|
Name |
Accession |
Description |
Interval |
E-value |
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
59-430 |
0e+00 |
|
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: 639.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 59 DEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASVAVF 138
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 139 CEVQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWVSSAEYAGLF 217
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 218 LVMANVDPTIGYKGITTFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGSLNEGRIGI 297
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 298 AAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEI 377
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 795167001 378 AGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDA 430
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
56-428 |
2.04e-170 |
|
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: 482.42 E-value: 2.04e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 56 TLTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASV 135
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 136 AVFCEVQNTLINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWVSSAEYA 214
Cdd:COG1960 84 ALPVGVHNGAAEALLR-FGTEEQKERYLPRLASgEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 215 GLFLVMANVDPTIGYKGITTFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGSLNEGR 294
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 295 IGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYA 374
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 795167001 375 SEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:COG1960 323 TEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRL 376
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
57-430 |
1.57e-122 |
|
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: 360.57 E-value: 1.57e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 57 LTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASVA 136
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 137 V-FCEVQNTLINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWVSSAEYA 214
Cdd:cd01156 82 LsYGAHSNLCINQIYR-NGSAAQKEKYLPKLISgEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 215 GLFLVMANVDPTIGYKGITTFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGSLNEGR 294
Cdd:cd01156 161 DTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 295 IGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYA 374
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 795167001 375 SEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDA 430
Cdd:cd01156 321 AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
148-426 |
1.92e-119 |
|
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: 351.20 E-value: 1.92e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 148 TLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWVSSAEYAGLFLVMANVDP- 225
Cdd:cd00567 46 ALLLAYGTEEQKERYLPPLASgEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEe 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 226 TIGYKGITTFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGSLNEGRIGIAAQMLGLA 305
Cdd:cd00567 126 GPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 306 QGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFI-KEASMAKYYASEIAGQTTSK 384
Cdd:cd00567 206 RAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEArLEAAMAKLFATEAAREVADL 285
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 795167001 385 CIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:cd00567 286 AMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
60-428 |
1.01e-105 |
|
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: 317.52 E-value: 1.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 60 EEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASVAVFc 139
Cdd:cd01160 2 EHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 140 EVQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWVSSAEYAGLFL 218
Cdd:cd01160 81 SLHTDIVSPYITRAGSPEQKERVLPQMVAgKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 219 VMANVD-PTIGYKGITTFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGSLNEGRIGI 297
Cdd:cd01160 161 VVARTGgEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 298 AAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEI 377
Cdd:cd01160 241 AAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATEL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 795167001 378 AGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01160 321 QNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
57-428 |
2.63e-105 |
|
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: 316.69 E-value: 2.63e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 57 LTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASVA 136
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 137 VFCEVQNtLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWVSSAEYAG 215
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTmEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 216 LFLVMANVDPTiGYKGITTFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGSLNEGRI 295
Cdd:cd01162 160 VYVVMARTGGE-GPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 296 GIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKP-FIKEASMAKYYA 374
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAKRFA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 795167001 375 SEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01162 319 TDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARAL 372
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
57-426 |
5.23e-100 |
|
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: 304.39 E-value: 5.23e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 57 LTDEEMMIKSSVKKFAQEQIAPLVstMDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAkVDASVA 136
Cdd:cd01161 27 QTEELNMLVGPVEKFFEEVNDPAK--NDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVG-MDLGFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 137 VFCEVQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADK--EGDYYVLNGSKMWVSSAEY 213
Cdd:cd01161 104 VTLGAHQSIGFKGILLFGTEAQKEKYLPKLASgEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITNGGI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 214 AGLFLVMAN---VDPTIGYK-GITTFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGS 289
