|
Name |
Accession |
Description |
Interval |
E-value |
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
56-372 |
0e+00 |
|
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: 581.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 56 EHDIFRKSIRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNTAEHLGGIGGDLYYAAVVWEEQAYSNCSGPGFS 135
Cdd:cd01160 2 EHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 136 VHSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSK-------------- 201
Cdd:cd01160 82 LHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKtfitngmladvviv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 ----------------------------------------DTAELFFEDVRLPASALLGEENKGFYYIMKELPQERLLIA 241
Cdd:cd01160 162 vartggeargaggislflvergtpgfsrgrklkkmgwkaqDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 242 DMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASELQ 321
Cdd:cd01160 242 AGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQ 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1777253557 322 NSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 372
Cdd:cd01160 322 NRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
53-372 |
3.67e-116 |
|
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: 342.59 E-value: 3.67e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 53 FSSEHDIFRKSIRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNTAEHLGGIGGDLYYAAVVWEEQAYSNCS-G 131
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASlA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 132 PGFSVHSGiVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSK---------- 201
Cdd:COG1960 85 LPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKtfitnapvad 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 -------------------------------------------DTAELFFEDVRLPASALLGEENKGFYYIMKELPQERL 238
Cdd:COG1960 164 vilvlartdpaaghrgislflvpkdtpgvtvgriedkmglrgsDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 239 LIADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWAS 318
Cdd:COG1960 244 GLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFAT 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1777253557 319 ELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 372
Cdd:COG1960 324 EAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
55-371 |
1.30e-85 |
|
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: 264.13 E-value: 1.30e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 55 SEHDIFRKSIRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNTAEHLGGIGGDLYYAAVVWEEQAYSNCS-GPG 133
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASvAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 134 FSVHSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSK------------ 201
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKmwitnggeadfy 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 -----------------------------------------DTAELFFEDVRLPASALLGEENKGFYYIMKELPQERLLI 240
Cdd:cd01158 161 ivfavtdpskgyrgitafiverdtpglsvgkkedklgirgsSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 241 ADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASEL 320
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1777253557 321 QNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREI 371
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
56-369 |
2.22e-76 |
|
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: 238.72 E-value: 2.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 56 EHDIFRKSIRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKqgLLGVNTaehlggiggdlyyaavvweeqaysncsgpgfs 135
Cdd:cd00567 2 EQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGL--LLGAAL-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 136 vhsgivmsyITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSK-------------- 201
Cdd:cd00567 48 ---------LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKifisnggdadlfiv 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 ----------------------------------------DTAELFFEDVRLPASALLGEENKGFYYIMKELPQERLLIA 241
Cdd:cd00567 119 lartdeegpghrgisaflvpadtpgvtvgriwdkmgmrgsGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 242 DMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDN-CLQLHEAKRLDSATACMAKYWASEL 320
Cdd:cd00567 199 AVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRaAWLLDQGPDEARLEAAMAKLFATEA 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1777253557 321 QNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAR 369
Cdd:cd00567 279 AREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
53-372 |
3.06e-72 |
|
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: 229.99 E-value: 3.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 53 FSSEHDIFRKSIRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNTAEHLGGIGGDLYYAAVVWEEQAYSNCS-G 131
