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Conserved domains on  [gi|2251036518|gb|URZ09119|]
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2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (plasmid) [Clostridium felsineum]

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, ...
 10-276 2.37e-41

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: 142.06  E-value: 2.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  10 TLKLRNIDMFYLDTRTEKTAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKPKEPYTIKIMAEDIVELLKA 89
Cdd:COG0596     6 FVTVDGVRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  90 LKLQAAILVGHSMGGGIAAYLAANYPEYIKALAILDKSPTNLnatnklsidRNTLIDPltGNWPLPFATLTEAtsfiksa 169
Cdd:COG0596    86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAAL---------AEPLRRP--GLAPEALAALLRA------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 170 scsdleytyfmnslmetssgykmmfdskamasifLNSLDFWDILSRIKCLTMIVRSSSHEGIPNEDFKRMEACLKNHLAF 249
Cdd:COG0596   148 ----------------------------------LARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELV 193

                         250       260
                  ....*....|....*....|....*..
gi 2251036518 250 EMSNKDHNVHLSNKEEFYTCFDKFLSS 276
Cdd:COG0596   194 VLPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 10-276 2.37e-41

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: 142.06  E-value: 2.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  10 TLKLRNIDMFYLDTRTEKTAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKPKEPYTIKIMAEDIVELLKA 89
Cdd:COG0596     6 FVTVDGVRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  90 LKLQAAILVGHSMGGGIAAYLAANYPEYIKALAILDKSPTNLnatnklsidRNTLIDPltGNWPLPFATLTEAtsfiksa 169
Cdd:COG0596    86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAAL---------AEPLRRP--GLAPEALAALLRA------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 170 scsdleytyfmnslmetssgykmmfdskamasifLNSLDFWDILSRIKCLTMIVRSSSHEGIPNEDFKRMEACLKNHLAF 249
Cdd:COG0596   148 ----------------------------------LARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELV 193

                         250       260
                  ....*....|....*....|....*..
gi 2251036518 250 EMSNKDHNVHLSNKEEFYTCFDKFLSS 276
Cdd:COG0596   194 VLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 28-262 4.21e-25

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: 99.89  E-value: 4.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  28 TAIICLHGMYGRAETWQAFIQN-YGTKYRIISPDQRGHGLTSKPKEP--YTIKIMAEDIVELLKALKLQAAILVGHSMGG 104
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAlARDGFRVIALDLRGFGKSSRPKAQddYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 105 GIAAYLAANYPEYIKALAILDkSPTNLNATNKLSIDRNTLIDPLTGNWPLPFATLTEATSFIKSAScSDLEYTYFMNSLM 184
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLG-ALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLA-LLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 185 ETSSGYKMMFDSKAMASIF--LNSLDFWDILSRIKCL------TMIVRSSSHEGIPNEDFKRMEACLKNHLAFEMSNKDH 256
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTgaLLFIETWSTELRAKFLgrldepTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ....*.
gi 2251036518 257 NVHLSN 262
Cdd:pfam00561 239 FAFLEG 244
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 26-274 1.82e-24

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: 98.44  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  26 EKTAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKPK--EPYTIKIMAEDI-VELLKALKLQAAILVGHSM 102
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSdiERYDFEEAAQLLlATLLDQLGIEPFFLVGYSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 103 GGGIAAYLAANYPEYIKALAILDKSPTNLNATNKLS-----------IDRNTLIDPLTgNW---PLpFATLTEATSFIKS 168
Cdd:TIGR03695  81 GGRIALYYALQYPERVQGLILESGSPGLQTEEERAArrqndeqlaqrFEQEGLEAFLD-DWyqqPL-FASQKNLPPEQRQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 169 A------SCSDLEYTyfmNSLMETSSGykmmfdskamasiflNSLDFWDILSRIKCLTMIV---RSSSHEGIPnedfKRM 239
Cdd:TIGR03695 159 AlraerlANNPEGLA---KMLRATGLG---------------KQPSLWPKLQALKIPVLYLcgeRDEKFVQIA----KEM 216

