|
Name |
Accession |
Description |
Interval |
E-value |
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
42-412 |
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: 633.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 42 EEESSIVGTVRRFAVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVSVF 121
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 122 VDVQNTLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGHAQFF 200
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 201 LVFANADSAKGYKGITCFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEYGKGYKYAIECLNAGRIGI 280
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 281 GAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLPFVREAAMAKLFASQV 360
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1845970424 361 ATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAKLVD 412
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
39-411 |
7.76e-168 |
|
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: 475.48 E-value: 7.76e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 39 QLSEEESSIVGTVRRFAVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSV 118
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 119 SVFVDVQNtLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGHA 197
Cdd:COG1960 84 ALPVGVHN-GAAEALLRFGTEEQKERYLPRLASgEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 198 QFFLVFANADSAKGYKGITCFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEYGKGYKYAIECLNAGR 277
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 278 IGIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLPFVREAAMAKLFA 357
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1845970424 358 SQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAKLV 411
Cdd:COG1960 323 TEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRL 376
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
128-409 |
2.21e-121 |
|
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: 355.44 E-value: 2.21e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 128 LVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGHAQFFLVFAN- 205
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASgEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARt 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 206 ADSAKGYKGITCFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEYGKGYKYAIECLNAGRIGIGAQML 285
Cdd:cd00567 123 DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVAL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 286 GLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLPFVR-EAAMAKLFASQVATTA 364
Cdd:cd00567 203 GAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARlEAAMAKLFATEAAREV 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1845970424 365 TSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAK 409
Cdd:cd00567 283 ADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
40-409 |
1.02e-105 |
|
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: 317.43 E-value: 1.02e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 40 LSEEESSIVGTVRRFAVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVS 119
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 120 VFVDVQNTLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGHAQ 198
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISgEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 199 FFLVFANADSAKGYKGITCFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEYGKGYKYAIECLNAGRI 278
Cdd:cd01156 162 TLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 279 GIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLPFVREAAMAKLFAS 358
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1845970424 359 QVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAK 409
Cdd:cd01156 322 EKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGR 372
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
34-409 |
7.78e-99 |
|
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: 300.92 E-value: 7.78e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 34 PSPLQ-QLSEEESSIVGTVRRFAVNVIKPlvREMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPGssfFDAVL--VIEE 110
Cdd:cd01161 20 PSVLTeEQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLG---LNNTQyaRLAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 111 LAKVDPSVSVFVDVQNTLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKK--DGDDFVISGS 187
Cdd:cd01161 95 IVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASgEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 188 KMWITNAGHAQFFLVFAN-----ADSAKGYKgITCFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEY 262
Cdd:cd01161 175 KIWITNGGIADIFTVFAKtevkdATGSVKDK-ITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 263 GKGYKYAIECLNAGRIGIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQN 342
Cdd:cd01161 254 GDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDR 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845970424 343 GL--PFVREAAMAKLFASQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAK 409
Cdd:cd01161 334 GLkaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIAL 402
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
40-409 |
7.43e-95 |
|
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: 289.34 E-value: 7.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 40 LSEEESSIVGTVRRFAVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVS 119
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 120 VFVDVQNtLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGHAQ 198
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTmEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 199 FFLVFANADsAKGYKGITCFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEYGKGYKYAIECLNAGRI 278
Cdd:cd01162 160 VYVVMARTG-GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 279 GIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLP-FVREAAMAKLFA 357
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAKRFA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1845970424 358 SQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAK 409
Cdd:cd01162 319 TDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIAR 370
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
42-409 |
3.29e-93 |
|
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: 285.16 E-value: 3.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 42 EEESSIVGTVRRFAVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDpSVSVF 121
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAG-GSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 122 VDVQNTLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGHAQFF 200
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAgKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 201 LVFANAD-SAKGYKGITCFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEYGKGYKYAIECLNAGRIG 279
Cdd:cd01160 160 IVVARTGgEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 280 IGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLPFVREAAMAKLFASQ 359
Cdd:cd01160 240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1845970424 360 VATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAK 409
Cdd:cd01160 320 LQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
40-411 |
2.92e-89 |
|
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: 275.23 E-value: 2.92e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 40 LSEEESSIVGTVRRFAVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVS 119
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 120 VFVDVQNTLVAPLIIQlGTEEQKQKYLPKIVTEA-IGSFALSETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGHAQ 198
Cdd:cd01157 81 TAIEANSLGQMPVIIS-GNDEQKKKYLGRMTEEPlMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 199 FFLVFANADS---AKGYKGITCFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEYGKGYKYAIECLNA 275
Cdd:cd01157 160 WYFLLARSDPdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 276 GRIGIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLPFVREAAMAKL 355
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1845970424 356 FASQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAKLV 411
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREH 375
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
38-402 |
4.29e-78 |
|
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: 246.89 E-value: 4.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 38 QQLSEEESSIVGTVRRFAVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIeIPEKYGGPGSSFFDAVLVIEELAKVDPS 117
Cdd:cd01151 11 DLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERVDSG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 118 VSVFVDVQNTLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGH 196
Cdd:cd01151 90 YRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASgELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 197 AQFFLVFANADSAKGYKGitcFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEyGKGYKYAIECLNAG 276
Cdd:cd01151 170 ADVFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPG-AEGLRGPFKCLNNA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 277 RIGIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLPFVREAAMAKLF 356
Cdd:cd01151 246 RYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRN 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1845970424 357 ASQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNI 402
Cdd:cd01151 326 NCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDI 371
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
50-409 |
2.67e-77 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 245.17 E-value: 2.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 50 TVRRFAVNVIKPLVREMDDKSQMHQSV----ITGTFenGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVSVFVDVQ 125
Cdd:PLN02519 36 SVQQFAQENIAPHAAAIDATNSFPKDVnlwkLMGDF--NLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 126 NTLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGHAQFFLVFA 204
Cdd:PLN02519 114 SNLCINQLVRNGTPAQKEKYLPKLISgEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 205 NADSAKGYKGITCFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEYGKGYKYAIECLNAGRIGIGAQM 284
Cdd:PLN02519 194 KTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 285 LGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLPFVREAAMAKLFASQVATTA 364
Cdd:PLN02519 274 LGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQV 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1845970424 365 TSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAK 409
Cdd:PLN02519 354 ALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
19-409 |
9.54e-74 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 236.37 E-value: 9.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 19 ATMSTKPRAHIDGHVPSPlqqlseEESSIVGTVRRFAVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPG 98
Cdd:PTZ00461 22 ATMTSASRAFMDLYNPTP------EHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 99 SSFFDAVLVIEELAKVDPSVSVFVDVQNTLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKK 177
Cdd:PTZ00461 96 MDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTgEHVGAMGMSEPGAGTDVLGMRTTAKK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 178 DGD-DFVISGSKMWITNAGHAQFFLVFANADSAkgykgITCFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKS 256
Cdd:PTZ00461 176 DSNgNYVLNGSKIWITNGTVADVFLIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 257 SILGEYGKGYKYAIECLNAGRIGIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNA 336
Cdd:PTZ00461 251 NLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSV 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845970424 337 ARMKQNGLPFVREAAMAKLFASQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAK 409
Cdd:PTZ00461 331 SHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITK 403
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
40-402 |
4.44e-60 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 199.95 E-value: 4.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 40 LSEEESSIVGTVRRF-AVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSV 118
Cdd:PRK12341 5 LTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 119 SVFvdvQNTLVAPLIIQLGTEEQKQKYLPKIVTEAIGSFAL--SETGSGSDAFALKTTA-KKDGDDFvISGSKMWITNAG 195
Cdd:PRK12341 85 FLI---TNGQCIHSMRRFGSAEQLRKTAESTLETGDPAYALalTEPGAGSDNNSATTTYtRKNGKVY-LNGQKTFITGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 196 HAQFFLVFA-NADSAKGYKGITCFLVDRNQEGVSVGKKEdKLGIRASSTCSVHFDNVRVHKSSILGEYGKGYKYAIECLN 274
Cdd:PRK12341 161 EYPYMLVLArDPQPKDPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 275 AGRIGIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLPFVREAAMAK 354
Cdd:PRK12341 240 MERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAK 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1845970424 355 LFASQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNI 402
Cdd:PRK12341 320 LYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
81-409 |
2.29e-59 |
|
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: 197.96 E-value: 2.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 81 FENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVSVFVDVQNtLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFAL 159
Cdd:cd01152 45 AAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGID-LAGPTILAYGTDEQKRRFLPPILSgEEIWCQGF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 160 SETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGHAQFFLVFANAD-SAKGYKGITCFLVDRNQEGVSVGKKEDKLGi 238
Cdd:cd01152 124 SEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDpEAPKHRGISILLVDMDSPGVTVRPIRSING- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 239 rASSTCSVHFDNVRVHKSSILGEYGKGYKYAIECLNAGRigigAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQ 318
Cdd:cd01152 203 -GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFER----VSIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 319 IGQTRMEIEAARLLVYNAARMKQNGLPFVREAAMAKLFASQVATTATSKCVEWLGGVGFTKEFP--------VEKFYRDS 390
Cdd:cd01152 278 LARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEADYLRS 357
|
330
....*....|....*....
