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Conserved domains on  [gi|1215507674|gb|ASK90467|]
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alpha/beta hydrolase [Xanthomonas citri pv. vignicola]

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

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
416-508 5.88e-15

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 pfam08386:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 98  Bit Score: 70.44  E-value: 5.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 416 GNAVAEMFfAPCKVWPSKPAPAAASAPFRSTLPVLLLSGALDPVTPPRYAERVLQGLPNGRHVIAPGQGHGVFRLG--CM 493
Cdd:pfam08386   4 GAYWAEGL-LSCAGWPVPPVPPPDESTAKGAPPVLLVQGERDPATPYEGARELARALGGAVLVTVQGAGHGAYIGGnaCV 82
                          90
                  ....*....|....*
gi 1215507674 494 PKVLSQFMQTADAKA 508
Cdd:pfam08386  83 DKAVDAYLLTGTLPA 97
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
148-261 4.15e-09

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: 57.13  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 148 RKQRDIFLVDQRGTGGSHPLECRDAagkplaldnsseataeqltayaarcadglrndadpryYTTSEAIGDLDAVRAALG 227
Cdd:pfam00561  25 RDGFRVIALDLRGFGKSSRPKAQDD-------------------------------------YRTDDLAEDLEYILEALG 67
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1215507674 228 VQTLNLIGASYGTRVAQHYAARYPQHTRTVVIDG 261
Cdd:pfam00561  68 LEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLG 101
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
104-320 4.79e-08

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: 53.85  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 104 LKIAWLESdagGGSAPdPVFFIAGGPGqSATEVAAIVDmglhEVRKQRDIFLVDQRGTGGShplecrdaagkplaldnss 183
Cdd:COG0596    12 VRLHYREA---GPDGP-PVVLLHGLPG-SSYEWRPLIP----ALAAGYRVIAPDLRGHGRS------------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 184 eataeqltayaarcadglrnDADPRYYTTSEAIGDLDAVRAALGVQTLNLIGASYGTRVAQHYAARYPQHTRTvvidgva 263
Cdd:COG0596    64 --------------------DKPAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAG------- 116
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1215507674 264 pndLVIGGEFARTFEDAIALQSaqcRQQPACAKRFPVDTATQLRQVVERLRqAPVAV 320
Cdd:COG0596   117 ---LVLVDEVLAALAEPLRRPG---LAPEALAALLRALARTDLRERLARIT-VPTLV 166
 
Name Accession Description Interval E-value
Abhydrolase_4 pfam08386
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear ...
416-508 5.88e-15

TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.


Pssm-ID: 429964 [Multi-domain]  Cd Length: 98  Bit Score: 70.44  E-value: 5.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 416 GNAVAEMFfAPCKVWPSKPAPAAASAPFRSTLPVLLLSGALDPVTPPRYAERVLQGLPNGRHVIAPGQGHGVFRLG--CM 493
Cdd:pfam08386   4 GAYWAEGL-LSCAGWPVPPVPPPDESTAKGAPPVLLVQGERDPATPYEGARELARALGGAVLVTVQGAGHGAYIGGnaCV 82
                          90
                  ....*....|....*
gi 1215507674 494 PKVLSQFMQTADAKA 508
Cdd:pfam08386  83 DKAVDAYLLTGTLPA 97
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
148-261 4.15e-09

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: 57.13  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 148 RKQRDIFLVDQRGTGGSHPLECRDAagkplaldnsseataeqltayaarcadglrndadpryYTTSEAIGDLDAVRAALG 227
Cdd:pfam00561  25 RDGFRVIALDLRGFGKSSRPKAQDD-------------------------------------YRTDDLAEDLEYILEALG 67
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1215507674 228 VQTLNLIGASYGTRVAQHYAARYPQHTRTVVIDG 261
Cdd:pfam00561  68 LEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLG 101
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
104-320 4.79e-08

