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Conserved domains on  [gi|148230460|ref|NP_001086632|]
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medium-chain acyl-CoA dehydrogenase [Xenopus laevis]

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List of domain hits

Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
43-420 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: 772.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  43 LSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTGVQ 122
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 123 TAIEANSLGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGKANW 202
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 203 YFLLARTNPDPKVPAGKAFTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGAFDKT 282
Cdd:cd01157  161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 283 RPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASIAKAY 362
Cdd:cd01157  241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148230460 363 AGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLGK 420
Cdd:cd01157  321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
40-423 8.90e-120

Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism];


:

Pssm-ID: 224871 [Multi-domain]  Cd Length: 393  Bit Score: 357.20  E-value: 8.90e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  40 NFELSEQQKEFQVTARKFAREEVMPVAAHYD---KTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAY 116
Cdd:COG1960    2 DFDLSEEQEALRAEVREFAEEELAPEAAEIDrriEDERFPRELLRALAEAGLLGLTIPEEYGGLGLSPLEQAAVLEELAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 117 GC--TGVQTAIEANSLGQMPVIIA--GNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLK-TRAEKKGNEYIINGQK 191
Cdd:COG1960   82 ADagGALALGLTHGGLGALAPTILrfGTEEQKRRYLPRLASGELIGAFALTEPGAGSDLASLRtTAAVRDDGDYVLNGQK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 192 MWITNGGKANWYFLLARTNPDPkvPAGKAFTGFIVDAN-SPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGA 270
Cdd:COG1960  162 IWISNAPVADWLLVLARTDPAP--GKHKGISLFLVPKDlTPGVSVGPILKKMGLRGSATGEVFFDDVRVPAENLLGEEGD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 271 GFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGR 350
Cdd:COG1960  240 GFKIAMETLNVERLGIAAQALGIAEAALEEAVAYARERKQFGRPIADFQLVQFKLADMAAELEAARLLVLRAAELADAGD 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148230460 351 RNTYYASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLGKYKA 423
Cdd:COG1960  320 DAGAEAAMAKLFATEAALEVADEAVQVHGGYGYTEEYPVERYYRDARILRIYEGTSEIQRLIIARRLLGLPAG 392
 
Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
43-420 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: 772.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  43 LSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTGVQ 122
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 123 TAIEANSLGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGKANW 202
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 203 YFLLARTNPDPKVPAGKAFTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGAFDKT 282
Cdd:cd01157  161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 283 RPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASIAKAY 362
Cdd:cd01157  241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148230460 363 AGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLGK 420
Cdd:cd01157  321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
269-415 2.88e-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: 249861  Cd Length: 150  Bit Score: 168.60  E-value: 2.88e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  269 GAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDL 348
Cdd:pfam00441   1 GRGFAVAMETLNHERLLIAAAALGAARRALDEAIEYARQRKAFGRPLIDFQLIRHRLADMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148230460  349 GRRNTYYASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISR 415
Cdd:pfam00441  81 GGPDPAEAAMAKLFASELAQEVADLAMQLLGGYGYSREYPLERLYRDARVLRIGEGTSEIQRNIIAR 147
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
40-423 8.90e-120

Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism];


Pssm-ID: 224871 [Multi-domain]  Cd Length: 393  Bit Score: 357.20  E-value: 8.90e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  40 NFELSEQQKEFQVTARKFAREEVMPVAAHYD---KTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAY 116
Cdd:COG1960    2 DFDLSEEQEALRAEVREFAEEELAPEAAEIDrriEDERFPRELLRALAEAGLLGLTIPEEYGGLGLSPLEQAAVLEELAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 117 GC--TGVQTAIEANSLGQMPVIIA--GNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLK-TRAEKKGNEYIINGQK 191
Cdd:COG1960   82 ADagGALALGLTHGGLGALAPTILrfGTEEQKRRYLPRLASGELIGAFALTEPGAGSDLASLRtTAAVRDDGDYVLNGQK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 192 MWITNGGKANWYFLLARTNPDPkvPAGKAFTGFIVDAN-SPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGA 270
Cdd:COG1960  162 IWISNAPVADWLLVLARTDPAP--GKHKGISLFLVPKDlTPGVSVGPILKKMGLRGSATGEVFFDDVRVPAENLLGEEGD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 271 GFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGR 350
Cdd:COG1960  240 GFKIAMETLNVERLGIAAQALGIAEAALEEAVAYARERKQFGRPIADFQLVQFKLADMAAELEAARLLVLRAAELADAGD 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148230460 351 RNTYYASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLGKYKA 423
Cdd:COG1960  320 DAGAEAAMAKLFATEAALEVADEAVQVHGGYGYTEEYPVERYYRDARILRIYEGTSEIQRLIIARRLLGLPAG 392
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
43-416 5.29e-80

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 254.80  E-value: 5.29e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  43 LSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYP--VPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTG 120
Cdd:PLN02519  26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 121 VQTAIEANS-LGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGK 199
Cdd:PLN02519 106 VGLSYGAHSnLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 200 ANWYFLLARTNPdpkvPAG-KAFTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGA 278
Cdd:PLN02519 186 AQTLVVYAKTDV----AAGsKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSG 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 279 FDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASI 358
Cdd:PLN02519 262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAG 341
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148230460 359 AKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISRE 416
Cdd:PLN02519 342 VILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRE 399
cyc_hxne_CoA_dh TIGR03207
cyclohexanecarboxyl-CoA dehydrogenase; Cyclohex-1-ene-1carboxyl-CoA is an intermediate in the ...
43-418 1.42e-63

cyclohexanecarboxyl-CoA dehydrogenase; Cyclohex-1-ene-1carboxyl-CoA is an intermediate in the anaerobic degradation of benzoyl-CoA derived from varioius aromatic compounds, in Rhodopseudomonas palustris but not Thauera aromatica. The aliphatic compound cyclohexanecarboxylate, can be converted to the same intermediate in two steps. The first step is its ligation to coenzyme A. The second is the action of this enzyme, cyclohexanecarboxyl-CoA dehydrogenase.