Cdd:cd01161 184 ADIFTVFAKtevKDATGSVKdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 290 LNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAG--KPFIKEA 367
Cdd:cd01161 264 LNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGlkAEYQIEA 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 795167001 368 SMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:cd01161 344 AISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIAL 402
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
57-430 |
4.04e-92 |
|
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: 282.94 E-value: 4.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 57 LTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASVA 136
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 137 VFCEVqNTLINTLIRKHGTEEQKATYLPQLTTEK-VGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWVSSAEYAG 215
Cdd:cd01157 81 TAIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPlMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 216 LFLVMANVDP---TIGYKGITTFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGSLNE 292
Cdd:cd01157 160 WYFLLARSDPdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 293 GRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFIKEASMAKY 372
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 795167001 373 YASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAK-HIDA 430
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISReHLGK 378
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
57-428 |
5.69e-89 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 275.99 E-value: 5.69e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 57 LTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSI----IQGLFqqGLMGIEVDPKYGGTGASFLSTVIVIEELAKVD 132
Cdd:PLN02519 26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlwkLMGDF--NLHGITAPEEYGGLGLGYLYHCIAMEEISRAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 133 ASVAV-FCEVQNTLINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWVSS 210
Cdd:PLN02519 104 GSVGLsYGAHSNLCINQLVR-NGTPAQKEKYLPKLISgEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 211 AEYAGLFLVMANVDPTIGYKGITTFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGSL 290
Cdd:PLN02519 183 GPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 291 NEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFIKEASMA 370
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGV 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 795167001 371 KYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:PLN02519 343 ILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
57-419 |
2.50e-83 |
|
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: 260.75 E-value: 2.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 57 LTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSIIQGLFQQGLMGIEVDpKYGGTGASFLSTVIVIEELAKVDASVA 136
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 137 VFCEVQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWVSSAEYAG 215
Cdd:cd01151 92 SFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASgELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 216 LFLVMANVDPTIGYKGittFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQVgHGYKYAIGSLNEGRI 295
Cdd:cd01151 172 VFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 296 GIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYAS 375
Cdd:cd01151 248 GIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNC 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 795167001 376 EIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNI 419
Cdd:cd01151 328 GKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDI 371
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
45-419 |
9.22e-71 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 229.05 E-value: 9.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 45 TNNGLHLAPLQTLTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIV 124
Cdd:PTZ00461 25 TSASRAFMDLYNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVII 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 125 IEELAKVDASVAVFCEVQNTLINTLIRKHGTEEQKATYLPQ-LTTEKVGSFCLSEAGAGSDSFALKTRADKEGD-YYVLN 202
Cdd:PTZ00461 105 HHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKvLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 203 GSKMWVSSAEYAGLFLVMANVDPTIgykgiTTFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQVGHG 282
Cdd:PTZ00461 185 GSKIWITNGTVADVFLIYAKVDGKI-----TAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 283 YKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKP 362
Cdd:PTZ00461 260 MVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNK 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795167001 363 FIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKI-----GTIYEGASNI 419
Cdd:PTZ00461 340 NRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLleiggGTIEAHHKNI 401
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
68-428 |
8.01e-63 |
|
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: 208.01 E-value: 8.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 68 VKKFAQEQIAPLVSTMDEN------------SKMEKSIiQGLFQQGLMGIEVDPKYGGTGASfLSTVIVIEELAKVDASV 135
Cdd:cd01153 5 VARLAENVLAPLNADGDREgpvfddgrvvvpPPFKEAL-DAFAEAGWMALGVPEEYGGQGLP-ITVYSALAEIFSRGDAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 136 AVFCEVQNTLINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGD-YYVLNGSKMWVSSAEY 213
Cdd:cd01153 83 LMYASGTQGAAATLLA-HGTEAQREKWIPRLAEgEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 214 AG----LFLVMANV-DPTIGYKGITTFLV-----DRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPeanILGQVGHGY 283
Cdd:cd01153 162 DMseniVHLVLARSeGAPPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 284 KYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQG--------LQHQVAHMATQLEAARLLTYNAAR 355
Cdd:cd01153 239 AQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAvtiihhpdVRRSLMTQKAYAEGSRALDLYTAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 356 L--LEAGKPFIKEAS------------MAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQL 421
Cdd:cd01153 319 VqdLAERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQA 398
|
....*..