gi 1845970424 391 KIGTIYEGTSNIQLNTIAK 409
Cdd:cd01152 358 RATTIYGGTSEIQRNIIAE 376
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
263-409 |
1.90e-58 |
|
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: 187.85 E-value: 1.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 263 GKGYKYAIECLNAGRIGIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQN 342
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845970424 343 GLPFVREAAMAKLFASQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAK 409
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
47-408 |
2.04e-57 |
|
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: 193.76 E-value: 2.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 47 IVGTVRRFAVNVIKPLVREMD------DKSQMHqsVITGTFEN-------GLMGIEIPEKYGGPGSSFFDAVLVIEELAK 113
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDregpvfDDGRVV--VPPPFKEAldafaeaGWMALGVPEEYGGQGLPITVYSALAEIFSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 114 VDPSVSVFVDVQNTlvAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKDGD-DFVISGSKMWI 191
Cdd:cd01153 79 GDAPLMYASGTQGA--AATLLAHGTEAQREKWIPRLAEgEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 192 TNAGHAQ----FFLVFANADSA-KGYKGITCFLV-----DRNQEGVSVGKKEDKLGIRASSTCSVHFDNvrvHKSSILGE 261
Cdd:cd01153 157 SAGEHDMseniVHLVLARSEGApPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDN---AKGELIGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 262 YGKGYKYAIECLNAGRIGIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQG---MQH-----QIGQTRMEIEAARLLV 333
Cdd:cd01153 234 EGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAvtiIHHpdvrrSLMTQKAYAEGSRALD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 334 -YNA-----ARMKQNGLPFVREAA--------MAKLFASQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGT 399
Cdd:cd01153 314 lYTAtvqdlAERKATEGEDRKALSaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGT 393
|
....*....
gi 1845970424 400 SNIQLNTIA 408
Cdd:cd01153 394 TGIQALDLI 402
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
130-403 |
3.86e-49 |
|
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: 172.17 E-value: 3.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 130 APLIIQLGTEEQKQKYLPKIVTEA----IGSFALSETGSGSDAFALKTTAKKDGDDF-VISGSKmWITNAGHAQFFLVFA 204
Cdd:cd01154 120 VYALRKYGPEELKQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSGGGVyRLNGHK-WFASAPLADAALVLA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 205 NADSAK-GYKGITCFLVDR-----NQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHkssILGEYGKGYKYAIECLNAGRI 278
Cdd:cd01154 199 RPEGAPaGARGLSLFLVPRlledgTRNGYRIRRLKDKLGTRSVATGEVEFDDAEAY---LIGDEGKGIYYILEMLNISRL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 279 GIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARM---KQNGLP----FVREA- 350
Cdd:cd01154 276 DNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAfdrAAADKPveahMARLAt 355
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1845970424 351 AMAKLFASQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQ 403
Cdd:cd01154 356 PVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
39-416 |
5.02e-49 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 170.78 E-value: 5.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 39 QLSEEESSIVGTVRRF-AVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPS 117
Cdd:PRK03354 4 NLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 118 VSVFVDVQNTLVAplIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGH 196
Cdd:PRK03354 84 TYVLYQLPGGFNT--FLREGTQEQIDKIMAFRGTgKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 197 AQFFLVFANADSAKGYKGITCFLVDRNQEGVSVGKKEdKLGIRASSTCSVHFDNVRVHKSSILGEYGKGYKYAIECLNAG 276
Cdd:PRK03354 162 TPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 277 RIGIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLPFVREAAMAKLF 356
Cdd:PRK03354 241 RFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYF 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 357 ASQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAKLVDIEYQ 416
Cdd:PRK03354 321 CANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
40-402 |