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: 53.85  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 104 LKIAWLESdagGGSAPdPVFFIAGGPGqSATEVAAIVDmglhEVRKQRDIFLVDQRGTGGShplecrdaagkplaldnss 183
Cdd:COG0596    12 VRLHYREA---GPDGP-PVVLLHGLPG-SSYEWRPLIP----ALAAGYRVIAPDLRGHGRS------------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 184 eataeqltayaarcadglrnDADPRYYTTSEAIGDLDAVRAALGVQTLNLIGASYGTRVAQHYAARYPQHTRTvvidgva 263
Cdd:COG0596    64 --------------------DKPAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAG------- 116
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1215507674 264 pndLVIGGEFARTFEDAIALQSaqcRQQPACAKRFPVDTATQLRQVVERLRqAPVAV 320
Cdd:COG0596   117 ---LVLVDEVLAALAEPLRRPG---LAPEALAALLRALARTDLRERLARIT-VPTLV 166
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
446-488 6.86e-06

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: 47.30  E-value: 6.86e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1215507674 446 TLPVLLLSGALDPVTPPRYAERVLQGLPNGRHVIAPGQGHGVF 488
Cdd:COG0596   161 TVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPP 203
 
Name Accession Description Interval E-value
Abhydrolase_4 pfam08386
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear ...
416-508 5.88e-15

TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.


Pssm-ID: 429964 [Multi-domain]  Cd Length: 98  Bit Score: 70.44  E-value: 5.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 416 GNAVAEMFfAPCKVWPSKPAPAAASAPFRSTLPVLLLSGALDPVTPPRYAERVLQGLPNGRHVIAPGQGHGVFRLG--CM 493
Cdd:pfam08386   4 GAYWAEGL-LSCAGWPVPPVPPPDESTAKGAPPVLLVQGERDPATPYEGARELARALGGAVLVTVQGAGHGAYIGGnaCV 82
                          90
                  ....*....|....*
gi 1215507674 494 PKVLSQFMQTADAKA 508
Cdd:pfam08386  83 DKAVDAYLLTGTLPA 97
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
148-261 4.15e-09

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: 57.13  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 148 RKQRDIFLVDQRGTGGSHPLECRDAagkplaldnsseataeqltayaarcadglrndadpryYTTSEAIGDLDAVRAALG 227
Cdd:pfam00561  25 RDGFRVIALDLRGFGKSSRPKAQDD-------------------------------------YRTDDLAEDLEYILEALG 67
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1215507674 228 VQTLNLIGASYGTRVAQHYAARYPQHTRTVVIDG 261
Cdd:pfam00561  68 LEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLG 101
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
104-320 4.79e-08

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: 53.85  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 104 LKIAWLESdagGGSAPdPVFFIAGGPGqSATEVAAIVDmglhEVRKQRDIFLVDQRGTGGShplecrdaagkplaldnss 183
Cdd:COG0596    12 VRLHYREA---GPDGP-PVVLLHGLPG-SSYEWRPLIP----ALAAGYRVIAPDLRGHGRS------------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215507674 184 eataeqltayaarcadglrnDADPRYYTTSEAIGDLDAVRAALGVQTLNLIGASYGTRVAQHYAARYPQHTRTvvidgva 263
Cdd:COG0596    64 --------------------DKPAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAG------- 116
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1215507674 264 pndLVIGGEFARTFEDAIALQSaqcRQQPACAKRFPVDTATQLRQVVERLRqAPVAV 320
Cdd:COG0596   117 ---LVLVDEVLAALAEPLRRPG---LAPEALAALLRALARTDLRERLARIT-VPTLV 166
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
446-488 6.86e-06

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: 47.30  E-value: 6.86e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1215507674 446 TLPVLLLSGALDPVTPPRYAERVLQGLPNGRHVIAPGQGHGVF 488
Cdd:COG0596   161 TVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPP 203
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
446-489 1.72e-03

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 39.99  E-value: 1.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1215507674 446 TLPVLLLSGALDPVTPPRYAERVLQGL-PNGRHVIAPGQGHGVFR 489
Cdd:COG2267   160 DVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLLPGARHELLN 204
 
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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