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Conserved domains on  [gi|2462591573|ref|XP_054203345|]
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monoacylglycerol lipase ABHD6 isoform X1 [Homo sapiens]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 51-328 1.76e-39

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: 138.98  E-value: 1.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  51 RYVHHEDYQFCYSFRGRPGhkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596     5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 131 FVEclKLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVcpaglqystdNQFVQRLKElqgsaavekiplipstpeem 210
Cdd:COG0596    82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 211 semlqlcsyvrfkvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDqQVLDVSGADML 290
Cdd:COG0596   130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKD-PIVPPALARRL 183

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2462591573 291 AKSIANCQVELLENCGHSVVMERPRKTAKLIIDFLASV 328
Cdd:COG0596   184 AELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 51-328 1.76e-39

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: 138.98  E-value: 1.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  51 RYVHHEDYQFCYSFRGRPGhkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596     5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 131 FVEclKLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVcpaglqystdNQFVQRLKElqgsaavekiplipstpeem 210
Cdd:COG0596    82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 211 semlqlcsyvrfkvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDqQVLDVSGADML 290
Cdd:COG0596   130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKD-PIVPPALARRL 183

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2462591573 291 AKSIANCQVELLENCGHSVVMERPRKTAKLIIDFLASV 328
Cdd:COG0596   184 AELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-314 1.23e-27

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: 108.36  E-value: 1.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  72 PSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH-EGTTRSSLDDLSIDGQVKRIHQFVEclKLNKKPFHLVGTSM 149
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFgKSSRPKAQDDYRTDDLAEDLEYILE--ALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 150 GGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGS-----AAVEKIPLIPSTPEEMSEmLQLCSYVRFKV 224
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLAL-LLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 225 PQQILQGLVDVRIPHNN--FYRKLFLEIVSEKSRYSLHQNmdkIKVPTQIIWGKQDqQVLDVSGADMLAKSIANCQVELL 302
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSlvTGALLFIETWSTELRAKFLGR---LDEPTLIIWGDQD-PLVPPQALEKLAQLFPNARLVVI 233

                         250
                  ....*....|..
gi 2462591573 303 ENCGHSVVMERP 314
Cdd:pfam00561 234 PDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 62-328 2.68e-27

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 110.03  E-value: 2.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  62 YSFRGrPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKp 141
Cdd:PRK14875  123 YLRLG-EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERA- 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 142 fHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGSAAVEkiPLIpstpeemsEMLqlcsyvr 221
Cdd:PRK14875  200 -HLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEINGDYIDGFVAAESRRELK--PVL--------ELL------- 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 222 FKVPQQILQGLVD--VRiphnnfYRKL-----FLEIVSE------KSRYSLHQNMDKIKVPTQIIWGKQDqQVLDVSGAD 288
Cdd:PRK14875  262 FADPALVTRQMVEdlLK------YKRLdgvddALRALADalfaggRQRVDLRDRLASLAIPVLVIWGEQD-RIIPAAHAQ 334

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2462591573 289 MLAksiANCQVELLENCGHSVVMERPRKTAKLIIDFLASV 328
Cdd:PRK14875  335 GLP---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 71-325 2.51e-23

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 96.90  E-value: 2.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  71 KPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDL--SIDGQVKRI-HQFVEclKLNKKPFHLVGT 147
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGH-GSSQSPSDIEryDFEEAAQLLlATLLD--QLGIEPFFLVGY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 148 SMGGQVAGVYAAYYPSDVSSLCLV-CPAGLQ--------YSTDNQFVQRLkELQGSAAV----EKIPLIpSTPEEMseml 214
Cdd:TIGR03695  79 SMGGRIALYYALQYPERVQGLILEsGSPGLQteeeraarRQNDEQLAQRF-EQEGLEAFlddwYQQPLF-ASQKNL---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 215 qlcsyvrfkvPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQQVLDvsgadmLAKSI 294
Cdd:TIGR03695 153 ----------PPEQRQALRAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQ------IAKEM 216

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2462591573 295 ANCQV----ELLENCGHSVVMERPRKTAKLIIDFL 325
Cdd:TIGR03695 217 QKLIPnltlHIIPNAGHNIHLENPEAFAKILLAFL 251
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 51-328 1.76e-39