1.45e-47 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 167.72 E-value: 1.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 40 LSEEESSIVGTVRRFAVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIEIpEKYGGPGSSFFDAVLVIEELAKVDPSVS 119
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDASCS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 120 VFVDVQNTLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKDGDDFVISGSKMWITNAGHAQ 198
Cdd:PLN02526 108 TFILVHSSLAMLTIALCGSEAQKQKYLPSLAQlDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 199 FFLVFANADSAKGYKGitcFLVDRNQEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEYgKGYKYAIECLNAGRI 278
Cdd:PLN02526 188 VLVIFARNTTTNQING---FIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 279 GIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAARMKQNGLPFVREAAMAKLFAS 358
Cdd:PLN02526 264 MVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWIT 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1845970424 359 QVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNI 402
Cdd:PLN02526 344 KKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDI 387
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
84-410 |
1.42e-42 |
|
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: 154.08 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 84 GLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVSVF----VDVQNTLVaplIIQLGTEEQKQKYLPKIVTEAIGS-FA 158
Cdd:cd01155 54 GLWNLFLPEVSGLSGLTNLEYAYLAEETGRSFFAPEVFncqaPDTGNMEV---LHRYGSEEQKKQWLEPLLDGKIRSaFA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 159 LSETG-SGSDAFALKTTAKKDGDDFVISGSKMWITNAGHAQ----FFLVFANADSAKGYKGITCFLVDRNQEGVSVgkke 233
Cdd:cd01155 131 MTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRckiaIVMGRTDPDGAPRHRQQSMILVPMDTPGVTI---- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 234 dklgIRASST----------CSVHFDNVRVHKSSILGEYGKGYKYAIECLNAGRIGIGAQMLGLAQGCFDQTIPYLQQRE 303
Cdd:cd01155 207 ----IRPLSVfgyddaphghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSRE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 304 QFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAA-RMKQNGLPFVR-EAAMAKLFASQVATTATSKCVEWLGGVGFTKEF 381
Cdd:cd01155 283 AFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAhMIDTVGNKAARkEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDT 362
|
330 340
....*....|....*....|....*....
gi 1845970424 382 PVEKFYRDSKIGTIYEGTSNIQLNTIAKL 410
Cdd:cd01155 363 PLANMYAWARTLRIADGPDEVHLRSIARM 391
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
41-151 |
4.91e-40 |
|
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: 138.75 E-value: 4.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 41 SEEESSIVGTVRRFAVNVIKPLVREMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVSV 120
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|.
gi 1845970424 121 FVDVQNTLVAPLIIQLGTEEQKQKYLPKIVT 151
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
82-403 |
1.14e-35 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 138.46 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 82 ENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVSVF----VDVQNTLVApliiqLGTEEQKQKYLPKIVT-EAIGS 156
Cdd:PTZ00456 110 AGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYpglsIGAANTLMA-----WGSEEQKEQYLTKLVSgEWSGT 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 157 FALSETGSGSDAFALKTTAKKDGD-DFVISGSKMWITNAGHAQ----FFLVFAN-ADSAKGYKGITCFLVDR---NQEG- 226
Cdd:PTZ00456 185 MCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDHDLteniVHIVLARlPNSLPTTKGLSLFLVPRhvvKPDGs 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 227 ------VSVGKKEDKLGIRASSTCSVHFDNvrvHKSSILGEYGKGYKYAIECLNAGRIGIGAQMLGLAQGCFDQTIPYLQ 300
Cdd:PTZ00456 265 letaknVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYAR 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 301 QR------------EQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAAR----MKQNGLPFVREA---------AMAKL 355
Cdd:PTZ00456 342 ERrsmralsgtkepEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRlldiHAAAKDAATREAldheigfytPIAKG 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1845970424 356 FASQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQ 403