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 132 PGFSVHSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSK---------- 201
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKmwitngpdad 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 -------------------------------------------DTAELFFEDVRLPASALLGEENKGFYYIMKELPQERL 238
Cdd:cd01156 162 tlvvyaktdpsagahgitafivekgmpgfsraqkldklgmrgsNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 239 LIADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWAS 318
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1777253557 319 ELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 372
Cdd:cd01156 322 EKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELF 375
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
54-371 |
1.43e-66 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 215.00 E-value: 1.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 54 SSEHDIFRKSIRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNTAEHLGGIGGDLYYAAVVWEEQAYSNCSGPG 133
Cdd:cd01162 2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 134 F-SVHSgIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSKD---------- 202
Cdd:cd01162 82 YiSIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAfisgagdsdv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 203 ------------------------------------------TAELFFEDVRLPASALLGEENKGFYYIMKELPQERLLI 240
Cdd:cd01162 161 yvvmartggegpkgiscfvvekgtpglsfganekkmgwnaqpTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 241 ADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATAC-MAKYWASE 319
Cdd:cd01162 241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCaMAKRFATD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1777253557 320 LQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREI 371
Cdd:cd01162 321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARAL 372
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
53-372 |
1.62e-51 |
|
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: 176.24 E-value: 1.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 53 FSSEHDIFRKSIRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNTAEHLGGIGGDLYYAAVVWEEQAYSnCSGP 132
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYG-CTGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 133 GFSVHS---GIVMSYITnyGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSK-------- 201
Cdd:cd01157 80 QTAIEAnslGQMPVIIS--GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKmwitnggk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 ------------------------------------------------DTAELFFEDVRLPASALLGEENKGFYYIMKEL 233
Cdd:cd01157 158 anwyfllarsdpdpkcpaskaftgfiveadtpgiqpgrkelnmgqrcsDTRGITFEDVRVPKENVLIGEGAGFKIAMGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 234 PQERLLIADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMA 313
Cdd:cd01157 238 DKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1777253557 314 KYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 372
Cdd:cd01157 318 KAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
54-368 |
2.32e-49 |
|
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: 171.11 E-value: 2.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 54 SSEHDIFRKSIRKFFQEEVIPHHSEWEkaGEVSREVWEKAGKQGLLGVNTAEHLGGIGGDLYYAAVVWEEQAYSNCSGPG 133
Cdd:cd01161 28 TEELNMLVGPVEKFFEEVNDPAKNDQL--EKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSVT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 134 FSVHSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKK--DGSDWILNGSK---------- 201
Cdd:cd01161 106 LGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKiwitnggiad 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 -----------------------------------------------DTAELFFEDVRLPASALLGEENKGFYYIMKELP 234
Cdd:cd01161 186 iftvfaktevkdatgsvkdkitafiversfggvtngppekkmgikgsNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILN 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 235 QERLLIADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTR--AFVDNCLQLHEAKRLDSATACM 312
Cdd:cd01161 266 NGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATEsmAYMTSGNMDRGLKAEYQIEAAI 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1777253557 313 AKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIA 368
Cdd:cd01161 346 SKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA 401
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
54-371 |
1.38e-48 |
|
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: 168.69 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 54 SSEHDIFRKSIRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNTAEHlgGIGGDLY--YAAVVWE-EQAYSNCS 130
Cdd:cd01151 14 TEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGY--GCAGLSSvaYGLIAREvERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 131 GpGFSVHSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSKD-------- 202