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2251036518 240 EACLKNhLAFEM-SNKDHNVHLSNKEEFYTCFDKFL 274
Cdd:TIGR03695 217 QKLIPN-LTLHIiPNAGHNIHLENPEAFAKILLAFL 251
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 17-124 4.95e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 82.68  E-value: 4.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  17 DMFYLDTRTEK-TAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKPKEPYTIKIMAEDIVELLKALKLQAA 95
Cdd:PRK14875  120 TVRYLRLGEGDgTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALGIERA 199

                          90       100
                  ....*....|....*....|....*....
gi 2251036518  96 ILVGHSMGGGIAAYLAANYPEYIKALAIL 124
Cdd:PRK14875  200 HLVGHSMGGAVALRLAARAPQRVASLTLI 228
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 91-121 1.47e-03

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 39.53  E-value: 1.47e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2251036518  91 KLQAAILVGHSMGGGIAAYLAANYPEYIKAL 121
Cdd:cd12808   186 RVGPCIVVAHSQGGGFAFEAARARPDLVRAV 216
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 10-276 2.37e-41

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: 142.06  E-value: 2.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  10 TLKLRNIDMFYLDTRTEKTAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKPKEPYTIKIMAEDIVELLKA 89
Cdd:COG0596     6 FVTVDGVRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  90 LKLQAAILVGHSMGGGIAAYLAANYPEYIKALAILDKSPTNLnatnklsidRNTLIDPltGNWPLPFATLTEAtsfiksa 169
Cdd:COG0596    86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAAL---------AEPLRRP--GLAPEALAALLRA------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 170 scsdleytyfmnslmetssgykmmfdskamasifLNSLDFWDILSRIKCLTMIVRSSSHEGIPNEDFKRMEACLKNHLAF 249
Cdd:COG0596   148 ----------------------------------LARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELV 193

                         250       260
                  ....*....|....*....|....*..
gi 2251036518 250 EMSNKDHNVHLSNKEEFYTCFDKFLSS 276
Cdd:COG0596   194 VLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 28-262 4.21e-25

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: 99.89  E-value: 4.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  28 TAIICLHGMYGRAETWQAFIQN-YGTKYRIISPDQRGHGLTSKPKEP--YTIKIMAEDIVELLKALKLQAAILVGHSMGG 104
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAlARDGFRVIALDLRGFGKSSRPKAQddYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 105 GIAAYLAANYPEYIKALAILDkSPTNLNATNKLSIDRNTLIDPLTGNWPLPFATLTEATSFIKSAScSDLEYTYFMNSLM 184
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLG-ALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLA-LLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 185 ETSSGYKMMFDSKAMASIF--LNSLDFWDILSRIKCL------TMIVRSSSHEGIPNEDFKRMEACLKNHLAFEMSNKDH 256
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTgaLLFIETWSTELRAKFLgrldepTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ....*.
gi 2251036518 257 NVHLSN 262
Cdd:pfam00561 239 FAFLEG 244
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 26-274 1.82e-24

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: 98.44  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  26 EKTAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKPK--EPYTIKIMAEDI-VELLKALKLQAAILVGHSM 102
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSdiERYDFEEAAQLLlATLLDQLGIEPFFLVGYSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 103 GGGIAAYLAANYPEYIKALAILDKSPTNLNATNKLS-----------IDRNTLIDPLTgNW---PLpFATLTEATSFIKS 168
Cdd:TIGR03695  81 GGRIALYYALQYPERVQGLILESGSPGLQTEEERAArrqndeqlaqrFEQEGLEAFLD-DWyqqPL-FASQKNLPPEQRQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 169 A------SCSDLEYTyfmNSLMETSSGykmmfdskamasiflNSLDFWDILSRIKCLTMIV---RSSSHEGIPnedfKRM 239
Cdd:TIGR03695 159 AlraerlANNPEGLA---KMLRATGLG---------------KQPSLWPKLQALKIPVLYLcgeRDEKFVQIA----KEM 216

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2251036518 240 EACLKNhLAFEM-SNKDHNVHLSNKEEFYTCFDKFL 274
Cdd:TIGR03695 217 QKLIPN-LTLHIiPNAGHNIHLENPEAFAKILLAFL 251
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
20-124 4.01e-19