Cdd:PTZ00456 422 CLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQ 469
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
156-249 |
1.07e-33 |
|
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: 121.23 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 156 SFALSETGSGSDAFALKTTA-KKDGDDFVISGSKMWITNAGHAQFFLVFANADSAKGYKGITCFLVDRNQEGVSVGKKED 234
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 1845970424 235 KLGIRASSTCSVHFD 249
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
82-361 |
4.82e-25 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 107.74 E-value: 4.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 82 ENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVSVFVDVQNTLvAP--LIIQLGTEEQKQKYLPKIVT-EAIGSFA 158
Cdd:PRK13026 119 KEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSL-GPgeLLTHYGTQEQKDYWLPRLADgTEIPCFA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 159 LSETGSGSDAFALKTTA-----KKDGDD---FVISGSKMWITNAGHAQFF-LVFANAD-----SAKGYKGITCFLVDRNQ 224
Cdd:PRK13026 198 LTGPEAGSDAGAIPDTGivcrgEFEGEEvlgLRLTWDKRYITLAPVATVLgLAFKLRDpdgllGDKKELGITCALIPTDH 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 225 EGVSVGKKEDKLGIRasstcsvhFDN-------VRVHKSSILG--EY-GKGYKYAIECLNAGRiGIGAQMLGLAQG--CF 292
Cdd:PRK13026 278 PGVEIGRRHNPLGMA--------FMNgttrgkdVFIPLDWIIGgpDYaGRGWRMLVECLSAGR-GISLPALGTASGhmAT 348
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845970424 293 DQTIPYLQQREQFGQRLIDFQGMQH---QIGQTRMEIEAARLLVYNAARMKQNglPFVrEAAMAKLFASQVA 361
Cdd:PRK13026 349 RTTGAYAYVRRQFGMPIGQFEGVQEalaRIAGNTYLLEAARRLTTTGLDLGVK--PSV-VTAIAKYHMTELA 417
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
279-400 |
7.85e-23 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 93.18 E-value: 7.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 279 GIGAQMLGLAQGCFDQTIPYLQQREQ--FGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAA--------RMKQNGLPFVR 348
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieaaaaAGKPVTPALRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1845970424 349 EAAMAKLFASQVATTATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTS 400
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| sulfur_SfnB |
TIGR04022 |
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the ... |
84-408 |
2.67e-22 |
|
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the greater family of acyl-CoA dehydrogenases. This family includes the sulfate starvation induced protein SfnB of Pseudomonas putida strain DS1, which is both encoded nearby to and phylogenetically closely correlated with the dimethyl sulphone monooxygenase SfnG. This family shows considerable sequence similarity to the Rhodococcus dibenzothiophene desulfurization enzyme DszC, although that enzyme falls outside of the scope of this family. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 274924 [Multi-domain] Cd Length: 391 Bit Score: 97.72 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 84 GLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVSVFvdVQNTLVAPLIIQL-GTEEQKQKYLPKIVT-EAIGSfALSE 161
Cdd:TIGR04022 46 GLWGITVPRAYGGAGVSYATLAEVIAIISAADPSLGQI--PQNHFYALEVLRLtGSEEQKRFFFGEVLAgERFGN-AFSE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 162 TGSgSDAFALKTTAKKDGDDFVISGSKMWITNAGHAQFFLVFANADSAKGYKGItcflVDRNQEGVSVGKKEDKLGIRAS 241
Cdd:TIGR04022 123 RGT-RNVLDFQTRLRRDGDGYRLNGRKFYSTGALFAHWIPVLALDDEGRAVLAF----VPRDAPGLTVIDDWSGFGQRTT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 242 STCSVHFDNVRVHKSSILgEYGKGYKyaieclNAGRIGIGAQML------GLAQGCFDQTIPYLQQR-----EQFGQRLI 310
Cdd:TIGR04022 198 ASGTVLLDDVRVPAEHVV-PIQRAFD------RPTAAGPVAQIIhaaidaGIARAALADTLAFVRERarpwiDSGVERAS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 311 DFQGMQHQIGQTRMEIEAARLLVYNAARmkqnglpFVREA----------------AMAKLFASQVATTATSKCVEwLGG 374
Cdd:TIGR04022 271 DDPLTIAEVGDLAIRLHAAEALLERAGR-------AVDAAraepteesvaaasiavAEAKVLTTEIALLAASKLFE-LAG 342
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1845970424 375 VGFT-KEFPVEKFYRDSKIGTI-------YEGTSNIQLNTIA 408
