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Conserved domains on  [gi|754529350|ref|WP_041932464|]
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alpha/beta fold hydrolase [Cytophaga hutchinsonii]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 1001822)

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

CATH:  3.40.50.1820
Gene Ontology:  GO:0016787
PubMed:  12369917|15381402|1409539
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10673 super family cl30399
esterase;
1-253 4.98e-66

esterase;


The actual alignment was detected with superfamily member PRK10673:

Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 205.35  E-value: 4.98e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   1 MKLFYR-ETGEGK----PLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQSPHENVHTYQAMAADLKQFLDDHNI 75
Cdd:PRK10673   1 MKLNIRaQTAQNPhnnsPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  76 EKPVLIGHSMGGKTIMRFAAEYKGVAEKLIVVDISPRFYG-RHHQDILAGLNAINLETLQTRNEADAILSNFVGDIGVRM 154
Cdd:PRK10673  81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHvRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350 155 FLLKSlYRSSEgkfqWRINLPVIEEQIDNI--GEPLPEEAHidtPTLFIRGSESGYIEDKDKAVIEKHFTQYTLETVQGA 232
Cdd:PRK10673 161 FLLKS-FVDGE----WRFNVPVLWDQYPHIvgWEKIPAWPH---PALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGA 232

                        250       260
                 ....*....|....*....|.
gi 754529350 233 SHFVHAEKPKEVIQLIENFIE 253
Cdd:PRK10673 233 GHWVHAEKPDAVLRAIRRYLN 253
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
1-253 4.98e-66

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 205.35  E-value: 4.98e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   1 MKLFYR-ETGEGK----PLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQSPHENVHTYQAMAADLKQFLDDHNI 75
Cdd:PRK10673   1 MKLNIRaQTAQNPhnnsPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  76 EKPVLIGHSMGGKTIMRFAAEYKGVAEKLIVVDISPRFYG-RHHQDILAGLNAINLETLQTRNEADAILSNFVGDIGVRM 154
Cdd:PRK10673  81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHvRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350 155 FLLKSlYRSSEgkfqWRINLPVIEEQIDNI--GEPLPEEAHidtPTLFIRGSESGYIEDKDKAVIEKHFTQYTLETVQGA 232
Cdd:PRK10673 161 FLLKS-FVDGE----WRFNVPVLWDQYPHIvgWEKIPAWPH---PALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGA 232

                        250       260
                 ....*....|....*....|.
gi 754529350 233 SHFVHAEKPKEVIQLIENFIE 253
Cdd:PRK10673 233 GHWVHAEKPDAVLRAIRRYLN 253
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-253 2.71e-45

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: 151.31  E-value: 2.71e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   1 MKLFYRETG-EGKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQSPH-ENVHTYQAMAADLKQFLDDHNIEKP 78
Cdd:COG0596   12 VRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  79 VLIGHSMGGKTIMRFAAEYKGVAEKLIVVDISPRFYGRHHQDILAGLNAInLETLQTRNEADailsnfvgdigvrmfllk 158
Cdd:COG0596   92 VLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEAL-AALLRALARTD------------------ 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350 159 slyrssegkfqwrinlpvieeqidnigePLPEEAHIDTPTLFIRGSESGYIEDKDKAVIEKHFTQYTLETVQGASHFVHA 238
Cdd:COG0596  153 ----------------------------LRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPL 204

                        250
                 ....*....|....*
gi 754529350 239 EKPKEVIQLIENFIE 253
Cdd:COG0596  205 EQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 12-241 2.03e-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: 100.27  E-value: 2.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   12 KPLVILHGLFGSSDNWMTVTKELALK-YNVYVLDARNHGQS-PHENVHTYQ--AMAADLKQFLDDHNIEKPVLIGHSMGG 87
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSsRPKAQDDYRtdDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   88 KTIMRFAAEYKGVAEKLIVVDISPRFYgrHHQDILAGLNAINLETLQTRNEADA------ILSNFVGDIGVR---MFLLK 158
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPH--ELDEADRFILALFPGFFDGFVADFApnplgrLVAKLLALLLLRlrlLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  159 SLYRSSEGKFQWRINLPVIEE----QIDNIGEPLPEEAHIDTPTLFIRGSESGYIEDKDKAVIEKHFTQYTLETVQGASH 234
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGAllfiETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ....*..
gi 754529350  235 FVHAEKP 241
Cdd:pfam00561 239 FAFLEGP 245
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 10-253 1.52e-18