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: 138.98  E-value: 1.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  51 RYVHHEDYQFCYSFRGRPGhkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596     5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 131 FVEclKLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVcpaglqystdNQFVQRLKElqgsaavekiplipstpeem 210
Cdd:COG0596    82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 211 semlqlcsyvrfkvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDqQVLDVSGADML 290
Cdd:COG0596   130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKD-PIVPPALARRL 183

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2462591573 291 AKSIANCQVELLENCGHSVVMERPRKTAKLIIDFLASV 328
Cdd:COG0596   184 AELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-314 1.23e-27

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: 108.36  E-value: 1.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  72 PSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH-EGTTRSSLDDLSIDGQVKRIHQFVEclKLNKKPFHLVGTSM 149
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFgKSSRPKAQDDYRTDDLAEDLEYILE--ALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 150 GGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGS-----AAVEKIPLIPSTPEEMSEmLQLCSYVRFKV 224
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLAL-LLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 225 PQQILQGLVDVRIPHNN--FYRKLFLEIVSEKSRYSLHQNmdkIKVPTQIIWGKQDqQVLDVSGADMLAKSIANCQVELL 302
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSlvTGALLFIETWSTELRAKFLGR---LDEPTLIIWGDQD-PLVPPQALEKLAQLFPNARLVVI 233

                         250
                  ....*....|..
gi 2462591573 303 ENCGHSVVMERP 314
Cdd:pfam00561 234 PDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 62-328 2.68e-27

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 110.03  E-value: 2.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  62 YSFRGrPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKp 141
Cdd:PRK14875  123 YLRLG-EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERA- 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 142 fHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGSAAVEkiPLIpstpeemsEMLqlcsyvr 221
Cdd:PRK14875  200 -HLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEINGDYIDGFVAAESRRELK--PVL--------ELL------- 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 222 FKVPQQILQGLVD--VRiphnnfYRKL-----FLEIVSE------KSRYSLHQNMDKIKVPTQIIWGKQDqQVLDVSGAD 288
Cdd:PRK14875  262 FADPALVTRQMVEdlLK------YKRLdgvddALRALADalfaggRQRVDLRDRLASLAIPVLVIWGEQD-RIIPAAHAQ 334

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2462591573 289 MLAksiANCQVELLENCGHSVVMERPRKTAKLIIDFLASV 328
Cdd:PRK14875  335 GLP---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
60-327 6.93e-24

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 97.38  E-value: 6.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  60 FCYSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGHEGTTRSSLDDLSIDGQVKRIHQFVECLK-L 137
Cdd:COG2267    17 RGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRaR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 138 NKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAglqYSTDnqfvqrlkelqgsaavekiPLIPSTPEEMSEMLqlc 217
Cdd:COG2267    97 PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA---YRAD-------------------PLLGPSARWLRALR--- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 218 syvrfkvpqqilqglvdvriphnnfyrklfleivseksrysLHQNMDKIKVPTQIIWGKQDQQVlDVSGADMLAKSIA-N 296
Cdd:COG2267   152 -----------------------------------------LAEALARIDVPVLVLHGGADRVV-PPEAARRLAARLSpD 189

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2462591573 297 CQVELLENCGHSVVMERPRKTA-KLIIDFLAS 327
Cdd:COG2267   190 VELVLLPGARHELLNEPAREEVlAAILAWLER 221
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 71-325 2.51e-23

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 96.90  E-value: 2.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  71 KPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDL--SIDGQVKRI-HQFVEclKLNKKPFHLVGT 147
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGH-GSSQSPSDIEryDFEEAAQLLlATLLD--QLGIEPFFLVGY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 148 SMGGQVAGVYAAYYPSDVSSLCLV-CPAGLQ--------YSTDNQFVQRLkELQGSAAV----EKIPLIpSTPEEMseml 214
Cdd:TIGR03695  79 SMGGRIALYYALQYPERVQGLILEsGSPGLQteeeraarRQNDEQLAQRF-EQEGLEAFlddwYQQPLF-ASQKNL---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 215 qlcsyvrfkvPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQQVLDvsgadmLAKSI 294
Cdd:TIGR03695 153 ----------PPEQRQALRAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQ------IAKEM 216

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2462591573 295 ANCQV----ELLENCGHSVVMERPRKTAKLIIDFL 325
Cdd:TIGR03695 217 QKLIPnltlHIIPNAGHNIHLENPEAFAKILLAFL 251
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
68-330 1.00e-18

