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Conserved domains on  [gi|17538151|ref|NP_496090|]
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Acetyl-CoA hydrolase [Caenorhabditis elegans]

Protein Classification

acetyl-CoA hydrolase/transferase family protein( domain architecture ID 11418019)

acetyl-CoA hydrolase/transferase family protein such as acetyl-CoA hydrolase, which catalyzes the hydrolysis of acetyl-CoA to form CoA and acetate, and 4-hydroxybutyrate CoA-transferase, which ferments gamma-aminobutyrate (GABA) to ammonia, acetate and butyrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACH1 COG0427
Propionyl CoA:succinate CoA transferase [Energy production and conversion];
41-466 0e+00

Propionyl CoA:succinate CoA transferase [Energy production and conversion];


:

Pssm-ID: 440196 [Multi-domain]  Cd Length: 427  Bit Score: 542.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151  41 KYVSADEALAMVNSDSDIYVGNHASAPNVLLEALCRRVDsaNLNNIRMSHLILSGNCPQFDPKYHGKIQNNSLFICPGNR 120
Cdd:COG0427   8 KLVSAEEAASLIKSGDRVGVSTGAGEPKALPKALAARAE--ELFDVELVTGASLGPGALAEADLEEHFRHRSPFSGGNLR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 121 KNVNLGAADYTPIFLSEVPSLYTSGTLNVDFALITVSPPDELGFCTLGVDIDTTLAAATSAKKIIALVNSTMPRTRGHTT 200
Cdd:COG0427  86 KAINEGRVDYIPIHLSEVPRLLRSGFLPIDVALIEVSPPDEHGYFSLGTSVDNTPAAVEKAKKVIAEVNPNMPRTLGDIF 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 201 VHSSHFAAMVQTDRPIafRQSGGEEMSETEQRIGKIIAEnLVDNGATLQLGIGAIPDSALAAMKQHKDLGVHTEMFSDGV 280
Cdd:COG0427 166 IHISKIDAIVETDEPL--PELPFAPPDEVDRAIAEHIAE-LIEDGATLQLGIGGIPNAVLAGLADSKDLGIHTEMLQDGM 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 281 IDLIDRGIINNQKKAFMPGKTVSSFAFGTKEFYKKIDNNPEFYFAPCDFTNHIDIVRRNSKMTSINSAIEIDLTGQIVSD 360
Cdd:COG0427 243 LDLIEAGVITNASKTIDPGKIVTSFALGSKRLYDFLDDNPKVELRPVEYSNDPEVIARNLGVIAINSALEVDLYGQVNSE 322

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 361 SIGRNFFSGFGGQVDFM---AASPHgfdglGKAIIALPSRTTKGQT-KIVPFLTQGSGVVTTRAHARYIVTEHGIANLWG 436
Cdd:COG0427 323 SIGTRQYSGIGGQGDFArgaYLSKG-----GKSIIALPSTAKGGKIsRIVPMLKPGSHVTTTRHDVDYVVTEYGVADLRG 397

                       410       420       430
                ....*....|....*....|....*....|
gi 17538151 437 KSIRQRAYELIQISHPDDREALEKAAFDRF 466
Cdd:COG0427 398 KSPRERAEALIEIAHPDFREELREYAERAG 427
 
Name Accession Description Interval E-value
ACH1 COG0427
Propionyl CoA:succinate CoA transferase [Energy production and conversion];
41-466 0e+00

Propionyl CoA:succinate CoA transferase [Energy production and conversion];