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: 81.88  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   10 EGKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQSP-HENVHTY---QAMAADLKQFLDDHNIEKPVLIGHSM 85
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQsPSDIERYdfeEAAQLLLATLLDQLGIEPFFLVGYSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   86 GGKTIMRFAAEYKGVAEKLIVVDISPrfygrhhqdilaGLNaiNLETLQTRNEADAILSNFVGDIGVRMFLlksLYRSSE 165
Cdd:TIGR03695  81 GGRIALYYALQYPERVQGLILESGSP------------GLQ--TEEERAARRQNDEQLAQRFEQEGLEAFL---DDWYQQ 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  166 GKFQWRINLP------VIEEQIDNIGEPL----------------PEEAHIDTPTLFIRGsesgyieDKDKAV------I 217
Cdd:TIGR03695 144 PLFASQKNLPpeqrqaLRAERLANNPEGLakmlratglgkqpslwPKLQALKIPVLYLCG-------ERDEKFvqiakeM 216

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 754529350  218 EKHFTQYTLETVQGASHFVHAEKPKEVIQLIENFIE 253
Cdd:TIGR03695 217 QKLIPNLTLHIIPNAGHNIHLENPEAFAKILLAFLE 252
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 12-87 4.17e-03

Pancreatic lipase-like enzymes. 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: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 37.61  E-value: 4.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  12 KPLVIL-HGlFGSS--DNWMTVTKELALK---YNVYVLDARNhGQSPH-----ENVhtyQAMAADLKQFLD------DHN 74
Cdd:cd00707   36 RPTRFIiHG-WTSSgeESWISDLRKAYLSrgdYNVIVVDWGR-GANPNypqavNNT---RVVGAELAKFLDflvdntGLS 110

                         90
                 ....*....|...
gi 754529350  75 IEKPVLIGHSMGG 87
Cdd:cd00707  111 LENVHLIGHSLGA 123
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
1-253 4.98e-66

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 205.35  E-value: 4.98e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   1 MKLFYR-ETGEGK----PLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQSPHENVHTYQAMAADLKQFLDDHNI 75
Cdd:PRK10673   1 MKLNIRaQTAQNPhnnsPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  76 EKPVLIGHSMGGKTIMRFAAEYKGVAEKLIVVDISPRFYG-RHHQDILAGLNAINLETLQTRNEADAILSNFVGDIGVRM 154
Cdd:PRK10673  81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHvRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350 155 FLLKSlYRSSEgkfqWRINLPVIEEQIDNI--GEPLPEEAHidtPTLFIRGSESGYIEDKDKAVIEKHFTQYTLETVQGA 232
Cdd:PRK10673 161 FLLKS-FVDGE----WRFNVPVLWDQYPHIvgWEKIPAWPH---PALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGA 232

                        250       260
                 ....*....|....*....|.
gi 754529350 233 SHFVHAEKPKEVIQLIENFIE 253
Cdd:PRK10673 233 GHWVHAEKPDAVLRAIRRYLN 253
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-253 2.71e-45

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: 151.31  E-value: 2.71e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   1 MKLFYRETG-EGKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQSPH-ENVHTYQAMAADLKQFLDDHNIEKP 78
Cdd:COG0596   12 VRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  79 VLIGHSMGGKTIMRFAAEYKGVAEKLIVVDISPRFYGRHHQDILAGLNAInLETLQTRNEADailsnfvgdigvrmfllk 158
Cdd:COG0596   92 VLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEAL-AALLRALARTD------------------ 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350 159 slyrssegkfqwrinlpvieeqidnigePLPEEAHIDTPTLFIRGSESGYIEDKDKAVIEKHFTQYTLETVQGASHFVHA 238
Cdd:COG0596  153 ----------------------------LRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPL 204