gi 795167001 422 NTIAKHI 428
Cdd:cd01153 399 LDLIGRK 405
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
280-428 |
3.94e-61 |
|
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: 195.17 E-value: 3.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 280 GHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEA 359
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795167001 360 GKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
19-419 |
1.46e-60 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 202.39 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 19 FPTCLSSWKIPPHVSKSSQSEALLditnnglhlaplqtlTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSIIQGLF 98
Cdd:PLN02526 6 FPQATPASIFPPSVSDYYQFDDLL---------------TPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 99 QQGLMGIEVDpKYGGTGASFLSTVIVIEELAKVDASVAVFCEVQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLS 177
Cdd:PLN02526 71 SLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQlDTVACWALT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 178 EAGAGSDSFALKTRADKEGDYYVLNGSKMWVSSAEYAGLFLVMANVDPTigyKGITTFLVDRDTPGLHIGKPENKLGLRA 257
Cdd:PLN02526 150 EPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTT---NQINGFIVKKGAPGLKATKIENKIGLRM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 258 SSTCPLTFENVKVPEANILGQVgHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVA 337
Cdd:PLN02526 227 VQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 338 HMATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGAS 417
Cdd:PLN02526 306 RMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTY 385
|
..
gi 795167001 418 NI 419
Cdd:PLN02526 386 DI 387
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
57-432 |
1.65e-60 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 201.50 E-value: 1.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 57 LTDE-EMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASV 135
Cdd:PRK12341 5 LTEEqELLLASIRELITRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 136 AVFCEVQNtlINTlIRKHGTEEQKA-TYLPQLTTEKVGsFCL--SEAGAGSDSFALKTRAD-KEGDYYvLNGSKMWVSSA 211
Cdd:PRK12341 85 FLITNGQC--IHS-MRRFGSAEQLRkTAESTLETGDPA-YALalTEPGAGSDNNSATTTYTrKNGKVY-LNGQKTFITGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 212 EYAGLFLVMA-NVDPTIGYKGITTFLVDRDTPGLHIgKPENKLGLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGSL 290
Cdd:PRK12341 160 KEYPYMLVLArDPQPKDPKKAFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 291 NEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFIKEASMA 370
Cdd:PRK12341 239 EMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795167001 371 KYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY 432
Cdd:PRK12341 319 KLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDY 380
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
97-428 |
2.11e-56 |
|
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: 190.64 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 97 LFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASVAVFCEVQNTLINTLIRkHGTEEQKATYLPQ-LTTEKVgsFC 175
Cdd:cd01152 44 LAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILA-YGTDEQKRRFLPPiLSGEEI--WC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 176 L--SEAGAGSDSFALKTRADKEGDYYVLNGSKMWVSSAEYAGLFLVMANVDPTI-GYKGITTFLVDRDTPGLHIgKPENK 252
Cdd:cd01152 121 QgfSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEApKHRGISILLVDMDSPGVTV-RPIRS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 253 LgLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGSLNEGR---IGIAAQMLGLAQGcfdytipYIKERMQFGKRLFDF 329
Cdd:cd01152 200 I-NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERvsiGGSAATFFELLLA-------RLLLLTRDGRPLIDD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 330 QGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMG--------GVGYTKDYPVE 401
Cdd:cd01152 272 PLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGtaallrdpAPGAELAGRWE 351
|
330 340
....*....|....*....|....*..
gi 795167001 402 KYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01152 352 ADYLRSRATTIYGGTSEIQRNIIAERL 378
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
56-432 |
4.24e-51 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 176.56 E-value: 4.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 56 TLTDEEMMIKSSVKKF-AQEQIAPLVSTMDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDAS 134
Cdd:PRK03354 4 NLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 135 VAVFCEVQNTlINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWVSSAEY 213