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 83.84  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  68 PGHKPSILMLHGFSAHKdmwlSVVKFLPKNLH-----LVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPF 142
Cdd:COG1647    12 EGGRKGVLLLHGFTGSP----AEMRPLAEALAkagytVYAPRLPGH-GTSPEDLLKTTWEDWLEDVEEAYEILKAGYDKV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 143 HLVGTSMGGQVAGVYAAYYPsDVSSLCLVCPAgLQYSTDNQFVQRLkelqGSAAVEKIPLIPSTPEEmsemLQLCSYVRF 222
Cdd:COG1647    87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPA-LKIDDPSAPLLPL----LKYLARSLRGIGSDIED----PEVAEYAYD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 223 KVPQQILQglvdvriphnNFYRklFLEIVSEksryslhqNMDKIKVPTQIIWGKQDQQVlDVSGADMLAKSIANCQVEL- 301
Cdd:COG1647   157 RTPLRALA----------ELQR--LIREVRR--------DLPKITAPTLIIQSRKDEVV-PPESARYIYERLGSPDKELv 215

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2462591573 302 -LENCGHSVVMERPRKT-AKLIIDFLASVHN 330
Cdd:COG1647   216 wLEDSGHVITLDKDREEvAEEILDFLERLAA 246
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 74-320 1.52e-11

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 62.88  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  74 ILMLHGFSAHKDmwlSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSidgQVKRIHQFVECLKlNKKPFHLVGTSMGGQV 153
Cdd:pfam12697   1 VVLVHGAGLSAA---PLAALLAAGVAVLAPDLPGH-GSSSPPPLDLA---DLADLAALLDELG-AARPVVLVGHSLGGAV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 154 AgvyAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGSAAVEKIPLIPSTPEEMsemlqlcsyVRFKVPQQILQGLV 233
Cdd:pfam12697  73 A---LAAAAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGF---------LDDLPADAEWAAAL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 234 DVRIPHNNFYRKLFLEivseksryslhqNMDKIKVPTQIIWGkQDQQVLDVsgADMLAKSIANCQVELLENCGHSvVMER 313
Cdd:pfam12697 141 ARLAALLAALALLPLA------------AWRDLPVPVLVLAE-EDRLVPEL--AQRLLAALAGARLVVLPGAGHL-PLDD 204


                  ....*..
gi 2462591573 314 PRKTAKL 320
Cdd:pfam12697 205 PEEVAEA 211
PLN02578 PLN02578
hydrolase
 9-327 5.18e-10

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 59.85  E-value: 5.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573   9 FVIAGGTLAIPILAFVASFLLWP-SALIRI-------YYWYWRrtlGMQVRYVhhedyqfcysfrgRPGHKPSILMLHGF 80
Cdd:PLN02578   32 IFIFGGIVASGVSVMGSSSASQSvQGLERLpfkkegyNFWTWR---GHKIHYV-------------VQGEGLPIVLIHGF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  81 SAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLddLSIDGQVKRiHQFVECLK-LNKKPFHLVGTSMGGQVAGVYAA 159
Cdd:PLN02578   96 GASAFHWRYNIPELAKKYKVYALDLLGF-GWSDKAL--IEYDAMVWR-DQVADFVKeVVKEPAVLVGNSLGGFTALSTAV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 160 YYPSDVSSLCLVCPAGlqystdnQFVQRLKELQGSAAVEKIPLIPSTPEEMSEMLQ----LCSYVRFKVPQQILQGLVDV 235
Cdd:PLN02578  172 GYPELVAGVALLNSAG-------QFGSESREKEEAIVVEETVLTRFVVKPLKEWFQrvvlGFLFWQAKQPSRIESVLKSV 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 236 RIPHNN---------------------FYRkLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQQVlDVSGADMLAKSI 294
Cdd:PLN02578  245 YKDKSNvddylvesitepaadpnagevYYR-LMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWV-GPAKAEKIKAFY 322

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2462591573 295 ANCQVELLEnCGHSVVMERPRKTAKLIIDFLAS 327
Cdd:PLN02578  323 PDTTLVNLQ-AGHCPHDEVPEQVNKALLEWLSS 354
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 70-313 1.72e-09

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: 57.22  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  70 HKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH---EGTTR--SSLDDLsidgqVKRIHQFVECLKLN--KKP 141
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHgrsDGKRGhvPSFDDY-----VDDLDTFVDKIREEhpGLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 142 FHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPA-GLQYSTDNQFVQRLKELQGSAAVEKIPLIPSTPEEMS---EMLQLC 217
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVDGLILSAPAlKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSLSrdpEVVAAY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 218 ---SYVRFKVPQQILQGLVDVRIphnnfyrklfleivseksrySLHQNMDKIKVPTQIIWGKQDqQVLDVSGADMLAKSI 294
Cdd:pfam12146 158 aadPLVHGGISARTLYELLDAGE--------------------RLLRRAAAITVPLLLLHGGAD-RVVDPAGSREFYERA 216

                         250       260
                  ....*....|....*....|.
gi 2462591573 295 --ANCQVELLENCGHSVVMER 313
Cdd:pfam12146 217 gsTDKTLKLYPGLYHELLNEP 237
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 72-324 1.12e-08

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 55.21  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  72 PSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTrsSLDDLSIDGQVKRIHQFVEclklnkKPFHLVGTSMGG 151
Cdd:TIGR01738   5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSR--GFGPLSLADMAEAIAAQAP------DPAIWLGWSLGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 152 QVAGVYAAYYPSDVSSLCLVC-----------PAGLQYSTDNQFVQRLKElqgsaavekiplipSTPEEMSEMLQL---- 216
Cdd:TIGR01738  77 LVALHIAATHPDRVRALVTVAsspcfsaredwPEGIKPDVLTGFQQQLSD--------------DYQRTIERFLALqtlg 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 217 CSYVRFKVpQQILQGLVDVRIPHNnfyrKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQQVLDVSGaDMLAKSIAN 296
Cdd:TIGR01738 143 TPTARQDA-RALKQTLLARPTPNV----QVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVV-PMLDKLAPH 216

                         250       260
                  ....*....|....*....|....*...
gi 2462591573 297 CQVELLENCGHSVVMERPRKTAKLIIDF 324
Cdd:TIGR01738 217 SELYIFAKAAHAPFLSHAEAFCALLVAF 244
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 42-314 3.24e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 54.53  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  42 WRRTLGMQVRYVHhedyqfCYSFRGRPGhKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSI 121
Cdd:PLN02894   83 WFRSASNEPRFIN------TVTFDSKED-APTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKST 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 122 D-GQVKRIHQFVECLKL-NKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKelqgsaavek 199
Cdd:PLN02894  156 EeTEAWFIDSFEEWRKAkNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEWLTK---------- 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 200 ipLIPSTPEEMSEMLQLCSYvrfkVPQQILQGL-----------VDVRIPHNN----------------FYRKLFLEIVS 252
Cdd:PLN02894  226 --FRATWKGAVLNHLWESNF----TPQKIIRGLgpwgpnlvrryTTARFGAHStgdilseeesklltdyVYHTLAAKASG 299

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462591573 253 EK-----------SRYSLHQNMDKIKVPTQIIWGKQDQqvLDVSGADMLAKSI-ANCQVELLENCGHSVVMERP 314
Cdd:PLN02894  300 ELclkyifsfgafARKPLLESASEWKVPTTFIYGRHDW--MNYEGAVEARKRMkVPCEIIRVPQGGHFVFLDNP 371
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
68-326 3.42e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.48  E-value: 3.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  68 PGHKPSILMLHGFSAHKD-MWLSVVKFLPKN-LHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPFHLV 145
Cdd:COG1506    20 GKKYPVVVYVHGGPGSRDdSFLPLAQALASRgYAVLAPDYRGY-GESAGDWGGDEVDDVLAAIDYLAARPYVDPDRIGIY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 146 GTSMGGQVAGVYAAYYPSDVSSLCLVCPA---GLQYSTDNQFVQRLKElqgsaavekiplipsTPEEMSEMLQlcsyvrf 222
Cdd:COG1506    99 GHSYGGYMALLAAARHPDRFKAAVALAGVsdlRSYYGTTREYTERLMG---------------GPWEDPEAYA------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 223 kvpqqilqglvdvriphnnfyrklfleivseksRYSLHQNMDKIKVPTQIIWGKQDQQVlDVSGADMLAKSI--ANCQVE 300
Cdd:COG1506   157 ---------------------------------ARSPLAYADKLKTPLLLIHGEADDRV-PPEQAERLYEALkkAGKPVE 202

