEDVVANAGLRDL-------FDAVLSAEDVRAYKPAPAVYELAAERLGVPPDE 166

                         90       100
                 ....*....|....*....|....*..
gi 374532800 127 VVFlddIGAN---LKPARDLGMVTILV 150
Cdd:cd02588  167 ILH---VASHawdLAGARALGLRTAWI 190
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
203-327 1.98e-07

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 51.89  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 203 GSGPAVCLCHGfpesWYSWRYQIPA----LAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVT--------FL-- 268
Cdd:COG0412   27 GPRPGVVVLHE----IFGLNPHIRDvarrLAAAGYVVLAPDLYGRGGPGDDPDEARALMGALDPELLAadlraaldWLka 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374532800 269 ------DKLGLsqavfIGHDWGGMLVWYMALFYPeRVRAVASLNtPFIPANPNMSPLESIKAnPV 327
Cdd:COG0412  103 qpevdaGRVGV-----VGFCFGGGLALLAAARGP-DLAAAVSFY-GGLPADDLLDLAARIKA-PV 159
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
50-150 3.98e-07

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 50.70  E-value: 3.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  50 RPMLQAalmLRKKGFTTAILTNtwlddrAERDGLAQLMCELKM--HFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEV 127
Cdd:COG0546   90 RELLEA---LKARGIKLAVVTN------KPREFAERLLEALGLddYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEV 160

                         90       100
                 ....*....|....*....|....*..
gi 374532800 128 VF----LDDIGAnlkpARDLGMVTILV 150
Cdd:COG0546  161 LMvgdsPHDIEA----ARAAGVPFIGV 183
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 196-365 1.31e-06

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 50.65  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 196 RLHFVELGS--GPAVCLCHGFPESWYSWRYQIPALAQaGYRVLAMDMKGYGESSAPP-------EIEEY--CMEVLCKEM 264
Cdd:PLN03084 116 RWFCVESGSnnNPPVLLIHGFPSQAYSYRKVLPVLSK-NYHAIAFDWLGFGFSDKPQpgygfnyTLDEYvsSLESLIDEL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 265 VTflDKLGLsqaVFIGHdWGGMLVWYmALFYPERVRAVASLNTPFIPANPNMSPLESIKANpVFDYQLYFQEPgvaeael 344
Cdd:PLN03084 195 KS--DKVSL---VVQGY-FSPPVVKY-ASAHPDKIKKLILLNPPLTKEHAKLPSTLSEFSN-FLLGEIFSQDP------- 259

                        170       180
                 ....*....|....*....|.
gi 374532800 345 eqnlsrtfkslFRASDESVLS 365
Cdd:PLN03084 260 -----------LRASDKALTS 269
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
35-163 1.30e-05

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 45.97  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  35 IKEIFDKAISARKIN-RPMLQAAL-MLRKKGFTTAILTNT---WLDDRAERDGLAQlmcelkmHFDFLIESCQVGMVKPE 109
Cdd:COG0637   72 KEELYRELLAEEGLPlIPGVVELLeALKEAGIKIAVATSSpreNAEAVLEAAGLLD-------YFDVIVTGDDVARGKPD 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 374532800 110 PQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKV 163
Cdd:COG0637  145 PDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGA 198
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
59-150 1.78e-05

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 45.27  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800   59 LRKKGFTTAILTNTwldDRAE-RDGLAQLmcELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANL 137
Cdd:pfam13419  91 LKEQGYKLGIVTSK---SRENvEEFLKQL--GLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDSPRDI 165

                          90
                  ....*....|...
gi 374532800  138 KPARDLGMVTILV 150
Cdd:pfam13419 166 EAAKNAGIKVIAV 178
PRK10673 PRK10673
esterase;
230-492 2.39e-05

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 45.88  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 230 QAGYRVLAMDMKGYGESSAPPEIEEYCMevlCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERV-RAVAslntp 308
Cdd:PRK10673  40 VNDHDIIQVDMRNHGLSPRDPVMNYPAM---AQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIdKLVA----- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 309 fipanpnmsplesIKANPVfDYQLyfqepgvaeaeleqnlsrtfkslfRASDESVLSMHKVCEAGglfVNSPEEPS-LSR 387
Cdd:PRK10673 112 -------------IDIAPV-DYHV------------------------RRHDEIFAAINAVSEAG---ATTRQQAAaIMR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 388 MVTEEE--IQFYVQQFKKSgfrgplNWYRNMERNWKWACKSLGRKILI----PALMVTAEkdfvLVPQMSQHMEDWI--- 458
Cdd:PRK10673 151 QHLNEEgvIQFLLKSFVDG------EWRFNVPVLWDQYPHIVGWEKIPawphPALFIRGG----NSPYVTEAYRDDLlaq 220

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 374532800 459 -PHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSD 492
Cdd:PRK10673 221 fPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLNDK 255
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 58-150 3.25e-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: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800   58 MLRKKGFTTAILTN-----TWLDDRAERDGLAQLMCELKMHFDFLIeSCQvGMVKPEPQIYKFLLDTL-KASPSEVVFL- 130
Cdd:TIGR01662  36 ELKEAGYKVVIVTNqsgigRGYFSRSFSGRVARRLEELGVPIDILY-ACP-GCRKPKPGMFLEALKRFnEIDPEESVYVg 113

                          90       100
                  ....*....|....*....|
gi 374532800  131 DDIGANLKPARDLGMVTILV 150
Cdd:TIGR01662 114 DQDLTDLQAAKRVGLATILV 133
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 50-150 4.74e-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: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  50 RPMLQAalmLRKKGFTTAILTNTwLDDRAERdGLAqlMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVF 129
Cdd:cd02616   86 YETLAR---LKSQGIKLGVVTTK-LRETALK-GLK--LLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEEALM 158

