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Conserved domains on  [gi|1443441175|emb|SUW23406|]
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putative hydrolase [Brucella abortus]

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, ...
 37-230 5.68e-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: 139.37  E-value: 5.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  37 SPAAFAEVNGIEMYYRVVG-KGPPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRSTRTDEPITYRLMADDYVA 115
Cdd:COG0596     2 STPRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175 116 LLDYLHIDKVDLVGWSDGGIIGLDIAMRYPDRLNSLFAQAANVspagnAGYIEARAAGKPLPelrhyENIEREIRALWAN 195
Cdd:COG0596    82 LLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL-----AALAEPLRRPGLAP-----EALAALLRALART 151

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1443441175 196 EPnytDEDLAAIRVRTAIVIGDHDTVVTRAVLRFI 230
Cdd:COG0596   152 DL---RERLARITVPTLVIWGEKDPIVPPALARRL 183
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 37-230 5.68e-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: 139.37  E-value: 5.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  37 SPAAFAEVNGIEMYYRVVG-KGPPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRSTRTDEPITYRLMADDYVA 115
Cdd:COG0596     2 STPRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175 116 LLDYLHIDKVDLVGWSDGGIIGLDIAMRYPDRLNSLFAQAANVspagnAGYIEARAAGKPLPelrhyENIEREIRALWAN 195
Cdd:COG0596    82 LLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL-----AALAEPLRRPGLAP-----EALAALLRALART 151

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1443441175 196 EPnytDEDLAAIRVRTAIVIGDHDTVVTRAVLRFI 230
Cdd:COG0596   152 DL---RERLARITVPTLVIWGEKDPIVPPALARRL 183
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 58-161 6.61e-17

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: 76.77  E-value: 6.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  58 PPILLIHGGLSDQHVWDAQLPILAR-HHSVIVADSRGQGRSTRTDEPITYRL--MADDYVALLDYLHIDKVDLVGWSDGG 134
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKAQDDYRTddLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100
                  ....*....|....*....|....*..
gi 1443441175 135 IIGLDIAMRYPDRLNSLFAQAANVSPA 161
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPH 107
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 41-181 2.57e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 76.91  E-value: 2.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  41 FAEVNGIEMYYRVVGK--GPPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRSTRTDEPITYRLMADDYVALLD 118
Cdd:PRK14875  113 KARIGGRTVRYLRLGEgdGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLD 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443441175 119 YLHIDKVDLVGWSDGGIIGLDIAMRYPDRLNSLfaqaANVSPAG-----NAGYIEARAAGKPLPELRH 181
Cdd:PRK14875  193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASL----TLIAPAGlgpeiNGDYIDGFVAAESRRELKP 256
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 58-156 9.78e-10

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: 56.75  E-value: 9.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  58 PPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRStRTDEPITYRLMADDYVALLDylhiDKVDLVGWSDGGIIG 137
Cdd:TIGR01738   5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRS-RGFGPLSLADMAEAIAAQAP----DPAIWLGWSLGGLVA 79

                          90
                  ....*....|....*....
gi 1443441175 138 LDIAMRYPDRLNSLFAQAA 156
Cdd:TIGR01738  80 LHIAATHPDRVRALVTVAS 98
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 37-230 5.68e-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: 139.37  E-value: 5.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  37 SPAAFAEVNGIEMYYRVVG-KGPPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRSTRTDEPITYRLMADDYVA 115
Cdd:COG0596     2 STPRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175 116 LLDYLHIDKVDLVGWSDGGIIGLDIAMRYPDRLNSLFAQAANVspagnAGYIEARAAGKPLPelrhyENIEREIRALWAN 195
Cdd:COG0596    82 LLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL-----AALAEPLRRPGLAP-----EALAALLRALART 151

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1443441175 196 EPnytDEDLAAIRVRTAIVIGDHDTVVTRAVLRFI 230
Cdd:COG0596   152 DL---RERLARITVPTLVIWGEKDPIVPPALARRL 183
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 58-161 6.61e-17

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: 76.77  E-value: 6.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  58 PPILLIHGGLSDQHVWDAQLPILAR-HHSVIVADSRGQGRSTRTDEPITYRL--MADDYVALLDYLHIDKVDLVGWSDGG 134
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKAQDDYRTddLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100
                  ....*....|....*....|....*..
gi 1443441175 135 IIGLDIAMRYPDRLNSLFAQAANVSPA 161
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPH 107
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 41-181 2.57e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 76.91  E-value: 2.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  41 FAEVNGIEMYYRVVGK--GPPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRSTRTDEPITYRLMADDYVALLD 118
Cdd:PRK14875  113 KARIGGRTVRYLRLGEgdGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLD 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443441175 119 YLHIDKVDLVGWSDGGIIGLDIAMRYPDRLNSLfaqaANVSPAG-----NAGYIEARAAGKPLPELRH 181
Cdd:PRK14875  193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASL----TLIAPAGlgpeiNGDYIDGFVAAESRRELKP 256
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 35-147 1.08e-14