Pssm-ID: 132251 [Multi-domain]  Cd Length: 372  Bit Score: 210.93  E-value: 1.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460   43 LSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTGVQ 122
Cdd:TIGR03207   1 LNEDLQALADTARRFARERIAPGFKERDKTRVLDRELMRDMGEMGFIGPELPEEHGGLGMGCLAAGVIHEQIARADLSMS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  123 TAIEANSL-GQmpvIIAGNEAQQ--KKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGK 199
Cdd:TIGR03207  81 YVNLLASLnGQ---ILAQHARPEiaKPWLGQLIAGEALFAIALTEPRGGSDAARLRLRAERDGDDYVLNGEKTSISAADQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  200 ANWYFLLARTNPDPKvpAGKAFTGFIVDANSPGIQIGRKElNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGAF 279
Cdd:TIGR03207 158 ADAAVVFARTGSEAE--GARGISAFLVPMDLPGITRNRFD-CHGQRAIGRGSIFFENVRVPADHMLGNEGQGFVQVMQGF 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  280 DKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASIA 359
Cdd:TIGR03207 235 DFSRALIGLQVLAVARAALDETWRYVAERQAFGKPLSAFQGVSHPLADAETQVEAARLLCLQTLWLKDHGLPHTSEAAMC 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148230460  360 KAYAGDIANQVASDAVQVFGGNGFNSDyPVEKLMRDAKIYQIYEGTAQIQRLIISREHL 418
Cdd:TIGR03207 315 KWWAPKLAYDVIHQCLLTHGHGGYDRG-DMEQRLRDVLGFQIGDGTAQIMKTIIARHRA 372
HpaB_N pfam11794
4-hydroxyphenylacetate 3-hydroxylase N terminal; HpaB encodes part of the ...
145-266 8.42e-04

4-hydroxyphenylacetate 3-hydroxylase N terminal; HpaB encodes part of the 4-hydroxyphenylacetate 3-hydroxylase from Escherichia coli. HpaB is part of a heterodimeric enzyme that also requires HpaC. The enzyme is NADH-dependent and uses FAD as the redox chromophore. This family also includes PvcC, which may play a role in one of the proposed hydroxylation steps of pyoverdine chromophore biosynthesis.


Pssm-ID: 256625 [Multi-domain]  Cd Length: 265  Bit Score: 39.41  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  145 KKYLGRMTEEPLMCAYCVTEP------GAGSDVAGLKTRAEKKGNEYI-INGQKMWITNGGKANWYFLLArTNPDPKVPA 217
Cdd:pfam11794 127 RRYYKYAQENDLYLTHAITDPkgdrskPPHQEDPDVYVHVVEETDDGIvVRGAKALATGAAIADEIFVMP-TRAMPEEDK 205
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148230460  218 GKAFtGFIVDANSPGI-QIGRKELNMGqRCSD------TRG------IVFEDVRVPAENVLI 266
Cdd:pfam11794 206 DYAV-AFAVPMDAPGLkLICRRSYEDG-RASPfdyplsSRFdendalVVFDDVFVPWERVFM 265
 
Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
43-420 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: 772.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  43 LSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTGVQ 122
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 123 TAIEANSLGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGKANW 202
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 203 YFLLARTNPDPKVPAGKAFTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGAFDKT 282
Cdd:cd01157  161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 283 RPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASIAKAY 362
Cdd:cd01157  241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148230460 363 AGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLGK 420
Cdd:cd01157  321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
45-419 1.32e-145

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: 422.45  E-value: 1.32e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  45 EQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTGVQTA 124
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 125 IEA-NSLGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGKANWY 203
Cdd:cd01158   81 VSVhNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 204 FLLARTNPDPKvpaGKAFTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGAFDKTR 283
Cdd:cd01158  161 IVFAVTDPSKG---YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 284 PPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASIAKAYA 363
Cdd:cd01158  238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFA 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230460 364 GDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLG 419
Cdd:cd01158  318 SEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
45-415 8.73e-131

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: 382.79  E-value: 8.73e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  45 EQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGlmnghipeqygglalgifdtcliteeiaygctgvqta 124
Cdd:cd00567    1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 125 ieanslGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGKANWYF 204
Cdd:cd00567   44 ------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 205 LLARTNPDPkvPAGKAFTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGAFDKTRP 284
Cdd:cd00567  118 VLARTDEEG--PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRL 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 285 PVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRN-TYYASIAKAYA 363
Cdd:cd00567  196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEaRLEAAMAKLFA 275
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148230460 364 GDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISR 415
Cdd:cd00567  276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
43-420 4.47e-109

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: 329.02  E-value: 4.47e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  43 LSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTGVQ 122
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 123 TAIEANSLGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGKANW 202
Cdd:cd01162   81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 203 YFLLARTNPDpkvpAGKAFTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGAFDKT 282
Cdd:cd01162  161 YVVMARTGGE----GPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 283 RPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRN-TYYASIAKA 361
Cdd:cd01162  237 RLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDaVKLCAMAKR 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148230460 362 YAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLGK 420
Cdd:cd01162  317 FATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
43-416 5.77e-108

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: 326.29  E-value: 5.77e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  43 LSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTGVQ 122
Cdd:cd01156    2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 123 TAIEANS---LGQMpvIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGK 199
Cdd:cd01156   82 LSYGAHSnlcINQI--YRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 200 ANWYFLLARTNPDPKvpaGKAFTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGAF 279
Cdd:cd01156  160 ADTLVVYAKTDPSAG---AHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 280 DKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASIA 359
Cdd:cd01156  237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGV 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148230460 360 KAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISRE 416
Cdd:cd01156  317 ILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRE 373
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
45-416 2.69e-101

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: 309.05  E-value: 2.69e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  45 EQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAY-GCTGVQT 123
Cdd:cd01160    1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 124 AIEaNSLGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGKANWY 203
Cdd:cd01160   81 SLH-TDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 204 FLLARTNPDPKVPAGKAFtgFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGAFDKTR 283
Cdd:cd01160  160 IVVARTGGEARGAGGISL--FLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQER 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 284 PPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASIAKAYA 363
Cdd:cd01160  238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWA 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148230460 364 GDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISRE 416
Cdd:cd01160  318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
38-421 2.11e-88

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: 276.66  E-value: 2.11e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  38 GFNFELSEQQKEFQVTARKFAREEVMPvaAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYG 117
Cdd:cd01161   22 VLTEEQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 118 cTGVQTAIEAN-SLGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKK--GNEYIINGQKMWI 194
Cdd:cd01161  100 -LGFSVTLGAHqSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWI 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 195 TNGGKANWYFLLARTN-PDPKVPAGKAFTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFK 273
Cdd:cd01161  179 TNGGIADIFTVFAKTEvKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFK 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 274 IAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNT 353
Cdd:cd01161  259 VAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAE 338
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 354 YY--ASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLGKY 421
Cdd:cd01161  339 YQieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
39-419 1.26e-71