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 83.51  E-value: 4.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  20 YLDTRTEKTAIICLHGMYGRAETWQAFIQNY---GtkYRIISPDQRGHGLTSKPK-EPYTIKIMAEDIVELLKALKLQAA 95
Cdd:COG2267    21 WRPAGSPRGTVVLVHGLGEHSGRYAELAEALaaaG--YAVLAFDLRGHGRSDGPRgHVDSFDDYVDDLRAALDALRARPG 98

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2251036518  96 ---ILVGHSMGGGIAAYLAANYPEYIKALAIL 124
Cdd:COG2267    99 lpvVLLGHSMGGLIALLYAARYPDRVAGLVLL 130
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 17-124 4.95e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 82.68  E-value: 4.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  17 DMFYLDTRTEK-TAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKPKEPYTIKIMAEDIVELLKALKLQAA 95
Cdd:PRK14875  120 TVRYLRLGEGDgTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALGIERA 199

                          90       100
                  ....*....|....*....|....*....
gi 2251036518  96 ILVGHSMGGGIAAYLAANYPEYIKALAIL 124
Cdd:PRK14875  200 HLVGHSMGGAVALRLAARAPQRVASLTLI 228
PRK10673 PRK10673
esterase;
25-130 2.38e-16

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 76.31  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  25 TEKTAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTskPKEP-YTIKIMAEDIVELLKALKLQAAILVGHSMG 103
Cdd:PRK10673   14 HNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLS--PRDPvMNYPAMAQDLLDTLDALQIEKATFIGHSMG 91

                          90       100
                  ....*....|....*....|....*..
gi 2251036518 104 GGIAAYLAANYPEYIKALAILDKSPTN 130
Cdd:PRK10673   92 GKAVMALTALAPDRIDKLVAIDIAPVD 118
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
29-131 2.07e-11

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 62.34  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  29 AIICLHGM-YGRAETWQAFIQNY---GtkYRIISPDQRGHGLTSKPkepyTIKIMAEDIVELLKALKLQAAI------LV 98
Cdd:COG1506    25 VVVYVHGGpGSRDDSFLPLAQALasrG--YAVLAPDYRGYGESAGD----WGGDEVDDVLAAIDYLAARPYVdpdrigIY 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2251036518  99 GHSMGGGIAAYLAANYPEYIKAlAILDKSPTNL 131
Cdd:COG1506    99 GHSYGGYMALLAAARHPDRFKA-AVALAGVSDL 130
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
27-277 5.19e-11

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 61.11  E-value: 5.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  27 KTAIICLHG-------MYGRAEtwqaFIQNYGtkYRIISPDQRGHGLTSKPKEPYTIKIMAEDIVELLKALKLQAA--IL 97
Cdd:COG1647    15 RKGVLLLHGftgspaeMRPLAE----ALAKAG--YTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGYDkvIV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  98 VGHSMGGGIAAYLAANYPEyIKALAILdkSPTnlnatnkLSIDRNTLidpltgnWPLPFatLTEATSFIKSASCSDLEYT 177
Cdd:COG1647    89 IGLSMGGLLALLLAARYPD-VAGLVLL--SPA-------LKIDDPSA-------PLLPL--LKYLARSLRGIGSDIEDPE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518 178 YFMNSLMETSsgykmmfdSKAMASIFLNSLDFWDILSRIKCLTMIVRSSSHEGIPNED----FKRMEACLKNHLAFEmsN 253
Cdd:COG1647   150 VAEYAYDRTP--------LRALAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESaryiYERLGSPDKELVWLE--D 219

                         250       260
                  ....*....|....*....|....*
gi 2251036518 254 KDHNVHLSN-KEEFYTCFDKFLSSI 277
Cdd:COG1647   220 SGHVITLDKdREEVAEEILDFLERL 244
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 3-121 8.66e-11

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 61.85  E-value: 8.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518   3 KIKIFRNTL-KLRNIDMFYLDTRTEKTAIICLHGmYGRAETWqaFIQNY---GTKYRIISPDQRGHGLTSKPkePYTIKI 78
Cdd:PLN02894   80 KVRWFRSASnEPRFINTVTFDSKEDAPTLVMVHG-YGASQGF--FFRNFdalASRFRVIAIDQLGWGGSSRP--DFTCKS 154

