NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|30688480|ref|NP_851055|]
View 

alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11427000)

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

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
46-162 4.78e-12

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: 64.64  E-value: 4.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480  46 DGRYLAYRESGVDRDNanykIIVVHGFNSSKDTefpiPKDVIEELGIYF--VFYDRAGYGESD-PHPSRTVKSEAYDIQE 122
Cdd:COG0596  10 DGVRLHYREAGPDGPP----VVLLHGLPGSSYE----WRPLIPALAAGYrvIAPDLRGHGRSDkPAGGYTLDDLADDLAA 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 30688480 123 LADKLKIGPkFYVLGISLGAYSVYSCLKYIPHRLAGAVLM 162
Cdd:COG0596  82 LLDALGLER-VVLVGHSMGGMVALELAARHPERVAGLVLV 120
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
66-327 5.96e-12

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam00561:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 64.83  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480    66 IIVVHGFNSSKDTEFPIPKDvIEELGiYFVF-YDRAGYGESDPHPSRT---VKSEAYDIQELADKLKIGpKFYVLGISLG 141
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPA-LARDG-FRVIaLDLRGFGKSSRPKAQDdyrTDDLAEDLEYILEALGLE-KVNLVGHSMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480   142 AY-SVYSCLKYiPHRLAGAVLMVPFVnywwtkvPQEKLSKALELMPKKDQWTFKVahYVPWLLYWWLTQklFPSSSMVTg 220
Cdd:pfam00561  80 GLiALAYAAKY-PDRVKALVLLGALD-------PPHELDEADRFILALFPGFFDG--FVADFAPNPLGR--LVAKLLAL- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480   221 nnaLCSDKDLVVIKKKMENPRPGLEKVRQQGdhecLHRDMIAGFATWefdPTELENPF-AEGEGSVHVWQGMEDRIIPYE 299
Cdd:pfam00561 147 ---LLLRLRLLKALPLLNKRFPSGDYALAKS----LVTGALLFIETW---STELRAKFlGRLDEPTLIIWGDQDPLVPPQ 216
                         250       260
                  ....*....|....*....|....*...
gi 30688480   300 INRYISEKLPWIKYHEVLGYGHLLNAEE 327
Cdd:pfam00561 217 ALEKLAQLFPNARLVVIPDAGHFAFLEG 244
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
46-162 4.78e-12

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: 64.64  E-value: 4.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480  46 DGRYLAYRESGVDRDNanykIIVVHGFNSSKDTefpiPKDVIEELGIYF--VFYDRAGYGESD-PHPSRTVKSEAYDIQE 122
Cdd:COG0596  10 DGVRLHYREAGPDGPP----VVLLHGLPGSSYE----WRPLIPALAAGYrvIAPDLRGHGRSDkPAGGYTLDDLADDLAA 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 30688480 123 LADKLKIGPkFYVLGISLGAYSVYSCLKYIPHRLAGAVLM 162
Cdd:COG0596  82 LLDALGLER-VVLVGHSMGGMVALELAARHPERVAGLVLV 120
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
66-327 5.96e-12

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: 64.83  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480    66 IIVVHGFNSSKDTEFPIPKDvIEELGiYFVF-YDRAGYGESDPHPSRT---VKSEAYDIQELADKLKIGpKFYVLGISLG 141
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPA-LARDG-FRVIaLDLRGFGKSSRPKAQDdyrTDDLAEDLEYILEALGLE-KVNLVGHSMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480   142 AY-SVYSCLKYiPHRLAGAVLMVPFVnywwtkvPQEKLSKALELMPKKDQWTFKVahYVPWLLYWWLTQklFPSSSMVTg 220
Cdd:pfam00561  80 GLiALAYAAKY-PDRVKALVLLGALD-------PPHELDEADRFILALFPGFFDG--FVADFAPNPLGR--LVAKLLAL- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480   221 nnaLCSDKDLVVIKKKMENPRPGLEKVRQQGdhecLHRDMIAGFATWefdPTELENPF-AEGEGSVHVWQGMEDRIIPYE 299
Cdd:pfam00561 147 ---LLLRLRLLKALPLLNKRFPSGDYALAKS----LVTGALLFIETW---STELRAKFlGRLDEPTLIIWGDQDPLVPPQ 216
                         250       260
                  ....*....|....*....|....*...
gi 30688480   300 INRYISEKLPWIKYHEVLGYGHLLNAEE 327
Cdd:pfam00561 217 ALEKLAQLFPNARLVVIPDAGHFAFLEG 244
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
66-174 1.36e-06

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: 48.75  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480    66 IIVVHGFNSSKDTEFpipkDVIEEL---GIYFVFYDRAGYGESDPHPSRtVKS-EAY--DIQELADKLK---IGPKFYVL 136
Cdd:pfam12146   7 VVLVHGLGEHSGRYA----HLADALaaqGFAVYAYDHRGHGRSDGKRGH-VPSfDDYvdDLDTFVDKIReehPGLPLFLL 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 30688480   137 GISLGAYSVYS-CLKYiPHRLAGAVLMVPFVNYWWTKVP 174
Cdd:pfam12146  82 GHSMGGLIAALyALRY-PDKVDGLILSAPALKIKPYLAP 119
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
46-162 4.78e-12

