|
Name |
Accession |
Description |
Interval |
E-value |
| PaaC-3OHAcCoADH |
TIGR02279 |
3-hydroxyacyl-CoA dehydrogenase PaaC; This 3-hydroxyacyl-CoA dehydrogenase is involved in the ... |
1-475 |
0e+00 |
|
3-hydroxyacyl-CoA dehydrogenase PaaC; This 3-hydroxyacyl-CoA dehydrogenase is involved in the degradation of phenylacetic acid, presumably in steps following the opening of the phenyl ring. The sequences included in this model are all found in aparrent operons with other related genes such as paaA, paaB, paaD, paaE, paaF and paaN. Some genomes contain these other genes without an apparent paaC in the same operon - possibly in these cases a different dehydrogenase involved in fatty acid degradation may fill in the needed activity. This enzyme has domains which are members of the pfam02737 and pfam00725 families.
Pssm-ID: 188207 [Multi-domain] Cd Length: 503 Bit Score: 788.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 1 MMINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIH 80
Cdd:TIGR02279 1 ALTNVVTVAVIGAGAMGAGIAQVAASAGHQVLLYDIRAEALARAIAGIEARLNSLVTKGKLTAEECERTLKRLIPVTDLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 81 ALAAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLA 160
Cdd:TIGR02279 81 ALADAGLVIEAIVENLEVKKALFAQLEELCPADTIIASNTSSLSITAIAAGLARPERVAGLHFFNPAPVMALVEVVSGLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 161 TAAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQD 240
Cdd:TIGR02279 161 TAAEVAEQLYETALAWGKQPVHCHSTPGFIVNRVARPYYAEALRALEEQVAAPAVLDAALRDGAGFPMGPFELTDLIGHD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 241 VNFAVTCSVFNAFWQERRFLPSLVQQELVIGGRLGKKSGLGVYDWRAEREEVVGLEAVSDSFSP---------------- 304
Cdd:TIGR02279 241 VNFAVTCSVFNAFWQDRRFLPSLVQQELVIAGRLGRKSGLGVYDYREEAEAVVPLEAVSDSFSPrvtvvgdigaaaplla 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 305 ------MKVENKSD-GVTEIDDVLLIETQGETAQALATRLARP-----VVVVDKMTGKVVTIAAAAVNPDSATRKAIYYL 372
Cdd:TIGR02279 321 rleaagIKVEKKSGmGVTQIGDALLALTDGRTAQARAIELARPnlvlfDLVLDYSTGKRIAIAAAAVNPDSATRKAIYYL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 373 QQQGKTVLQIADYPGMLIWRTVAMIINEALDALQKGVASEQDIDTAMRLGVNYPYGPLAWGAQLGWQRILRFLENLQHHY 452
Cdd:TIGR02279 401 QQAGKKVLQIADYPGLLILRTVAMLANEAADAVLQGVASAQDIDTAMRLGVNYPYGPLAWAAQLGWQRILRVLENLQHHY 480
|
490 500
....*....|....*....|...
gi 446896099 453 GEERYRPCSLLRQRALLESGYES 475
Cdd:TIGR02279 481 GEERYRPSSLLRRRALLGSGYED 503
|
|
| PRK08268 |
PRK08268 |
3-hydroxy-acyl-CoA dehydrogenase; Validated |
1-475 |
0e+00 |
|
3-hydroxy-acyl-CoA dehydrogenase; Validated
Pssm-ID: 236211 [Multi-domain] Cd Length: 507 Bit Score: 730.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 1 MMINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIH 80
Cdd:PRK08268 3 ALPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAALARLRPVEALA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 81 ALAAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLA 160
Cdd:PRK08268 83 DLADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSGLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 161 TAAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQD 240
Cdd:PRK08268 163 TDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLIGLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 241 VNFAVTCSVFNAFWQERRFLPSLVQQELVIGGRLGKKSGLGVYDWRAEREEVVGLEAVSDSFSPMKV------------- 307
Cdd:PRK08268 243 VNHAVMESVYRQFYQEPRFRPSLIQQELVAAGRLGRKSGQGFYRYADGAKQPPAEAAPPAALPPVWVsadvegdlaalar 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 308 --------ENKSDGVTEIDDVLLIETQGETAQALATRL--ARPVVVVDKM----TGKVVTIAAAAVNPDSATRKAIYYLQ 373
Cdd:PRK08268 323 llerlgatIETGEGPSADGLVLLAPTGGDTTTAAAREGldAARVVLIDLLldyaAAKRRTLMAAPATSPAARDAAHALFQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 374 QQGKTVLQIADYPGMLIWRTVAMIINEALDALQKGVASEQDIDTAMRLGVNYPYGPLAWGAQLGWQRILRFLENLQHHYG 453
Cdd:PRK08268 403 QDGKAVSVIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWGDRLGAARILRVLENLQALYG 482
|
490 500
....*....|....*....|..
gi 446896099 454 EERYRPCSLLRQRALLESGYES 475
Cdd:PRK08268 483 DPRYRPSPWLRRRAALGLSLRS 504
|
|
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
4-285 |
2.00e-141 |
|
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440862 [Multi-domain] Cd Length: 281 Bit Score: 406.80 E-value: 2.00e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 4 NVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIHALA 83
Cdd:COG1250 1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARITPTTDLAALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 84 AADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAA 163
Cdd:COG1250 81 DADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 164 EVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVNF 243
Cdd:COG1250 161 ETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLVGLDTAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446896099 244 AVTCSVFNAFwQERRFLPSLVQQELVIGGRLGKKSGLGVYDW 285
Cdd:COG1250 241 AVLEVLYEAL-GDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
|
|
| PRK05808 |
PRK05808 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
3-285 |
3.13e-101 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 180269 [Multi-domain] Cd Length: 282 Bit Score: 304.58 E-value: 3.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 3 INVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIHAL 82
Cdd:PRK05808 1 MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARITGTTDLDDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 83 AAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATA 162
Cdd:PRK05808 81 KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 163 AEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVN 242
Cdd:PRK05808 161 DATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIGLDTC 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446896099 243 FAVTCSVFNAFwQERRFLPSLVQQELVIGGRLGKKSGLGVYDW 285
Cdd:PRK05808 241 LAIMEVLYEGF-GDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
|
|
| PLN02545 |
PLN02545 |
3-hydroxybutyryl-CoA dehydrogenase |
2-290 |
2.47e-96 |
|
3-hydroxybutyryl-CoA dehydrogenase
Pssm-ID: 215300 [Multi-domain] Cd Length: 295 Bit Score: 292.40 E-value: 2.47e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 2 MINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIHA 81
Cdd:PLN02545 1 MAEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATLGRIRCTTNLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 82 LAAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLAT 161
Cdd:PLN02545 81 LRDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 162 AAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDV 241
Cdd:PLN02545 161 SDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIGLDT 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446896099 242 NFAVTcSVFNAFWQERRFLPSLVQQELVIGGRLGKKSGLGVYDWRAERE 290
Cdd:PLN02545 241 CLSIM-KVLHEGLGDSKYRPCPLLVQYVDAGRLGRKSGRGVYHYDGKKR 288
|
|
| PRK07530 |
PRK07530 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
2-288 |
2.94e-94 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181018 [Multi-domain] Cd Length: 292 Bit Score: 286.90 E-value: 2.94e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 2 MINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIHA 81
Cdd:PRK07530 1 MMAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARQVAKGKISEEARAAALARISTATDLED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 82 LAAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLAT 161
Cdd:PRK07530 81 LADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIRGIAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 162 AAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDv 241
Cdd:PRK07530 161 DEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIYTLYEGVGSVEAIDTAMKLGANHPMGPLELADFIGLD- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446896099 242 nfavTC-SVFNAFWQ-----ERRFLPSLVQqeLVIGGRLGKKSGLGVYDWRAE 288
Cdd:PRK07530 240 ----TClSIMQVLHDgladsKYRPCPLLVK--YVEAGWLGRKTGRGFYDYRGE 286
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
7-186 |
2.10e-85 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 260.16 E-value: 2.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 7 TVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIHALAAAD 86
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARISFTTDLAAAVDAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 87 LVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAAEVV 166
Cdd:pfam02737 81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160
|
170 180
....*....|....*....|
gi 446896099 167 EQLCELTLSWGKQPVRCHST 186
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVKDT 180
|
|
| PRK07819 |
PRK07819 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
1-285 |
1.13e-84 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181133 [Multi-domain] Cd Length: 286 Bit Score: 262.23 E-value: 1.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 1 MMINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIH 80
Cdd:PRK07819 1 MSDAIQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERAVSRGKLTERERDAALARLRFTTDLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 81 ALAAADLVIEAASERLEVKKALFAQLAEVCP-PQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGL 159
Cdd:PRK07819 81 DFADRQLVIEAVVEDEAVKTEIFAELDKVVTdPDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 160 ATAAEVV---EQLCELTLswGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDL 236
Cdd:PRK07819 161 VTSEATVaraEEFASDVL--GKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446896099 237 IGQDVNFAVTCSVFNAFWQERRFLPSLVQQeLVIGGRLGKKSGLGVYDW 285
Cdd:PRK07819 239 VGLDTVKAIADSMYEEFKEPLYAPPPLLLR-MVEAGLLGKKSGRGFYTY 286
|
|
| PRK09260 |
PRK09260 |
3-hydroxyacyl-CoA dehydrogenase; |
5-288 |
2.25e-78 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 236434 [Multi-domain] Cd Length: 288 Bit Score: 245.86 E-value: 2.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 5 VQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIHALAA 84
Cdd:PRK09260 1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGKLTEAARQAALARLSYSLDLKAAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 85 -ADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAA 163
Cdd:PRK09260 81 dADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLETSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 164 EVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVNF 243
Cdd:PRK09260 161 ETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLVGLDTRL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446896099 244 AVTCSVFNAFWQERRFLPSLVQqeLVIGGRLGKKSGLGVYDWRAE 288
Cdd:PRK09260 241 NNLKYLHETLGEKYRPAPLLEK--YVKAGRLGRKTGRGVYDYTNR 283
|
|
| PRK06130 |
PRK06130 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
2-296 |
3.67e-67 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 235707 [Multi-domain] Cd Length: 311 Bit Score: 217.72 E-value: 3.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 2 MINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNsrVKRGKLTAETCERTLKRLIPVTDihA 81
Cdd:PRK06130 1 MNPIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALG--VYAPLGIASAGMGRIRMEAGLAA--A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 82 LAAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLAT 161
Cdd:PRK06130 77 VSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 162 AAEVVEQLCELTLSWGKQPVRCH-STPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPM---GPLELTDLI 237
Cdd:PRK06130 157 SPQTVATTMALLRSIGKRPVLVKkDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQRDMN 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446896099 238 GQDVNFAVTCSVFNAFwqERRFLPSLVQQELVIGGRLGKKSGLGVYDWRAEREEVVGLE 296
Cdd:PRK06130 237 GLDVHLAVASYLYQDL--ENRTTPSPLLEEKVEAGELGAKSGQGFYAWPPERREEVLAD 293
|
|
| PRK06035 |
PRK06035 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
4-277 |
6.16e-61 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 180361 [Multi-domain] Cd Length: 291 Bit Score: 200.87 E-value: 6.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 4 NVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHAR---LNSRVKRGKLTAETCERTLKRLIPVTDIH 80
Cdd:PRK06035 2 DIKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKGKMSEDEAKAIMARIRTSTSYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 81 ALAAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLA 160
Cdd:PRK06035 82 SLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVRAAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 161 TAAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQD 240
Cdd:PRK06035 162 TSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELMDIIGID 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 446896099 241 VNFAVTCSVFNAFwQERRFLPSLVQQELVIGGRLGKK 277
Cdd:PRK06035 242 TVYHIAEYLYEET-GDPQFIPPNSLKQMVLNGYVGDK 277
|
|
| fa_ox_alpha_mit |
TIGR02441 |
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ... |
5-467 |
1.42e-54 |
|
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase (EC 4.2.1.17) _ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35). Some characterization in human (SP:P40939), pig (SP:Q29554), and rat (SP:Q64428). The beta subunit has activity: acetyl-CoA C-acyltransferase (EC 2.3.1.16).
Pssm-ID: 131494 [Multi-domain] Cd Length: 737 Bit Score: 194.29 E-value: 1.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 5 VQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIHALAA 84
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLDYSGFKN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 85 ADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAAE 164
Cdd:TIGR02441 415 ADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDGTSKD 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 165 VVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVaAPEVIDaALRDGAGFPMGPLELTDLIGQDVNFA 244
Cdd:TIGR02441 495 TLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGV-DPKKLD-KLTTKFGFPVGAATLADEVGVDVAEH 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 245 VTCSVFNAFwQERRFLPSL-VQQELVIGGRLGKKSGLGVYDWraeREEVVGLEAVsdsfspmkvenkSDGVTEIddvlli 323
Cdd:TIGR02441 573 VAEDLGKAF-GERFGGGSAeLLSELVKAGFLGRKSGKGIFIY---QEGKKGSKKV------------NSDADEI------ 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 324 etqgetaqalatrlarpvvvvdkmtgkvvtiaaaavnpdsatrkaiyyLQQQGKTVLQIADYPGMLIWRTVAMIINEALD 403
Cdd:TIGR02441 631 ------------------------------------------------LAQYKLPPKAEVSSPEDIQIRLVSRFVNEAVL 662
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446896099 404 ALQKGV-ASEQDIDTAMRLGVNYPY---GPLAWGAQLGWQRILRFLENLQHHYGEErYRPCSLLRQRA 467
Cdd:TIGR02441 663 CLEEGIlASPSEGDIGAVFGLGFPPflgGPFRFVDLYGADKLVDKMEKYAAAYGVQ-FTPCQLLLDHA 729
|
|
| fadJ |
PRK11154 |
fatty acid oxidation complex subunit alpha FadJ; |
5-467 |
2.37e-52 |
|
fatty acid oxidation complex subunit alpha FadJ;
Pssm-ID: 236864 [Multi-domain] Cd Length: 708 Bit Score: 187.80 E-value: 2.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 5 VQTVAVIGSGTMGAGIAEV-AASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIHALA 83
Cdd:PRK11154 309 VNKVGVLGGGLMGGGIAYVtATKAGLPVRIKDINPQGINHALKYSWDLLDKKVKRRHLKPSERDKQMALISGTTDYRGFK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 84 AADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAA 163
Cdd:PRK11154 389 HADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVIPHAKTSA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 164 EVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAApEVIDAALRDgAGFPMGPLELTDLIGQDVNF 243
Cdd:PRK11154 469 ETIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLEGEPI-EHIDAALVK-FGFPVGPITLLDEVGIDVGT 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 244 AVTCSVFNAFWQerRFLPSLVQQELVIGGRLGKKSGLGVY----DWRAEREEVvgleavsDSfspmkvenksdgvtEIDD 319
Cdd:PRK11154 547 KIIPILEAALGE--RFSAPAAFDKLLNDDRKGRKNGRGFYlygqKGKKSKKQV-------DE--------------SVYP 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 320 VLLIETQGETAQAlatrlarpvvvvdkmtgkvvtiaaaavnpdsatrkaiyylqqqgktvlQIADypgmliwRTVAMIIN 399
Cdd:PRK11154 604 LLGITPQSRLSAN------------------------------------------------EIAE-------RCVMLMLN 628
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446896099 400 EALDALQKGV-ASEQDIDTAMRLGVNYPY---GPLAWGAQLGWQRILRFLENLQHHYGeERYRPCSLLRQRA 467
Cdd:PRK11154 629 EAVRCLDEGIiRSARDGDIGAVFGIGFPPflgGPFRYMDSLGAGEVVAILERLAAQYG-DRFTPCERLVEMA 699
|
|
| fadB |
PRK11730 |
fatty acid oxidation complex subunit alpha FadB; |
5-289 |
2.13e-50 |
|
fatty acid oxidation complex subunit alpha FadB;
Pssm-ID: 183293 [Multi-domain] Cd Length: 715 Bit Score: 182.37 E-value: 2.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 5 VQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIHALAA 84
Cdd:PRK11730 313 VKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDLGMTEAAKLLNKQVERGKIDGAKMAGVLSSIRPTLDYAGFER 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 85 ADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAAE 164
Cdd:PRK11730 393 VDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKTSDE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 165 VVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSeAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVnfA 244
Cdd:PRK11730 473 TIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFA-GFSQLLRDGADFRQIDKVMEKQFGWPMGPAYLLDVVGIDT--A 549
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446896099 245 VTC-SVFNAFWQER--RFLPSLVQQeLVIGGRLGKKSGLGVYDWRAER 289
Cdd:PRK11730 550 HHAqAVMAEGFPDRmkKDYRDAIDV-LFEAKRFGQKNGKGFYRYEEDK 596
|
|
| PRK08293 |
PRK08293 |
3-hydroxyacyl-CoA dehydrogenase; |
4-286 |
9.06e-50 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 181359 [Multi-domain] Cd Length: 287 Bit Score: 171.28 E-value: 9.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 4 NVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAE-TCERTLKRLIPVTDIHAL 82
Cdd:PRK08293 2 DIKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATKEaPAEAALNRITLTTDLAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 83 AA-ADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLAT 161
Cdd:PRK08293 82 VKdADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 162 AAEVVEQLCELTLSWGKQPVRCH-STPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQD 240
Cdd:PRK08293 162 DPEVFDTVVAFAKAIGMVPIVLKkEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIVGLD 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446896099 241 vnfavTCSVFNAFWQERRFLPSLVQ-----QELVIGGRLGKKSGLGVYDWR 286
Cdd:PRK08293 242 -----TAYNITSNWAEATDDENAKKaaallKEYIDKGKLGVATGEGFYNYP 287
|
|
| PRK08269 |
PRK08269 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
16-287 |
7.64e-46 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181340 [Multi-domain] Cd Length: 314 Bit Score: 161.76 E-value: 7.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 16 MGAGIAEVAASHGHQVLLYDI---SAEA----LTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTD---IHALAAA 85
Cdd:PRK08269 1 MGQGIALAFAFAGHDVTLIDFkprDAAGwralDAEARAEIERTLAALVALGRIDAAQADAVLARIAVVARdgaADALADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 86 DLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAAEV 165
Cdd:PRK08269 81 DLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATDPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 166 VEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFP---MGPLELTDLIGQDVN 242
Cdd:PRK08269 161 VDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRfavLGLLEFIDWGGCDIL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446896099 243 FAVTCSVFNAFWQErRFLPSLVQQELVIGGRLGKKSGLGVYDWRA 287
Cdd:PRK08269 241 YYASRYLAGEIGPD-RFAPPAIVVRNMEEGRDGLRTGAGFYDYAG 284
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
8-236 |
2.27e-42 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 152.50 E-value: 2.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 8 VAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDI-HALAAAD 86
Cdd:PRK06129 5 VAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEAPDAVLARIRVTDSLaDAVADAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 87 LVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAAEVV 166
Cdd:PRK06129 85 YVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTAPATL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446896099 167 EQLCELTLSWGKQPVRCH-STPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFP---MGPLELTDL 236
Cdd:PRK06129 165 ARAEALYRAAGQSPVRLRrEIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRwsfMGPFETIDL 238
|
|
| 3HCDH |
pfam00725 |
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ... |
188-285 |
1.62e-36 |
|
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda crystallin. Some proteins include two copies of this domain.
Pssm-ID: 395588 [Multi-domain] Cd Length: 97 Bit Score: 130.03 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 188 GFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVNFAVTCsVFNAFWQERRFLPSLVQQE 267
Cdd:pfam00725 1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILE-VLAEEFGDRAYRPPPLLEK 79
|
90
....*....|....*...
gi 446896099 268 LVIGGRLGKKSGLGVYDW 285
Cdd:pfam00725 80 LVEAGRLGRKTGKGFYKY 97
|
|
| PRK07066 |
PRK07066 |
L-carnitine dehydrogenase; |
4-225 |
1.94e-25 |
|
L-carnitine dehydrogenase;
Pssm-ID: 168796 [Multi-domain] Cd Length: 321 Bit Score: 106.46 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 4 NVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISaealtraiDGIHARLNSRV-------KRGKLTAETcerTLKRLIPV 76
Cdd:PRK07066 6 DIKTFAAIGSGVIGSGWVARALAHGLDVVAWDPA--------PGAEAALRANVanawpalERQGLAPGA---SPARLRFV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 77 TDIHA-LAAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEV 155
Cdd:PRK07066 75 ATIEAcVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446896099 156 VSGLATAAEVVEQLCELTLSWGKQPVRCH-STPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAG 225
Cdd:PRK07066 155 LGGERTAPEAVDAAMGIYRALGMRPLHVRkEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAG 225
|
|
| PRK07531 |
PRK07531 |
carnitine 3-dehydrogenase; |
2-225 |
9.65e-20 |
|
carnitine 3-dehydrogenase;
Pssm-ID: 236044 [Multi-domain] Cd Length: 495 Bit Score: 91.72 E-value: 9.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 2 MINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEAlTRAIDGIHArlNSRVKRGKLTAETCERTLKRLIPVTDIHA 81
Cdd:PRK07531 1 MTMIMKAACIGGGVIGGGWAARFLLAGIDVAVFDPHPEA-ERIIGEVLA--NAERAYAMLTDAPLPPEGRLTFCASLAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 82 LAAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLAT 161
Cdd:PRK07531 78 VAGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVELVGGGKT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446896099 162 AAEVVEQLCELTLSWGKQPVRC-HSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAG 225
Cdd:PRK07531 158 SPETIRRAKEILREIGMKPVHIaKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFG 222
|
|
| 3HCDH |
pfam00725 |
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ... |
392-473 |
2.85e-15 |
|
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda crystallin. Some proteins include two copies of this domain.
Pssm-ID: 395588 [Multi-domain] Cd Length: 97 Bit Score: 71.09 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 392 RTVAMIINEALDALQKGVASEQDIDTAMRLGVNYPYGPLAWGAQLGWQRILRFLENLQHHYGEERYRPCSLLRQraLLES 471
Cdd:pfam00725 6 RLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAEEFGDRAYRPPPLLEK--LVEA 83
|
..
gi 446896099 472 GY 473
Cdd:pfam00725 84 GR 85
|
|
| 3HCDH_RFF |
pfam18321 |
3-hydroxybutyryl-CoA dehydrogenase reduced Rossmann-fold domain; This domain is found in ... |
325-386 |
8.89e-12 |
|
3-hydroxybutyryl-CoA dehydrogenase reduced Rossmann-fold domain; This domain is found in 3-hydroxybutyryl-CoA dehydrogenase present in E. coli. 3-hydroxybutyryl-CoA dehydrogenase catalyzes the second step in the biosynthesis of n-butanol from acetyl-CoA, in which acetoacetyl-CoA is reduced to 3-hydroxybutyryl-CoA. This domain is a reduced Rossmann-fold domain and, unlike the first Rossmann-fold domain, it is missing the catalytic residues and an NAD(H) binding cleft.
Pssm-ID: 436408 [Multi-domain] Cd Length: 69 Bit Score: 60.34 E-value: 8.89e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446896099 325 TQGETAQALATRLARPVVVVDKM----TGKVVTIAAAAVNPDSATRKAIYYLQQQGKTVLQIADYP 386
Cdd:pfam18321 4 TDGRTATQRAAELGRPVVLFDLAldydSATRLAVAPAAQCSPQALAQAVALLQALGKAVLVLADAP 69
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
7-92 |
6.28e-05 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 42.88 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 7 TVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRaidgIHARLNSRVKRGKLTAETCERtlkrlipvtdihALAAAD 86
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQ----LESLLGARFTTLYSQAELLEE------------AVKEAD 85
|
....*.
gi 446896099 87 LVIEAA 92
Cdd:smart01002 86 LVIGAV 91
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
7-149 |
6.72e-05 |
|
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.
Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 43.23 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 7 TVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAID-GIharlnsrvkRGKLTAETCERTLKRLIpvTDIHALAAA 85
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAaGA---------IAAASPAEFVAGLDVVI--TMVPAGAAV 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446896099 86 DLVIEAASerlevkkalfaqLAEVCPPQTLL--TTNTSSISITAIAAEVKNpervAGLHFFNpAPV 149
Cdd:pfam03446 70 DAVIFGEG------------LLPGLKPGDIIidGSTSSPEDARRRAKELKE----KGLHFLD-APV 118
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
7-183 |
7.65e-05 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 44.34 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 7 TVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAidgiharlnsrVKRGKLTAETCERtlkrlipvtdihALAAAD 86
Cdd:COG2084 3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEAL-----------VAAGARVAASPAE------------AAAAAD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 87 LVI------EAASERLEVKKALFAQLAevcPPQTLLttNTSSISIT---AIAAEVKNpervAGLHFFNpAPVM------- 150
Cdd:COG2084 60 VVItmlpddAAVEEVLLGEDGLLAALR---PGAVVV--DMSTISPEtarELAAAAAA----RGVRYLD-APVSggpagae 129
|
170 180 190
....*....|....*....|....*....|....*
gi 446896099 151 --KLVEVVSGlatAAEVVEQLCELTLSWGKQPVRC 183
Cdd:COG2084 130 agTLTIMVGG---DEAAFERARPVLEAMGKRIVHV 161
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
6-91 |
1.47e-04 |
|
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440010 [Multi-domain] Cd Length: 327 Bit Score: 43.87 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 6 QTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEaltrAIDGIHA-RLNSRVKRG-KLTaetcertlKRLIPVTDI-HAL 82
Cdd:COG0240 1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPE----VAEEINEtRENPRYLPGvKLP--------ENLRATSDLeEAL 68
|
....*....
gi 446896099 83 AAADLVIEA 91
Cdd:COG0240 69 AGADLVLLA 77
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
7-89 |
3.78e-04 |
|
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.
Pssm-ID: 274399 [Multi-domain] Cd Length: 409 Bit Score: 42.60 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 7 TVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEaltrAIDGIHARLNSRVKRGKLTAETCERTLKRLIPVTDIH-ALAAA 85
Cdd:TIGR03026 2 KIAVIGLGYVGLPLAALLADLGHDVTGVDIDQE----KVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEeAIRDA 77
|
....
gi 446896099 86 DLVI 89
Cdd:TIGR03026 78 DVII 81
|
|
| YqeC |
COG1023 |
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; |
8-90 |
3.97e-04 |
|
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
Pssm-ID: 440646 [Multi-domain] Cd Length: 300 Bit Score: 42.39 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 8 VAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTR-AIDGIH---------ARLNSR------VKRGKLTaetcERTLK 71
Cdd:COG1023 3 IGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAAlAAEGATgadsleelvAKLPAPrvvwlmVPAGEIT----DQVIE 78
|
90
....*....|....*....
gi 446896099 72 RLIPVtdihaLAAADLVIE 90
Cdd:COG1023 79 ELAPL-----LEPGDIVID 92
|
|
| ApbA |
pfam02558 |
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ... |
8-114 |
5.15e-04 |
|
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.