Cdd:TIGR04022 343 TRSTlAEHNLDRHWRNARTHTLhdpvrwkYHAIGNYYLNGVN 384
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
132-410 |
6.05e-22 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 98.33 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 132 LIIQLGTEEQKQKYLPKIVTEAIGS-FALSETG-SGSDAFALKTTAKKDGDDFVISGSKMWITNA--GHAQFFLVFANAD 207
Cdd:PLN02876 528 VLLRYGNKEQQLEWLIPLLEGKIRSgFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTD 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 208 -SAKGYKGITCFLVDRNQEGVSVGKKEDKLGIRAS--STCSVHFDNVRVHKSSILGEYGKGYKYAIECLNAGRIGIGAQM 284
Cdd:PLN02876 608 fNAPKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRL 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 285 LGLAQGCFDQTIPYLQQREQFGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAA-RMKQNGLPFVREA-AMAKLFASQVAT 362
Cdd:PLN02876 688 IGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAAdQLDRLGNKKARGIiAMAKVAAPNMAL 767
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1845970424 363 TATSKCVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAKL 410
Cdd:PLN02876 768 KVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKL 815
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
102-419 |
7.07e-22 |
|
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: 97.78 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 102 FDAVLVIEELAKVDPSVSVFVDVQNTLVAPLIIQLGTEEQKQKYLPKI-VTEAIGSFALSETGSGSDAFALKTTAKKD-- 178
Cdd:cd01150 82 EKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGAnNLEIIGCFAQTELGHGSNLQGLETTATYDpl 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 179 GDDFVI-----SGSKMWITNAGH-AQFFLVFANADSAKGYKGITCFLV---DRNQE----GVSVGKKEDKLGIRASSTCS 245
Cdd:cd01150 162 TQEFVIntpdfTATKWWPGNLGKtATHAVVFAQLITPGKNHGLHAFIVpirDPKTHqplpGVTVGDIGPKMGLNGVDNGF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 246 VHFDNVRVHKSSILGEYG----------------KGYKYAIECLNAGRIGI-GAQMLGLAQGCfdqTIP--YLQQREQFG 306
Cdd:cd01150 242 LQFRNVRIPRENLLNRFGdvspdgtyvspfkdpnKRYGAMLGTRSGGRVGLiYDAAMSLKKAA---TIAirYSAVRRQFG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 307 QR-------LIDFQGMQH----QIGQTRMEIEAARLLVYNAARMK----QNGLPFVRE----AAMAKLFASQVATTATSK 367
Cdd:cd01150 319 PKpsdpevqILDYQLQQYrlfpQLAAAYAFHFAAKSLVEMYHEIIkellQGNSELLAElhalSAGLKAVATWTAAQGIQE 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1845970424 368 CVEWLGGVGFTKEFPVEKFYRDSKIGTIYEGTSNIQLNTIAKLVDIEYQQKA 419
Cdd:cd01150 399 CREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAF 450
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
82-389 |
5.12e-21 |
|
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: 93.93 E-value: 5.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 82 ENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVSVFVDVQNTLVAPLIIqLGTEEQKQKYLPKIVTEAIGSFALSE 161
Cdd:cd01163 33 QSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEALLL-AGPEQFRKRWFGRVLNGWIFGNAVSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 162 TGSGSDAFALKTTAkKDGDDFVISGSKMWITNAGHAQFFLVFANADSAKgykgITCFLVDRNQEGVSVGKKEDKLGIRAS 241
Cdd:cd01163 112 RGSVRPGTFLTATV-RDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK----LVFAAVPTDRPGITVVDDWDGFGQRLT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 242 STCSVHFDNVRVHKSSILGeYGKGYKYAIECLNAGRIGIGAQMLGLAQGCFDQTIPYLQQREQ------FGQRLIDFQGM 315
Cdd:cd01163 187 ASGTVTFDNVRVEPDEVLP-RPNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYVRSRTRpwihsgAESARDDPYVQ 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 316 QHqIGQTRMEIEAARLLVYNAARMKQNGL--PFVREA----------AMAKLFASQVATTATSKCVEWLGGVGFTKEFPV 383
Cdd:cd01163 266 QV-VGDLAARLHAAEALVLQAARALDAAAaaGTALTAeargeaalavAAAKVVVTRLALDATSRLFEVGGASATAREHNL 344
|
....*.
gi 1845970424 384 EKFYRD 389
Cdd:cd01163 345 DRHWRN 350
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
82-336 |
1.72e-19 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 91.03 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 82 ENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVSVFVDVQNTL-VAPLIIQLGTEEQKQKYLPKIVT-EAIGSFAL 159