                        250
                 ....*....|....*
gi 754529350 239 EKPKEVIQLIENFIE 253
Cdd:COG0596  205 EQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 12-241 2.03e-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: 100.27  E-value: 2.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   12 KPLVILHGLFGSSDNWMTVTKELALK-YNVYVLDARNHGQS-PHENVHTYQ--AMAADLKQFLDDHNIEKPVLIGHSMGG 87
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSsRPKAQDDYRtdDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   88 KTIMRFAAEYKGVAEKLIVVDISPRFYgrHHQDILAGLNAINLETLQTRNEADA------ILSNFVGDIGVR---MFLLK 158
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPH--ELDEADRFILALFPGFFDGFVADFApnplgrLVAKLLALLLLRlrlLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  159 SLYRSSEGKFQWRINLPVIEE----QIDNIGEPLPEEAHIDTPTLFIRGSESGYIEDKDKAVIEKHFTQYTLETVQGASH 234
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGAllfiETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ....*..
gi 754529350  235 FVHAEKP 241
Cdd:pfam00561 239 FAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
2-253 1.59e-21

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 89.29  E-value: 1.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   2 KLFYR----ETGEGKPLVILHGLFGSSDNWMTVTKELALK-YNVYVLDARNHGQSPHENVH--TYQAMAADLKQFLD--- 71
Cdd:COG2267   15 RLRGRrwrpAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHvdSFDDYVDDLRAALDalr 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  72 DHNIEKPVLIGHSMGGKTIMRFAAEYKGVAEKLIVvdISPRFYGRHHQDILAGLnainLETLQTRNEAdailsnfvgdig 151
Cdd:COG2267   95 ARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVL--LAPAYRADPLLGPSARW----LRALRLAEAL------------ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350 152 vrmfllkslyrssegkfqwrinlpvieeqidnigeplpeeAHIDTPTLFIRGSESGYIEDKD-KAVIEKHFTQYTLETVQ 230
Cdd:COG2267  157 ----------------------------------------ARIDVPVLVLHGGADRVVPPEAaRRLAARLSPDVELVLLP 196

                        250       260
                 ....*....|....*....|....
gi 754529350 231 GASHFVHAEKPKE-VIQLIENFIE 253
Cdd:COG2267  197 GARHELLNEPAREeVLAAILAWLE 220
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 10-253 1.52e-18

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: 81.88  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   10 EGKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQSP-HENVHTY---QAMAADLKQFLDDHNIEKPVLIGHSM 85
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQsPSDIERYdfeEAAQLLLATLLDQLGIEPFFLVGYSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   86 GGKTIMRFAAEYKGVAEKLIVVDISPrfygrhhqdilaGLNaiNLETLQTRNEADAILSNFVGDIGVRMFLlksLYRSSE 165
Cdd:TIGR03695  81 GGRIALYYALQYPERVQGLILESGSP------------GLQ--TEEERAARRQNDEQLAQRFEQEGLEAFL---DDWYQQ 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  166 GKFQWRINLP------VIEEQIDNIGEPL----------------PEEAHIDTPTLFIRGsesgyieDKDKAV------I 217
Cdd:TIGR03695 144 PLFASQKNLPpeqrqaLRAERLANNPEGLakmlratglgkqpslwPKLQALKIPVLYLCG-------ERDEKFvqiakeM 216

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 754529350  218 EKHFTQYTLETVQGASHFVHAEKPKEVIQLIENFIE 253
Cdd:TIGR03695 217 QKLIPNLTLHIIPNAGHNIHLENPEAFAKILLAFLE 252
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 6-254 3.20e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 82.68  E-value: 3.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   6 RETGEGKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQS-PHENVHTYQAMAADLKQFLDDHNIEKPVLIGHS 84
Cdd:PRK14875 126 LGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAFLDALGIERAHLVGHS 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  85 MGGKTIMRFAAEYKG-VAEkliVVDISPrfygrhhqdilAGLN-AINLETLQ------TRNE---------ADAIL--SN 145
Cdd:PRK14875 206 MGGAVALRLAARAPQrVAS---LTLIAP-----------AGLGpEINGDYIDgfvaaeSRRElkpvlellfADPALvtRQ 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350 146 FVGDI-------GVRMFL---LKSLYRSSegkfqwrinlpvieEQIDNIGEPLpeeAHIDTPTLFIRGSEsgyiedkDKA 215
Cdd:PRK14875 272 MVEDLlkykrldGVDDALralADALFAGG--------------RQRVDLRDRL---ASLAIPVLVIWGEQ-------DRI 327