Cdd:cd01151 92 S-FMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTwitnspia 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 203 ------------------------------------------TAELFFEDVRLPASALLGEENkGFYYIMKELPQERLLI 240
Cdd:cd01151 171 dvfvvwarndetgkirgfilergmkglsapkiqgkfslrasiTGEIVMDNVFVPEENLLPGAE-GLRGPFKCLNNARYGI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 241 ADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHIcvtRAFVDNCLQ---LHEAKRLDSATACMAKYWA 317
Cdd:cd01151 250 AWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEI---ALGLLACLRvgrLKDQGKATPEQISLLKRNN 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1777253557 318 SelqnSVAYDCV----QLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREI 371
Cdd:cd01151 327 C----GKALEIArtarEMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
60-371 |
1.66e-48 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 168.90 E-value: 1.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 60 FRKSIRKFFQEEVIPHHSEWEKAGEVSREV--WEKAGKQGLLGVNTAEHLGGIG-GDLYYAAVVWEEQAYSNCSGPGFSV 136
Cdd:PLN02519 33 FKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGlGYLYHCIAMEEISRASGSVGLSYGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 137 HSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSK--------------- 201
Cdd:PLN02519 113 HSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKmwctngpvaqtlvvy 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 --------------------------------------DTAELFFEDVRLPASALLGEENKGFYYIMKELPQERLLIADM 243
Cdd:PLN02519 193 aktdvaagskgitafiiekgmpgfstaqkldklgmrgsDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 244 AVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASELQNS 323
Cdd:PLN02519 273 PLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQ 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1777253557 324 VAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREI 371
Cdd:PLN02519 353 VALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
223-371 |
1.33e-44 |
|
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: 150.87 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 223 NKGFYYIMKELPQERLLIADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEA 302
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1777253557 303 KRLDSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREI 371
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
4-372 |
1.86e-44 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 158.18 E-value: 1.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 4 RLLRGSLRFLGGHCAARPLpAVRCSHSGGEERLETPSaknltdigirrifsSEHDIFRKSIRKFFQEEVIPHHSEWEKAG 83
Cdd:PTZ00461 3 RVLQSSLGRRSATCGWTAA-ATMTSASRAFMDLYNPT--------------PEHAALRETVAKFSREVVDKHAREDDINM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 84 EVSREVWEKAGKQGLLGVNTAEHLGGIGGDLYYAAVVWEEqaYSNCSgPGFSV----HSGIVMSYITNYGSEEQIKHFIP 159
Cdd:PTZ00461 68 HFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHE--LSKYD-PGFCLaylaHSMLFVNNFYYSASPAQRARWLP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 160 QMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSD---------WILNGS-------------KDTA------------- 204
Cdd:PTZ00461 145 KVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnyvlngskiWITNGTvadvfliyakvdgKITAfvvergtkgftqg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 205 --------------ELFFEDVRLPASALLGEENKGFYYIMKELPQERLLIADMAVSASEFMFEETRNYVKQRKAFGKTVA 270
Cdd:PTZ00461 225 pkidkcgmrashmcQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPIS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 271 HLQTVQHKLAELKTHICVTRAFV---------DNClqlheaKRLDSATacmAKYWASELQNSVAYDCVQLHGGWGYMWEY 341
Cdd:PTZ00461 305 NFGQIQRYIAEGYADTEAAKALVysvshnvhpGNK------NRLGSDA---AKLFATPIAKKVADSAIQVMGGMGYSRDM 375
|
410 420 430
....*....|....*....|....*....|.
gi 1777253557 342 PIAKAYVDARVQPIYGGTNEIMKELIAREIV 372
Cdd:PTZ00461 376 PVERLWRDAKLLEIGGGTIEAHHKNITKDLL 406
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
54-372 |
4.01e-44 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 156.43 E-value: 4.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 54 SSEHDIFRKSIRKFFQEEViPHH--SEWEKAGEVSREVWEKAGKQG--LLGVntAEHLGGIGGDLYYAAVVWEEqaYSNC 129
Cdd:PRK12341 6 TEEQELLLASIRELITRNF-PEEyfRTCDENGTYPREFMRALADNGisMLGV--PEEFGGTPADYVTQMLVLEE--VSKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 130 SGPGFSVHSGIVMSYITNYGSEEQIKH-FIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSK------- 201
Cdd:PRK12341 81 GAPAFLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKtfitgak 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 ----------------------------------------------DTAELFFEDVRLPASALLGEENKGFYYIMKELPQ 235
Cdd:PRK12341 161 eypymlvlardpqpkdpkkaftlwwvdsskpgikinplhkigwhmlSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 236 ERLLIADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFV-------DNclqlHEAKRLDSA 308
Cdd:PRK12341 241 ERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVykvawqaDN----GQSLRTSAA 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777253557 309 tacMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 372
Cdd:PRK12341 317 ---LAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQIL 377
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
54-165 |
3.44e-37 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 130.28 E-value: 3.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 54 SSEHDIFRKSIRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNTAEHLGGIGGDLYYAAVVWEEQAYSNCS-GP 132
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASvAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 1777253557 133 GFSVHSGIVMSYITNYGSEEQIKHFIPQMTAGK 165
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
60-371 |
9.25e-36 |
|
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: 134.01 E-value: 9.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 60 FRKSIRKFFQEEVIP-----HHSEWEKAGEVSREvWEKA-GKQGLLGVNTAEHLGGIGGDLYYAAVVWEEQAYSNCSGPG 133
Cdd:cd01152 6 FRAEVRAWLAAHLPPelreeSALGYREGREDRRR-WQRAlAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 134 FSVHSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSK------------ 201
Cdd:cd01152 85 NQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKiwtsgahyadwa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 ----------------------------------------DTAELFFEDVRLPASALLGEENKGFYYIMKELPQERLLIA 241
Cdd:cd01152 165 wllvrtdpeapkhrgisillvdmdspgvtvrpirsinggeFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 242 DMAVSAsefmFEETRNYVK--QRKAFGKTVAHLqtVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASE 319
Cdd:cd01152 245 GSAATF----FELLLARLLllTRDGRPLIDDPL--VRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSE 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 320 LQNSVAYDCVQLHGGWG---YMWEYPIAKA-----YVDARVQPIYGGTNEIMKELIAREI 371
Cdd:cd01152 319 LAQELAELALELLGTAAllrDPAPGAELAGrweadYLRSRATTIYGGTSEIQRNIIAERL 378
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
97-372 |
1.06e-27 |
|
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: 112.48 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 97 GLLGVNTAEHLGGIGGDLyyaAVVW--EEQAYSNCSGPGFSVHSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTE 174
Cdd:cd01153 49 GWMALGVPEEYGGQGLPI---TVYSalAEIFSRGDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 175 LGAGSDLQGIKTNA--KKDGSdWILNGSK--------------------------------------------------- 201
Cdd:cd01153 126 PDAGSDLGALRTKAvyQADGS-WRINGVKrfisagehdmsenivhlvlarsegappgvkglslflvpkflddgerngvtv 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 ------------DTAELFFEDVRlpaSALLGEENKGFYYIMKELPQERLLIADMAVSASEFMFEETRNYVKQRKAFGK-- 267
Cdd:cd01153 205 arieekmglhgsPTCELVFDNAK---GELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDli 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 268 ------TVAHLQTVQHKLAELKTHICVTRAFVDNC---LQLHEAK-----------RLDSATACMAKYWASELQNSVAYD 327
Cdd:cd01153 282 kaapavTIIHHPDVRRSLMTQKAYAEGSRALDLYTatvQDLAERKategedrkalsALADLLTPVVKGFGSEAALEAVSD 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1777253557 328 CVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIM-KELIAREIV 372
Cdd:cd01153 362 AIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQaLDLIGRKIV 407
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
52-371 |
1.53e-27 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 112.25 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 52 IFSSEHDIFRKSIRKFFQEEVIPHHSE-WEKAgEVSREVWEKAGKQGLLGvNTAEHLGGIGGDLYYAAVVWEEQAYSNCS 130
Cdd:PLN02526 28 LLTPEEQALRKRVRECMEKEVAPIMTEyWEKA-EFPFHIIPKLGSLGIAG-GTIKGYGCPGLSITASAIATAEVARVDAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 131 GPGFS-VHSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSK-------- 201
Cdd:PLN02526 106 CSTFIlVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKrwignstf 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 -DTAELFFED----------VRLPASALLGE--ENK----------------------------GFYYIMKELPQERLLI 240
Cdd:PLN02526 186 aDVLVIFARNtttnqingfiVKKGAPGLKATkiENKiglrmvqngdivlkdvfvpdedrlpgvnSFQDTNKVLAVSRVMV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 241 ADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASEL 320
Cdd:PLN02526 266 AWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITKK 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1777253557 321 QNSVAYDCVQLHGGWGYMWEYPIAKAYVDarVQPIYG--GTNEIMKELIAREI 371
Cdd:PLN02526 346 ARETVALGRELLGGNGILADFLVAKAFCD--LEPIYTyeGTYDINALVTGREI 396
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
53-363 |
3.94e-27 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 110.69 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 53 FSSEHDIFRKSIRKFFQEEviphhsEWEK------AGEVSREVWEKA-GKQGLLGVNTAEHLGGIGGDLYYAAVVWEEqa 125
Cdd:PRK03354 5 LNDEQELFVAGIRELMASE------NWEAyfaecdRDSVYPERFVKAlADMGIDSLLIPEEHGGLDAGFVTLAAVWME-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 126 YSNCSGPGFSVH---SGIvmSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKDGSDWILNGSK- 201
Cdd:PRK03354 77 LGRLGAPTYVLYqlpGGF--NTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKc 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 ---------------------------------------------------DTAELFFEDVRLPASALLGEENKGFYYIM 230
Cdd:PRK03354 155 fitssaytpyivvmardgaspdkpvytewfvdmskpgikvtkleklglrmdSCCEITFDDVELDEKDMFGREGNGFNRVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 231 KELPQERLLIADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATA 310
Cdd:PRK03354 235 EEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDA 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1777253557 311 CMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIM 363
Cdd:PRK03354 315 AMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQ 367
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
61-369 |
1.80e-25 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). 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 ACAD 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. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 105.93 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 61 RKSIRKFFQEEVIPHHSE-----------WEKAGEVSREVWEKAGKQGLLGVNTAEHLGGIG-GDLYYAAVVwEEQAYS- 127
Cdd:cd01155 7 RARVKAFMEEHVYPAEQEfleyyaeggdrWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGlTNLEYAYLA-EETGRSf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 128 ------NCSGPgfsvHSGiVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELG-AGSDLQGIKTNAKKDGSDWILNGS 200
Cdd:cd01155 86 fapevfNCQAP----DTG-NMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 201 K--------------------------------------DT---------------------AELFFEDVRLPASALLGE 221
Cdd:cd01155 161 KwwssgagdprckiaivmgrtdpdgaprhrqqsmilvpmDTpgvtiirplsvfgyddaphghAEITFDNVRVPASNLILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 222 ENKGFYYIMKELPQERLLIADMAVSASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVdnclqLHE 301
Cdd:cd01155 241 EGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLV-----LKA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777253557 302 AKRLD---SATA----CMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAR 369
Cdd:cd01155 316 AHMIDtvgNKAArkeiAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
145-363 |
4.17e-24 |
|
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: 102.45 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 145 ITNYGSEEqIKHFIPQMTAGKC----IGAIAMTELGAGSDLQGIKTNAKKDGSD-WILNGSK--------DTA------- 204
Cdd:cd01154 123 LRKYGPEE-LKQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSGGGvYRLNGHKwfasaplaDAAlvlarpe 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 205 ---------ELFFEDVRLP---------------------ASA----------LLGEENKGFYYIMKELPQERLliaDMA 244
Cdd:cd01154 202 gapagarglSLFLVPRLLEdgtrngyrirrlkdklgtrsvATGevefddaeayLIGDEGKGIYYILEMLNISRL---DNA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 245 VSASEFM---FEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFV-DNCLQLHEAKRLDSATACMA------- 313
Cdd:cd01154 279 VAALGIMrraLSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTfRAARAFDRAAADKPVEAHMArlatpva 358
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1777253557 314 KYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIM 363
Cdd:cd01154 359 KLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
84-369 |
6.03e-13 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 70.21 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 84 EVSREVWEKAGKQGLLGvNTAEHLGGIG-GDLYYAAV-------VWEEQAYsNCSGPgfsvHSGiVMSYITNYGSEEQIK 155
Cdd:PLN02876 467 ARARKLLFEDNKHMVSG-DSADQLLGAGlSNLEYGYLceimgrsVWAPQVF-NCGAP----DTG-NMEVLLRYGNKEQQL 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 156 HFIPQMTAGKCIGAIAMTELG-AGSDLQGIKTNAKKDGSDWILNGSK--------------------------------- 201
Cdd:PLN02876 540 EWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKwwtsgamdprcrvlivmgktdfnapkhkqqsmi 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 202 -------------------------DTAELFFEDVRLPASALLGEENKGFYYIMKELPQERLLIADMAVSASEFMFEETR 256
Cdd:PLN02876 620 lvdiqtpgvqikrpllvfgfddaphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMV 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 257 NYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNC---LQLHEAKRLDSATAcMAKYWASELQNSVAYDCVQLHG 333
Cdd:PLN02876 700 QRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAadqLDRLGNKKARGIIA-MAKVAAPNMALKVLDMAMQVHG 778
|
330 340 350
....*....|....*....|....*....|....*.
gi 1777253557 334 GWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAR 369
Cdd:PLN02876 779 AAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
38-191 |
9.00e-10 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 60.04 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 38 TPSAKNLTDIGIRrifSSEHDIFRKSIRKFFQEEviPHHSEWEKAGEVSRE-VWEKAGKQGLLGVNTAEHLGGIGGDLYY 116
Cdd:cd01150 11 TFDWKALTHILEG---GEENLRRKREVERELESD--PLFQRELPSKHLSREeLYEELKRKAKTDVERMGELMADDPEKML 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777253557 117 AAVVWEEQAYSNCSGPgFSVHSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKD 191
Cdd:cd01150 86 ALTNSLGGYDLSLGAK-LGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYD 159
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
169-201 |
8.19e-09 |
|
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: 52.28 E-value: 8.19e-09
10 20 30
....*....|....*....|....*....|....
gi 1777253557 169 AIAMTELGAGSDLQGIKTNA-KKDGSDWILNGSK 201
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTK 34
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
240-361 |
1.34e-07 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 50.04 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 240 IADMAVSASEFMFEETRNYVKQRK--AFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDS--------AT 309
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGkpvtpalrAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1777253557 310 ACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNE 361
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
75-201 |
1.40e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 53.33 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 75 HHSEWEKAGEVS-----REVWEKAGKQGLLGVNTAEHLGGIGGDLYYAAVVWEEQAYSNcsgPGFSVHSGI---VMSYIT 146
Cdd:PTZ00456 85 EGCVLLKDGNVTtpkgfKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATAN---WGFSMYPGLsigAANTLM 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1777253557 147 NYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKK--DGSdWILNGSK 201
Cdd:PTZ00456 162 AWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPsaDGS-YKITGTK 217
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
132-191 |
3.47e-06 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 49.06 E-value: 3.47e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1777253557 132 PGFS-VHSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKD 191
Cdd:PLN02443 96 PGYTdLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFD 156
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
135-191 |
2.82e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 45.99 E-value: 2.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1777253557 135 SVHSGIVMSYITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGIKTNAKKD 191
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYD 152
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
77-229 |
1.88e-04 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 43.08 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 77 SEWEKAGEVSREVWEKAGKQGLLGVNTAEHLGGIGGDL--YYAAVVWEEQAYSNCsGPGFSVHSGIVMSyITNYGSEEQI 154
Cdd:cd01163 15 AERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLpdLYEVVRELAAADSNI-AQALRAHFGFVEA-LLLAGPEQFR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777253557 155 KHFIPQMTAGKCIGAiAMTELGaGSDLQGIKTNAKKDGSDWILNGSK--DTAELFFEdvRLPASALLGEENKGFYYI 229
Cdd:cd01163 93 KRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKfySTGALFSD--WVTVSALDEEGKLVFAAV 165
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
78-184 |
7.07e-03 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 38.40 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777253557 78 EWE---KAGEVSREVWEKAGKQGLLGVNTAEHLGGIGGDLY-YAAVVWEEQAYS----------NCSGPGfsvhsgivmS 143
Cdd:PRK13026 99 DWDivqNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYaNSTIVSKIATRSvsaavtvmvpNSLGPG---------E 169
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1777253557 144 YITNYGSEEQIKHFIPQMTAGKCIGAIAMTELGAGSDLQGI 184
Cdd:PRK13026 170 LLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAI 210
|
|
| |