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: 232.25  E-value: 1.26e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  39 FNFE--LSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMnGHIPEQYGGLALGIFDTCLITEEIAY 116
Cdd:cd01151    7 LNLDdlLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLL-GATIKGYGCAGLSSVAYGLIAREVER 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 117 GCTGVQTAIEA-NSLGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWIT 195
Cdd:cd01151   86 VDSGYRSFMSVqSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWIT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 196 NGGKANWYFLLARTNPDPKVpagkafTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLiGEGAGFKIA 275
Cdd:cd01151  166 NSPIADVFVVWARNDETGKI------RGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 276 MGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYY 355
Cdd:cd01151  239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148230460 356 ASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLG 419
Cdd:cd01151  319 ISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITG 382
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
53-409 5.37e-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: 207.63  E-value: 5.37e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  53 TARKFAREEVMPVAAHYDKTG--------EYPVP---LIKRAWELGLMNGHIPEQYGGLAL---------GIFDTCLITE 112
Cdd:cd01153    4 EVARLAENVLAPLNADGDREGpvfddgrvVVPPPfkeALDAFAEAGWMALGVPEEYGGQGLpitvysalaEIFSRGDAPL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 113 EIAYGCTGVQTAIEANslgqmpviiaGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGN-EYIINGQK 191
Cdd:cd01153   84 MYASGTQGAAATLLAH----------GTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 192 MWITNGGKANW----YFLLARTnpdPKVPAG-KAFTGFIV-----DANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPa 261
Cdd:cd01153  154 RFISAGEHDMSenivHLVLARS---EGAPPGvKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 262 envLIGE-GAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKL--------IAEHQAVSFLLAEMAMKV 332
Cdd:cd01153  230 ---LIGEeGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLikaapavtIIHHPDVRRSLMTQKAYA 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 333 ELARLAYQRAAWEIDLGRR--------------NTYYASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKI 398
Cdd:cd01153  307 EGSRALDLYTATVQDLAERkategedrkalsalADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARI 386
                        410
                 ....*....|.
gi 148230460 399 YQIYEGTAQIQ 409
Cdd:cd01153  387 TTIYEGTTGIQ 397
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
45-419 2.01e-61

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: 205.27  E-value: 2.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  45 EQQKEFQVTARKFAREEVMP-----VAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCT 119
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHLPPelreeSALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 120 GVQtaieANSLGQM---PVIIA-GNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWIT 195
Cdd:cd01152   81 PVP----FNQIGIDlagPTILAyGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 196 NGGKANWYFLLARTNPDpkVPAGKAFTGFIVDANSPGIQIgR--KELNMGqrcSDTRGIVFEDVRVPAENVLIGEGAGFK 273
Cdd:cd01152  157 GAHYADWAWLLVRTDPE--APKHRGISILLVDMDSPGVTV-RpiRSINGG---EFFNEVFLDDVRVPDANRVGEVNDGWK 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 274 IAMGAFDKTRPPVAAGAVGLAQRALDEAtkyAVERKTFGKLIAEHqAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNT 353
Cdd:cd01152  231 VAMTTLNFERVSIGGSAATFFELLLARL---LLLTRDGRPLIDDP-LVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148230460 354 YYASIAKAYAGDIANQVASDAVQVFG--------GNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLG 419
Cdd:cd01152  307 AEASIAKLFGSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
45-419 2.65e-54

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: 186.83  E-value: 2.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  45 EQQKEFQVTARKFAREEVMPVAAHYDK---TGEYPVP--------LIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEE 113
Cdd:cd01155    1 RKAQELRARVKAFMEEHVYPAEQEFLEyyaEGGDRWWtpppiiekLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 114 I--------AYGCTGVQTaieanslGQMPVIIA-GNEAQQKKYLgrmteEPLM-----CAYCVTEPG-AGSDVAGLKTRA 178
Cdd:cd01155   81 TgrsffapeVFNCQAPDT-------GNMEVLHRyGSEEQKKQWL-----EPLLdgkirSAFAMTEPDvASSDATNIECSI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 179 EKKGNEYIINGQKMWITNGG--KANWYFLLARTNPDpKVPAGKAFTGFIVDANSPGIQIGRKELNMGQrcSDTRG----I 252
Cdd:cd01155  149 ERDGDDYVINGRKWWSSGAGdpRCKIAIVMGRTDPD-GAPRHRQQSMILVPMDTPGVTIIRPLSVFGY--DDAPHghaeI 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 253 VFEDVRVPAENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKV 332
Cdd:cd01155  226 TFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEI 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 333 ELARLAYQRAAWEIDLGRRNTYYASIA--KAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQR 410
Cdd:cd01155  306 EQARLLVLKAAHMIDTVGNKAARKEIAmiKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHL 385

                 ....*....
gi 148230460 411 LIISREHLG 419
Cdd:cd01155  386 RSIARMELK 394
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
269-415 2.88e-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: 249861  Cd Length: 150  Bit Score: 168.60  E-value: 2.88e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  269 GAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDL 348
Cdd:pfam00441   1 GRGFAVAMETLNHERLLIAAAALGAARRALDEAIEYARQRKAFGRPLIDFQLIRHRLADMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148230460  349 GRRNTYYASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISR 415
Cdd:pfam00441  81 GGPDPAEAAMAKLFASELAQEVADLAMQLLGGYGYSREYPLERLYRDARVLRIGEGTSEIQRNIIAR 147
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
64-415 2.03e-36

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: 138.27  E-value: 2.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  64 PVAAHYDKTGE------YP---VPLIKRAWELGLMNG--HIPEQYGGLALGIFDTCLITEEIAYGCTGVQTAIEANSLGQ 132
Cdd:cd01154   46 PVLEMWDRWGRrvdrvwVHpawHALMRRLIEEGVINIedGPAGEGRRHVHFAAGYLLSDAAAGLLCPLTMTDAAVYALRK 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 133 MpviiAGNEAQQK--KYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEK-KGNEYIINGQKmWITNGGKANWYFLLART 209
Cdd:cd01154  126 Y----GPEELKQYlpGLLSDRYKTGLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARP 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 210 NPDPkvPAGKAFTGFIV-----DANSPGIQIGRKELNMGQRCSDTRGIVFEDvrvpAENVLIG-EGAGFKIAMGAFDKTR 283
Cdd:cd01154  201 EGAP--AGARGLSLFLVprlleDGTRNGYRIRRLKDKLGTRSVATGEVEFDD----AEAYLIGdEGKGIYYILEMLNISR 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 284 PPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAA--WEIDLGRRNTYYA----- 356
Cdd:cd01154  275 LDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAAraFDRAAADKPVEAHmarla 354
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 357 -SIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISR 415
Cdd:cd01154  355 tPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLR 414
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
44-151 1.39e-35

Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.


Pssm-ID: 251519  Cd Length: 113  Bit Score: 127.98  E-value: 1.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460   44 SEQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTGVQT 123
Cdd:pfam02771   1 TEEQEALRDTVREFAEEELAPHAAEWDEEGEFPRELWRKLGELGLLGLTIPEEYGGAGLDYLAYALVAEELARADASVGL 80
                          90       100
                  ....*....|....*....|....*....
gi 148230460  124 AIEA-NSLGQMPVIIAGNEAQQKKYLGRM 151
Cdd:pfam02771  81 ALSVhSSLVAPPILRFGTEEQKEKYLPKL 109
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
159-209 2.73e-19

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


Pssm-ID: 145755  Cd Length: 52  Bit Score: 80.99  E-value: 2.73e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 148230460  159 AYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGKANWYFLLART 209
Cdd:pfam02770   1 AFALTEPGAGSDLASLETTAERDGDGWVLNGRKWWITNAALADLALVLART 51
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
286-405 4.18e-19

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 254591  Cd Length: 134  Bit Score: 82.73  E-value: 4.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  286 VAAGAVGLAQRALDEATKYAVERKT--FGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEI----DLGRRNTY----Y 355
Cdd:pfam08028   3 FAAPALGAARGALAAFIERARERVRayGGAPLAEDPATQTRLAEAAAEIDAARLLLERAADRIwahaDRGDEVTPeeraR 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 148230460  356 ASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGT 405
Cdd:pfam08028  83 ARRDAALAAELAVAAVDRLFRAAGGSALFKDSPLQRFWRDAHAGAAHAGL 132
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
133-423 3.96e-14

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: 72.75  E-value: 3.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 133 MPVIIA-GNEAQQKKYL-GRMTEEPLMCaYCVTEPGAGSDVAGLKTRA--EKKGNEYIIN-----GQKMWITNGGK-ANW 202
Cdd:cd01150  110 GNAIKNlGTDEHQDYWLqGANNLEIIGC-FAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGNLGKtATH 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 203 YFLLARTnpdpkVPAGK--AFTGFIV---DANS----PGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEG---- 269
Cdd:cd01150  189 AVVFAQL-----ITPGKnhGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGdvsp 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 270 ------------AGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKL-------IAEHQ----------- 319
Cdd:cd01150  264 dgtyvspfkdpnKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKpsdpevqILDYQlqqyrlfpqla 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 320 ---AVSFLLAEMAMK-VELARLAYQRAAweiDLGRRNTYYASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRD 395
Cdd:cd01150  344 aayAFHFAAKSLVEMyHEIIKELLQGNS---ELLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDD 420
                        330       340
                 ....*....|....*....|....*...
gi 148230460 396 AKIYQIYEGTAQIQRLIISREHLGKYKA 423
Cdd:cd01150  421 NDPFCTYEGDNTVLLQQTANYLLKKYAQ 448
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
66-408 2.14e-12

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: 66.60  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  66 AAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTGvqTAIEANSLGQMPVIIA--GNEAQ 143
Cdd:cd01159   14 APEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGS--AAWVASIVATHSRMLAafPPEAQ 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 144 QKKYlgrmTEEPLMCAYCVTEPGAgsdvaglktRAEKKGNEYIINGQKMWITNGGKANWYFLLARTNPDPkvpAGKAFTG 223
Cdd:cd01159   92 EEVW----GDGPDTLLAGSYAPGG---------RAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDD---GGPLPRA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 224 FIVDANspGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEG--AGFKiAMGAFDKTRPPV--------AAGAVGL 293
Cdd:cd01159  156 FVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDmmAGDG-PGGSTPVYRMPLrqvfplsfAAVSLGA 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 294 AQRALDEATKYAVER---KTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEID---------------LGRRNTYY 355
Cdd:cd01159  233 AEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWahalaggpidveeraRIRRDAAY 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148230460 356 ASIAKAYAGDIANQVAsdavqvfGGNGFNSDYPVEKLMRDAK-----IYQIYEGTAQI 408
Cdd:cd01159  313 AAKLSAEAVDRLFHAA-------GGSALYTASPLQRIWRDIHaaaqhAALNPETAAEA 363
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
66-378 3.79e-12

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: 66.19  E-value: 3.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  66 AAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAygctgvqtaiEANS-LGQMP---------V 135
Cdd:cd01163   14 AAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELA----------AADSnIAQALrahfgfveaL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 136 IIAGNEAQQKKYLGRMTEEPLM-CAycVTEPGAGSDVAGLkTRAEKKGNEYIINGQKMWITNGGKANWYFLLARTNPDPK 214
Cdd:cd01163   84 LLAGPEQFRKRWFGRVLNGWIFgNA--VSERGSVRPGTFL-TATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 215 VpagkaftGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMgafdktRPPV-----AAG 289
Cdd:cd01163  161 V-------FAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTL------LTAIyqlvlAAV 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 290 AVGLAQRALDEATKYAVER-KTFGKLIAEHQA----VSFLLAEMAMKVELARLAYQRAAWEIDlgrrntyyaSIAKAYAG 364
Cdd:cd01163  228 LAGIARAALDDAVAYVRSRtRPWIHSGAESARddpyVQQVVGDLAARLHAAEALVLQAARALD---------AAAAAGTA 298
                        330
                 ....*....|....
gi 148230460 365 DIANQVASDAVQVF 378
Cdd:cd01163  299 LTAEARGEAALAVA 312
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
40-423 8.90e-120

Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism];


Pssm-ID: 224871 [Multi-domain]  Cd Length: 393  Bit Score: 357.20  E-value: 8.90e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  40 NFELSEQQKEFQVTARKFAREEVMPVAAHYD---KTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAY 116
Cdd:COG1960    2 DFDLSEEQEALRAEVREFAEEELAPEAAEIDrriEDERFPRELLRALAEAGLLGLTIPEEYGGLGLSPLEQAAVLEELAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 117 GC--TGVQTAIEANSLGQMPVIIA--GNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLK-TRAEKKGNEYIINGQK 191
Cdd:COG1960   82 ADagGALALGLTHGGLGALAPTILrfGTEEQKRRYLPRLASGELIGAFALTEPGAGSDLASLRtTAAVRDDGDYVLNGQK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 192 MWITNGGKANWYFLLARTNPDPkvPAGKAFTGFIVDAN-SPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGA 270
Cdd:COG1960  162 IWISNAPVADWLLVLARTDPAP--GKHKGISLFLVPKDlTPGVSVGPILKKMGLRGSATGEVFFDDVRVPAENLLGEEGD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 271 GFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGR 350
Cdd:COG1960  240 GFKIAMETLNVERLGIAAQALGIAEAALEEAVAYARERKQFGRPIADFQLVQFKLADMAAELEAARLLVLRAAELADAGD 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148230460 351 RNTYYASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLGKYKA 423
Cdd:COG1960  320 DAGAEAAMAKLFATEAALEVADEAVQVHGGYGYTEEYPVERYYRDARILRIYEGTSEIQRLIIARRLLGLPAG 392
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
43-416 5.29e-80

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 254.80  E-value: 5.29e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  43 LSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYP--VPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTG 120
Cdd:PLN02519  26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 121 VQTAIEANS-LGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGK 199
Cdd:PLN02519 106 VGLSYGAHSnLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 200 ANWYFLLARTNPdpkvPAG-KAFTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGA 278
Cdd:PLN02519 186 AQTLVVYAKTDV----AAGsKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSG 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 279 FDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASI 358
Cdd:PLN02519 262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAG 341
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148230460 359 AKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISRE 416
Cdd:PLN02519 342 VILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRE 399
cyc_hxne_CoA_dh TIGR03207
cyclohexanecarboxyl-CoA dehydrogenase; Cyclohex-1-ene-1carboxyl-CoA is an intermediate in the ...
43-418 1.42e-63

cyclohexanecarboxyl-CoA dehydrogenase; Cyclohex-1-ene-1carboxyl-CoA is an intermediate in the anaerobic degradation of benzoyl-CoA derived from varioius aromatic compounds, in Rhodopseudomonas palustris but not Thauera aromatica. The aliphatic compound cyclohexanecarboxylate, can be converted to the same intermediate in two steps. The first step is its ligation to coenzyme A. The second is the action of this enzyme, cyclohexanecarboxyl-CoA dehydrogenase.


Pssm-ID: 132251 [Multi-domain]  Cd Length: 372  Bit Score: 210.93  E-value: 1.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460   43 LSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTGVQ 122
Cdd:TIGR03207   1 LNEDLQALADTARRFARERIAPGFKERDKTRVLDRELMRDMGEMGFIGPELPEEHGGLGMGCLAAGVIHEQIARADLSMS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  123 TAIEANSL-GQmpvIIAGNEAQQ--KKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGK 199
Cdd:TIGR03207  81 YVNLLASLnGQ---ILAQHARPEiaKPWLGQLIAGEALFAIALTEPRGGSDAARLRLRAERDGDDYVLNGEKTSISAADQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  200 ANWYFLLARTNPDPKvpAGKAFTGFIVDANSPGIQIGRKElNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGAF 279
Cdd:TIGR03207 158 ADAAVVFARTGSEAE--GARGISAFLVPMDLPGITRNRFD-CHGQRAIGRGSIFFENVRVPADHMLGNEGQGFVQVMQGF 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  280 DKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASIA 359
Cdd:TIGR03207 235 DFSRALIGLQVLAVARAALDETWRYVAERQAFGKPLSAFQGVSHPLADAETQVEAARLLCLQTLWLKDHGLPHTSEAAMC 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148230460  360 KAYAGDIANQVASDAVQVFGGNGFNSDyPVEKLMRDAKIYQIYEGTAQIQRLIISREHL 418
Cdd:TIGR03207 315 KWWAPKLAYDVIHQCLLTHGHGGYDRG-DMEQRLRDVLGFQIGDGTAQIMKTIIARHRA 372
PRK12341 PRK12341
putative acyl-CoA dehydrogenase; Provisional
40-422 7.48e-63

putative acyl-CoA dehydrogenase; Provisional


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 209.20  E-value: 7.48e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  40 NFELSEQQKEF-----QVTARKFAREEVmpvaAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEI 114
Cdd:PRK12341   2 DFSLTEEQELLlasirELITRNFPEEYF----RTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 115 AYgcTGVQTAIEANSLGQMPVIIAGNEAQQKKYLgRMTEEPLMCAYC--VTEPGAGSDVAGLKTRAEKKGNEYIINGQKM 192
Cdd:PRK12341  78 SK--CGAPAFLITNGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYAlaLTEPGAGSDNNSATTTYTRKNGKVYLNGQKT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 193 WITNGGKANWYFLLARtNPDPKVPAgKAFTGFIVDANSPGIQIGRKElNMGQRCSDTRGIVFEDVRVpAENVLIG-EGAG 271
Cdd:PRK12341 155 FITGAKEYPYMLVLAR-DPQPKDPK-KAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEV-EESDLVGeEGMG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 272 FKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRR 351
Cdd:PRK12341 231 FLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148230460 352 NTYYASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLGKYK 422
Cdd:PRK12341 311 LRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDYQ 381
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
46-422 2.86e-58

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 197.85  E-value: 2.86e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  46 QQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIAYGCTGVQTAI 125
Cdd:PTZ00461  40 EHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAY 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 126 EANS-LGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNE-YIINGQKMWITNGGKANWY 203
Cdd:PTZ00461 120 LAHSmLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGTVADVF 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 204 FLLARTNpdpkvpaGKaFTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFKIAMGAFDKTR 283
Cdd:PTZ00461 200 LIYAKVD-------GK-ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELER 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 284 PPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASIAKAYA 363
Cdd:PTZ00461 272 VTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFA 351
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148230460 364 GDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLGKYK 422
Cdd:PTZ00461 352 TPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGLK 410
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
40-422 2.66e-50

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 175.79  E-value: 2.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  40 NFELSEQQKEFQVTARKF-AREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGIFDTCLITEEIayGC 118
Cdd:PRK03354   2 DFNLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 119 TGVQTAIeansLGQMP-----VIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMW 193
Cdd:PRK03354  80 LGAPTYV----LYQLPggfntFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 194 ITNGGKANWYFLLARTNPDPKVPAgkaFTGFIVDANSPGIQIGRKElNMGQRCSDTRGIVFEDVRVPAENVLIGEGAGFK 273
Cdd:PRK03354 156 ITSSAYTPYIVVMARDGASPDKPV---YTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFN 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 274 IAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNT 353
Cdd:PRK03354 232 RVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITS 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148230460 354 YYASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLGKYK 422
Cdd:PRK03354 312 GDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
PLN02526 PLN02526
acyl-coenzyme A oxidase
43-419 2.11e-46

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 165.80  E-value: 2.11e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  43 LSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIpEQYGGLALGIFDTCLITEEIAYGCTGVQ 122
Cdd:PLN02526  29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDASCS 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 123 TAIEANS-LGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKMWITNGGKAN 201
Cdd:PLN02526 108 TFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 202 WYFLLARTNPDPKVpagkafTGFIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIGEGAgFKIAMGAFDK 281
Cdd:PLN02526 188 VLVIFARNTTTNQI------NGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-FQDTNKVLAV 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 282 TRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYYASIAKA 361
Cdd:PLN02526 261 SRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKA 340
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148230460 362 YAGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISREHLG 419
Cdd:PLN02526 341 WITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITG 398
PLN02876 PLN02876
acyl-CoA dehydrogenase
131-419 1.26e-37

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 144.94  E-value: 1.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 131 GQMPVIIA-GNEAQQKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGLKTRAEKKGNEYIINGQKMWITNGGKANWYFLLAR 208
Cdd:PLN02876 524 GNMEVLLRyGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVM 603
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 209 TNPDPKVPAGKAFTGFIVDANSPGIQIGRKELNMGqrCSDT----RGIVFEDVRVPAENVLIGEGAGFKIAMGAFDKTRP 284
Cdd:PLN02876 604 GKTDFNAPKHKQQSMILVDIQTPGVQIKRPLLVFG--FDDAphghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRL 681
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 285 PVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEID-LGRRNTYYA-SIAKAY 362
Cdd:PLN02876 682 HHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrLGNKKARGIiAMAKVA 761
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148230460 363 AGDIANQVASDAVQVFGGNGFNSDYPVEKLMRDAKIYQIYEGTAQIqrliisreHLG 419
Cdd:PLN02876 762 APNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV--------HLG 810
pimC_large TIGR03204
pimeloyl-CoA dehydrogenase, large subunit; Members of this protein family are the PimC ...
40-419 3.78e-37

pimeloyl-CoA dehydrogenase, large subunit; Members of this protein family are the PimC proteins of species such as Rhodopseudomonas palustris and Bradyrhizobium japonicum. The pimFABCDE operon encodes proteins for the metabolism of straight chain dicarboxylates of seven to fourteen carbons. Especially relevant is pimeloyl-CoA, basis of the gene symbol, as it is a catabolite of benzoyl-CoA degradation, which occurs in Rhodopseudomonas palustris.


Pssm-ID: 132248 [Multi-domain]  Cd Length: 395  Bit Score: 139.77  E-value: 3.78e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460   40 NFELSEQQKEFQVTARKFAREEVMPVAAHYDKTGEYPVP---------LIKRAWELGlmngHIPEQYGGLALGIFDTCLI 110
Cdd:TIGR03204   1 DLAFSKEEQAFRDEVRSFFKDNVPADTRQKLVEGRHLTKdemvtwwriLNKKGWGVS----HWPKQYGGTGWTSVQHYIF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  111 TEEIAYGCTGVQTAIEANSLGqmPVIIA-GNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIING 189
Cdd:TIGR03204  77 NEELQSAPAPQPLAFGVSMVG--PVIYTfGNEEQKKRFLPRIANVDDWWCQGFSEPGSGSDLASLKTKAEKKGDKWIING 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  190 QKMWITNGGKANWYFLLARTNPDPKVPAGKAFtgFIVDANSPGIQIgrKELNMGQRCSDTRGIVFEDVRVPAENVLIGEG 269
Cdd:TIGR03204 155 QKTWTTLAQHADWIFCLCRTDPTAKKQMGISF--ILVDMKSKGITV--RPIQTIDGGVEVNEVFFDDVEVPYENLVGEEN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  270 AGFKIAMGAFDKTRPPVAagAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAemAMKVELARLAYQRAAWEIDLG 349
Cdd:TIGR03204 231 KGWDYAKFLLGNERTGIA--RVGVSKERIRRIKDLAAKVESGGKPVIEDAKFREKLA--AVEIELKALELTQLRVVADEG 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  350 R----RNTYYASIAKAYAGDIANQVASDAVQVFGgnGFNSDYPV-------EKLMRDAKI---------YQIYEGTAQIQ 409
Cdd:TIGR03204 307 KhgkgKPNPASSVLKIKGSEIQQATTELLMEVIG--PFAAPYDVhgddgsnEAMDWTAQIapsyfnnrkVSIYGGSNEIQ 384
                         410
                  ....*....|
gi 148230460  410 RLIISREHLG 419
Cdd:TIGR03204 385 RNIIAKAVLG 394
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
54-411 5.41e-25

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 106.11  E-value: 5.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  54 ARKFAREEVMPVAAHYD-------KTGEYPVPL-IKRAWEL----GLMNGHIPEQYGGLALGiFDTCLITEEIAYGCTGV 121
Cdd:PTZ00456  67 ASKLATQTLLPLYESSDsegcvllKDGNVTTPKgFKEAYQAlkagGWTGISEPEEYGGQALP-LSVGFITRELMATANWG 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 122 QTAIEANSLGQMPVIIA-GNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGN-EYIINGQKMWITNGG- 198
Cdd:PTZ00456 146 FSMYPGLSIGAANTLMAwGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDh 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 199 --KAN-WYFLLARTnPDpKVPAGKAFTGFIVD---ANSPG-------IQIGRKELNMGQRCSDTRGIVFEDvrvpAENVL 265
Cdd:PTZ00456 226 dlTENiVHIVLARL-PN-SLPTTKGLSLFLVPrhvVKPDGsletaknVKCIGLEKKMGIKGSSTCQLSFEN----SVGYL 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 266 IGE-GAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKT----------------------------FGKLIA 316
Cdd:PTZ00456 300 IGEpNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSmralsgtkepekpadriichanvrqnilFAKAVA 379
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 317 EhqAVSFLLAEMAMKVEL---ARLAYQRAAWEIDLGrrntYYASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPVEKLM 393
Cdd:PTZ00456 380 E--GGRALLLDVGRLLDIhaaAKDAATREALDHEIG----FYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQIL 453
                        410
                 ....*....|....*...
gi 148230460 394 RDAKIYQIYEGTAQIQRL 411
Cdd:PTZ00456 454 RDARIGTLYEGTTGIQAL 471
pimD_small TIGR03203
pimeloyl-CoA dehydrogenase, small subunit; Members of this protein family are the PimD ...
40-389 7.82e-19

pimeloyl-CoA dehydrogenase, small subunit; Members of this protein family are the PimD proteins of species such as Rhodopseudomonas palustris, Bradyrhizobium japonicum. The pimFABCDE operon encodes proteins for the metabolism of straight chain dicarboxylates of seven to fourteen carbons. Especially relevant is pimeloyl-CoA, basis of the gene symbol, as it is a catabolite of benzoyl-CoA degradation, which occurs in Rhodopseudomonas palustris.


Pssm-ID: 132247 [Multi-domain]  Cd Length: 378  Bit Score: 86.21  E-value: 7.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460   40 NFELSEQQKEFqvtarKFAREEVMPVAAHYDKTGEY---PVPLIKRAW----ELGLMNGHIPEQYGGLALGIFDTCLITE 112
Cdd:TIGR03203   1 DFDLSEEQRLL-----KESVEGLLKTSYDFDSRKKYqkeKGGWSKAVWgklaEQGLLGLPFSEADGGFGAGSVETMIVME 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  113 EIAYGCTgVQTAIEANSLGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRAEKKGNEYIINGQKM 192
Cdd:TIGR03203  76 ALGKALV-LEPYLATVVIGGGFLRHAGSAAQKAAHLPGIIDGSKTFAFAQLEKNSRYDLGDVSTTAKKTGDGWVIDGEKF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  193 WITNGGKANWYFLLARTNPDPKVPAGKAFtgFIVDANSPGIQIGRKELNMGQRCSDtrgIVFEDVRVPAENVLIGEGAGF 272
Cdd:TIGR03203 155 VVLNGETADTLIVTARTKGARRDRTGIGV--FLVPAGAKGVTIKGYPTQDGLHAAD---ITFTGVVVGADAAIGDPENAL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  273 KIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELAR--LAYQRAAWEIDLGR 350
Cdd:TIGR03203 230 PLIERVVDDARAALCAEAVGLMDESLKTTVEYIKTRKQFGVPIGSFQVLQHRAADMFVAVEQARsmAMFATMASDFDDAK 309
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 148230460  351 RNTYYASIAKAYAGDIANQVASDAVQVFGGNGFNSDYPV 389
Cdd:TIGR03203 310 ERANAIAAAKVQIGKSLKFVGQQSIQLHGGIGMTMEAKI 348
sulfur_SfnB TIGR04022
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the ...
53-361 5.41e-13

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: 68.83  E-value: 5.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460   53 TARKFArEEVMPVAAHYDKTGEYPVPLIKRAWELGLMNGHIPEQYGGLALGiFDTclITEEIAygctgvqTAIEAN-SLG 131
Cdd:TIGR04022  13 IARRLA-AEFAPGAAERDRERRLPWAELDAFSQSGLWGITVPRAYGGAGVS-YAT--LAEVIA-------IISAADpSLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  132 QMP---------VIIAGNEAQQKKYLGRMTE-EPLMCAycVTEPGaGSDVAGLKTRAEKKGNEYIINGQKMWITNGGKAN 201
Cdd:TIGR04022  82 QIPqnhfyalevLRLTGSEEQKRFFFGEVLAgERFGNA--FSERG-TRNVLDFQTRLRRDGDGYRLNGRKFYSTGALFAH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  202 WYFLLARTNPDPKVPAgkaftgfIVDANSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVLigegAGFKiamgAFDk 281
Cdd:TIGR04022 159 WIPVLALDDEGRAVLA-------FVPRDAPGLTVIDDWSGFGQRTTASGTVLLDDVRVPAEHVV----PIQR----AFD- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  282 trPPVAAGAV----------GLAQRALDEATKY-----------AVERKTFGKLIAEHqavsflLAEMAMKVELARLAYQ 340
Cdd:TIGR04022 223 --RPTAAGPVaqiihaaidaGIARAALADTLAFvrerarpwidsGVERASDDPLTIAE------VGDLAIRLHAAEALLE 294
                         330       340
                  ....*....|....*....|.
gi 148230460  341 RAAWEIDLGRRNTYYASIAKA 361
Cdd:TIGR04022 295 RAGRAVDAARAEPTEESVAAA 315
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
163-415 6.43e-12

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 65.93  E-value: 6.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 163 TEPGAGSDVAGLKTRAEK-KGNEYIINGQKmwitnggkanWYFLLARTnpDPKVPAGKAFTG--------FIVDANSPGI 233
Cdd:PRK11561 185 TEKQGGSDVLSNTTRAERlADGSYRLVGHK----------WFFSVPQS--DAHLVLAQAKGGlscffvprFLPDGQRNAI 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 234 QIGRKELNMGQRCSDTRGIVFEDvrvpAENVLIG-EGAGFK--IAMGAFdkTRPPVAAGAVGLAQRALDEATKYAVERKT 310
Cdd:PRK11561 253 RLERLKDKLGNRSNASSEVEFQD----AIGWLLGeEGEGIRliLKMGGM--TRFDCALGSHGLMRRAFSVAIYHAHQRQV 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 311 FGKLIAEHQAVSFLLAEMAMKVE-----LARLA----YQRAAWEIDLGRRNTYYA--SIAKAYAGDIAnqvasDAVQVFG 379
Cdd:PRK11561 327 FGKPLIEQPLMRQVLSRMALQLEgqtalLFRLArawdRRADAKEALWARLFTPAAkfVICKRGIPFVA-----EAMEVLG 401
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148230460 380 GNGFNSDYPVEKLMRDAKIYQIYEGTAQIQRLIISR 415
Cdd:PRK11561 402 GIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
93-382 4.18e-11

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 63.44  E-value: 4.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  93 IPEQYGGLALGIFDTCLITEEIAYGC--TGVqTAIEANSLGQMPVIIA-GNEAQQKKYLGRM---TEEPlmCaYCVTEPG 166
Cdd:PRK13026 127 IPKEYGGKGFSAYANSTIVSKIATRSvsAAV-TVMVPNSLGPGELLTHyGTQEQKDYWLPRLadgTEIP--C-FALTGPE 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 167 AGSDVA-----GLKTRAEKKGNEYI---INGQKMWITNGGKANwyFL-LARTNPDP-KVPAGKAFTGF---IVDANSPGI 233
Cdd:PRK13026 203 AGSDAGaipdtGIVCRGEFEGEEVLglrLTWDKRYITLAPVAT--VLgLAFKLRDPdGLLGDKKELGItcaLIPTDHPGV 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 234 QIGRKELNMGQRCSD--TRGivfEDVRVPAENVLIGE---GAGFKIAMGAFDKTR----PPVAAGAVGLAQRAldeATKY 304
Cdd:PRK13026 281 EIGRRHNPLGMAFMNgtTRG---KDVFIPLDWIIGGPdyaGRGWRMLVECLSAGRgislPALGTASGHMATRT---TGAY 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 305 AVERKTFGKLIAEHQAVSFLLAEMAMK---VELARLAYQRAaweIDLGRRNTYYASIAKAYAGDIANQVASDAVQVFGGN 381
Cdd:PRK13026 355 AYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLTTTG---LDLGVKPSVVTAIAKYHMTELARDVVNDAMDIHAGK 431

                 .
gi 148230460 382 G 382
Cdd:PRK13026 432 G 432
PLN02443 PLN02443
acyl-coenzyme A oxidase
139-312 1.21e-09

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 58.69  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 139 GNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRA--EKKGNEYIIN-----GQKMWITNGGKANWYFLL-ARTN 210
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHsptltSSKWWPGGLGKVSTHAVVyARLI 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 211 PDPKvpaGKAFTGFIVDANS-------PGI---QIGRKELNMGQRCSDTRGIVFEDVRVPAENVLIG------EGAGF-- 272
Cdd:PLN02443 194 TNGK---DHGIHGFIVQLRSlddhsplPGVtvgDIGMKFGNGAYNTMDNGFLRFDHVRIPRDQMLMRlskvtrEGKYVqs 270
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148230460 273 ----KIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFG 312
Cdd:PLN02443 271 dvprQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFG 314
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
88-300 7.45e-09