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 754529350 216 VIEKHFT----QYTLETVQGASHFVHAEKPKEVIQLIENFIEN 254
Cdd:PRK14875 328 IPAAHAQglpdGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 14-247 3.74e-15

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 72.12  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   14 LVILHGLFGSSDNwmtVTKELALKYNVYVLDARNHGQSPHENvHTYQAmAADLKQFLDDH-NIEKPVLIGHSMGGKTIMR 92
Cdd:pfam12697   1 VVLVHGAGLSAAP---LAALLAAGVAVLAPDLPGHGSSSPPP-LDLAD-LADLAALLDELgAARPVVLVGHSLGGAVALA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   93 FAAeykgvAEKLIVVDISPRFYGrhhqdilAGLNAINLETLQTRNEADAILsnfvgDIGVRMFLLKSLYRSSEGKFQWRI 172
Cdd:pfam12697  76 AAA-----AALVVGVLVAPLAAP-------PGLLAALLALLARLGAALAAP-----AWLAAESLARGFLDDLPADAEWAA 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754529350  173 NLPVIEEQIDNIGEPLPEEAHIDTPTLFIRGSESGYIEDKDKAVIEKhFTQYTLETVQGASHFVHaEKPKEVIQL 247
Cdd:pfam12697 139 ALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPELAQRLLAA-LAGARLVVLPGAGHLPL-DDPEEVAEA 211
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 14-117 4.78e-14

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: 69.17  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   14 LVILHGLFGSSDNWMTVTKELALK-YNVYVLDARNHGQSP--HENVHTYQAMAADLKQFLD----DHNIEKPVLIGHSMG 86
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSDgkRGHVPSFDDYVDDLDTFVDkireEHPGLPLFLLGHSMG 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 754529350   87 GKTIMRFAAEYKGVAEKLIVVdiSPRFYGRH 117
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLILS--APALKIKP 115
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 13-104 5.94e-12

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 60.61  E-value: 5.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  13 PLVILHGLFGSSDNWMTVTKEL-ALKYNVYVLDARNHGQSPHENVhtyQAMAADLKQFLDDHNIEKPVLIGHSMGGkTIM 91
Cdd:COG1075    7 PVVLVHGLGGSAASWAPLAPRLrAAGYPVYALNYPSTNGSIEDSA---EQLAAFVDAVLAATGAEKVDLVGHSMGG-LVA 82

                         90
                 ....*....|...
gi 754529350  92 RFAAEYKGVAEKL 104
Cdd:COG1075   83 RYYLKRLGGAAKV 95
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 11-96 2.73e-11

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 61.78  E-value: 2.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  11 GKP-LVILHGLFGSSDNWMTVTKELAlKYNVYVLDARNHGQSPHENVHTYQAMAADLKQFLDDHNIEKPVLIGHSMGGKT 89
Cdd:PRK11126   1 GLPwLVFLHGLLGSGQDWQPVGEALP-DYPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRI 79


                 ....*..
gi 754529350  90 IMRFAAE 96
Cdd:PRK11126  80 AMYYACQ 86
PLN02578 PLN02578
hydrolase
 2-113 8.68e-10

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 58.31  E-value: 8.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   2 KLFYRETGEGKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQSPHENVHtYQAM--AADLKQFLDDHNIEKPV 79
Cdd:PLN02578  77 KIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIE-YDAMvwRDQVADFVKEVVKEPAV 155

                         90       100       110
                 ....*....|....*....|....*....|....
gi 754529350  80 LIGHSMGGKTIMRFAAEYKGVAEKLIVVDISPRF 113
Cdd:PLN02578 156 LVGNSLGGFTALSTAVGYPELVAGVALLNSAGQF 189
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
15-254 8.49e-09