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: 64.64  E-value: 4.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480  46 DGRYLAYRESGVDRDNanykIIVVHGFNSSKDTefpiPKDVIEELGIYF--VFYDRAGYGESD-PHPSRTVKSEAYDIQE 122
Cdd:COG0596  10 DGVRLHYREAGPDGPP----VVLLHGLPGSSYE----WRPLIPALAAGYrvIAPDLRGHGRSDkPAGGYTLDDLADDLAA 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 30688480 123 LADKLKIGPkFYVLGISLGAYSVYSCLKYIPHRLAGAVLM 162
Cdd:COG0596  82 LLDALGLER-VVLVGHSMGGMVALELAARHPERVAGLVLV 120
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
66-327 5.96e-12

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: 64.83  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480    66 IIVVHGFNSSKDTEFPIPKDvIEELGiYFVF-YDRAGYGESDPHPSRT---VKSEAYDIQELADKLKIGpKFYVLGISLG 141
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPA-LARDG-FRVIaLDLRGFGKSSRPKAQDdyrTDDLAEDLEYILEALGLE-KVNLVGHSMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480   142 AY-SVYSCLKYiPHRLAGAVLMVPFVnywwtkvPQEKLSKALELMPKKDQWTFKVahYVPWLLYWWLTQklFPSSSMVTg 220
Cdd:pfam00561  80 GLiALAYAAKY-PDRVKALVLLGALD-------PPHELDEADRFILALFPGFFDG--FVADFAPNPLGR--LVAKLLAL- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480   221 nnaLCSDKDLVVIKKKMENPRPGLEKVRQQGdhecLHRDMIAGFATWefdPTELENPF-AEGEGSVHVWQGMEDRIIPYE 299
Cdd:pfam00561 147 ---LLLRLRLLKALPLLNKRFPSGDYALAKS----LVTGALLFIETW---STELRAKFlGRLDEPTLIIWGDQDPLVPPQ 216
                         250       260
                  ....*....|....*....|....*...
gi 30688480   300 INRYISEKLPWIKYHEVLGYGHLLNAEE 327
Cdd:pfam00561 217 ALEKLAQLFPNARLVVIPDAGHFAFLEG 244
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
41-165 1.66e-08

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 54.24  E-value: 1.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480  41 RIKLSDGRYLAYRESGVDrDNANYKIIVVHGFNSSKDTeFpipKDVIEEL---GIYFVFYDRAGYGESDPHPSRTVKSEA 117
Cdd:COG2267   7 TLPTRDGLRLRGRRWRPA-GSPRGTVVLVHGLGEHSGR-Y---AELAEALaaaGYAVLAFDLRGHGRSDGPRGHVDSFDD 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 30688480 118 Y--DIQELADKLKIGP--KFYVLGISLGAYSVYSCLKYIPHRLAGAVLMVPF 165
Cdd:COG2267  82 YvdDLRAALDALRARPglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA 133
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
59-168 3.44e-07

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 50.40  E-value: 3.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480  59 RDNANYKIIV-VHGFNSSKDTEFPIPKDVIEELGIYFVFYDRAGYGESDPHPSRtvkSEAYDIQELADKLK----IGP-K 132
Cdd:COG1506  18 ADGKKYPVVVyVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGG---DEVDDVLAAIDYLAarpyVDPdR 94
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30688480 133 FYVLGISLGAYSVYSCLKYIPHRLAGAVLMVPFVNY 168
Cdd:COG1506  95 IGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDL 130
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
66-174 1.36e-06

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: 48.75  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480    66 IIVVHGFNSSKDTEFpipkDVIEEL---GIYFVFYDRAGYGESDPHPSRtVKS-EAY--DIQELADKLK---IGPKFYVL 136
Cdd:pfam12146   7 VVLVHGLGEHSGRYA----HLADALaaqGFAVYAYDHRGHGRSDGKRGH-VPSfDDYvdDLDTFVDKIReehPGLPLFLL 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 30688480   137 GISLGAYSVYS-CLKYiPHRLAGAVLMVPFVNYWWTKVP 174
Cdd:pfam12146  82 GHSMGGLIAALyALRY-PDKVDGLILSAPALKIKPYLAP 119
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
66-166 9.62e-06

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 45.93  E-value: 9.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480    66 IIVVHGFNSSkdtefpiPKDVIEEL--GIYFVFYDRAGYGESDPHPSRTVKSEayDIQELADKLKIGPKFYVLGISLGAY 143
Cdd:pfam12697   1 VVLVHGAGLS-------AAPLAALLaaGVAVLAPDLPGHGSSSPPPLDLADLA--DLAALLDELGAARPVVLVGHSLGGA 71
                          90       100
                  ....*....|....*....|...
gi 30688480   144 SVYSCLKYIPHRlagAVLMVPFV 166
Cdd:pfam12697  72 VALAAAAAALVV---GVLVAPLA 91
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
66-169 5.41e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 44.14  E-value: 5.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688480  66 IIVVHGFNSSKDT------EFPipkdvieELGIYFVFYDRAGYGESDPHPSRTVKSEAYDIQELADKL---------KIG 130
Cdd:COG1073  40 VVVAHGNGGVKEQralyaqRLA-------ELGFNVLAFDYRGYGESEGEPREEGSPERRDARAAVDYLrtlpgvdpeRIG 112
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 30688480 131 pkfyVLGISLG-AYSvyscLKY--IPHRLAGAVLMVPFVNYW 169
Cdd:COG1073 113 ----LLGISLGgGYA----LNAaaTDPRVKAVILDSPFTSLE 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH