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Conserved domains on  [gi|740851284|ref|WP_038636537|]
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MULTISPECIES: isovaleryl-CoA dehydrogenase [Citrobacter]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 11485399)

acyl-CoA dehydrogenase family protein such as Escherichia coli AidB, which is involved in the SOS adaptive response to DNA alkylation damage

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
1-538 0e+00

isovaleryl CoA dehydrogenase; Provisional


:

Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 1154.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284   1 MHWQTHTVFNQPVPLNNSNLYLSDGALCEAVIREGAGWDSDVLASIGQQLGTAESLELGRLANAFPPELLRYDPQGQRLD 80
Cdd:PRK11561   1 MHWQTHTVFNQPIPLNNSNLFLSDGALCEAVTREGAGWDSDLLASIGQQLGTAESLELGRLANANPPELLRYDAQGQRLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284  81 DVRFHPAWHLLMQGLCANRVHNLAWEDEARQGTFVARAARFMLHAQVEAGTLCPVTMTFAATPLLLQMLPSQFHDWFTPL 160
Cdd:PRK11561  81 DVRFHPAWHLLMQGLCANRVHNLAWEEDARSGAFVARAARFMLHAQVEAGTLCPITMTFAATPLLLQMLPAPFQDWLTPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 161 LSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFFV 240
Cdd:PRK11561 161 LSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFFV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 241 PRFLPDGQRNAIRLERLKDKLGNRSNASCEVEFHDAIGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYH 320
Cdd:PRK11561 241 PRFLPDGQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 321 AHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKYSVCKSGMPFVAEAMEVL 400
Cdd:PRK11561 321 AHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKFVICKRGIPFVAEAMEVL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 401 GGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPGIYDMLSEAFAEVKGQDRHYDRMVRQLQQHLRKPIEE 480
Cdd:PRK11561 401 GGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQPGVYDLLSEAFVEVKGQDRHFDRAVRQLQQRLRKPAEE 480
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 740851284 481 LGREITQQLFLLGCGAQMLRYASPPVAQAWCQMMLDTRGGRRLSEQVQNDLLLRATGG 538
Cdd:PRK11561 481 QGREITQQLFLLGCGAQMLRHASPPLAQAWCQMMLDTRGGVRLSEQVQNDLLLRATGG 538
 
Name Accession Description Interval E-value
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
1-538 0e+00

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 1154.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284   1 MHWQTHTVFNQPVPLNNSNLYLSDGALCEAVIREGAGWDSDVLASIGQQLGTAESLELGRLANAFPPELLRYDPQGQRLD 80
Cdd:PRK11561   1 MHWQTHTVFNQPIPLNNSNLFLSDGALCEAVTREGAGWDSDLLASIGQQLGTAESLELGRLANANPPELLRYDAQGQRLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284  81 DVRFHPAWHLLMQGLCANRVHNLAWEDEARQGTFVARAARFMLHAQVEAGTLCPVTMTFAATPLLLQMLPSQFHDWFTPL 160
Cdd:PRK11561  81 DVRFHPAWHLLMQGLCANRVHNLAWEEDARSGAFVARAARFMLHAQVEAGTLCPITMTFAATPLLLQMLPAPFQDWLTPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 161 LSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFFV 240
Cdd:PRK11561 161 LSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFFV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 241 PRFLPDGQRNAIRLERLKDKLGNRSNASCEVEFHDAIGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYH 320
Cdd:PRK11561 241 PRFLPDGQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 321 AHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKYSVCKSGMPFVAEAMEVL 400
Cdd:PRK11561 321 AHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKFVICKRGIPFVAEAMEVL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 401 GGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPGIYDMLSEAFAEVKGQDRHYDRMVRQLQQHLRKPIEE 480
Cdd:PRK11561 401 GGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQPGVYDLLSEAFVEVKGQDRHFDRAVRQLQQRLRKPAEE 480
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 740851284 481 LGREITQQLFLLGCGAQMLRYASPPVAQAWCQMMLDTRGGRRLSEQVQNDLLLRATGG 538
Cdd:PRK11561 481 QGREITQQLFLLGCGAQMLRHASPPLAQAWCQMMLDTRGGVRLSEQVQNDLLLRATGG 538
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
21-441 0e+00

Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.


Pssm-ID: 173843 [Multi-domain]  Cd Length: 418  Bit Score: 583.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284  21 YLSDGALCEAVIREGAGWDSDVLASIGQQLGtAESLELGRLANAFPPELLRYDPQGQRLDDVRFHPAWHLLMQGLCANRV 100
Cdd:cd01154    1 YLDDPVLQQTLRYFGDPEEEPDLSRLGELAG-GELYELARLADRNPPVLEMWDRWGRRVDRVWVHPAWHALMRRLIEEGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 101 HNLAWEDEARQGTFVARAARFMLHAQvEAGTLCPVTMTFAATPLLLQMLPSQFHDWFTPLLSDRYdshllpggqKRGLLI 180
Cdd:cd01154   80 INIEDGPAGEGRRHVHFAAGYLLSDA-AAGLLCPLTMTDAAVYALRKYGPEELKQYLPGLLSDRY---------KTGLLG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 181 GMGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKG------GLSCFFVPRFLPDGQRNAIRL 254
Cdd:cd01154  150 GTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLADAALVLARPEGapagarGLSLFLVPRLLEDGTRNGYRI 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 255 ERLKDKLGNRSNASCEVEFHDAIGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQ 334
Cdd:cd01154  230 RRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDH 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 335 PMMRQVLSRMALQLEGQTALLFRLARAWDRRADAK--EALWARLFTPAAKYSVCKSGMPFVAEAMEVLGGVGYCEESELP 412
Cdd:cd01154  310 PLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKpvEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVA 389
                        410       420
                 ....*....|....*....|....*....
gi 740851284 413 RLYREMPVNSIWEGSGNIMCLDVLRVLAK 441
Cdd:cd01154  390 RLHREAQVTPIWEGTGNIQALDVLRVLVK 418
AidB_N pfam18158
Adaptive response protein AidB N-terminal domain; This is the N-terminal domain of Adaptive ...
10-167 9.34e-66

Adaptive response protein AidB N-terminal domain; This is the N-terminal domain of Adaptive response protein AidB present in E. coli. AidB is upregulated in response to small doses of DNA-methylating agents initiates a response that mitigates the mutagenic and cytotoxic effects of DNA methylation. Tetramer formation is thought to be carried out by the N-terminal domain.


Pssm-ID: 436317 [Multi-domain]  Cd Length: 156  Bit Score: 210.18  E-value: 9.34e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284   10 NQPVPLNNSNLYLSDGALCEAVIREGAGWDSDVLASIGQQLGTAESLELGRLANAFPPELLRYDPQGQRLDDVRFHPAWH 89
Cdd:pfam18158   1 NQPPPLEDYNLFASDPALQEAVAREGAAWATEALAALGALAGSAEALELARLANRNPPQLHTHDRFGRRIDEVEFHPAYH 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740851284   90 LLMQGLCANRVHNLAWEDeARQGTFVARAARFMLHAQVEAGTLCPVTMTFAATPlLLQMLPSQFHDWFTPLLSDRYDS 167
Cdd:pfam18158  81 ALMALAIEAGLHASPWTD-ARPGAHVARAALFYLHAQVEAGHLCPLTMTYAAVP-ALRAEPALAEEWLPKLLSRDYDP 156
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
61-444 3.82e-64

Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 441563 [Multi-domain]  Cd Length: 381  Bit Score: 213.93  E-value: 3.82e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284  61 LANAFPPELLRYDPQGqrlddvRFHPAWhllMQGLCANRVHNLAWEDEA--RQGTFVARAARFMLHAQVEAGTLCPVTMT 138
Cdd:COG1960   20 AEEEIAPEAREWDREG------EFPREL---WRKLAELGLLGLTIPEEYggLGLSLVELALVLEELARADASLALPVGVH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 139 FAATPLLLQML-PSQFHDWFTPLLSdrydshllpgGQKRGlliGMGMTEKQGGSDVLSNTTQAERlADGSYRLVGHKWFF 217
Cdd:COG1960   91 NGAAEALLRFGtEEQKERYLPRLAS----------GEWIG---AFALTEPGAGSDAAALRTTAVR-DGDGYVLNGQKTFI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 218 S-VPQSDAHLVLAQ---AKG--GLSCFFVPRFLPDgqrnaIRLERLKDKLGNRSNASCEVEFHD---AIGWLLGEEGEGI 288
Cdd:COG1960  157 TnAPVADVILVLARtdpAAGhrGISLFLVPKDTPG-----VTVGRIEDKMGLRGSDTGELFFDDvrvPAENLLGEEGKGF 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 289 RHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADa 368
Cdd:COG1960  232 KIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGED- 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740851284 369 kealwARLFTPAAKYSVCKSGMPFVAEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPG 444
Cdd:COG1960  311 -----AALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
 