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 54.56  E-value: 8.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  15 VILHGLFGSSDNWMTVTKELALK-YNVYVLDARNHGQSPHENVH-TYQAMAADLKQFLDD--HNIEKPVLIGHSMGGKTI 90
Cdd:COG1647   19 LLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSPEDLLKtTWEDWLEDVEEAYEIlkAGYDKVIVIGLSMGGLLA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  91 MRFAAEYKGVAeKLIVvdISPRFYGRHHQDILAGLNAINLETLQTRNEADAILSNFVGDI-GVRMFLLKSLYRSSEgkfQ 169
Cdd:COG1647   99 LLLAARYPDVA-GLVL--LSPALKIDDPSAPLLPLLKYLARSLRGIGSDIEDPEVAEYAYdRTPLRALAELQRLIR---E 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350 170 WRINLPvieeqidnigeplpeeaHIDTPTLFIRGSESGYIEDKDKAVIEKHFTQYTLETV--QGASHFVHAEKPKE-VIQ 246
Cdd:COG1647  173 VRRDLP-----------------KITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVwlEDSGHVITLDKDREeVAE 235


                 ....*...
gi 754529350 247 LIENFIEN 254
Cdd:COG1647  236 EILDFLER 243
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 4-254 4.84e-07

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 49.53  E-value: 4.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   4 FYRETGEGKP---LVILHGLFGSSDNWMTVTKELA-LKYNVYVLDARNHGQS---PHE----NVHTYQAMAADLKQ--FL 70
Cdd:COG1073   27 LYLPAGASKKypaVVVAHGNGGVKEQRALYAQRLAeLGFNVLAFDYRGYGESegePREegspERRDARAAVDYLRTlpGV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  71 DDHNIekpVLIGHSMGGKTIMRFAAEYKGVaeKLIVVDisprfygrhhqdilAGLNAINLETLQTRNEADailsnfvgdi 150
Cdd:COG1073  107 DPERI---GLLGISLGGGYALNAAATDPRV--KAVILD--------------SPFTSLEDLAAQRAKEAR---------- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350 151 GVRMFLLKSLYRSSEGKFqwrinlpvIEEQIDnigePLPEEAHIDTPTLFIRGsesgyieDKDKAV----IEKHFTQYT- 225
Cdd:COG1073  158 GAYLPGVPYLPNVRLASL--------LNDEFD----PLAKIEKISRPLLFIHG-------EKDEAVpfymSEDLYEAAAe 218

                        250       260       270
                 ....*....|....*....|....*....|...
gi 754529350 226 ---LETVQGASHF-VHAEKPKEVIQLIENFIEN 254
Cdd:COG1073  219 pkeLLIVPGAGHVdLYDRPEEEYFDKLAEFFKK 251
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 5-112 2.65e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 47.43  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   5 YRETG-EGKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQS--------PHENVHTYQAMAADLKQFLDDHNI 75
Cdd:PLN02824  22 YQRAGtSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSdkpnprsaPPNSFYTFETWGEQLNDFCSDVVG 101

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 754529350  76 EKPVLIGHSMGGKTIMRFAAEYKGVAEKLIVVDISPR 112
Cdd:PLN02824 102 DPAFVICNSVGGVVGLQAAVDAPELVRGVMLINISLR 138
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 6-87 3.84e-06

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: 47.78  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   6 RETGEGKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDAR--NHGQSPHENVhtyQAMAADLKQFLDDHNIEKP-VLIG 82
Cdd:COG3319  596 RAGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPglDGGEPPPASV---EEMAARYVEAIRAVQPEGPyHLLG 672


                 ....*
gi 754529350  83 HSMGG 87
Cdd:COG3319  673 WSFGG 677
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
4-117 5.91e-06

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 46.68  E-value: 5.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   4 FYRETGEGKPLVIL-HGLFGSSDNW-MTVTKELALK--YNVYVLDARNHGQSPHENVHTY--------QAMAADLKQFLD 71
Cdd:COG0429   53 WSDPPAPSKPLVVLlHGLEGSSDSHyARGLARALYArgWDVVRLNFRGCGGEPNLLPRLYhsgdtedlVWVLAHLRARYP 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754529350  72 DHNIekpVLIGHSMGGKTIMRFAAEYKGVAEKLI-VVDISP----------------RFYGRH 117
Cdd:COG0429  133 YAPL---YAVGFSLGGNLLLKYLGEQGDDAPPLKaAVAVSPpldlaasadrlergfnRLYQRY 192
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
3-125 1.04e-05