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2251036518  79 MAE-------DIVELLKALKLQAAILVGHSMGGGIAAYLAANYPEYIKAL 121
Cdd:PLN02894  155 TEEteawfidSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHL 204
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 30-112 1.13e-10

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 59.79  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  30 IICLHGMYGRAETWQAFiqnYGTKYRIISPDQRGHGLTSKPKEPYTikiMAEDIVELLKALK-LQAAILVGHSMGGGIAA 108
Cdd:pfam12697   1 VVLVHGAGLSAAPLAAL---LAAGVAVLAPDLPGHGSSSPPPLDLA---DLADLAALLDELGaARPVVLVGHSLGGAVAL 74


                  ....
gi 2251036518 109 YLAA 112
Cdd:pfam12697  75 AAAA 78
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 29-124 6.20e-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: 55.30  E-value: 6.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  29 AIICL-HGM---YGR----AETWQAfiQNYGTkYRIispDQRGHGLtSKPKEPY--TIKIMAEDIVELLKALKLQAA--- 95
Cdd:pfam12146   5 AVVVLvHGLgehSGRyahlADALAA--QGFAV-YAY---DHRGHGR-SDGKRGHvpSFDDYVDDLDTFVDKIREEHPglp 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 2251036518  96 -ILVGHSMGGGIAAYLAANYPEYIKALaIL 124
Cdd:pfam12146  78 lFLLGHSMGGLIAALYALRYPDKVDGL-IL 106
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 18-162 1.46e-08

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 54.62  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  18 MFYLDTrTEKTAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKPKEPYTIKIMAEDIVELLKALKLQAAIL 97
Cdd:PRK03592   19 MAYIET-GEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDIDYTFADHARYLDAWFDALGLDDVVL 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2251036518  98 VGHSMGGGIAAYLAANYPEYIKALAILDksptnlnatnklsidrnTLIDPLT-GNWPLPFATLTEA 162
Cdd:PRK03592   98 VGHDWGSALGFDWAARHPDRVRGIAFME-----------------AIVRPMTwDDFPPAVRELFQA 146
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 25-128 2.69e-08

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 54.86  E-value: 2.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518   25 TEKTAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHG---LTSKPKEP-----YTIKIMAEDIVELLKALKLQAAI 96
Cdd:PLN02980  1369 AEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGgskIQNHAKETqteptLSVELVADLLYKLIEHITPGKVT 1448

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2251036518   97 LVGHSMGGGIAAYLAANYPEYIKALAILDKSP 128
Cdd:PLN02980  1449 LVGYSMGARIALYMALRFSDKIEGAVIISGSP 1480
PLN02578 PLN02578
hydrolase
 30-127 4.01e-07

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 50.61  E-value: 4.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  30 IICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKPKEPYTIKIMAEDIVELLKALKLQAAILVGHSMGGGIAAY 109
Cdd:PLN02578   89 IVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTALS 168

                          90
                  ....*....|....*...
gi 2251036518 110 LAANYPEYIKALAILDKS 127
Cdd:PLN02578  169 TAVGYPELVAGVALLNSA 186
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 29-128 1.37e-06

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: 48.27  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  29 AIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGlTSKPKEPYTIKIMAEDIVELLKAlklqAAILVGHSMGGGIAA 108
Cdd:TIGR01738   6 HLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHG-RSRGFGPLSLADMAEAIAAQAPD----PAIWLGWSLGGLVAL 80

                          90       100
                  ....*....|....*....|
gi 2251036518 109 YLAANYPEYIKALAILDKSP 128
Cdd:TIGR01738  81 HIAATHPDRVRALVTVASSP 100
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 30-113 3.10e-06

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 47.14  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  30 IICLHGMYGRAETWQAFIQNYgTKYRIISPDQRGHGlTSKPKEPYTIKIMAEDIVELLKALKLQAAILVGHSMGGGIAAY 109
Cdd:PRK11126    5 LVFLHGLLGSGQDWQPVGEAL-PDYPRLYIDLPGHG-GSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRIAMY 82


                  ....
gi 2251036518 110 LAAN 113
Cdd:PRK11126   83 YACQ 86
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 23-114 3.19e-06