                         90       100
                 ....*....|....*....|.
gi 374532800 130 LDDIGANLKPARDLGMVTILV 150
Cdd:cd02616  159 VGDSPHDILAGKNAGVKTVGV 179
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 206-300 6.03e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 45.29  E-value: 6.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 206 PAVCLCHGFPESWYSWRYQIPALAqAGYRVLAMDMKGYGESSAPP-------EIEEYcmevlckemvtFLDKL------- 271
Cdd:PLN02894 106 PTLVMVHGYGASQGFFFRNFDALA-SRFRVIAIDQLGWGGSSRPDftcksteETEAW-----------FIDSFeewrkak 173

                         90       100
                 ....*....|....*....|....*....
gi 374532800 272 GLSQAVFIGHDWGGMLVWYMALFYPERVR 300
Cdd:PLN02894 174 NLSNFILLGHSFGGYVAAKYALKHPEHVQ 202
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 203-309 7.61e-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: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800 203 GSGPAVCLCHGFPES-WYSWRYqIPALAQAGYRVLAMDMKGYGESS------APPEIEEYcmevlcKEMVTFLDKLGL-- 273
Cdd:COG1073   35 KKYPAVVVAHGNGGVkEQRALY-AQRLAELGFNVLAFDYRGYGESEgepreeGSPERRDA------RAAVDYLRTLPGvd 107

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 374532800 274 -SQAVFIGHDWGGMLVWYMALFYPeRVRAVASLnTPF 309
Cdd:COG1073  108 pERIGLLGISLGGGYALNAAATDP-RVKAVILD-SPF 142
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 61-148 1.45e-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: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  61 KKGFTTAILTNtwlddraerdGLAQLM------CELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFL-DDI 133
Cdd:cd04305   22 KKGYKLGIITN----------GPTEVQwekleqLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVgDSL 91

                         90
                 ....*....|....*
gi 374532800 134 GANLKPARDLGMVTI 148
Cdd:cd04305   92 ESDILGAKNAGIKTV 106
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 51-150 3.03e-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: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  51 PMLQAalmLRKKGFTTAILTNTWldDRAERdglaqlMCE---LKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEV 127
Cdd:cd16421   14 ELLKA---LRQKGIKLAVLSNKP--NEAVQ------VLVeelFPGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEV 82

                         90       100
                 ....*....|....*....|...
gi 374532800 128 VFLDDIGANLKPARDLGMVTILV 150
Cdd:cd16421   83 LYVGDSGVDMQTARNAGMDEIGV 105
PHA_depoly_arom TIGR02240
poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid ...
 235-494 3.20e-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: 42.68  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  235 VLAMDMKGYGESSAPPEieEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPER----VRAVASLNTPFI 310
Cdd:TIGR02240  54 VIAFDVPGVGGSSTPRH--PYRFPGLAKLAARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERckklILAATAAGAVMV 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  311 PANPNMSpleSIKANPvfdyQLYFQEPGVAeaeleqnlsRTFKSLFrasdesvlsmhkvceaGGLFVNSPEepslsrmvt 390
Cdd:TIGR02240 132 PGKPKVL---MMMASP----RRYIQPSHGI---------HIAPDIY----------------GGAFRRDPE--------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  391 eeeiqFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDfVLVPQMSQHMEDW-IPHLKRgHIEDC 469
Cdd:TIGR02240 171 -----LAMAHASKVRSGGKLGYYWQLFAGLGWTSIHWLHKIQQPTLVLAGDDD-PIIPLINMRLLAWrIPNAEL-HIIDD 243

                         250       260
                  ....*....|....*....|....*
gi 374532800  470 GHWTQMDKPTEVNQILIKWLDSDAR 494
Cdd:TIGR02240 244 GHLFLITRAEAVAPIIMKFLAEERQ 268
Hydrolase_like pfam13242
HAD-hyrolase-like;
107-150 3.38e-04

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 39.14  E-value: 3.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 374532800  107 KPEPQIYKFLLDTLKASPSEVVF-----LDDIGAnlkpARDLGMVTILV 150
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMigdrlDTDILG----AREAGARTILV 48
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 50-150 1.10e-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: 39.52  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  50 RPMLQAALM-LRKKGFTTAILTNTWLDDRAERDGLAQLmceLKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVV 128
Cdd:cd07505   43 KPGVVELLDaLKAAGIPVAVATSSSRRNVELLLLELGL---LRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCL 119

                         90       100
                 ....*....|....*....|..
gi 374532800 129 FLDDIGANLKPARDLGMVTILV 150
Cdd:cd07505  120 VFEDSLAGIEAAKAAGMTVVAV 141
HAD_EP cd01629
Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. ...
 107-150 1.11e-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: 1.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 374532800 107 KPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILV 150
Cdd:cd01629  157 KREAASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLL 200
homoserO_Ac_trn TIGR01392
homoserine O-acetyltransferase; This family describes homoserine-O-acetyltransferase, an ...
 267-308 3.29e-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: 3.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 374532800  267 FLDKLGLSQ-AVFIGHDWGGMLVWYMALFYPERVRAVASLNTP 308
Cdd:TIGR01392 119 LLDHLGIEQiAAVVGGSMGGMQALEWAIDYPERVRAIVVLATS 161
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 66-149 4.68e-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: 4.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532800  66 TAILTNTWLDDRAERdglaqlmcelkmhFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGM 145
Cdd:cd07528  126 DALLSALLGPERRAI-------------FDAIAAGDDVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGL 192


                 ....
gi 374532800 146 VTIL 149
Cdd:cd07528  193 PCIV 196
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 107-150 5.00e-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: 5.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 374532800 107 KPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILV 150
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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