Cdd:PRK03354 84 TYVLYQLPGG-FNTFLR-EGTQEQIDKIMAFRGTgKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 214 AGLFLVMANVDPTIGYKGITTFLVDRDTPGLHIGKPEnKLGLRASSTCPLTFENVKVPEANILGQVGHGYKYAIGSLNEG 293
Cdd:PRK03354 162 TPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 294 RIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFIKEASMAKYY 373
Cdd:PRK03354 241 RFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 795167001 374 ASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY 432
Cdd:PRK03354 321 CANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQY 379
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
132-420 |
1.03e-43 |
|
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: 157.92 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 132 DASVAVFCEVQNTLINT-LIRKHGTEEQKaTYLPQLTTEKV-----GSFCLSEAGAGSDSFALKTRADK-EGDYYVLNGS 204
Cdd:cd01154 104 DAAAGLLCPLTMTDAAVyALRKYGPEELK-QYLPGLLSDRYktgllGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 205 KmWVSSAEYAGLFLVMAN-VDPTIGYKGITTFLVDRDTP-----GLHIGKPENKLGLRASSTCPLTFENVkvpEANILGQ 278
Cdd:cd01154 183 K-WFASAPLADAALVLARpEGAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGD 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 279 VGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLL- 357
Cdd:cd01154 259 EGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFd 338
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795167001 358 --EAGKPfiKEASMA-------KYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQ 420
Cdd:cd01154 339 raAADKP--VEAHMArlatpvaKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
68-426 |
5.56e-38 |
|
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: 141.76 E-value: 5.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 68 VKKFAQEQIAPLVSTMDE------NSKMEKS-IIQGLFQ----QGLMGIEVDPKYGGTGASFLSTVIVIEELAK-VDASV 135
Cdd:cd01155 10 VKAFMEEHVYPAEQEFLEyyaeggDRWWTPPpIIEKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRsFFAPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 136 AVFCEVQNTLINTLIRKHGTEEQKATYLPQLTTEKVGS-FCLSEAG-AGSDSFALKTRADKEGDYYVLNGSKMWVSSA-- 211
Cdd:cd01155 90 VFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSaFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAgd 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 212 EYAGLFLVMANVDPTIG--YKGITTFLVDRDTPGLHIGKPENKLGLRAS--STCPLTFENVKVPEANILGQVGHGYKYAI 287
Cdd:cd01155 170 PRCKIAIVMGRTDPDGAprHRQQSMILVPMDTPGVTIIRPLSVFGYDDAphGHAEITFDNVRVPASNLILGEGRGFEIAQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 288 GSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGKPFI--K 365
Cdd:cd01155 250 GRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAarK 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795167001 366 EASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:cd01155 330 EIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
58-168 |
1.76e-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: 132.20 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 58 TDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASVAV 137
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|.
gi 795167001 138 FCEVQNTLINTLIRKHGTEEQKATYLPQLTT 168
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
33-428 |
3.48e-36 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 140.39 E-value: 3.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 33 SKSSQSEALLDITNNGLHLAP----LQTLTDE--------EMMIKSSVK------------KFAQEQIAPLVSTMDENS- 87
Cdd:PTZ00456 8 SAAASHAAAVSASARSLQYQPrirdVQFLVEEvfnmydhyEKLGKTDVTkelmdslleeasKLATQTLLPLYESSDSEGc 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 88 -----------KMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASVAVFCEVQNTLINTLIrKHGTE 156
Cdd:PTZ00456 88 vllkdgnvttpKGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLM-AWGSE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 157 EQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGD-YYVLNGSKMWVSSAEYAG----LFLVMANVDPTI-GY 229
Cdd:PTZ00456 167 EQKEQYLTKLVSgEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDHDLteniVHIVLARLPNSLpTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 230 KGITTFLVDRdtpglHIGKP---------------ENKLGLRASSTCPLTFENVKvpeANILGQVGHGYKYAIGSLNEGR 294
Cdd:PTZ00456 247 KGLSLFLVPR-----HVVKPdgsletaknvkciglEKKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTFMNTAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 295 IGIAAQMLGLAQGCFDYTIPYIKERMQF------------GKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLL----E 358
Cdd:PTZ00456 319 VGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLdihaA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 359 AGKPFIKEA---------SMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQ-LNTIAKHI 428