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 45.39  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   3 LFYRETGEGK-PLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQSPHENVHTYQAMAADLKQFLDDhnieKPVLI 81
Cdd:PRK10349   4 IWWQTKGQGNvHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPD----KAIWL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 754529350  82 GHSMGGKTIMRFAAEYKGVAEKLIVVDISPRFYGRH-----HQDILAGL 125
Cdd:PRK10349  80 GWSLGGLVASQIALTHPERVQALVTVASSPCFSARDewpgiKPDVLAGF 128
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
3-100 1.33e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.01  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   3 LFYRETGEGKPLVIL-HGLFGSSDN-WMTVTKELALK-YNVYVLDARNHGQSPHEnvhTYQAMAADLKQFLD------DH 73
Cdd:COG1506   14 LYLPADGKKYPVVVYvHGGPGSRDDsFLPLAQALASRgYAVLAPDYRGYGESAGD---WGGDEVDDVLAAIDylaarpYV 90

                         90       100
                 ....*....|....*....|....*..
gi 754529350  74 NIEKPVLIGHSMGGKTIMRFAAEYKGV 100
Cdd:COG1506   91 DPDRIGIYGHSYGGYMALLAAARHPDR 117
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 14-104 1.51e-05

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 45.65  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  14 LVILHGLFGSSDNWMTVTKEL-ALKYNVYVLDARNHGQSP--HENVHTYQAMAADLKQFLDDHNIEKP----VLIGHSMG 86
Cdd:PLN02652 139 LIIIHGLNEHSGRYLHFAKQLtSCGFGVYAMDWIGHGGSDglHGYVPSLDYVVEDTEAFLEKIRSENPgvpcFLFGHSTG 218

                         90
                 ....*....|....*...
gi 754529350  87 GKTIMRfAAEYKGVAEKL 104
Cdd:PLN02652 219 GAVVLK-AASYPSIEDKL 235
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
14-87 2.13e-05

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 44.44  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  14 LVILHGLFGSSDNWMTVT--KELALKYNVYV-----------LDARNHGqSPHENVHTYqaMAADLKQFLDDH-----NI 75
Cdd:COG0627   36 LYLLHGLTGTHENWTRKTgaQRLAAELGVIVvmpdggqasfyVDWTQGP-AGHYRWETY--LTEELPPLIEANfpvsaDR 112

                         90
                 ....*....|..
gi 754529350  76 EKPVLIGHSMGG 87
Cdd:COG0627  113 ERRAIAGLSMGG 124
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 13-128 9.32e-05

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 42.38  E-value: 9.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   13 PLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGqSPHENVHTYQAMAADLKQFLDDHNIEKP-VLIGHSMGGKTIM 91
Cdd:pfam00975   2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRG-RGEPPLNSIEALADEYAEALRQIQPEGPyALFGHSMGGMLAF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 754529350   92 RFAAEYKGVAEK---LIVVDISPRFYGRHHQDILAGLNAI 128
Cdd:pfam00975  81 EVARRLERQGEAvrsLFLSDASAPHTVRYEASRAPDDDEV 120
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
3-101 1.08e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 42.26  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   3 LFYRETGEGKPLVIL-HGLFGSSDNWMTVTKELALK-YNVYVLDARNHGQSPHE--------NVHTYQAMAADLKQFLD- 71
Cdd:COG0412   20 LARPAGGGPRPGVVVlHEIFGLNPHIRDVARRLAAAgYVVLAPDLYGRGGPGDDpdearalmGALDPELLAADLRAALDw 99

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 754529350  72 -----DHNIEKPVLIGHSMGGKTIMRFAAEYKGVA 101
Cdd:COG0412  100 lkaqpEVDAGRVGVVGFCFGGGLALLAAARGPDLA 134
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 7-111 4.47e-04

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 41.38  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350    7 ETGEGKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQS-----PHENVHTYQ---AMAADLKQFLDDHNIE-K 77
Cdd:PLN02980 1367 QNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSkiqnhAKETQTEPTlsvELVADLLYKLIEHITPgK 1446

                          90       100       110
                  ....*....|....*....|....*....|....
gi 754529350   78 PVLIGHSMGGKTIMRFAAEYKGVAEKLIVVDISP 111
Cdd:PLN02980 1447 VTLVGYSMGARIALYMALRFSDKIEGAVIISGSP 1480
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 11-127 4.92e-04