Cdd:PRK09463 120 EHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLgPGELLLHYGTDEQKDHYLPRLARgEEIPCFAL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 160 SETGSGSDAFALKTTA-----KKDGDDFV---ISGSKMWITNAGHAQFF-LVFANAD-----SAKGYKGITCFLVDRNQE 225
Cdd:PRK09463 200 TSPEAGSDAGSIPDTGvvckgEWQGEEVLgmrLTWNKRYITLAPIATVLgLAFKLYDpdgllGDKEDLGITCALIPTDTP 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 226 GVSVGKKEDKLGirasstcsVHFDN-------VRVHKSSILG--EY-GKGYKYAIECLNAGRiGI--------GAQMLGL 287
Cdd:PRK09463 280 GVEIGRRHFPLN--------VPFQNgptrgkdVFIPLDYIIGgpKMaGQGWRMLMECLSVGR-GIslpsnstgGAKLAAL 350
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1845970424 288 AQGCfdqtipYLQQREQFGQRLIDFQGMQH---QIGQTRMEIEAARLLVYNA 336
Cdd:PRK09463 351 ATGA------YARIRRQFKLPIGKFEGIEEplaRIAGNAYLMDAARTLTTAA 396
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
88-418 |
2.85e-16 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 81.06 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 88 IEIPEKYggpgssffdaVLVIEELAKVDPSVSVFVDVQNTLVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGS 166
Cdd:PLN02636 117 VEDPAKY----------FAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNlDYPGCFAMTELHHGS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 167 DAFALKTTAKKD--GDDFVIS-----GSKMWITNAG-HAQFFLVFAN----ADSAKGYK--GITCFLVD-RNQE------ 225
Cdd:PLN02636 187 NVQGLQTTATFDplTDEFVINtpndgAIKWWIGNAAvHGKFATVFARlklpTHDSKGVSdmGVHAFIVPiRDMKthqvlp 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 226 GVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEYGK-----GYKYAIECLN-----------AGRIGIGAQMLGLAQ 289
Cdd:PLN02636 267 GVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDvsrdgKYTSSLPTINkrfaatlgelvGGRVGLAYGSVGVLK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 290 GCFDQTIPYLQQREQFGQ------RLIDFQGMQHQ----IGQTRMEIEAARLLVYNAARMKQNGLPFVRE-----AAMAK 354
Cdd:PLN02636 347 ASNTIAIRYSLLRQQFGPpkqpeiSILDYQSQQHKlmpmLASTYAFHFATEYLVERYSEMKKTHDDQLVAdvhalSAGLK 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845970424 355 LFASQVATTATSKCVEWLGGVGFTKefpVEKF---YRDSKIGTIYEGTSNIQLNTIAKLVDIEYQQK 418
Cdd:PLN02636 427 AYITSYTAKALSTCREACGGHGYAA---VNRFgslRNDHDIFQTFEGDNTVLLQQVAADLLKQYKEK 490
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
159-402 |
3.55e-16 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 80.18 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 159 LSETGSGSDAFALKTTAKK-DGDDFVISGSKmWITNAGHAQFFLVFANADSakgykGITCFLVDR-----NQEGVSVGKK 232
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAKG-----GLSCFFVPRflpdgQRNAIRLERL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 233 EDKLGIRASSTCSVHFDNVrvhKSSILGEYGKGYKYAIECLNAGRIGIGAQMLGLAQGCFDQTIPYLQQREQFGQRLIDF 312
Cdd:PRK11561 258 KDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 313 QGMQHQIGQTRMEIEAARLLVYNAARM-KQNGLPfvREAAMAKLF--ASQVATTA-----TSKCVEWLGGVGFTKEFPVE 384
Cdd:PRK11561 335 PLMRQVLSRMALQLEGQTALLFRLARAwDRRADA--KEALWARLFtpAAKFVICKrgipfVAEAMEVLGGIGYCEESELP 412
|
250
....*....|....*...
gi 1845970424 385 KFYRDSKIGTIYEGTSNI 402
Cdd:PRK11561 413 RLYREMPVNSIWEGSGNI 430
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
128-410 |
2.02e-12 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 68.72 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 128 LVAPLIIQLGTEEQKQKYLPKIVT-EAIGSFALSETGSGSDAFALKTTAKKD--GDDFVI-----SGSKMWITNAG-HAQ 198
Cdd:PTZ00460 101 MVIPAFQVLGTDEQINLWMPSLLNfEIVGCYAQTELGHGSDVQNLETTATYDkqTNEFVIhtpsvEAVKFWPGELGfLCN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 199 FFLVFANADSAKGYKGITCFLV---DRNQ----EGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSILGEY------GKG 265
Cdd:PTZ00460 181 FALVYAKLIVNGKNKGVHPFMVrirDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYikvsedGQV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 266 YKYAIEclnagRIGIGAQMLGLAQGCFDQT----------IPYLQQREQF----GQ--RLIDFQGMQHQI--------GQ 321
Cdd:PTZ00460 261 ERQGNP-----KVSYASMMYMRNLIIDQYPrfaaqaltvaIRYSIYRQQFtndnKQenSVLEYQTQQQKLlpllaefyAC 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 322 TRMEIEAARLLVYNAARMKQNGLPFVREA----AMAKLFASQVattaTSKCVEW----LGGVGFTKefpvekfYrdSKIG 393
Cdd:PTZ00460 336 IFGGLKIKELVDDNFNRVQKNDFSLLQLThailSAAKANYTYF----VSNCAEWcrlsCGGHGYAH-------Y--SGLP 402
|
330 340
....*....|....*....|.