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 71.56  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  35 PASPAAFAEVNGIEMYYRVVGKGPPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRSTRTDepITYRLmAD--D 112
Cdd:PRK03592    5 PPGEMRRVEVLGSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPD--IDYTF-ADhaR 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1443441175 113 YV-ALLDYLHIDKVDLVGWSDGGIIGLDIAMRYPDR 147
Cdd:PRK03592   82 YLdAWFDALGLDDVVLVGHDWGSALGFDWAARHPDR 117
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
41-231 4.17e-12

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 63.10  E-value: 4.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  41 FAEVNGIEMYYRVVGK----GPPILLIHGGLSDQHVWDAQLPILARH-HSVIVADSRGQGRSTRTDEPI-TYRLMADDYV 114
Cdd:COG2267     8 LPTRDGLRLRGRRWRPagspRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVdSFDDYVDDLR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175 115 ALLDYLHID---KVDLVGWSDGGIIGLDIAMRYPDRLNSLFAqaanVSPAGNAgyiearaagKPLPELRHyenieREIRA 191
Cdd:COG2267    88 AALDALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVL----LAPAYRA---------DPLLGPSA-----RWLRA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1443441175 192 LWANepnytdEDLAAIRVRTAIVIGDHDTVV-TRAVLRFID 231
Cdd:COG2267   150 LRLA------EALARIDVPVLVLHGGADRVVpPEAARRLAA 184
PRK10673 PRK10673
esterase;
58-153 9.70e-12

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 62.83  E-value: 9.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  58 PPILLIHGGLSDQHvwdaQLPILAR----HHSVIVADSRGQGRSTRTDEpITYRLMADDYVALLDYLHIDKVDLVGWSDG 133
Cdd:PRK10673   17 SPIVLVHGLFGSLD----NLGVLARdlvnDHDIIQVDMRNHGLSPRDPV-MNYPAMAQDLLDTLDALQIEKATFIGHSMG 91

                          90       100
                  ....*....|....*....|
gi 1443441175 134 GIIGLDIAMRYPDRLNSLFA 153
Cdd:PRK10673   92 GKAVMALTALAPDRIDKLVA 111
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 58-156 9.78e-10

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: 56.75  E-value: 9.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  58 PPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRStRTDEPITYRLMADDYVALLDylhiDKVDLVGWSDGGIIG 137
Cdd:TIGR01738   5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRS-RGFGPLSLADMAEAIAAQAP----DPAIWLGWSLGGLVA 79

                          90
                  ....*....|....*....
gi 1443441175 138 LDIAMRYPDRLNSLFAQAA 156
Cdd:TIGR01738  80 LHIAATHPDRVRALVTVAS 98
PRK05855 PRK05855
SDR family oxidoreductase;
44-129 1.02e-09

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 57.68  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  44 VNGIEMYYRVVG--KGPPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRSTRTDEPITYRL--MADDYVALLDY 119
Cdd:PRK05855   10 SDGVRLAVYEWGdpDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLarLADDFAAVIDA 89

                          90
                  ....*....|.
gi 1443441175 120 LHIDK-VDLVG 129
Cdd:PRK05855   90 VSPDRpVHLLA 100
PLN02578 PLN02578
hydrolase
 13-178 7.37e-09

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 54.85  E-value: 7.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  13 ALGLAAFFPSAVSVESHARMTIPASPAA--FAEVNGIEMYYRVVGKGPPILLIHG-GLSDQHvWDAQLPILARHHSVIVA 89
Cdd:PLN02578   40 ASGVSVMGSSSASQSVQGLERLPFKKEGynFWTWRGHKIHYVVQGEGLPIVLIHGfGASAFH-WRYNIPELAKKYKVYAL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  90 DSRGQGRSTRTDEPITYRLMADDYVALLDYLHIDKVDLVGWSDGGIIGLDIAMRYPDRLNSLfaqaANVSPAGNAGYIEA 169
Cdd:PLN02578  119 DLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGV----ALLNSAGQFGSESR 194