Cdd:PTZ00456 399 AKDAATREAldheigfytPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQaLDFIGRKV 478
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
173-266 |
8.17e-30 |
|
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: 111.22 E-value: 8.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 173 SFCLSEAGAGSDSFALKTRA-DKEGDYYVLNGSKMWVSSAEYAGLFLVMANVDPTIGYKGITTFLVDRDTPGLHIGKPEN 251
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 795167001 252 KLGLRASSTCPLTFE 266
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
296-417 |
6.80e-29 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 110.13 E-value: 6.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 296 GIAAQMLGLAQGCFDYTIPYIKER--MQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAA----RLLEAGKPF----IK 365
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRvrAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVtpalRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 795167001 366 EASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGAS 417
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
152-426 |
1.46e-27 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 115.66 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 152 KHGTEEQKATYLPQLTTEKVGS-FCLSEAG-AGSDSFALKTRADKEGDYYVLNGSKMWVSSA--EYAGLFLVMANVDPTI 227
Cdd:PLN02876 531 RYGNKEQQLEWLIPLLEGKIRSgFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNA 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 228 G-YKGITTFLVDRDTPGLHIGKPENKLGLRAS--STCPLTFENVKVPEANILGQVGHGYKYAIGSLNEGRIGIAAQMLGL 304
Cdd:PLN02876 611 PkHKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGA 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 305 AQGCFDYTIPYIKERMQFGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLE--AGKPFIKEASMAKYYASEIAGQTT 382
Cdd:PLN02876 691 AERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrlGNKKARGIIAMAKVAAPNMALKVL 770
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 795167001 383 SKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:PLN02876 771 DMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
47-378 |
1.38e-24 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 106.58 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 47 NGLHLAPLQTLTDEEmmikssvKKFAQEQIAPLVSTMDE-----NSK-MEKSIIQGLFQQGLMGIEVDPKYGGTGASFLS 120
Cdd:PRK13026 68 QKLHSYPKPTLTAEE-------QAFIDNEVETLLTMLDDwdivqNRKdLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 121 TVIVIEELAKVDASVAVFCEVQNTL-INTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALK-----TRAD 193
Cdd:PRK13026 141 NSTIVSKIATRSVSAAVTVMVPNSLgPGELLTHYGTQEQKDYWLPRLADgTEIPCFALTGPEAGSDAGAIPdtgivCRGE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 194 KEGDYYV---LNGSKMWVSSAEYA---GLFLVMANVDPTIGYK---GITTFLVDRDTPGLHIGKPENKLGLrASSTCPLT 264
Cdd:PRK13026 221 FEGEEVLglrLTWDKRYITLAPVAtvlGLAFKLRDPDGLLGDKkelGITCALIPTDHPGVEIGRRHNPLGM-AFMNGTTR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 265 FENVKVPEANILG---QVGHGYKYAIGSLNEGRiGIAAQMLGLAQG--CFDYTIPYIKERMQFGKRLFDFQGLQHQVAHM 339
Cdd:PRK13026 300 GKDVFIPLDWIIGgpdYAGRGWRMLVECLSAGR-GISLPALGTASGhmATRTTGAYAYVRRQFGMPIGQFEGVQEALARI 378
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 795167001 340 AT---QLEAARLLTYNAarlLEAG-KPFIKEAsMAKYYASEIA 378
Cdd:PRK13026 379 AGntyLLEAARRLTTTG---LDLGvKPSVVTA-IAKYHMTELA 417
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
109-381 |
2.03e-17 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 84.87 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 109 PK-YGGTGASFLSTVIVIEELAKVDASVAVFCEVQNTL-INTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDS 185
Cdd:PRK09463 129 PKeYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLgPGELLLHYGTDEQKDHYLPRLARgEEIPCFALTSPEAGSDA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 186 FALK-----TRADKEGD---YYVLNGSKMWVSSAEYAGLF-LVMANVDPT--IGYK---GITTFLVDRDTPGLHIGKPEN 251
Cdd:PRK09463 209 GSIPdtgvvCKGEWQGEevlGMRLTWNKRYITLAPIATVLgLAFKLYDPDglLGDKedlGITCALIPTDTPGVEIGRRHF 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 252 KLGLrASSTCPLTFENVKVPEANILG---QVGHGYKYAIGSLNEGR-IGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLF 327
Cdd:PRK09463 289 PLNV-PFQNGPTRGKDVFIPLDYIIGgpkMAGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIG 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 795167001 328 DFQGLQHQVAHMAT---QLEAARLLTYNAARLLEagKPFIKEAsMAKYYASEIAGQT 381
Cdd:PRK09463 368 KFEGIEEPLARIAGnayLMDAARTLTTAAVDLGE--KPSVLSA-IAKYHLTERGRQV 421
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
74-407 |