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 56.04  E-value: 7.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  88 LMNGHIPEQYGGLALGIFDTCLITEEIAYGCTG--VQTaIEANSLGQMPVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEp 165
Cdd:PTZ00457  65 LYGARIATEYGGLGLGHTAHALIYEEVGTNCDSklLST-IQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEE- 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 166 GAGSDVAGLKTRAEKKGN-EYIINGQKMWItNGGKANWYFLLARTNPDPKVPAGKA----FTGFIVDANSPGIQIgrkel 240
Cdd:PTZ00457 143 GCGSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKTLTQTAAEEGATevsrNSFFICAKDAKGVSV----- 216
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 241 nmgqrcsDTRGIVFEDvrVPAENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDE 300
Cdd:PTZ00457 217 -------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQE 267
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
80-382 5.48e-08

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 53.67  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  80 IKRAWELGLMnghIPEQYGGLALGIFDTCLITEEIAYGC-TGVQTAIEANSLGqmPviiA------GNEAQQKKYLGRM- 151
Cdd:PRK09463 118 IKEHGFFGMI---IPKEYGGLEFSAYAHSRVLQKLASRSgTLAVTVMVPNSLG--P---GelllhyGTDEQKDHYLPRLa 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 152 --TEEPlmCaYCVTEPGAGSDVA-----GLKTRAEKKGNEYI---INGQKMWITNGGKANwyfLLartnpdpkvpaGKAF 221
Cdd:PRK09463 190 rgEEIP--C-FALTSPEAGSDAGsipdtGVVCKGEWQGEEVLgmrLTWNKRYITLAPIAT---VL-----------GLAF 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 222 -----------------TGFIVDANSPGIQIGRKELNMGQRCSD--TRGivfEDVRVPAENVLIGE---GAGFKIAMGAF 279
Cdd:PRK09463 253 klydpdgllgdkedlgiTCALIPTDTPGVEIGRRHFPLNVPFQNgpTRG---KDVFIPLDYIIGGPkmaGQGWRMLMECL 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 280 DKTR----PPVAAGAVGLAQRAldeATKYAVERKTFGKLIAEHQAVSFLLAEMAMKVELARLAYQRAAWEIDLGRRNTYY 355
Cdd:PRK09463 330 SVGRgislPSNSTGGAKLAALA---TGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKPSVL 406
                        330       340
                 ....*....|....*....|....*..
gi 148230460 356 ASIAKAYAGDIANQVASDAVQVFGGNG 382
Cdd:PRK09463 407 SAIAKYHLTERGRQVINDAMDIHGGKG 433
PLN02312 PLN02312
acyl-CoA oxidase
139-311 2.68e-07

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 51.31  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 139 GNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRA--EKKGNEYIIN-----GQKMWItnGGKANW---YFLLAR 208
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpcesAQKYWI--GGAANHathTIVFSQ 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 209 TNPDPKVPAGKAFTGFIVDANS---PGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVL-----IGEGAGFKIAM---- 276
Cdd:PLN02312 246 LHINGKNEGVHAFIAQIRDQDGnicPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLnsvadVSPDGKYVSAIkdpd 325
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148230460 277 ---GAF----DKTRPPVAAGAVGLAQRALDEATKYAVERKTF 311
Cdd:PLN02312 326 qrfGAFlaplTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
PLN02636 PLN02636
acyl-coenzyme A oxidase
120-312 2.14e-06

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 48.70  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 120 GVQTAIEANSlgqmpVIIAGNEAQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLKTRA--EKKGNEYIIN-----GQKM 192
Cdd:PLN02636 142 GVQYSLWGGS-----VINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFVINtpndgAIKW 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 193 WITNG---GK-ANWYFLLARTNPDPKVPAGKAFTGFIVDANS-------PGIQIGRKELNMGQRCSDTRGIVFEDVRVPA 261
Cdd:PLN02636 217 WIGNAavhGKfATVFARLKLPTHDSKGVSDMGVHAFIVPIRDmkthqvlPGVEIRDCGHKVGLNGVDNGALRFRSVRIPR 296
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148230460 262 ENVLIGEG----------------AGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYAVERKTFG 312
Cdd:PLN02636 297 DNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFG 363
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
159-311 2.97e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 47.92  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 159 AYCVTEPGAGSDVAGLKTRA--EKKGNEYIIN-----GQKMWITN-GGKANWYFLLARTNPDPKVPAGKAFTGFIVDANS 230
Cdd:PTZ00460 130 CYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLIVNGKNKGVHPFMVRIRDKET 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460 231 ----PGIQIGRKELNMGQRCSDTRGIVFEDVRVPAENVL-----IGEGAGF------KIAMGAFDKTRPPVAAGAVGLAQ 295
Cdd:PTZ00460 210 hkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikVSEDGQVerqgnpKVSYASMMYMRNLIIDQYPRFAA 289
                        170
                 ....*....|....*.
gi 148230460 296 RALDEATKYAVERKTF 311
Cdd:PTZ00460 290 QALTVAIRYSIYRQQF 305
HpaB_N pfam11794
4-hydroxyphenylacetate 3-hydroxylase N terminal; HpaB encodes part of the ...
145-266 8.42e-04

4-hydroxyphenylacetate 3-hydroxylase N terminal; HpaB encodes part of the 4-hydroxyphenylacetate 3-hydroxylase from Escherichia coli. HpaB is part of a heterodimeric enzyme that also requires HpaC. The enzyme is NADH-dependent and uses FAD as the redox chromophore. This family also includes PvcC, which may play a role in one of the proposed hydroxylation steps of pyoverdine chromophore biosynthesis.


Pssm-ID: 256625 [Multi-domain]  Cd Length: 265  Bit Score: 39.41  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230460  145 KKYLGRMTEEPLMCAYCVTEP------GAGSDVAGLKTRAEKKGNEYI-INGQKMWITNGGKANWYFLLArTNPDPKVPA 217
Cdd:pfam11794 127 RRYYKYAQENDLYLTHAITDPkgdrskPPHQEDPDVYVHVVEETDDGIvVRGAKALATGAAIADEIFVMP-TRAMPEEDK 205
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148230460  218 GKAFtGFIVDANSPGI-QIGRKELNMGqRCSD------TRG------IVFEDVRVPAENVLI 266
Cdd:pfam11794 206 DYAV-AFAVPMDAPGLkLICRRSYEDG-RASPfdyplsSRFdendalVVFDDVFVPWERVFM 265
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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