|
Name |
Accession |
Description |
Interval |
E-value |
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
25-400 |
0e+00 |
|
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: 659.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 25 LSDTQKEIQSHAIKFSKDVLVPNAAKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSYGCSGLQ 104
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 105 IAIFGPSLAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGDEYIINGSKAWITGGGHAKW 184
Cdd:cd01157 81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 185 FFVLARTDDNPKTPAGKAFTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILGAPGAGFKVAMGAFDLT 264
Cdd:cd01157 161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 265 RPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSYGVSSYNASIAKCF 344
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 17534899 345 AADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRTLF 400
Cdd:cd01157 321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
21-400 |
4.83e-166 |
|
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: 470.86 E-value: 4.83e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 21 MSFELSDTQKEIQSHAIKFSKDVLVPNAAKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSYGC 100
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 101 SGLQIAIFGPSLAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGDEYIINGSKAWITGGG 180
Cdd:COG1960 81 ASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 181 HAKWFFVLARTDDNPKTpagKAFTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILGAPGAGFKVAMGA 260
Cdd:COG1960 161 VADVILVLARTDPAAGH---RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMST 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 261 FDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSYGVSSYNASI 340
Cdd:COG1960 238 LNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAM 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 341 AKCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRTLF 400
Cdd:COG1960 318 AKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
27-400 |
6.84e-153 |
|
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: 437.08 E-value: 6.84e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 27 DTQKEIQSHAIKFSKDVLVPNAAKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSYGCSGLQIA 106
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 107 IFGP-SLAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGDEYIINGSKAWITGGGHAKWF 185
Cdd:cd01158 81 VSVHnSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 186 FVLARTDdnpKTPAGKAFTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILGAPGAGFKVAMGAFDLTR 265
Cdd:cd01158 161 IVFAVTD---PSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 266 PQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSYGVSSYNASIAKCFA 345
Cdd:cd01158 238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 17534899 346 ADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRTLF 400
Cdd:cd01158 318 SEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
27-397 |
2.35e-123 |
|
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: 360.06 E-value: 2.35e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 27 DTQKEIQSHAIKFSKDVLVPNAAKFDKSGEFPWEIVKQAhslgfmntiipekyggpglsnldtalivealsygcsGLQia 106
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAEL------------------------------------GLL-- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 107 ifgpsLAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGDEYIINGSKAWITGGGHAKWFF 186
Cdd:cd00567 43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 187 VLARTDDNPktPAGKAFTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILGAPGAGFKVAMGAFDLTRP 266
Cdd:cd00567 118 VLARTDEEG--PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 267 QVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSY-GVSSYNASIAKCFA 345
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGpDEARLEAAMAKLFA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 17534899 346 ADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGR 397
Cdd:cd00567 276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
25-401 |
6.14e-116 |
|
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: 343.27 E-value: 6.14e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 25 LSDTQKEIQSHAIKFSKDVLVPNAAKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSYGCSGLQ 104
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 105 IAIFGPSLAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGDEYIINGSKAWITGGGHAKW 184
Cdd:cd01162 81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 185 FFVLARTDDnpktPAGKAFTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILGAPGAGFKVAMGAFDLT 264
Cdd:cd01162 161 YVVMARTGG----EGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 265 RPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDS-YGVSSYNASIAKC 343
Cdd:cd01162 237 RLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRgDPDAVKLCAMAKR 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 17534899 344 FAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRTLFQ 401
Cdd:cd01162 317 FATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
25-401 |
5.46e-111 |
|
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: 330.53 E-value: 5.46e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 25 LSDTQKEIQSHAIKFSKDVLVPNAAKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSYGCSGLQ 104
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 105 IAiFGpslAAAPICLS-----GTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGDEYIINGSKAWITGG 179
Cdd:cd01156 82 LS-YG---AHSNLCINqiyrnGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 180 GHAKWFFVLARTDDNPKTpagKAFTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILGAPGAGFKVAMG 259
Cdd:cd01156 158 PDADTLVVYAKTDPSAGA---HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 260 AFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSYGVSSYNAS 339
Cdd:cd01156 235 GLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17534899 340 IAKCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRTLFQ 401
Cdd:cd01156 315 GVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
39-399 |
1.04e-97 |
|
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: 296.33 E-value: 1.04e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 39 FSKDVLvPNAAKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSY-GCSGLQIAIFGpSLAAAPI 117
Cdd:cd01160 14 FAKEVA-PFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGLSLHT-DIVSPYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 118 CLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGDEYIINGSKAWITGGGHAKWFFVLARTDdNPKT 197
Cdd:cd01160 92 TRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTG-GEAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 198 PAGkAFTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILGAPGAGFKVAMGAFDLTRPQVAASAVGLAW 277
Cdd:cd01160 171 GAG-GISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 278 RCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSYGVSSYNASIAKCFAADTANVAATNAC 357
Cdd:cd01160 250 FMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECV 329
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 17534899 358 QIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRTL 399
Cdd:cd01160 330 QLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
19-402 |
3.53e-96 |
|
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: 293.99 E-value: 3.53e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 19 RQMSFELSDTQKEIQSHAIKFSKDVLVPnaAKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSY 98
Cdd:cd01161 21 SVLTEEQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 99 GCSglqiaiFGPSLAA------APICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQ--GDEYIIN 170
Cdd:cd01161 99 DLG------FSVTLGAhqsigfKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 171 GSKAWITGGGHAKWFFVLARTDDNPKTPAGK-AFTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILGA 249
Cdd:cd01161 173 GSKIWITNGGIADIFTVFAKTEVKDATGSVKdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 250 PGAGFKVAMGAFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVD 329
Cdd:cd01161 253 VGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMD 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17534899 330 SYGVSSYN--ASIAKCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRTLFQN 402
Cdd:cd01161 333 RGLKAEYQieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQH 407
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
18-401 |
9.86e-80 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 251.33 E-value: 9.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 18 SRQMSFELSDTQKEIQSHAIKFSKDVLVPNAAKFDKSGEFPWEI--VKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVE- 94
Cdd:PLN02519 19 SSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 95 --------ALSYGCSGlqiaifgpSLAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGDE 166
Cdd:PLN02519 99 israsgsvGLSYGAHS--------NLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 167 YIINGSKAWITGGGHAKWFFVLARTDdnpkTPAG-KAFTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKEN 245
Cdd:PLN02519 171 YVLNGNKMWCTNGPVAQTLVVYAKTD----VAAGsKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEEN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 246 ILGAPGAGFKVAMGAFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAA 325
Cdd:PLN02519 247 VLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVA 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17534899 326 AEVDSYGVSSYNASIAKCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRTLFQ 401
Cdd:PLN02519 327 RDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
25-397 |
8.72e-68 |
|
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: 219.92 E-value: 8.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 25 LSDTQKEIQSHAIKFSKDVLVPNAAKFDKSGEFPWEIVKQAHSLGFMNTIIpEKYGGPGLSNLDTALI---VEALSYGCS 101
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATI-KGYGCAGLSSVAYGLIareVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 102 GLqIAIFGpSLAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGDEYIINGSKAWITGGGH 181
Cdd:cd01151 92 SF-MSVQS-SLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 182 AKWFFVLARTDDNPKtpagkaFTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILgaPGA-GFKVAMGA 260
Cdd:cd01151 170 ADVFVVWARNDETGK------IRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL--PGAeGLRGPFKC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 261 FDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSYGVSSYNASI 340
Cdd:cd01151 242 LNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 17534899 341 AKCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGR 397
Cdd:cd01151 322 LKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
2-401 |
7.33e-67 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 218.27 E-value: 7.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 2 LTRLSSGTTWnRIAVQSRQMSFELSDTQKEIQSHAI------KFSKDVLVPNAAKFDKSGEFPWEIVKQAHSLGFMNTII 75
Cdd:PTZ00461 9 LGRRSATCGW-TAAATMTSASRAFMDLYNPTPEHAAlretvaKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 76 PEKYGGPGLSNLDTALIVEALSYGCSGLQIAIFGPS-LAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVN 154
Cdd:PTZ00461 88 PEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSmLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 155 GVKTKAVKQGDE-YIINGSKAWITGGGHAKWFFVLARTDdnpktpaGKaFTAFIVDGDTPGITRGKKENNMGQRCSDTRS 233
Cdd:PTZ00461 168 GMRTTAKKDSNGnYVLNGSKIWITNGTVADVFLIYAKVD-------GK-ITAFVVERGTKGFTQGPKIDKCGMRASHMCQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 234 ITFEDVRVPKENILGAPGAGFKVAMGAFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAIN 313
Cdd:PTZ00461 240 LFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 314 LELSRLFTYRAAAEVDSYGVSSYNASIAKCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRM 393
Cdd:PTZ00461 320 TEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHK 399
|
....*...
gi 17534899 394 VIGRTLFQ 401
Cdd:PTZ00461 400 NITKDLLK 407
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
52-404 |
2.14e-62 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 205.73 E-value: 2.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 52 DKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSYgcSGLQIAIFGPSLAAAPICLSGTEEQKKKYLG 131
Cdd:PRK12341 33 DENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK--CGAPAFLITNGQCIHSMRRFGSAEQLRKTAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 132 MLAAEPIIA-SYCVTEPGAGSDVNGVKTKAVKQGDEYIINGSKAWITGGGHAKWFFVLARtDDNPKTPAgKAFTAFIVDG 210
Cdd:PRK12341 111 STLETGDPAyALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLAR-DPQPKDPK-KAFTLWWVDS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 211 DTPGITRGKKENnMGQRCSDTRSITFEDVRVPKENILGAPGAGFKVAMGAFDLTRPQVAASAVGLAWRCLDESTKYAMER 290
Cdd:PRK12341 189 SKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 291 HAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSYGVSSYNASIAKCFAADTANVAATNACQIFGGAGFNCEYP 370
Cdd:PRK12341 268 IQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEAR 347
|
330 340 350
....*....|....*....|....*....|....
gi 17534899 371 VEKLMRDAKIYQIYEGTSQIQRMVIGRTLFQNFA 404
Cdd:PRK12341 348 VSRFWRDVRCERIGGGTDEIMIYIAGRQILKDYQ 381
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
35-399 |
4.17e-62 |
|
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: 205.70 E-value: 4.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 35 HAIKFSKDVLVPNAAKFDKSG--------EFP---WEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSYGCSGL 103
Cdd:cd01153 4 EVARLAENVLAPLNADGDREGpvfddgrvVVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 104 QIAiFGPSLAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGD-EYIINGSKAWITGGGHA 182
Cdd:cd01153 84 MYA-SGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEHD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 183 KW----FFVLARTDDNPktPAGKAFTAFIV-----DGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPkenILGAPGAG 253
Cdd:cd01153 163 MSenivHLVLARSEGAP--PGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 254 FKVAMGAFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTP--------IANHQGVQFMIADMAINLELSRLFTYRAA 325
Cdd:cd01153 238 LAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLikaapavtIIHHPDVRRSLMTQKAYAEGSRALDLYTA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 326 AEVDSYGVSSYNAS--------------IAKCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQ 391
Cdd:cd01153 318 TVQDLAERKATEGEdrkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQ 397
|
....*....
gi 17534899 392 RM-VIGRTL 399
Cdd:cd01153 398 ALdLIGRKI 406
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
76-401 |
4.24e-58 |
|
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: 194.49 E-value: 4.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 76 PEKYGGPGLSNLDTALIVEALSYGCSGLQIAIFGPSLAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNG 155
Cdd:cd01152 55 PKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 156 VKTKAVKQGDEYIINGSKAWITGGGHAKWFFVLARTDdnPKTPAGKAFTAFIVDGDTPGITRGKKENNMGQrcSDTRSIT 235
Cdd:cd01152 135 LRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTD--PEAPKHRGISILLVDMDSPGVTVRPIRSINGG--EFFNEVF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 236 FEDVRVPKENILGAPGAGFKVAMGAFDLTRPQVAASAvglAWRC------LDESTKYAMERHAFgtpianhQGVQFMIAD 309
Cdd:cd01152 211 LDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSA---ATFFelllarLLLLTRDGRPLIDD-------PLVRQRLAR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 310 MAINLELSRLFTYRAAAEVDSYGVSSYNASIAKCFAADTANVAATNACQIFGGAGFNCEYP--------VEKLMRDAKIY 381
Cdd:cd01152 281 LEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEADYLRSRAT 360
|
330 340
....*....|....*....|
gi 17534899 382 QIYEGTSQIQRMVIGRTLFQ 401
Cdd:cd01152 361 TIYGGTSEIQRNIIAERLLG 380
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
30-398 |
7.41e-52 |
|
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: 178.35 E-value: 7.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 30 KEIQSHAIKFSKDVLVPNAAKFDK---SGEFPWEIVKQ--------AHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSY 98
Cdd:cd01155 4 QELRARVKAFMEEHVYPAEQEFLEyyaEGGDRWWTPPPiieklkakAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 99 gcsglqiAIFGPSL--AAAP-------ICLSGTEEQKKKYLGMLAAEPIIASYCVTEPG-AGSDVNGVKTKAVKQGDEYI 168
Cdd:cd01155 84 -------SFFAPEVfnCQAPdtgnmevLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 169 INGSKAWITGGGH--AKWFFVLARTdDNPKTPAGKAFTAFIVDGDTPGITRGKKENNMGQrcSDTR----SITFEDVRVP 242
Cdd:cd01155 157 INGRKWWSSGAGDprCKIAIVMGRT-DPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGY--DDAPhghaEITFDNVRVP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 243 KENILGAPGAGFKVAMGAFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTY 322
Cdd:cd01155 234 ASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17534899 323 RAAAEVDSYGVSSYNASIA--KCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRT 398
Cdd:cd01155 314 KAAHMIDTVGNKAARKEIAmiKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARM 391
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
49-403 |
1.02e-51 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 177.72 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 49 AKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALsyGCSGlqiaifGPS--LAAAP-----ICLSG 121
Cdd:PRK03354 30 AECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRLG------APTyvLYQLPggfntFLREG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 122 TEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGDEYIINGSKAWITGGGHAKWFFVLARTDDNPKTPAgk 201
Cdd:PRK03354 102 TQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPV-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 202 aFTAFIVDGDTPGITRGKKENnMGQRCSDTRSITFEDVRVPKENILGAPGAGFKVAMGAFDLTRPQVAASAVGLAWRCLD 281
Cdd:PRK03354 180 -YTEWFVDMSKPGIKVTKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 282 ESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSYGVSSYNASIAKCFAADTANVAATNACQIFG 361
Cdd:PRK03354 258 DAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLG 337
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 17534899 362 GAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRTLFQNF 403
Cdd:PRK03354 338 GVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQY 379
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
251-399 |
9.66e-50 |
|
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: 165.12 E-value: 9.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 251 GAGFKVAMGAFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDS 330
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17534899 331 YGVSSYNASIAKCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRTL 399
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
20-397 |
1.09e-46 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 165.41 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 20 QMSFELSDTQKEIQSHAIKFSKDVLVPNAAKFDKSGEFPWEIVKQAHSLGFMNTIIpEKYGGPGLSNLDTAL-IVEALSY 98
Cdd:PLN02526 24 QFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIaTAEVARV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 99 GCSGLQIAIFGPSLAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGDEYIINGSKAWITG 178
Cdd:PLN02526 103 DASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 179 GGHAKWFFVLARtddNPKTpagKAFTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILgaPGA-GFKVA 257
Cdd:PLN02526 183 STFADVLVIFAR---NTTT---NQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--PGVnSFQDT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 258 MGAFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSYGVSSYN 337
Cdd:PLN02526 255 NKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGH 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 338 ASIAKCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRMVIGR 397
Cdd:PLN02526 335 ASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGR 394
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
26-135 |
1.18e-34 |
|
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: 124.11 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 26 SDTQKEIQSHAIKFSKDVLVPNAAKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSYGCSGLQI 105
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|.
gi 17534899 106 AIFGPS-LAAAPICLSGTEEQKKKYLGMLAA 135
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLAS 111
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
81-401 |
3.39e-32 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 129.14 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 81 GPGLSNLDTALIVEALSYGCSGLQIAIFG-PSLAAAPICLS-GTEEQKKKYLGMLAAEPIIASYCVTEPG-AGSDVNGVK 157
Cdd:PLN02876 491 GAGLSNLEYGYLCEIMGRSVWAPQVFNCGaPDTGNMEVLLRyGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 158 TKAVKQGDEYIINGSKAWITGG--GHAKWFFVLARTDdnPKTPAGKAFTAFIVDGDTPG--ITR-----GKKENNMGQRc 228
Cdd:PLN02876 571 CSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTD--FNAPKHKQQSMILVDIQTPGvqIKRpllvfGFDDAPHGHA- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 229 sdtrSITFEDVRVPKENILGAPGAGFKVAMGAFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIA 308
Cdd:PLN02876 648 ----EISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLA 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 309 DMAINLELSRLFTYRAAAEVDSYGVSSYNASI--AKCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEG 386
Cdd:PLN02876 724 KCRVELEQTRLLVLEAADQLDRLGNKKARGIIamAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADG 803
|
330
....*....|....*
gi 17534899 387 TSQIQRMVIGRTLFQ 401
Cdd:PLN02876 804 PDEVHLGTIAKLELQ 818
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
120-391 |
4.16e-31 |
|
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: 122.86 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 120 SGTEEQKKKYLGMLA---AEPIIASYCVTEPGAGSDVNGVKTKAVKQ-GDEYIINGSKaWITGGGHAKWFFVLARTDDNP 195
Cdd:cd01154 126 YGPEELKQYLPGLLSdryKTGLLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHK-WFASAPLADAALVLARPEGAP 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 196 ktPAGKAFTAFIV-----DGDTPGITRGKKENNMGQRCSDTRSITFEDVrvpKENILGAPGAGFKVAMGAFDLTRPQVAA 270
Cdd:cd01154 205 --AGARGLSLFLVprlleDGTRNGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 271 SAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAINLE--------LSRLFTYRAAAEVDSYGVSSYNASIAK 342
Cdd:cd01154 280 AALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEaataltfrAARAFDRAAADKPVEAHMARLATPVAK 359
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17534899 343 CFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQ 391
Cdd:cd01154 360 LIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
141-237 |
1.10e-27 |
|
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: 105.05 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 141 SYCVTEPGAGSDVNGVKTKAVK-QGDEYIINGSKAWITGGGHAKWFFVLARTDdnpKTPAGKAFTAFIVDGDTPGITRGK 219
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADgDGGGWVLNGTKWWITNAGIADLFLVLARTG---GDDRHGGISLFLVPKDAPGVSVRR 77
|
90
....*....|....*...
gi 17534899 220 KENNMGQRCSDTRSITFE 237
Cdd:pfam02770 78 IETKLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
41-397 |
1.60e-27 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 114.58 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 41 KDVLVPNAAKfdksgefpwEIVKQAHSLGFMNTIIPEKYGGPGLS---NLDTALIVEALSYGC---SGLQIAifgpslAA 114
Cdd:PTZ00456 93 GNVTTPKGFK---------EAYQALKAGGWTGISEPEEYGGQALPlsvGFITRELMATANWGFsmyPGLSIG------AA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 115 APICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAVKQGD-EYIINGSKAWITGGGHAK----WFFVLA 189
Cdd:PTZ00456 158 NTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDHDLteniVHIVLA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 190 RTDDNPktPAGKAFTAFIVDGDTP---GITRGKK-------ENNMGQRCSDTRSITFEDvrvPKENILGAPGAGFKVAMG 259
Cdd:PTZ00456 238 RLPNSL--PTTKGLSLFLVPRHVVkpdGSLETAKnvkciglEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 260 AFDLTRPQVAASAVGLAWRCLDESTKYAMERHAF------------GTPIANHQGVQFMI--------ADMAINLELSRL 319
Cdd:PTZ00456 313 FMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNIlfakavaeGGRALLLDVGRL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 320 FTYRAAA----EVDSYGVS-SYNASIAKCFAADTANVAATNACQIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQIQRM- 393
Cdd:PTZ00456 393 LDIHAAAkdaaTREALDHEiGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALd 472
|
....
gi 17534899 394 VIGR 397
Cdd:PTZ00456 473 FIGR 476
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
42-364 |
3.23e-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: 94.31 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 42 DVLVPNAAKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSYGCSGL-QIaiFGPSLA-AAPICL 119
Cdd:cd01163 8 ARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIaQA--LRAHFGfVEALLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 120 SGTEEQKKKYLGMLAAEPIIAsycvtepGAGSDVNGVK-----TKAVKQGDEYIINGSKAWITGGGHAKWFFVLArTDDN 194
Cdd:cd01163 86 AGPEQFRKRWFGRVLNGWIFG-------NAVSERGSVRpgtflTATVRDGGGYVLNGKKFYSTGALFSDWVTVSA-LDEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 195 pktpaGKAfTAFIVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILGAPGAGFKvamGAFDLTRPQV--AASA 272
Cdd:cd01163 158 -----GKL-VFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDR---GTLLTAIYQLvlAAVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 273 VGLAWRCLDESTKYAMER-HAFGTPIANHQG----VQFMIADMAINLE------------LSRLFTYRAAAEVDSYGVSS 335
Cdd:cd01163 229 AGIARAALDDAVAYVRSRtRPWIHSGAESARddpyVQQVVGDLAARLHaaealvlqaaraLDAAAAAGTALTAEARGEAA 308
|
330 340
....*....|....*....|....*....
gi 17534899 336 YNASIAKCFAADTANVAATnacQIFGGAG 364
Cdd:cd01163 309 LAVAAAKVVVTRLALDATS---RLFEVGG 334
|
|
| sulfur_SfnB |
TIGR04022 |
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the ... |
46-356 |
3.20e-20 |
|
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: 91.56 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 46 PNAAKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSYGcsglqiaifGPSLAAAP--------- 116
Cdd:TIGR04022 23 PGAAERDRERRLPWAELDAFSQSGLWGITVPRAYGGAGVSYATLAEVIAIISAA---------DPSLGQIPqnhfyalev 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 117 ICLSGTEEQKKKYLG-MLAAEPIiaSYCVTEPGaGSDVNGVKTKAVKQGDEYIINGSKAWITGGGHAKWFFVLARTDDnp 195
Cdd:TIGR04022 94 LRLTGSEEQKRFFFGeVLAGERF--GNAFSERG-TRNVLDFQTRLRRDGDGYRLNGRKFYSTGALFAHWIPVLALDDE-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 196 ktpaGKAFTAFiVDGDTPGITRGKKENNMGQRCSDTRSITFEDVRVPKENILgapgAGFKvamgAFDltRPQV------- 268
Cdd:TIGR04022 169 ----GRAVLAF-VPRDAPGLTVIDDWSGFGQRTTASGTVLLDDVRVPAEHVV----PIQR----AFD--RPTAagpvaqi 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 269 --AASAVGLAWRCLDESTKYAMER----------HAFGTPIANHQgvqfmIADMAINLELSRLFTYRAAAEVDSYGVSSY 336
Cdd:TIGR04022 234 ihAAIDAGIARAALADTLAFVRERarpwidsgveRASDDPLTIAE-----VGDLAIRLHAAEALLERAGRAVDAARAEPT 308
|
330 340
....*....|....*....|.
gi 17534899 337 NASIAKC-FAADTANVAATNA 356
Cdd:TIGR04022 309 EESVAAAsIAVAEAKVLTTEI 329
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
59-364 |
8.66e-19 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 88.48 E-value: 8.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 59 WEIVKQAHSL-----------GFMNTIIPEKYGGPGLSNLDTALIVEALSYGCSGLQIAIFGP-SLAAAPICLS-GTEEQ 125
Cdd:PRK13026 100 WDIVQNRKDLppevwdylkkeGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPnSLGPGELLTHyGTQEQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 126 KKKYLGMLAAEPIIASYCVTEPGAGSDVN-----GVKTKAVKQGDEYI---INGSKAWITGGGHAkwffvlartddnpkT 197
Cdd:PRK13026 180 KDYWLPRLADGTEIPCFALTGPEAGSDAGaipdtGIVCRGEFEGEEVLglrLTWDKRYITLAPVA--------------T 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 198 PAGKAFTAFIVDG-----------------DTPGITRGKKENNMGQRCSD--TRSitfEDVRVPKENILGAP---GAGFK 255
Cdd:PRK13026 246 VLGLAFKLRDPDGllgdkkelgitcaliptDHPGVEIGRRHNPLGMAFMNgtTRG---KDVFIPLDWIIGGPdyaGRGWR 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 256 VAMGAFDLTR----PqvaASAVGLAWRCLDESTKYAMERHAFGTPIANHQGVQFMIADMAIN---LELSRLFTYRAAAEV 328
Cdd:PRK13026 323 MLVECLSAGRgislP---ALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLTTTGLDLG 399
|
330 340 350
....*....|....*....|....*....|....*.
gi 17534899 329 DSYGVSSynaSIAKCFAADTANVAATNACQIFGGAG 364
Cdd:PRK13026 400 VKPSVVT---AIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
59-364 |
5.24e-18 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 86.41 E-value: 5.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 59 WEIVKQAhslGFMNTIIPEKYGGPGLSNLDTALIVEALSYGCSGLQIAIFGP-SLAAAPICLS-GTEEQKKKYLGMLAAE 136
Cdd:PRK09463 115 WQFIKEH---GFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPnSLGPGELLLHyGTDEQKDHYLPRLARG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 137 PIIASYCVTEPGAGSDV-----NGVKTKAVKQGDEYI---INGSKAWITggghakwffvLArtddnP-KTPAGKAFTAFI 207
Cdd:PRK09463 192 EEIPCFALTSPEAGSDAgsipdTGVVCKGEWQGEEVLgmrLTWNKRYIT----------LA-----PiATVLGLAFKLYD 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 208 VDG-----------------DTPGITRGKKENNMGQRcsdtrsitF-------EDVRVPKENILGAP---GAGFKVAMGA 260
Cdd:PRK09463 257 PDGllgdkedlgitcaliptDTPGVEIGRRHFPLNVP--------FqngptrgKDVFIPLDYIIGGPkmaGQGWRMLMEC 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 261 FDLTR----PQVAASAVGLAWRCldeSTKYAMERHAFGTPIANHQGVQFMIADMAIN---LELSRLFTyraAAEVDSYGV 333
Cdd:PRK09463 329 LSVGRgislPSNSTGGAKLAALA---TGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLT---TAAVDLGEK 402
|
330 340 350
....*....|....*....|....*....|.
gi 17534899 334 SSYNASIAKCFAADTANVAATNACQIFGGAG 364
Cdd:PRK09463 403 PSVLSAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
102-386 |
5.61e-17 |
|
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: 82.76 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 102 GLQIAIFGPSLAAapiclSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAV--KQGDEYIIN-----GSKA 174
Cdd:cd01150 103 GLHLGLFGNAIKN-----LGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdftATKW 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 175 WITGGGH-AKWFFVLARTddnpkTPAGK--AFTAFIV---DGDT----PGITRGKKENNMGQRCSDTRSITFEDVRVPKE 244
Cdd:cd01150 178 WPGNLGKtATHAVVFAQL-----ITPGKnhGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 245 NILG----------------APGAGFKVAMGAFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFG-------TPIANHQ 301
Cdd:cd01150 253 NLLNrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGpkpsdpeVQILDYQ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 302 GVQFMIADMainleLSRLFTYRAAAE--VDSY---------GVSSYNASI------AKCFAADTANVAATNACQIFGGAG 364
Cdd:cd01150 333 LQQYRLFPQ-----LAAAYAFHFAAKslVEMYheiikellqGNSELLAELhalsagLKAVATWTAAQGIQECREACGGHG 407
|
330 340
....*....|....*....|..
gi 17534899 365 FNCEYPVEKLMRDAKIYQIYEG 386
Cdd:cd01150 408 YLAMNRLPTLRDDNDPFCTYEG 429
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
268-389 |
3.60e-15 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 71.99 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 268 VAASAVGLAWRCLDESTKYAMER--HAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEV-------DSYGVSSYN- 337
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRvrAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIeaaaaagKPVTPALRAe 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 17534899 338 ASIAKCFAADTAnVAATNAC-QIFGGAGFNCEYPVEKLMRDAKIYQIYEGTSQ 389
Cdd:pfam08028 82 ARRAAAFATELA-VAAVDALfRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
47-400 |
5.43e-14 |
|
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: 72.77 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 47 NAAKFDKSGEFPWEIVKQAHSLGFMNTIIPEKYGGPGLSNLDTALIVEALSYGCSGlqiAIFGPSLAAAP---ICLSGTE 123
Cdd:cd01159 13 RAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGS---AAWVASIVATHsrmLAAFPPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 124 EQKKKYlgmlAAEPIIASYCVTEPGAgsdvngvktKAVKQGDEYIINGSKAWITGGGHAKWFFVLARTDDNpktPAGKAF 203
Cdd:cd01159 90 AQEEVW----GDGPDTLLAGSYAPGG---------RAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDD---DGGPLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 204 TAFIVDGDTPGItrgkKEN--NMGQRCSDTRSITFEDVRVPKENIL--------GAPGAG---FKVAMGAFDLtrPQVAA 270
Cdd:cd01159 154 RAFVVPRAEYEI----VDTwhVVGLRGTGSNTVVVDDVFVPEHRTLtagdmmagDGPGGStpvYRMPLRQVFP--LSFAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 271 SAVGLAWRCLDESTKYAMER---HAFGTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSYGVSS--YNASIAKCFA 345
Cdd:cd01159 228 VSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGgpIDVEERARIR 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17534899 346 ADTANVAAT--NACQ-IFGGAGFNCEY---PVEKLMRDAK-----IYQIYEGTSQIqrmvIGRTLF 400
Cdd:cd01159 308 RDAAYAAKLsaEAVDrLFHAAGGSALYtasPLQRIWRDIHaaaqhAALNPETAAEA----YGRALL 369
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
121-326 |
2.29e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 62.55 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 121 GTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAV--KQGDEYIIN-----GSKAWITGGG----HAkwfFVLA 189
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdPKTDEFVIHsptltSSKWWPGGLGkvstHA---VVYA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 190 RTDDNPKTPAGKAFTAFIVDGDT----PGITRGK---KENNMGQRCSDTRSITFEDVRVPKENILGAPGAGFK------- 255
Cdd:PLN02443 191 RLITNGKDHGIHGFIVQLRSLDDhsplPGVTVGDigmKFGNGAYNTMDNGFLRFDHVRIPRDQMLMRLSKVTRegkyvqs 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17534899 256 -----VAMGAFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGtpiANHQGVQFMIADMaiNLELSRLFTYRAAA 326
Cdd:PLN02443 271 dvprqLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFG---SQDGGPETQVIDY--KTQQSRLFPLLASA 341
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
105-293 |
4.69e-10 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 61.33 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 105 IAIFGPSLAA----------APICLSGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAV--KQGDEYIIN-- 170