                  ....*....
gi 1443441175 170 RAAGKPLPE 178
Cdd:PLN02578  195 EKEEAIVVE 203
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
45-222 1.60e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.48  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  45 NGIEMYYRVV-----GKGPPILLIHGGLSDQ-HVWDAQLPILARH-HSVIVADSRGQGRSTRTdepiTYRLMADDYVALL 117
Cdd:COG1506     6 DGTTLPGWLYlpadgKKYPVVVYVHGGPGSRdDSFLPLAQALASRgYAVLAPDYRGYGESAGD----WGGDEVDDVLAAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175 118 DYLH------IDKVDLVGWSDGGIIGLDIAMRYPDRLNSLFAQAANVSPAGNAGYIEARAagkplpelrhyeniEREIRA 191
Cdd:COG1506    82 DYLAarpyvdPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYT--------------ERLMGG 147

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1443441175 192 LWANEPNYTD----EDLAAIRVRTAIVIGDHDTVV 222
Cdd:COG1506   148 PWEDPEAYAArsplAYADKLKTPLLLIHGEADDRV 182
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 57-147 1.33e-06

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 48.04  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  57 GPPILLIHGGLSDQHVWDAQLPILA-RHHSVIVADSRGQGRSTR--TDEPITYRLMADDYVALLDYLHIDKVDLVGWSDG 133
Cdd:PRK00870   46 GPPVLLLHGEPSWSYLYRKMIPILAaAGHRVIAPDLIGFGRSDKptRREDYTYARHVEWMRSWFEQLDLTDVTLVCQDWG 125

                          90
                  ....*....|....
gi 1443441175 134 GIIGLDIAMRYPDR 147
Cdd:PRK00870  126 GLIGLRLAAEHPDR 139
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
60-230 6.18e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 45.70  E-value: 6.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  60 ILLIHGGLSDQHVWDAQLPILARH-HSVIVADSRGQGRSTRTDEPITYRLMADDYVALLDYL--HIDKVDLVGWSDGGII 136
Cdd:COG1647    18 VLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILkaGYDKVIVIGLSMGGLL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175 137 GLDIAMRYPDrLNSLFAQAANVSPAGNAGYI-------------EARAAGKPLPELRHYENIE----REIRALWAnepnY 199
Cdd:COG1647    98 ALLLAARYPD-VAGLVLLSPALKIDDPSAPLlpllkylarslrgIGSDIEDPEVAEYAYDRTPlralAELQRLIR----E 172

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1443441175 200 TDEDLAAIRVRTAIVIGDHDTVVTRAVLRFI 230
Cdd:COG1647   173 VRRDLPKITAPTLIIQSRKDEVVPPESARYI 203
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 60-212 2.14e-05

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 44.00  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  60 ILLIHGGLSDQHVWDAQLpilARHHSVIVADSRGQGRSTRTDEPITyrlMADDYVALLDYLHIDK-VDLVGWSDGGIIGL 138
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALL---AAGVAVLAPDLPGHGSSSPPPLDLA---DLADLAALLDELGAARpVVLVGHSLGGAVAL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443441175 139 DIAMRYPDRlnSLFAQAANVSPAGNAGYIEARAAGKPLPELRHYENIEREIRALWANEPNYTDEDLAAIRVRTA 212
Cdd:pfam12697  75 AAAAAALVV--GVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAAL 146
COG4099 COG4099
Predicted peptidase [General function prediction only];
115-176 4.24e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 43.42  E-value: 4.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443441175 115 ALLDYL----HIDK--VDLVGWSDGGIIGLDIAMRYPDRlnslFAQAANVSPAGNAGYIEaRAAGKPL 176
Cdd:COG4099   111 ALLDDLiaeyRIDPdrIYLTGLSMGGYGTWDLAARYPDL----FAAAVPICGGGDPANAA-NLKKVPV 173
PRK08775 PRK08775
homoserine O-succinyltransferase;
47-156 4.52e-05

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 43.62  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  47 IEMYYRVVGK-GPPILLIHGGLS-DQHV----------WDAQL-----PILARHHSVIVADSRGQGRSTrtDEPITYRLM 109
Cdd:PRK08775   46 LRLRYELIGPaGAPVVFVAGGISaHRHVaatatfpekgWWEGLvgsgrALDPARFRLLAFDFIGADGSL--DVPIDTADQ 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1443441175 110 ADDYVALLDYLHIDKVD-LVGWSDGGIIGLDIAMRYPDRLNSLFAQAA 156
Cdd:PRK08775  124 ADAIALLLDALGIARLHaFVGYSYGALVGLQFASRHPARVRTLVVVSG 171
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 50-145 2.06e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 41.65  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  50 YYRVVGKGPPILLIHG-GLSDQHvWDAQLPILARHHSVIVADSRGQGRSTRTD------EPI-TYRLMADDYVALLDYLH 121
Cdd:PLN02824   22 YQRAGTSGPALVLVHGfGGNADH-WRKNTPVLAKSHRVYAIDLLGYGYSDKPNprsappNSFyTFETWGEQLNDFCSDVV 100