Pssm-ID: 440196 [Multi-domain]  Cd Length: 427  Bit Score: 542.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151  41 KYVSADEALAMVNSDSDIYVGNHASAPNVLLEALCRRVDsaNLNNIRMSHLILSGNCPQFDPKYHGKIQNNSLFICPGNR 120
Cdd:COG0427   8 KLVSAEEAASLIKSGDRVGVSTGAGEPKALPKALAARAE--ELFDVELVTGASLGPGALAEADLEEHFRHRSPFSGGNLR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 121 KNVNLGAADYTPIFLSEVPSLYTSGTLNVDFALITVSPPDELGFCTLGVDIDTTLAAATSAKKIIALVNSTMPRTRGHTT 200
Cdd:COG0427  86 KAINEGRVDYIPIHLSEVPRLLRSGFLPIDVALIEVSPPDEHGYFSLGTSVDNTPAAVEKAKKVIAEVNPNMPRTLGDIF 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 201 VHSSHFAAMVQTDRPIafRQSGGEEMSETEQRIGKIIAEnLVDNGATLQLGIGAIPDSALAAMKQHKDLGVHTEMFSDGV 280
Cdd:COG0427 166 IHISKIDAIVETDEPL--PELPFAPPDEVDRAIAEHIAE-LIEDGATLQLGIGGIPNAVLAGLADSKDLGIHTEMLQDGM 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 281 IDLIDRGIINNQKKAFMPGKTVSSFAFGTKEFYKKIDNNPEFYFAPCDFTNHIDIVRRNSKMTSINSAIEIDLTGQIVSD 360
Cdd:COG0427 243 LDLIEAGVITNASKTIDPGKIVTSFALGSKRLYDFLDDNPKVELRPVEYSNDPEVIARNLGVIAINSALEVDLYGQVNSE 322

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 361 SIGRNFFSGFGGQVDFM---AASPHgfdglGKAIIALPSRTTKGQT-KIVPFLTQGSGVVTTRAHARYIVTEHGIANLWG 436
Cdd:COG0427 323 SIGTRQYSGIGGQGDFArgaYLSKG-----GKSIIALPSTAKGGKIsRIVPMLKPGSHVTTTRHDVDYVVTEYGVADLRG 397

                       410       420       430
                ....*....|....*....|....*....|
gi 17538151 437 KSIRQRAYELIQISHPDDREALEKAAFDRF 466
Cdd:COG0427 398 KSPRERAEALIEIAHPDFREELREYAERAG 427
AcetylCoA_hyd_C pfam13336
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
 308-462 2.59e-79

Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.


Pssm-ID: 433126 [Multi-domain]  Cd Length: 154  Bit Score: 243.50  E-value: 2.59e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151   308 GTKEFYKKIDNNPEFYFAPCDFTNHIDIVRRNSKMTSINSAIEIDLTGQIVSDSIGRNFFSGFGGQVDFMAASPHGFDgl 387
Cdd:pfam13336   1 GSKRLYDFLDNNPKIEMRPVDYVNDPEVIARNDKMIAINSALEVDLTGQVNSESIGGRQYSGVGGQLDFVRGAYLSKG-- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17538151   388 GKAIIALPSRTTKGQ-TKIVPFLTQGSGVVTTRAHARYIVTEHGIANLWGKSIRQRAYELIQISHPDDREALEKAA 462
Cdd:pfam13336  79 GKSIIALPSTAKDGTiSRIVPMLSPGAHVTTTRHDVDYVVTEYGIADLRGKSLRERAEALISIAHPDFRDELLEEA 154
 
Name Accession Description Interval E-value
ACH1 COG0427
Propionyl CoA:succinate CoA transferase [Energy production and conversion];
41-466 0e+00

Propionyl CoA:succinate CoA transferase [Energy production and conversion];