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 44.82  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  23 TRTEKTAIICLHGMYGRAETWQAFIQ---NYGtkYRIISPDQRGHGltskpkepYTIKIMAEDIVELLKALKLQAA---- 95
Cdd:COG1075     1 YAATRYPVVLVHGLGGSAASWAPLAPrlrAAG--YPVYALNYPSTN--------GSIEDSAEQLAAFVDAVLAATGaekv 70

                          90
                  ....*....|....*....
gi 2251036518  96 ILVGHSMGGGIAAYLAANY 114
Cdd:COG1075    71 DLVGHSMGGLVARYYLKRL 89
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 18-122 4.15e-06

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 46.83  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  18 MFYLDTRTEKT--AIICLHGMYGRAETWQAFIQNY---GtkYRIISPDQRGHGLTS-KPKEpyTIKIMAEDIVELLKALK 91
Cdd:COG1073    26 DLYLPAGASKKypAVVVAHGNGGVKEQRALYAQRLaelG--FNVLAFDYRGYGESEgEPRE--EGSPERRDARAAVDYLR 101

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2251036518  92 LQAA------ILVGHSMGGGIAAYLAANYPEyIKALA 122
Cdd:COG1073   102 TLPGvdperiGLLGISLGGGYALNAAATDPR-VKAVI 137
PRK06489 PRK06489
hypothetical protein; Provisional
 29-146 2.10e-05

hypothetical protein; Provisional


Pssm-ID: 235815 [Multi-domain]  Cd Length: 360  Bit Score: 45.36  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  29 AIICLHGMYGRAetwQAFIQN------YG-------TKYRIISPDQRGHGLTSKPKE------P-YTIKIMAEDIVELL- 87
Cdd:PRK06489   71 AVLVLHGTGGSG---KSFLSPtfagelFGpgqpldaSKYFIILPDGIGHGKSSKPSDglraafPrYDYDDMVEAQYRLVt 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2251036518  88 -----KALKLqaaiLVGHSMGGGIAAYLAANYPEYIKALAILDKSPTNLNATNKLSidRNTLID 146
Cdd:PRK06489  148 eglgvKHLRL----ILGTSMGGMHAWMWGEKYPDFMDALMPMASQPTEMSGRNWMW--RRMLIE 205
COG4099 COG4099
Predicted peptidase [General function prediction only];
30-123 4.41e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 43.80  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  30 IICLHGMYGRAETWQAFIQNYGTKYrIISPDQRGHG---LT--SKPKEPYTIKIMAEDIVELLKALKLQAAI------LV 98
Cdd:COG4099    52 VLFLHGAGERGTDNEKQLTHGAPKF-INPENQAKFPaivLApqCPEDDYWSDTKALDAVLALLDDLIAEYRIdpdriyLT 130

                          90       100
                  ....*....|....*....|....*
gi 2251036518  99 GHSMGGGIAAYLAANYPEYIKALAI 123
Cdd:COG4099   131 GLSMGGYGTWDLAARYPDLFAAAVP 155
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
30-128 2.09e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 41.93  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  30 IICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKpkepytikIMAEDIVELLKALKLQA---AILVGHSMGGGI 106
Cdd:PRK10349   16 LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRG--------FGALSLADMAEAVLQQApdkAIWLGWSLGGLV 87

                          90       100
                  ....*....|....*....|..
gi 2251036518 107 AAYLAANYPEYIKALAILDKSP 128
Cdd:PRK10349   88 ASQIALTHPERVQALVTVASSP 109
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 21-107 5.54e-04

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 41.23  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  21 LDTRTEKTAIICLHGMYGRAETWQAFIQNygtkyriISPDQ-----RGHGLTSKPKEPYTIKIMAEDIVELLKALklQAA 95
Cdd:COG3319   595 LRAGGSGPPLFCVHPAGGNVLCYRPLARA-------LGPDRpvyglQAPGLDGGEPPPASVEEMAARYVEAIRAV--QPE 665