gi 1845970424 394 TIYEGTS-NIQL---NTIAKL 410
Cdd:PTZ00460 403 AIYFDMSpNITLegeNQIMYL 423
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
55-390 |
6.14e-11 |
|
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: 63.52 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 55 AVNVIKPLVR----EMDDKSQMHQSVITGTFENGLMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPS---VSVFVDVQNT 127
Cdd:cd01159 2 RAEDLAPLIRerapEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSaawVASIVATHSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 128 LVApliiQLGTEEQKQKYLPKIVTEAIGSFAlsETGsgsdafalktTAKKDGDDFVISGSKMWITNAGHAQFFLVFANAD 207
Cdd:cd01159 82 MLA----AFPPEAQEEVWGDGPDTLLAGSYA--PGG----------RAERVDGGYRVSGTWPFASGCDHADWILVGAIVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 208 SAKGYKGITCFLVDRnqEGVSVGKKEDKLGIRASSTCSVHFDNVRVHKSSIL-------GEYGKG----YKYAIECLNAg 276
Cdd:cd01159 146 DDDGGPLPRAFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdmmaGDGPGGstpvYRMPLRQVFP- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 277 rIGIGAQMLGLAQGCFDQTIPYLQQREQ---FGQRLIDFQGMQHQIGQTRMEIEAARLLVYNAAR-----MKQNGLPFVR 348
Cdd:cd01159 223 -LSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRdlwahALAGGPIDVE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1845970424 349 EAAMAKLFASQVATT---ATSKCVEWLGGVGFTKEFPVEKFYRDS 390
Cdd:cd01159 302 ERARIRRDAAYAAKLsaeAVDRLFHAAGGSALYTASPLQRIWRDI 346
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
121-259 |
5.26e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 58.31 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 121 FVDVQNTLVAPLIIQLGTEEQKQKYLPKIVTEA-IGSFALSETGSGSDAFALKTTAKKD--GDDFVI-----SGSKMWIT 192
Cdd:PLN02443 98 YTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQiIGCYAQTELGHGSNVQGLETTATFDpkTDEFVIhsptlTSSKWWPG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 193 NAG----HAqffLVFANADSAKGYKGITCFLVD-RNQE------GVSVGKKEDKLGIRASSTCS---VHFDNVRVHKSSI 258
Cdd:PLN02443 178 GLGkvstHA---VVYARLITNGKDHGIHGFIVQlRSLDdhsplpGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQM 254
|
.
gi 1845970424 259 L 259
Cdd:PLN02443 255 L 255
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
109-259 |
1.33e-05 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 47.46 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 109 EELAKVDPSVSVFVDVQNTLVAPLIIQLGTEEQKQKYLPKIVTEAI-GSFALSETGSGSDAFALKTTAKKD--GDDFVI- 184
Cdd:PLN02312 140 EVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVkGCFAMTELGHGSNVRGIETVTTYDpkTEEFVIn 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 185 ----SGSKMWITNAG-HAQFFLVFANADSAKGYKGITCFLVD-RNQEG-----VSVGKKEDKLGIRASSTCSVHFDNVRV 253
Cdd:PLN02312 220 tpceSAQKYWIGGAAnHATHTIVFSQLHINGKNEGVHAFIAQiRDQDGnicpnIRIADCGHKIGLNGVDNGRIWFDNLRI 299
|
....*.
gi 1845970424 254 HKSSIL 259
Cdd:PLN02312 300 PRENLL 305
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
64-287 |
1.39e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 44.10 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 64 REMD-DKSQMHQSVITGTFENG-----LMGIEIPEKYGGPGSSFFDAVLVIEELAKVDPSVSVFVDVQNTLVAPLIIQLG 137
Cdd:PTZ00457 38 RKLDgDEAENLQSLLEQIRSNDkilgnLYGARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845970424 138 TEEQKQKYLPKIVTEAIGSFALSETGSGSDaFALKTTAKKDGDD--FVISGSKMWItNAGHAQFFLVFANA-------DS 208
Cdd:PTZ00457 118 SKELKGKYLTAMSDGTIMMGWATEEGCGSD-ISMNTTKASLTDDgsYVLTGQKRCE-FAASATHFLVLAKTltqtaaeEG 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845970424 209 AKGYKGITCFLVDRNQEGVSVGKKedklgirasstcSVHFDNVRVhkSSILGEYGKGYKYAIECLNAGRIGIGAQMLGL 287
Cdd:PTZ00457 196 ATEVSRNSFFICAKDAKGVSVNGD------------SVVFENTPA--ADVVGVVGEGFKDAMITLFTEQYLYAASLLGI 260
|
|
| |