Name Accession Description Interval E-value
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
1-538 0e+00

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 1154.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284   1 MHWQTHTVFNQPVPLNNSNLYLSDGALCEAVIREGAGWDSDVLASIGQQLGTAESLELGRLANAFPPELLRYDPQGQRLD 80
Cdd:PRK11561   1 MHWQTHTVFNQPIPLNNSNLFLSDGALCEAVTREGAGWDSDLLASIGQQLGTAESLELGRLANANPPELLRYDAQGQRLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284  81 DVRFHPAWHLLMQGLCANRVHNLAWEDEARQGTFVARAARFMLHAQVEAGTLCPVTMTFAATPLLLQMLPSQFHDWFTPL 160
Cdd:PRK11561  81 DVRFHPAWHLLMQGLCANRVHNLAWEEDARSGAFVARAARFMLHAQVEAGTLCPITMTFAATPLLLQMLPAPFQDWLTPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 161 LSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFFV 240
Cdd:PRK11561 161 LSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFFV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 241 PRFLPDGQRNAIRLERLKDKLGNRSNASCEVEFHDAIGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYH 320
Cdd:PRK11561 241 PRFLPDGQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 321 AHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKYSVCKSGMPFVAEAMEVL 400
Cdd:PRK11561 321 AHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKFVICKRGIPFVAEAMEVL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 401 GGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPGIYDMLSEAFAEVKGQDRHYDRMVRQLQQHLRKPIEE 480
Cdd:PRK11561 401 GGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQPGVYDLLSEAFVEVKGQDRHFDRAVRQLQQRLRKPAEE 480
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 740851284 481 LGREITQQLFLLGCGAQMLRYASPPVAQAWCQMMLDTRGGRRLSEQVQNDLLLRATGG 538
Cdd:PRK11561 481 QGREITQQLFLLGCGAQMLRHASPPLAQAWCQMMLDTRGGVRLSEQVQNDLLLRATGG 538
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
21-441 0e+00

Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.


Pssm-ID: 173843 [Multi-domain]  Cd Length: 418  Bit Score: 583.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284  21 YLSDGALCEAVIREGAGWDSDVLASIGQQLGtAESLELGRLANAFPPELLRYDPQGQRLDDVRFHPAWHLLMQGLCANRV 100
Cdd:cd01154    1 YLDDPVLQQTLRYFGDPEEEPDLSRLGELAG-GELYELARLADRNPPVLEMWDRWGRRVDRVWVHPAWHALMRRLIEEGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 101 HNLAWEDEARQGTFVARAARFMLHAQvEAGTLCPVTMTFAATPLLLQMLPSQFHDWFTPLLSDRYdshllpggqKRGLLI 180
Cdd:cd01154   80 INIEDGPAGEGRRHVHFAAGYLLSDA-AAGLLCPLTMTDAAVYALRKYGPEELKQYLPGLLSDRY---------KTGLLG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 181 GMGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKG------GLSCFFVPRFLPDGQRNAIRL 254
Cdd:cd01154  150 GTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLADAALVLARPEGapagarGLSLFLVPRLLEDGTRNGYRI 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 255 ERLKDKLGNRSNASCEVEFHDAIGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQ 334
Cdd:cd01154  230 RRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDH 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 335 PMMRQVLSRMALQLEGQTALLFRLARAWDRRADAK--EALWARLFTPAAKYSVCKSGMPFVAEAMEVLGGVGYCEESELP 412
Cdd:cd01154  310 PLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKpvEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVA 389
                        410       420
                 ....*....|....*....|....*....
gi 740851284 413 RLYREMPVNSIWEGSGNIMCLDVLRVLAK 441
Cdd:cd01154  390 RLHREAQVTPIWEGTGNIQALDVLRVLVK 418
AidB_N pfam18158
Adaptive response protein AidB N-terminal domain; This is the N-terminal domain of Adaptive ...
10-167 9.34e-66

Adaptive response protein AidB N-terminal domain; This is the N-terminal domain of Adaptive response protein AidB present in E. coli. AidB is upregulated in response to small doses of DNA-methylating agents initiates a response that mitigates the mutagenic and cytotoxic effects of DNA methylation. Tetramer formation is thought to be carried out by the N-terminal domain.


