NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|514971580|ref|WP_016659861|]
View 

MULTISPECIES: alpha/beta fold hydrolase [Acinetobacter]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
50-234 1.15e-21

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 TIGR01738:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 89.88  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971580   50 LERAKGYSVLMGWSLGGqlaTLLADALAQSGQAPQALITLASNPCFVAQDAWPHGMVPETFQQFKQGFAKDAAATLKRFG 129
Cdd:TIGR01738  60 AAQAPDPAIWLGWSLGG---LVALHIAATHPDRVRALVTVASSPCFSAREDWPEGIKPDVLTGFQQQLSDDYQRTIERFL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971580  130 YLVCQGSAQSRQDL----QKLQSLIQPQSLTLLkQGLALLEQLNLVTILKNYPAPQYHLLAHEDQLVPCQVAEDLQNLAA 205
Cdd:TIGR01738 137 ALQTLGTPTARQDAralkQTLLARPTPNVQVLQ-AGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAP 215
                         170       180
                  ....*....|....*....|....*....
gi 514971580  206 TNLQVEVISGSHGIPLFETDVVTQKIIDY 234
Cdd:TIGR01738 216 HSELYIFAKAAHAPFLSHAEAFCALLVAF 244
 
Name Accession Description Interval E-value
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
50-234 1.15e-21

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: 89.88  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971580   50 LERAKGYSVLMGWSLGGqlaTLLADALAQSGQAPQALITLASNPCFVAQDAWPHGMVPETFQQFKQGFAKDAAATLKRFG 129
Cdd:TIGR01738  60 AAQAPDPAIWLGWSLGG---LVALHIAATHPDRVRALVTVASSPCFSAREDWPEGIKPDVLTGFQQQLSDDYQRTIERFL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971580  130 YLVCQGSAQSRQDL----QKLQSLIQPQSLTLLkQGLALLEQLNLVTILKNYPAPQYHLLAHEDQLVPCQVAEDLQNLAA 205
Cdd:TIGR01738 137 ALQTLGTPTARQDAralkQTLLARPTPNVQVLQ-AGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAP 215
                         170       180
                  ....*....|....*....|....*....
gi 514971580  206 TNLQVEVISGSHGIPLFETDVVTQKIIDY 234
Cdd:TIGR01738 216 HSELYIFAKAAHAPFLSHAEAFCALLVAF 244
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
47-203 1.31e-21

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 90.08  E-value: 1.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971580  47 QQQLERAKGYSVLMGWSLGGqlaTLLADALAQSGQAPQALITLASNPCFVAQDAWPhGMVPETFQQFKQGFAKDAAATLK 126
Cdd:PRK10349  66 EAVLQQAPDKAIWLGWSLGG---LVASQIALTHPERVQALVTVASSPCFSARDEWP-GIKPDVLAGFQQQLSDDFQRTVE 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971580 127 RFGYLVCQGSAQSRQDLQKLQSLIQPQSL---TLLKQGLALLEQLNLVTILKNYPAPQYHLLAHEDQLVPCQVAEDLQNL 203
Cdd:PRK10349 142 RFLALQTMGTETARQDARALKKTVLALPMpevDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKL 221
 
Name Accession Description Interval E-value
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
50-234 1.15e-21

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: 89.88  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971580   50 LERAKGYSVLMGWSLGGqlaTLLADALAQSGQAPQALITLASNPCFVAQDAWPHGMVPETFQQFKQGFAKDAAATLKRFG 129
Cdd:TIGR01738  60 AAQAPDPAIWLGWSLGG---LVALHIAATHPDRVRALVTVASSPCFSAREDWPEGIKPDVLTGFQQQLSDDYQRTIERFL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971580  130 YLVCQGSAQSRQDL----QKLQSLIQPQSLTLLkQGLALLEQLNLVTILKNYPAPQYHLLAHEDQLVPCQVAEDLQNLAA 205
Cdd:TIGR01738 137 ALQTLGTPTARQDAralkQTLLARPTPNVQVLQ-AGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAP 215
                         170       180
                  ....*....|....*....|....*....
gi 514971580  206 TNLQVEVISGSHGIPLFETDVVTQKIIDY 234
Cdd:TIGR01738 216 HSELYIFAKAAHAPFLSHAEAFCALLVAF 244
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
47-203 1.31e-21

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 90.08  E-value: 1.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971580  47 QQQLERAKGYSVLMGWSLGGqlaTLLADALAQSGQAPQALITLASNPCFVAQDAWPhGMVPETFQQFKQGFAKDAAATLK 126
Cdd:PRK10349  66 EAVLQQAPDKAIWLGWSLGG---LVASQIALTHPERVQALVTVASSPCFSARDEWP-GIKPDVLAGFQQQLSDDFQRTVE 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971580 127 RFGYLVCQGSAQSRQDLQKLQSLIQPQSL---TLLKQGLALLEQLNLVTILKNYPAPQYHLLAHEDQLVPCQVAEDLQNL 203
Cdd:PRK10349 142 RFLALQTMGTETARQDARALKKTVLALPMpevDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKL 221
 
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