                          90
                  ....*....|....*
gi 2251036518  96 ---ILVGHSMGGGIA 107
Cdd:COG3319   666 gpyHLLGWSFGGLVA 680
YpfH COG0400
Predicted esterase [General function prediction only];
23-124 7.67e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 39.51  E-value: 7.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  23 TRTEKTAIICLHGMYGRAETWQAFIQNYGT-KYRIISPdqrgHGLTSKPKEPYT--------IKIMAEDIVELLKAL--- 90
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALpGAAVLAP----RAPVPEGPGGRAwfdlsfleGREDEEGLAAAAEALaaf 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2251036518  91 --KLQAA--------ILVGHSMGGGIAAYLAANYPEYIKALAIL 124
Cdd:COG0400    77 idELEARygidperiVLAGFSQGAAMALSLALRRPELLAGVVAL 120
PRK05855 PRK05855
SDR family oxidoreductase;
26-103 7.82e-04

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 40.73  E-value: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  26 EKTAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKPK--EPYTIKIMAEDIVELLKALKLQAAI-LVGHSM 102
Cdd:PRK05855   24 DRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKrtAAYTLARLADDFAAVIDAVSPDRPVhLLAHDW 103


                  .
gi 2251036518 103 G 103
Cdd:PRK05855  104 G 104
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 91-121 1.47e-03

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 39.53  E-value: 1.47e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2251036518  91 KLQAAILVGHSMGGGIAAYLAANYPEYIKAL 121
Cdd:cd12808   186 RVGPCIVVAHSQGGGFAFEAARARPDLVRAV 216
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 18-123 1.49e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 39.45  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  18 MFYLDTRTEKTAIIClHGmygrAETW----QAFIQNYGTKYRIISPDQRGHGLTSKPKE-PYTIKIMAEDIVELLKALKL 92
Cdd:PRK03204   26 IHYIDEGTGPPILLC-HG----NPTWsflyRDIIVALRDRFRCVAPDYLGFGLSERPSGfGYQIDEHARVIGEFVDHLGL 100

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2251036518  93 QAAILVGHSMGGGIAAYLAANYPEYIKALAI 123
Cdd:PRK03204  101 DRYLSMGQDWGGPISMAVAVERADRVRGVVL 131
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 52-124 1.66e-03

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 39.41  E-value: 1.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2251036518  52 TKYRIISPDQRGHGLTSKPKEP-YTIKIMAEDIVE-LLKALKLQAAILVGHSMGGGIAAYLAANYPEYIKALAIL 124
Cdd:PLN03087  231 STYRLFAVDLLGFGRSPKPADSlYTLREHLEMIERsVLERYKVKSFHIVAHSLGCILALALAVKHPGAVKSLTLL 305
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
79-122 1.68e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 38.79  E-value: 1.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2251036518  79 MAEDIVELLKALKLQAAI------LVGHSMGGGIAAYLAANYPEyIKALA 122
Cdd:COG0412    89 LAADLRAALDWLKAQPEVdagrvgVVGFCFGGGLALLAAARGPD-LAAAV 137
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 83-123 1.97e-03

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 38.83  E-value: 1.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2251036518  83 IVELLKALKLQAAI------LVGHSMGGGIAAYLAANYPEYIKALAI 123
Cdd:COG3509   118 IAALVDDLAARYGIdpkrvyVTGLSAGGAMAYRLACEYPDVFAAVAP 164
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 28-127 3.14e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 38.18  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2251036518  28 TAIICLHGMYGRAETWQAFIQNYGTKYRIISPDQRGHGLTSKP-------KEPYTIKIMAEDIVELLKALKLQAAILVGH 100
Cdd:PLN02824   30 PALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPnprsappNSFYTFETWGEQLNDFCSDVVGDPAFVICN 109

                          90       100
                  ....*....|....*....|....*..
gi 2251036518 101 SMGGGIAAYLAANYPEYIKALAILDKS 127
Cdd:PLN02824  110 SVGGVVGLQAAVDAPELVRGVMLINIS 136
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 77-114 5.79e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 36.71  E-value: 5.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2251036518  77 KIMAEDIVELLKALKLQAA----ILVGHSMGGGIAAYLAANY 114
Cdd:cd00741     8 RSLANLVLPLLKSALAQYPdykiHVTGHSLGGALAGLAGLDL 49
 
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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