Pssm-ID: 436317 [Multi-domain]  Cd Length: 156  Bit Score: 210.18  E-value: 9.34e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284   10 NQPVPLNNSNLYLSDGALCEAVIREGAGWDSDVLASIGQQLGTAESLELGRLANAFPPELLRYDPQGQRLDDVRFHPAWH 89
Cdd:pfam18158   1 NQPPPLEDYNLFASDPALQEAVAREGAAWATEALAALGALAGSAEALELARLANRNPPQLHTHDRFGRRIDEVEFHPAYH 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740851284   90 LLMQGLCANRVHNLAWEDeARQGTFVARAARFMLHAQVEAGTLCPVTMTFAATPlLLQMLPSQFHDWFTPLLSDRYDS 167
Cdd:pfam18158  81 ALMALAIEAGLHASPWTD-ARPGAHVARAALFYLHAQVEAGHLCPLTMTYAAVP-ALRAEPALAEEWLPKLLSRDYDP 156
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
61-444 3.82e-64

Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 441563 [Multi-domain]  Cd Length: 381  Bit Score: 213.93  E-value: 3.82e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284  61 LANAFPPELLRYDPQGqrlddvRFHPAWhllMQGLCANRVHNLAWEDEA--RQGTFVARAARFMLHAQVEAGTLCPVTMT 138
Cdd:COG1960   20 AEEEIAPEAREWDREG------EFPREL---WRKLAELGLLGLTIPEEYggLGLSLVELALVLEELARADASLALPVGVH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 139 FAATPLLLQML-PSQFHDWFTPLLSdrydshllpgGQKRGlliGMGMTEKQGGSDVLSNTTQAERlADGSYRLVGHKWFF 217
Cdd:COG1960   91 NGAAEALLRFGtEEQKERYLPRLAS----------GEWIG---AFALTEPGAGSDAAALRTTAVR-DGDGYVLNGQKTFI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 218 S-VPQSDAHLVLAQ---AKG--GLSCFFVPRFLPDgqrnaIRLERLKDKLGNRSNASCEVEFHD---AIGWLLGEEGEGI 288
Cdd:COG1960  157 TnAPVADVILVLARtdpAAGhrGISLFLVPKDTPG-----VTVGRIEDKMGLRGSDTGELFFDDvrvPAENLLGEEGKGF 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 289 RHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADa 368
Cdd:COG1960  232 KIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGED- 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740851284 369 kealwARLFTPAAKYSVCKSGMPFVAEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPG 444
Cdd:COG1960  311 -----AALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
97-437 2.97e-55

Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)


Pssm-ID: 173838 [Multi-domain]  Cd Length: 327  Bit Score: 188.65  E-value: 2.97e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284  97 ANRVHNLAWEDEARQGTFVARAARfmlhaqvEAGTLcpvtmtFAATPLLLQMLPSQFHDWFTPLLSDrydshllpggqkr 176
Cdd:cd00567   14 AAEELEPYARERRETPEEPWELLA-------ELGLL------LGAALLLAYGTEEQKERYLPPLASG------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 177 GLLIGMGMTEKQGGSDVLSNTTQAERlADGSYRLVGHKWFFS-VPQSDAHLVLAQ------AKGGLSCFFVPRFLPdgqr 249
Cdd:cd00567   68 EAIAAFALTEPGAGSDLAGIRTTARK-DGDGYVLNGRKIFISnGGDADLFIVLARtdeegpGHRGISAFLVPADTP---- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 250 nAIRLERLKDKLGNRSNASCEVEFHDA---IGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQV 326
Cdd:cd00567  143 -GVTVGRIWDKMGMRGSGTGELVFDDVrvpEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQ 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 327 FGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAkealwARLFTPAAKYSVCKSGMPFVAEAMEVLGGVGYC 406
Cdd:cd00567  222 FGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDE-----ARLEAAMAKLFATEAAREVADLAMQIHGGRGYS 296
                        330       340       350
                 ....*....|....*....|....*....|.
gi 740851284 407 EESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
Cdd:cd00567  297 REYPVERYLRDARAARIAEGTAEIQRLIIAR 327
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
182-437 1.06e-43

Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.


Pssm-ID: 173842 [Multi-domain]  Cd Length: 407  Bit Score: 159.86  E-value: 1.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 182 MGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFSVPQSDA-----HLVLAQAKG------GLSCFFVPRFLPDGQRN 250
Cdd:cd01153  121 MCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAGEHDMsenivHLVLARSEGappgvkGLSLFLVPKFLDDGERN 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 251 AIRLERLKDKLGNRSNASCEVEFHDAIGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKP 330
Cdd:cd01153  201 GVTVARIEEKMGLHGSPTCELVFDNAKGELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDL 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 331 LIEQP---------MMRQVLSRMALqLEGQTALLFRLARAWD---RRADAKEA-----LWARLFTPAAKYSVCKSGMPFV 393
Cdd:cd01153  281 IKAAPavtiihhpdVRRSLMTQKAY-AEGSRALDLYTATVQDlaeRKATEGEDrkalsALADLLTPVVKGFGSEAALEAV 359
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 740851284 394 AEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
Cdd:cd01153  360 SDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALDLIG 403
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
129-430 1.74e-30

Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.


Pssm-ID: 173847 [Multi-domain]  Cd Length: 373  Bit Score: 122.38  E-value: 1.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 129 AGTLCPVTMTFAATPLLLQMLPSQFHDWFTPLLSdrydshllpgGQKRGlliGMGMTEKQGGSDVLSNTTQAERLADgSY 208
Cdd:cd01158   77 VAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLAT----------GEKIG---AFALSEPGAGSDAAALKTTAKKDGD-DY 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 209 RLVGHK-WFFSVPQSDAHLVLAQAKG-----GLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASCEVEFHDAI---GW 279
Cdd:cd01158  143 VLNGSKmWITNGGEADFYIVFAVTDPskgyrGITAFIVERDTP-----GLSVGKKEDKLGIRGSSTTELIFEDVRvpkEN 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 280 LLGEEGEGIRHILKMGGMTRFD---CALGshsMMRRAFSVAIYHAHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLF 356
Cdd:cd01158  218 ILGEEGEGFKIAMQTLDGGRIGiaaQALG---IAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTY 294
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740851284 357 RLARAWDRRAD-AKEALWARLFTPAAKYSVCKsgmpfvaEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNI 430
Cdd:cd01158  295 KAARLKDNGEPfIKEAAMAKLFASEVAMRVTT-------DAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEI 362
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
285-439 1.29e-28

Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.


Pssm-ID: 395354 [Multi-domain]  Cd Length: 149  Bit Score: 110.81  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284  285 GEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDR 364
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740851284  365 RADAKEAlwarlfTPAAKYSVCKSGMPFVAEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
Cdd:pfam00441  81 GGPDGAE------ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
152-430 4.41e-27

Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.


Pssm-ID: 173845 [Multi-domain]  Cd Length: 376  Bit Score: 112.89  E-value: 4.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 152 QFHDWFTPLLSDRYDSHLLPGGQkrgllIG-MGMTEKQGGSDVLSNTTQAERlADGSYRLVGHKwFFSVPQSDAHLVLAQ 230
Cdd:cd01156   94 QIYRNGSAAQKEKYLPKLISGEH-----IGaLAMSEPNAGSDVVSMKLRAEK-KGDRYVLNGSK-MWITNGPDADTLVVY 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 231 AKG-------GLSCFFVPRFLPdGQRNAIRLerlkDKLGNRSNASCEVEFHDAI---GWLLGEEGEGIRHIlkMGGMT-- 298
Cdd:cd01156  167 AKTdpsagahGITAFIVEKGMP-GFSRAQKL----DKLGMRGSNTCELVFEDCEvpeENILGGENKGVYVL--MSGLDye 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 299 RFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDR-RADAKEALWARLF 377
Cdd:cd01156  240 RLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRgNMDPKDAAGVILY 319
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 740851284 378 TPAAKYSVCKsgmpfvaEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNI 430
Cdd:cd01156  320 AAEKATQVAL-------DAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEI 365
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
182-444 5.95e-26

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 111.88  E-value: 5.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 182 MGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFSVPQSD-----AHLVLAQ------AKGGLSCFFVPRFL--PDG- 247
Cdd:PTZ00456 185 MCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDlteniVHIVLARlpnslpTTKGLSLFLVPRHVvkPDGs 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 248 ---QRNaIRLERLKDKLGNRSNASCEVEFHDAIGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQR 324
Cdd:PTZ00456 265 letAKN-VKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARER 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 325 ------------QVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWAR-------LFTPAAKYSV 385
Cdd:PTZ00456 344 rsmralsgtkepEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREaldheigFYTPIAKGCL 423
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740851284 386 CKSGMPFVAEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL--RVLAKQPG 444
Cdd:PTZ00456 424 TEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIgrKVLSLKGG 484
PRK12341 PRK12341
acyl-CoA dehydrogenase;
182-431 2.47e-25