4.12e-15 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 76.23 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 74 EQIAPLVST----MDENSKMEKSIIQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASVAVFCEVQntlintl 149
Cdd:cd01159 4 EDLAPLIRErapeAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIV------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 150 irkhGTEEQKATYLPQLTTEKVgsfcLSEAGAG--SDSFALKTRADKEGDYYVLNGSKMWVSSAEYAGLFLVMANVDPTI 227
Cdd:cd01159 77 ----ATHSRMLAAFPPEAQEEV----WGDGPDTllAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 228 GYKGITTFLVDRDtpGLHIGKPENKLGLRASSTCPLTFENVKVPEANIL----GQVGHG-------YKYAIGSLNEgrIG 296
Cdd:cd01159 149 GGPLPRAFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdMMAGDGpggstpvYRMPLRQVFP--LS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 297 IAAQMLGLAQGCFDYTIPYIKERMQ---FGKRLFDFQGLQHQVAHMATQLEAARLLTYNAARLLEA----GKPFIKEASM 369
Cdd:cd01159 225 FAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAhalaGGPIDVEERA 304
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 795167001 370 ----AKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDA 407
Cdd:cd01159 305 rirrDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDI 346
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
176-419 |
8.21e-14 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 73.25 E-value: 8.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 176 LSEAGAGSDSFALKTRADK-EGDYYVLNGSKmWVSSAEYAGLFLVMANVDptigyKGITTFLVDRDTP-----GLHIGKP 249
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-----GGLSCFFVPRFLPdgqrnAIRLERL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 250 ENKLGLRASSTCPLTFENVKvpeANILGQVGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRLFDf 329
Cdd:PRK11561 258 KDKLGNRSNASSEVEFQDAI---GWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIE- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 330 QGLQHQV-AHMATQLEA-----------------------ARLLTYNAA-RLLEAGKPFIKEAsmakyyaseiagqttsk 384
Cdd:PRK11561 334 QPLMRQVlSRMALQLEGqtallfrlarawdrradakealwARLFTPAAKfVICKRGIPFVAEA----------------- 396
|
250 260 270
....*....|....*....|....*....|....*
gi 795167001 385 cIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNI 419
Cdd:PRK11561 397 -MEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
94-408 |
1.71e-13 |
|
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: 71.59 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 94 IQGLFQQGLMGIEVDPKYGGTGASFLSTVIVIEELAKVDASVAvfcevqntlinTLIRKH----------GTEEQKATYL 163
Cdd:cd01163 28 VALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIA-----------QALRAHfgfvealllaGPEQFRKRWF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 164 PQLTTEKVGSFCLSEAGAGSDSFALkTRADKEGDYYVLNGSKMWVSSAEYAGLFLVMAnVDPTigyKGITTFLVDRDTPG 243
Cdd:cd01163 97 GRVLNGWIFGNAVSERGSVRPGTFL-TATVRDGGGYVLNGKKFYSTGALFSDWVTVSA-LDEE---GKLVFAAVPTDRPG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 244 LHIGKPENKLGLR--ASSTcpLTFENVKVPEANILGQvghGYKYAIGSLNEGRIGI--AAQMLGLAQGCFDYTIPYIKER 319
Cdd:cd01163 172 ITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPR---PNAPDRGTLLTAIYQLvlAAVLAGIARAALDDAVAYVRSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 320 mqfgKRLF----------DFQGLQHqVAHMATQLEAARLLTYNAARLLE----AGKPFIKEA--------SMAKYYASEI 377
Cdd:cd01163 247 ----TRPWihsgaesardDPYVQQV-VGDLAARLHAAEALVLQAARALDaaaaAGTALTAEArgeaalavAAAKVVVTRL 321
|
330 340 350
....*....|....*....|....*....|.
gi 795167001 378 AGQTTSKCIEWMGGVGYTKDYPVEKYFRDAK 408
Cdd:cd01163 322 ALDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
141-428 |
4.51e-13 |
|
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: 70.82 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 141 VQNTLINTLIRKHGTEEQKATYLP-QLTTEKVGSFCLSEAGAGSDSFALKTRA--DKEGDYYVLN-----GSKMWVS--- 209
Cdd:cd01150 104 LHLGLFGNAIKNLGTDEHQDYWLQgANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGnlg 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 210 -SAEYAGLF--LVMANVDptigyKGITTFLV---DRDT----PGLHIGKPENKLGLRASSTCPLTFENVKVPEANIL--- 276
Cdd:cd01150 184 kTATHAVVFaqLITPGKN-----HGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrf 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 277 GQV-------------GHGYKYAIGSLNEGRIGIAaqMLGLAQGCFDYTIP--YIKERMQFGKRlfdfqGLQHQVAHMAT 341
Cdd:cd01150 259 GDVspdgtyvspfkdpNKRYGAMLGTRSGGRVGLI--YDAAMSLKKAATIAirYSAVRRQFGPK-----PSDPEVQILDY 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 342 QLEAARLLTYNAA--------------------RLLEAGKPFIKE----ASMAKYYASEIAGQTTSKCIEWMGGVGYTKD 397
Cdd:cd01150 332 QLQQYRLFPQLAAayafhfaakslvemyheiikELLQGNSELLAElhalSAGLKAVATWTAAQGIQECREACGGHGYLAM 411
|
330 340 350
....*....|....*....|....*....|.