                         250       260
                  ....*....|....*....|....*...
gi 2462591573 301 LL--ENCGHSVVMERPRKTAKLIIDFLA 326
Cdd:COG1506   203 LLvyPGEGHGFSGAGAPDYLERILDFLD 230
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 71-160 3.87e-08

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 53.30  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  71 KPSILMLHGFSAHKDMWLSVVKFLPKNlHLVCVDMPGHeGTTRssldDLSIDGQVKRIHQFVECLK-LNKKPFHLVGTSM 149
Cdd:PRK11126    2 LPWLVFLHGLLGSGQDWQPVGEALPDY-PRLYIDLPGH-GGSA----AISVDGFADVSRLLSQTLQsYNILPYWLVGYSL 75

                          90
                  ....*....|.
gi 2462591573 150 GGQVAGVYAAY 160
Cdd:PRK11126   76 GGRIAMYYACQ 86
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 70-168 1.15e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 43.66  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  70 HKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVC-VDMPGHEGTTRSSLDDLsiDGQVKRIHQfveclKLNKKPFHLVGTS 148
Cdd:COG1075     4 TRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYaLNYPSTNGSIEDSAEQL--AAFVDAVLA-----ATGAEKVDLVGHS 76

                          90       100
                  ....*....|....*....|..
gi 2462591573 149 MGGQVAGVYAAYY--PSDVSSL 168
Cdd:COG1075    77 MGGLVARYYLKRLggAAKVARV 98
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 62-325 2.78e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 44.91  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  62 YSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH---EGTTRSSLDDLSIDgqvkrIHQFVEclKL 137
Cdd:COG1073    28 YLPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYgesEGEPREEGSPERRD-----ARAAVD--YL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 138 NKKPFH------LVGTSMGGQVAGVYAAYYPsDVSSLCLVCPAglqYSTDNQFVQRLKELQGsaavEKIPLIPSTPeems 211
Cdd:COG1073   101 RTLPGVdperigLLGISLGGGYALNAAATDP-RVKAVILDSPF---TSLEDLAAQRAKEARG----AYLPGVPYLP---- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 212 emlqlcsyvrfkvpqqilqglvdvRIPHNNFYRKLFleivseksrYSLHQnMDKIKVPTQIIWGKQDQQVLDVSGADMLA 291
Cdd:COG1073   169 ------------------------NVRLASLLNDEF---------DPLAK-IEKISRPLLFIHGEKDEAVPFYMSEDLYE 214

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2462591573 292 KSIANCQVELLENCGHSVVMERPRKTA-KLIIDFL 325
Cdd:COG1073   215 AAAEPKELLIVPGAGHVDLYDRPEEEYfDKLAEFF 249
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 67-329 5.05e-04

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 40.99  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573  67 RPGHKPSILMLH--GFSAHkdMWLSVVKFLPKNLHLVCVDMPGHEgtTR------SSLDDLsidgqVKRIHQFVecLKLN 138
Cdd:COG3208     2 RPDARLRLFCFPyaGGSAS--AYRPWAAALPPDIEVLAVQLPGRG--DRlgepplTSLEEL-----ADDLAEEL--APLL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 139 KKPFHLVGTSMGGQVAgvY-------AAYYPSDvssLCLV---CPA-GLQYS-------TDNQFVQRLKELQGsaaveki 200
Cdd:COG3208    71 DRPFALFGHSMGALLA--FelarrleRRGRPLP---AHLFvsgRRApHLPRRrrplhdlSDAELLAELRRLGG------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591573 201 plipsTPEEM---SEMLQLcsyvrfkvpqqILQGLV-DVRIphnnfyrklfLEivseksRYsLHQNMDKIKVPTQIIWGK 276
Cdd:COG3208   139 -----TPEEVladPELLEL-----------FLPILRaDFRL----------LE------TY-RYTPGPPLDCPITALGGD 185

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591573 277 QDQqvlDVSGADMLA---KSIANCQVELLENcGHSVVMERPRKTAKLIIDFLASVH 329
Cdd:COG3208   186 DDP---LVSPEELAAwreHTTGPFRLRVFPG-GHFFLRDHPAELLALIRAALAALA 237
 
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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