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 40.43  E-value: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   11 GKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQSpHENVHTY---QAMAA-------DLKQFLDD-------- 72
Cdd:pfam07819   4 GIPVLFIPGNAGSYKQVRSIASVAANLYQVLRKLLQNDNGF-HLDFFSVdfnEELSAfhgrtllDQAEYLNDairyilsl 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754529350   73 -----HNIEKPVLIGHSMGGKT--IMRFAAEYKGVAEKLIVV-----DISPRFYGRHHQDILAGLNA 127
Cdd:pfam07819  83 yasgrPGPTSVILIGHSMGGIVarAALTLPNYIPQSVNTIITlssphAKPPLTFDGDILKFYERLNA 149
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 8-86 2.13e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 38.67  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   8 TGEGKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQS--PHENVHTYQAMAADLKQFLDDhNIEKP-VLIGHS 84
Cdd:PLN02679  85 TSSGPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASdkPPGFSYTMETWAELILDFLEE-VVQKPtVLIGNS 163


                 ..
gi 754529350  85 MG 86
Cdd:PLN02679 164 VG 165
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 2-101 2.69e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 38.44  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   2 KLFYRETGEGKPLVILHGLFGSSDNWMTVTKELALKYNVYVLDARNHGQSPHENV-HTYQAMAADLKQFLDDHNIEKPVL 80
Cdd:PRK03592  18 RMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDIdYTFADHARYLDAWFDALGLDDVVL 97

                         90       100
                 ....*....|....*....|....*
gi 754529350  81 IGHSMGGKTIMRFAAEY----KGVA 101
Cdd:PRK03592  98 VGHDWGSALGFDWAARHpdrvRGIA 122
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
15-107 4.00e-03

Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 37.14  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  15 VILHGLFGSS-DNWMT-VTKELAlkyNVYVLDARNHgQSPHenvhtYQAMAADLKQFLDDHNiEKPVLIGHSMGGKTIMR 92
Cdd:COG3545    1 LIVPGLGGSGpDHWQSwWERELP---TVRRVEQPDW-DRPD-----LDDWLAALDAAVAAAD-GPVVLVAHSLGCLAVAH 70

                         90
                 ....*....|....*
gi 754529350  93 FAAEYKGVAEKLIVV 107
Cdd:COG3545   71 WAARLPRKVAGALLV 85
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 12-87 4.17e-03

Pancreatic lipase-like enzymes. 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: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 37.61  E-value: 4.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350  12 KPLVIL-HGlFGSS--DNWMTVTKELALK---YNVYVLDARNhGQSPH-----ENVhtyQAMAADLKQFLD------DHN 74
Cdd:cd00707   36 RPTRFIiHG-WTSSgeESWISDLRKAYLSrgdYNVIVVDWGR-GANPNypqavNNT---RVVGAELAKFLDflvdntGLS 110

                         90
                 ....*....|...
gi 754529350  75 IEKPVLIGHSMGG 87
Cdd:cd00707  111 LENVHLIGHSLGA 123
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 12-57 5.41e-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: 214008  Cd Length: 280  Bit Score: 37.21  E-value: 5.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 754529350  12 KPLVILHGLFGSSDNWMT--------VTKELALKYNVYVLDARNHGQSP-HENVH 57
Cdd:cd12809   40 YPIVLIHGGGQTGTNWLNtpdgrpgwASYFLEKGYEVYIVDQPGRGRSPwNPEVG 94
COG4099 COG4099
Predicted peptidase [General function prediction only];
7-97 8.92e-03

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 36.48  E-value: 8.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529350   7 ETGEGKPLVI-LHGLFGSSDNWMTVTKELALKYnVYVLDARNHG------QSPHENVHTYQAMAADLKQFLDDHNIEKPV 79
Cdd:COG4099   44 DPGKKYPLVLfLHGAGERGTDNEKQLTHGAPKF-INPENQAKFPaivlapQCPEDDYWSDTKALDAVLALLDDLIAEYRI 122

                         90       100
                 ....*....|....*....|....
gi 754529350  80 ------LIGHSMGGKTIMRFAAEY 97
Cdd:COG4099  123 dpdriyLTGLSMGGYGTWDLAARY 146
 
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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