gi 795167001 398 YPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01150 412 NRLPTLRDDNDPFCTYEGDNTVLLQQTANYL 442
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
124-432 |
5.36e-12 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 67.58 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 124 VIEELAKVDASVAVFCEVQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRA--DKEGDYYV 200
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNlDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 201 LN-----GSKMWVSSAEYAGLFL-VMANVD-PTIGYKGIT-----TFLVD-RDT------PGLHIGKPENKLGLRASSTC 261
Cdd:PLN02636 206 INtpndgAIKWWIGNAAVHGKFAtVFARLKlPTHDSKGVSdmgvhAFIVPiRDMkthqvlPGVEIRDCGHKVGLNGVDNG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 262 PLTFENVKVPEANIL---GQVGHGYKYA-------------IGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGK- 324
Cdd:PLN02636 286 ALRFRSVRIPRDNLLnrfGDVSRDGKYTsslptinkrfaatLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPp 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 325 -----RLFDFQGLQHQVAHMATQLEAARLLT-YNAARLLEAGKPFIKE--------ASMAKYYASEIAGQTTSKCIEWMG 390
Cdd:PLN02636 366 kqpeiSILDYQSQQHKLMPMLASTYAFHFATeYLVERYSEMKKTHDDQlvadvhalSAGLKAYITSYTAKALSTCREACG 445
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 795167001 391 GVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY 432
Cdd:PLN02636 446 GHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQY 487
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
102-304 |
9.43e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 47.95 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 102 LMGIEVDPKYGGTGASFLSTVIVIEEL-AKVDA---SVAVFCEVQNTLINTLirkhGTEEQKATYLPQLTTEKVGSFCLS 177
Cdd:PTZ00457 65 LYGARIATEYGGLGLGHTAHALIYEEVgTNCDSkllSTIQHSGFCTYLLSTV----GSKELKGKYLTAMSDGTIMMGWAT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 178 EAGAGSDSFALKTRADKEGD-YYVLNGSKMWVSsAEYAGLFLVMAN-VDPTIGYKGITT------FLVDRDTPGLHIGKP 249
Cdd:PTZ00457 141 EEGCGSDISMNTTKASLTDDgSYVLTGQKRCEF-AASATHFLVLAKtLTQTAAEEGATEvsrnsfFICAKDAKGVSVNGD 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 795167001 250 EnklglrasstcpLTFENVkvPEANILGQVGHGYKYAIGSLNEGRIGIAAQMLGL 304
Cdd:PTZ00457 220 S------------VVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGI 260
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
150-336 |
1.36e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 47.53 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 150 IRKHGTEEQKATYLPQ-LTTEKVGSFCLSEAGAGSDSFALKTRA--DKEGDYYVLN-----GSKMWVSS----AEYAglf 217
Cdd:PTZ00460 106 FQVLGTDEQINLWMPSlLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElgflCNFA--- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795167001 218 LVMANVDPTIGYKGITTFLV---DRDT----PGLHIGKPENKLGLRASSTCPLTFENVKVPEANIL---------GQVG- 280
Cdd:PTZ00460 183 LVYAKLIVNGKNKGVHPFMVrirDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikvsedGQVEr 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795167001 281 HGykyaigslNEgRIGIAAQMLGLAQGCFDYT----------IPYIKERMQFGK------RLFDFQGLQHQV 336
Cdd:PTZ00460 263 QG--------NP-KVSYASMMYMRNLIIDQYPrfaaqaltvaIRYSIYRQQFTNdnkqenSVLEYQTQQQKL 325
|
|
| |