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 107.89  E-value: 2.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 182 MGMTEKQGGSDVLSNTTQAERlADGSYRLVGHKWFFS-VPQSDAHLVLAQ------AKGGLSCFFVPRFLPdgqrnAIRL 254
Cdd:PRK12341 122 LALTEPGAGSDNNSATTTYTR-KNGKVYLNGQKTFITgAKEYPYMLVLARdpqpkdPKKAFTLWWVDSSKP-----GIKI 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 255 ERLKdKLGNRSNASCEVEFHDAI---GWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPL 331
Cdd:PRK12341 196 NPLH-KIGWHMLSTCEVYLDNVEveeSDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPI 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 332 IEQPMMRQVLSRMALQLEGQTALLFRLarAWdrRADAKEALwaRLFTPAAKYSVCKSGMPFVAEAMEVLGGVGYCEESEL 411
Cdd:PRK12341 275 GHNQLIQEKLTLMAIKIENMRNMVYKV--AW--QADNGQSL--RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARV 348
                        250       260
                 ....*....|....*....|
gi 740851284 412 PRLYREMPVNSIWEGSGNIM 431
Cdd:PRK12341 349 SRFWRDVRCERIGGGTDEIM 368
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
184-444 8.99e-25

Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.


Pssm-ID: 173850 [Multi-domain]  Cd Length: 409  Bit Score: 106.40  E-value: 8.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 184 MTEKQGGSDVLSNTTQAERLADGS-YRLVGHK-WFFSVPQSDAHLVLAQ---------AKGGLSCFFVPRFLpDGQRNAI 252
Cdd:cd01161  144 LTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKiWITNGGIADIFTVFAKtevkdatgsVKDKITAFIVERSF-GGVTNGP 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 253 RlerlKDKLGNRSNASCEVEFHDA---IGWLLGEEGEGIR---HILKMGgmtRFDCALGSHSMMRRAFSVAIYHAHQRQV 326
Cdd:cd01161  223 P----EKKMGIKGSNTAEVYFEDVkipVENVLGEVGDGFKvamNILNNG---RFGMGAALIGTMKRCIEKAVDYANNRKQ 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 327 FGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAK---EALWARLFTPAAKYSVCKsgmpfvaEAMEVLGGV 403
Cdd:cd01161  296 FGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEyqiEAAISKVFASEAAWLVVD-------EAIQIHGGM 368
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 740851284 404 GYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPG 444
Cdd:cd01161  369 GFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHAG 409
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
103-431 1.92e-20

Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.


Pssm-ID: 173849 [Multi-domain]  Cd Length: 372  Bit Score: 92.95  E-value: 1.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 103 LAWEDEARQGTFvarAARFMLHAQVEAGTLcpvtmTFAATPLLLQmlpsqfhdwftpllsdrydsHLLPG---GQKRGLL 179
Cdd:cd01160   65 VLWEELARAGGS---GPGLSLHTDIVSPYI-----TRAGSPEQKE--------------------RVLPQmvaGKKIGAI 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 180 igmGMTEKQGGSDVLSNTTQAERlaDGS-YRLVGHKWFFSVP-QSDAHLVLAQ------AKGGLSCFFVPRFLPDGQRNa 251
Cdd:cd01160  117 ---AMTEPGAGSDLQGIRTTARK--DGDhYVLNGSKTFITNGmLADVVIVVARtggearGAGGISLFLVERGTPGFSRG- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 252 irleRLKDKLGNRSNASCEVEFHDA---IGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFG 328
Cdd:cd01160  191 ----RKLKKMGWKAQDTAELFFDDCrvpAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFG 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 329 KPLIEQPMMRQVLSRMALQLEGQTALLFRLA-RAWDRRADAKEAlwarlftPAAKYsVCKSGMPFVA-EAMEVLGGVGYC 406
Cdd:cd01160  267 KTLAQLQVVRHKIAELATKVAVTRAFLDNCAwRHEQGRLDVAEA-------SMAKY-WATELQNRVAyECVQLHGGWGYM 338
                        330       340
                 ....*....|....*....|....*
gi 740851284 407 EESELPRLYREMPVNSIWEGSGNIM 431
Cdd:cd01160  339 REYPIARAYRDARVQPIYGGTTEIM 363
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
181-274 4.65e-20

Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.