Pssm-ID: 440196 [Multi-domain]  Cd Length: 427  Bit Score: 542.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151  41 KYVSADEALAMVNSDSDIYVGNHASAPNVLLEALCRRVDsaNLNNIRMSHLILSGNCPQFDPKYHGKIQNNSLFICPGNR 120
Cdd:COG0427   8 KLVSAEEAASLIKSGDRVGVSTGAGEPKALPKALAARAE--ELFDVELVTGASLGPGALAEADLEEHFRHRSPFSGGNLR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 121 KNVNLGAADYTPIFLSEVPSLYTSGTLNVDFALITVSPPDELGFCTLGVDIDTTLAAATSAKKIIALVNSTMPRTRGHTT 200
Cdd:COG0427  86 KAINEGRVDYIPIHLSEVPRLLRSGFLPIDVALIEVSPPDEHGYFSLGTSVDNTPAAVEKAKKVIAEVNPNMPRTLGDIF 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 201 VHSSHFAAMVQTDRPIafRQSGGEEMSETEQRIGKIIAEnLVDNGATLQLGIGAIPDSALAAMKQHKDLGVHTEMFSDGV 280
Cdd:COG0427 166 IHISKIDAIVETDEPL--PELPFAPPDEVDRAIAEHIAE-LIEDGATLQLGIGGIPNAVLAGLADSKDLGIHTEMLQDGM 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 281 IDLIDRGIINNQKKAFMPGKTVSSFAFGTKEFYKKIDNNPEFYFAPCDFTNHIDIVRRNSKMTSINSAIEIDLTGQIVSD 360
Cdd:COG0427 243 LDLIEAGVITNASKTIDPGKIVTSFALGSKRLYDFLDDNPKVELRPVEYSNDPEVIARNLGVIAINSALEVDLYGQVNSE 322

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151 361 SIGRNFFSGFGGQVDFM---AASPHgfdglGKAIIALPSRTTKGQT-KIVPFLTQGSGVVTTRAHARYIVTEHGIANLWG 436
Cdd:COG0427 323 SIGTRQYSGIGGQGDFArgaYLSKG-----GKSIIALPSTAKGGKIsRIVPMLKPGSHVTTTRHDVDYVVTEYGVADLRG 397

                       410       420       430
                ....*....|....*....|....*....|
gi 17538151 437 KSIRQRAYELIQISHPDDREALEKAAFDRF 466
Cdd:COG0427 398 KSPRERAEALIEIAHPDFREELREYAERAG 427
AcetylCoA_hyd_C pfam13336
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
 308-462 2.59e-79

Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.


Pssm-ID: 433126 [Multi-domain]  Cd Length: 154  Bit Score: 243.50  E-value: 2.59e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151   308 GTKEFYKKIDNNPEFYFAPCDFTNHIDIVRRNSKMTSINSAIEIDLTGQIVSDSIGRNFFSGFGGQVDFMAASPHGFDgl 387
Cdd:pfam13336   1 GSKRLYDFLDNNPKIEMRPVDYVNDPEVIARNDKMIAINSALEVDLTGQVNSESIGGRQYSGVGGQLDFVRGAYLSKG-- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17538151   388 GKAIIALPSRTTKGQ-TKIVPFLTQGSGVVTTRAHARYIVTEHGIANLWGKSIRQRAYELIQISHPDDREALEKAA 462
Cdd:pfam13336  79 GKSIIALPSTAKDGTiSRIVPMLSPGAHVTTTRHDVDYVVTEYGIADLRGKSLRERAEALISIAHPDFRDELLEEA 154
AcetylCoA_hydro pfam02550
Acetyl-CoA hydrolase/transferase N-terminal domain; This family contains several enzymes which ...
 41-202 4.79e-17

Acetyl-CoA hydrolase/transferase N-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.


Pssm-ID: 251367  Cd Length: 198  Bit Score: 79.50  E-value: 4.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151    41 KYVSADEALAMVNSDSDIYVGNH--ASAPNVLLEALCRRVDsaNLNNIRMSHLI---------LSGNCPQFDPKYHGKIQ 109
Cdd:pfam02550   8 KLISPEEAASLVEIGMHIERGGFtfAGTAKAIPKYLAKRKV--ELVNAKVKTFIdlavgaflsAGPEAEVTDWKDAFLYR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538151   110 NNSLFICPGNRKNVNLGAADYTPIFLSEVPSLYTSGTLNVDFALITVSPPDELGFCTLGVDIDTTLAAATSAKKIIALVN 189
Cdd:pfam02550  86 PAPKQSGELGRKAINQGLASFVDKHLSEVPQLFEYGFVPIDVALIETTAMDDHGYFNFGVGCDIVKVIIEVAELVDIVMP 165

                         170
                  ....*....|...
gi 17538151   190 STMPRTRGHTTVH 202
Cdd:pfam02550 166 SNPPRRNGYDEFI 178
 
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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