Cdd:PLN02312 142 IGIYDHSLAIklgvhfflwgGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTydPKTEEFVINtp 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 171 ---GSKAWITGGG-HAKWFFVLARTDDNPKTPAGKAFTAFIVDGD---TPGITRGKKENNMGQRCSDTRSITFEDVRVPK 243
Cdd:PLN02312 222 cesAQKYWIGGAAnHATHTIVFSQLHINGKNEGVHAFIAQIRDQDgniCPNIRIADCGHKIGLNGVDNGRIWFDNLRIPR 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17534899 244 ENILGA-----PGAGFKVAM-------GAF--DLT--RPQVAASAVGLAWRCLDESTKYAMERHAF 293
Cdd:PLN02312 302 ENLLNSvadvsPDGKYVSAIkdpdqrfGAFlaPLTsgRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
75-282 |
9.89e-10 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 60.28 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 75 IPEKYGGPGLSNLDTALIVEALSYGCSGLQIAIFGPS-LAAAPICLSGTEEQKKKYLGMLAAEPIIASYCVTEpGAGSDV 153
Cdd:PTZ00457 70 IATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSgFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEE-GCGSDI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 154 NGVKTKAVKQGD-EYIINGSKAWITGGGhAKWFFVLARTDDNPKTPAGKA----FTAFIVDGDTPGItrgKKENNmgqrc 228
Cdd:PTZ00457 149 SMNTTKASLTDDgSYVLTGQKRCEFAAS-ATHFLVLAKTLTQTAAEEGATevsrNSFFICAKDAKGV---SVNGD----- 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17534899 229 sdtrSITFEDvrVPKENILGAPGAGFKVAMGAFDLTRPQVAASAVGLAWRCLDE 282
Cdd:PTZ00457 220 ----SVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQE 267
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
121-247 |
1.56e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 53.31 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 121 GTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAV--KQGDEYIIN-----GSKAWiTG--GGHAKWFFVLART 191
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATydKQTNEFVIHtpsveAVKFW-PGelGFLCNFALVYAKL 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 192 DDNPKTPAGKAFTAFIVDGDT----PGITRGKKENNMGQRCSDTRSITFEDVRVPKENIL 247
Cdd:PTZ00460 189 IVNGKNKGVHPFMVRIRDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
102-386 |
5.42e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 51.78 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 102 GLQIAIFGPSLaaapICLsGTEEQKKKYLGMLAAEPIIASYCVTEPGAGSDVNGVKTKAV--KQGDEYIIN----GSKAW 175
Cdd:PLN02636 142 GVQYSLWGGSV----INL-GTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATfdPLTDEFVINtpndGAIKW 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 176 ITGGG--HAKWFFVLART-----DDNPKTPAG-KAFTAFIVDGDT----PGITRGKKENNMGQRCSDTRSITFEDVRVPK 243
Cdd:PLN02636 217 WIGNAavHGKFATVFARLklpthDSKGVSDMGvHAFIVPIRDMKThqvlPGVEIRDCGHKVGLNGVDNGALRFRSVRIPR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 244 ENILGAPG----------------AGFKVAMGAFDLTRPQVAASAVGLAWRCLDESTKYAMERHAFGTP------IANHQ 301
Cdd:PLN02636 297 DNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQ 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 302 GVQFMIADMainleLSRLFTYRAAAE--VDSYG-------------VSSYNASIAKCFAADTANVAAT--NACqifGGAG 364
Cdd:PLN02636 377 SQQHKLMPM-----LASTYAFHFATEylVERYSemkkthddqlvadVHALSAGLKAYITSYTAKALSTcrEAC---GGHG 448
|
330 340
....*....|....*....|..
gi 17534899 365 FNCEYPVEKLMRDAKIYQIYEG 386
Cdd:PLN02636 449 YAAVNRFGSLRNDHDIFQTFEG 470
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
145-399 |
9.02e-07 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 50.91 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 145 TEPGAGSDVNGVKTKAVK-QGDEYIINGskawitgggHaKWFFVLARTDDN---PKTPAGkaFTAFIV-----DGDTPGI 215
Cdd:PRK11561 185 TEKQGGSDVLSNTTRAERlADGSYRLVG---------H-KWFFSVPQSDAHlvlAQAKGG--LSCFFVprflpDGQRNAI 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 216 TRGKKENNMGQRCSDTRSITFEDVrvpKENILGAPGAGFK--VAMGAfdLTRPQVAASAVGLAWRCLDESTKYAMERHAF 293
Cdd:PRK11561 253 RLERLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRliLKMGG--MTRFDCALGSHGLMRRAFSVAIYHAHQRQVF 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534899 294 GTPIANHQGVQFMIADMAINLELSRLFTYRAAAEVDSYGvSSYNASIAKCF--AADTANVAA-----TNACQIFGGAGFN 366
Cdd:PRK11561 328 GKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRA-DAKEALWARLFtpAAKFVICKRgipfvAEAMEVLGGIGYC 406
|
250 260 270
....*....|....*....|....*....|...
gi 17534899 367 CEYPVEKLMRDAKIYQIYEGTSQIQRMVIGRTL 399
Cdd:PRK11561 407 EESELPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
|
|
| |