Pssm-ID: 460685 [Multi-domain]  Cd Length: 95  Bit Score: 85.02  E-value: 4.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284  181 GMGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFS-VPQSDAHLVLAQ-----AKGGLSCFFVPRFLPdgqrnAIRL 254
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITnAGIADLFLVLARtggddRHGGISLFLVPKDAP-----GVSV 75
                          90       100
                  ....*....|....*....|
gi 740851284  255 ERLKDKLGNRSNASCEVEFH 274
Cdd:pfam02770  76 RRIETKLGVRGLPTGELVFD 95
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
182-442 1.97e-19

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 90.32  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 182 MGMTEKQGGSDVLSNTTQAERLaDGSYRLVGHK-WFFSVPQSDAHLVLAQ---AKG--GLSCFFVPRFLPdGQRNAIRLe 255
Cdd:PLN02519 146 LAMSEPNSGSDVVSMKCKAERV-DGGYVLNGNKmWCTNGPVAQTLVVYAKtdvAAGskGITAFIIEKGMP-GFSTAQKL- 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 256 rlkDKLGNRSNASCEVEFHDAI---GWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLI 332
Cdd:PLN02519 223 ---DKLGMRGSDTCELVFENCFvpeENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIG 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 333 EQPMMRQVLSRMALQLEGQTALLFRLARAWDR-RADAKEALWARLFTPAAKYSVcksgmpfVAEAMEVLGGVGYCEESEL 411
Cdd:PLN02519 300 EFQFIQGKLADMYTSLQSSRSYVYSVARDCDNgKVDRKDCAGVILCAAERATQV-------ALQAIQCLGGNGYINEYPT 372
                        250       260       270
                 ....*....|....*....|....*....|.
gi 740851284 412 PRLYREMPVNSIWEGSGNIMCLDVLRVLAKQ 442
Cdd:PLN02519 373 GRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
184-442 9.69e-19

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 87.96  E-value: 9.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 184 MTEKQGGSDVLSNTTQAERlADGSYRLVGHKWFFSVPQSDAHLVL------AQAKGGLSCFFVPRFLPdgqrnAIRLERL 257
Cdd:PRK03354 124 ITEPGAGSDVGSLKTTYTR-RNGKVYLNGSKCFITSSAYTPYIVVmardgaSPDKPVYTEWFVDMSKP-----GIKVTKL 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 258 kDKLGNRSNASCEVEFhDAIGW----LLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIE 333
Cdd:PRK03354 198 -EKLGLRMDSCCEITF-DDVELdekdMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGR 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 334 QPMMRQVLSRMALQLEGQTALLFRLARAWDR----RADAKealwarlftpAAKYSVCKSGMPFVAEAMEVLGGVGYCEES 409
Cdd:PRK03354 276 FQLIQEKFAHMAIKLNSMKNMLYEAAWKADNgtitSGDAA----------MCKYFCANAAFEVVDSAMQVLGGVGIAGNH 345
                        250       260       270
                 ....*....|....*....|....*....|...
gi 740851284 410 ELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQ 442
Cdd:PRK03354 346 RISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
182-430 1.21e-18

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 88.07  E-value: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 182 MGMTEKQGGSDVLSNTTQAERLADGSYRLVGHK-WFFSVPQSDAHLVLAQAKGGLSCFFVPRFLPdGQRNAIRLerlkDK 260
Cdd:PTZ00461 155 MGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKiWITNGTVADVFLIYAKVDGKITAFVVERGTK-GFTQGPKI----DK 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 261 LGNRSNASCEVEFHDAI---GWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQPMM 337
Cdd:PTZ00461 230 CGMRASHMCQLFFEDVVvpaENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQI 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 338 RQVLSRMALQLEGQTALLFRLARawDRRADAKEALW---ARLF-TPAAKYsvcksgmpfVAE-AMEVLGGVGYCEESELP 412
Cdd:PTZ00461 310 QRYIAEGYADTEAAKALVYSVSH--NVHPGNKNRLGsdaAKLFaTPIAKK---------VADsAIQVMGGMGYSRDMPVE 378
                        250
                 ....*....|....*...
gi 740851284 413 RLYREMPVNSIweGSGNI 430
Cdd:PTZ00461 379 RLWRDAKLLEI--GGGTI 394
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
184-439 3.92e-13

Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.