                          90       100
                  ....*....|....*....|....
gi 1443441175 122 IDKVDLVGWSDGGIIGLDIAMRYP 145
Cdd:PLN02824  101 GDPAFVICNSVGGVVGLQAAVDAP 124
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 58-151 2.57e-04

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 41.40  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  58 PPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRSTRTDEPITYRLMADDYV----ALLDYLHIDKVDLVGWSDG 133
Cdd:PLN03084  128 PPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVssleSLIDELKSDKVSLVVQGYF 207

                          90
                  ....*....|....*...
gi 1443441175 134 GIIGLDIAMRYPDRLNSL 151
Cdd:PLN03084  208 SPPVVKYASAHPDKIKKL 225
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 58-162 3.35e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 41.05  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  58 PPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRSTRTDEPITYRLMADDYvaLLDYL-------HIDKVDLVGW 130
Cdd:PLN02894  106 PTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKSTEETEAW--FIDSFeewrkakNLSNFILLGH 183

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1443441175 131 SDGGIIGLDIAMRYPDRLNSLFAqaanVSPAG 162
Cdd:PLN02894  184 SFGGYVAAKYALKHPEHVQHLIL----VGPAG 211
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
48-164 4.93e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 40.39  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  48 EMYYRVVGKGP-PILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRStRTDEPITYRLMADDYVALLDylhiDKVD 126
Cdd:PRK10349    3 NIWWQTKGQGNvHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRS-RGFGALSLADMAEAVLQQAP----DKAI 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1443441175 127 LVGWSDGGIIGLDIAMRYPDRLNSLFAQAAnvSPAGNA 164
Cdd:PRK10349   78 WLGWSLGGLVASQIALTHPERVQALVTVAS--SPCFSA 113
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 55-225 9.80e-04

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 39.13  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  55 GKGPPILLIHG--GLSDQHVWDAQLpiLARH-HSVIVADSRGQGRStrTDEPITYRLMA-DDYVALLDYL-HIDKVD--- 126
Cdd:COG1073    35 KKYPAVVVAHGngGVKEQRALYAQR--LAELgFNVLAFDYRGYGES--EGEPREEGSPErRDARAAVDYLrTLPGVDper 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175 127 --LVGWSDGGIIGLDIAMRYPdRLNSLFAQAANVSPAGNAGYIEARAAGKPLPELRHYENIEreiRALWANEPNYTDEDL 204
Cdd:COG1073   111 igLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAYLPGVPYLPNVR---LASLLNDEFDPLAKI 186

                         170       180
                  ....*....|....*....|.
gi 1443441175 205 AAIRVRTAIVIGDHDTVVTRA 225
Cdd:COG1073   187 EKISRPLLFIHGEKDEAVPFY 207
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 49-148 1.17e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 39.07  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  49 MYYRVVGKGPPILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRSTRtdePITYRLMADDYVA----LLDYLHIDK 124
Cdd:PRK03204   26 IHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSER---PSGFGYQIDEHARvigeFVDHLGLDR 102

                          90       100
                  ....*....|....*....|....
gi 1443441175 125 VDLVGWSDGGIIGLDIAMRYPDRL 148
Cdd:PRK03204  103 YLSMGQDWGGPISMAVAVERADRV 126
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 90-222 1.39e-03

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: 38.73  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175  90 DSRGQGRS--TRTDEPiTYRLMADDYVALLDYL----HIDKVDLVGWSDGGIIGLDIAMRYPDRLNSLFAQAANVSPAGN 163
Cdd:pfam12146  38 DHRGHGRSdgKRGHVP-SFDDYVDDLDTFVDKIreehPGLPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175 164 AGY----IEARAAGKPLPELRHYENIE-------REIRALWANEPNYTD------------------EDLAAIRVRTAIV 214
Cdd:pfam12146 117 LAPpilkLLAKLLGKLFPRLRVPNNLLpdslsrdPEVVAAYAADPLVHGgisartlyelldagerllRRAAAITVPLLLL 196


                  ....*...
gi 1443441175 215 IGDHDTVV 222
Cdd:pfam12146 197 HGGADRVV 204
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 60-148 1.81e-03

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 39.07  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443441175   60 ILLIHGGLSDQHVWDAQLPILARHHSVIVADSRGQGRS--------TRTDEPITYRLMADDYVALLDYLHIDKVDLVGWS 131
Cdd:PLN02980  1374 VLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSkiqnhakeTQTEPTLSVELVADLLYKLIEHITPGKVTLVGYS 1453

                           90
                   ....*....|....*..
gi 1443441175  132 DGGIIGLDIAMRYPDRL 148
Cdd:PLN02980  1454 MGARIALYMALRFSDKI 1470
 
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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