Pssm-ID: 173846 [Multi-domain]  Cd Length: 378  Bit Score: 71.08  E-value: 3.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 184 MTEKQGGSDVLSNTTQAERLADgSYRLVGHK----------WFFSVPQSDAHlVLAQAKGGLSCFFVPRFLPDGQRNair 253
Cdd:cd01157  120 VTEPGAGSDVAGIKTKAEKKGD-EYIINGQKmwitnggkanWYFLLARSDPD-PKCPASKAFTGFIVEADTPGIQPG--- 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 254 leRLKDKLGNRSNASCEVEFHDAI---GWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKP 330
Cdd:cd01157  195 --RKELNMGQRCSDTRGITFEDVRvpkENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKL 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 331 LIEQPMMRQVLSRMALQLEgqTALLFRLARAWDRRADAKEALWARLftpaAKYSVCKSGMPFVAEAMEVLGGVGYCEESE 410
Cdd:cd01157  273 IAEHQAVSFMLADMAMKVE--LARLAYQRAAWEVDSGRRNTYYASI----AKAFAADIANQLATDAVQIFGGNGFNSEYP 346
                        250       260
                 ....*....|....*....|....*....
gi 740851284 411 LPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
Cdd:cd01157  347 VEKLMRDAKIYQIYEGTSQIQRLIISREH 375
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
170-433 3.81e-08

Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.


Pssm-ID: 173840 [Multi-domain]  Cd Length: 386  Bit Score: 55.44  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 170 LPGgQKRGLLIG-MGMTEKQGGSDVLSNTTQAERLADGsYRLVGHK-WFFSVPQSDAHLVLA--QAKGGLSCFFVPRFLP 245
Cdd:cd01151  118 LPK-LASGELIGcFGLTEPNHGSDPGGMETRARKDGGG-YKLNGSKtWITNSPIADVFVVWArnDETGKIRGFILERGMK 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 246 dgqrnAIRLERLKDKLGNRSNASCEVEFHDAigwLLGEEG-----EGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYH 320
Cdd:cd01151  196 -----GLSAPKIQGKFSLRASITGEIVMDNV---FVPEENllpgaEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQY 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 321 AHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEAlwarlfTPAAKYSVCKSGMPFVAEAMEVL 400
Cdd:cd01151  268 VLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ------ISLLKRNNCGKALEIARTAREML 341
                        250       260       270
                 ....*....|....*....|....*....|...
gi 740851284 401 GGVGYCEESELPRLYREMPVNSIWEGSGNIMCL 433
Cdd:cd01151  342 GGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL 374
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
303-417 1.12e-05

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 45.03  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284  303 ALGshsMMRRAFSVAIYHAHQRQ--VFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLA-RAWDRRADAKE---ALWARL 376
Cdd:pfam08028   6 ALG---AARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAaRIEAAAAAGKPvtpALRAEA 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 740851284  377 fTPAAKYSV--CKSGmpfVAEAMEVLGGVGYCEESELPRLYRE 417
Cdd:pfam08028  83 -RRAAAFATelAVAA---VDALFRAAGGSALFQDSPLQRIWRD 121
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
174-401 1.44e-04

Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.


Pssm-ID: 173841 [Multi-domain]  Cd Length: 380  Bit Score: 44.26  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 174 QKRGLLIGM---------GMTEKQGGSDVLSNTTQAERLADGsYRLVGHKWFFSVPQ-SDAHLVLAQAKG------GLSC 237
Cdd:cd01152  104 QKRRFLPPIlsgeeiwcqGFSEPGAGSDLAGLRTRAVRDGDD-WVVNGQKIWTSGAHyADWAWLLVRTDPeapkhrGISI 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 238 FFVPRFLPDGQRNAIRlerlkdkLGNRSNASCEVEFHD---AIGWLLGEEGEGIRHILKMGGMTRFdcALGSHSMMRRAF 314
Cdd:cd01152  183 LLVDMDSPGVTVRPIR-------SINGGEFFNEVFLDDvrvPDANRVGEVNDGWKVAMTTLNFERV--SIGGSAATFFEL 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 315 SVAIYHAHQRQvfGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWD--RRADAKEAL----WARLFTPAAKYsvcks 388
Cdd:cd01152  254 LLARLLLLTRD--GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAagKPPGAEASIaklfGSELAQELAEL----- 326
                        250
                 ....*....|...
gi 740851284 389 gmpfvaeAMEVLG 401
Cdd:cd01152  327 -------ALELLG 332
 
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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