Pssm-ID: 426831 [Multi-domain] Cd Length: 147 Bit Score: 40.29 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 8 VAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHarlnsrvkrgkLTAETCERTLKRLIPVTDIHALAAADL 87
Cdd:pfam02558 1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELAAIKKNGLR-----------LTSPGGERIVPPPAVTSASESLGPIDL 69
|
90 100 110
....*....|....*....|....*....|.
gi 446896099 88 VIeaaserLEVK----KALFAQLAEVCPPQT 114
Cdd:pfam02558 70 VI------VTVKayqtEEALEDIAPLLGPNT 94
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
7-91 |
2.46e-03 |
|
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.
Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 40.08 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 7 TVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRaidgIHARLNSRVKRGKLTAETCERTLKRlipvtdihalaaAD 86
Cdd:cd05305 170 KVVILGAGVVGENAARVALGLGAEVTVLDINLERLRY----LDDIFGGRVTTLYSNPANLEEALKE------------AD 233
|
....*
gi 446896099 87 LVIEA 91
Cdd:cd05305 234 LVIGA 238
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
8-90 |
2.56e-03 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 39.73 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 8 VAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRA----------IDGIHARLNSR------VKRGKLTaetcERTLK 71
Cdd:PRK09599 3 LGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALaeegatgadsLEELVAKLPAPrvvwlmVPAGEIT----DATID 78
|
90
....*....|....*....
gi 446896099 72 RLIPVtdihaLAAADLVIE 90
Cdd:PRK09599 79 ELAPL-----LSPGDIVID 92
|
|
| sugar_DH |
cd08236 |
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ... |
6-92 |
3.62e-03 |
|
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.
Pssm-ID: 176198 [Multi-domain] Cd Length: 343 Bit Score: 39.52 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 6 QTVAVIGSGTMGAGIAEVAASHG-HQVLLYDISAEALTRAID-GIHARLNSRvkrgkltaETCERTLKRLIPVtdihalA 83
Cdd:cd08236 161 DTVVVIGAGTIGLLAIQWLKILGaKRVIAVDIDDEKLAVARElGADDTINPK--------EEDVEKVRELTEG------R 226
|
....*....
gi 446896099 84 AADLVIEAA 92
Cdd:cd08236 227 GADLVIEAA 235
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
8-33 |
3.90e-03 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 38.61 E-value: 3.90e-03
10 20
....*....|....*....|....*.
gi 446896099 8 VAVIGSGTMGAGIAEVAASHGHQVLL 33
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAGHEVVI 26
|
|
| Zn_ADH7 |
cd08261 |
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ... |
6-92 |
4.42e-03 |
|
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
Pssm-ID: 176222 [Multi-domain] Cd Length: 337 Bit Score: 39.09 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 6 QTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAID-GIHARLNsrVKRGKLTAEtcertlkrlipVTDIHALAA 84
Cdd:cd08261 161 DTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARElGADDTIN--VGDEDVAAR-----------LRELTDGEG 227
|
....*...
gi 446896099 85 ADLVIEAA 92
Cdd:cd08261 228 ADVVIDAT 235
|
|
| PRK06522 |
PRK06522 |
2-dehydropantoate 2-reductase; Reviewed |
8-114 |
6.27e-03 |
|
2-dehydropantoate 2-reductase; Reviewed
Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 38.68 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 8 VAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALtraidgihARLNsrvKRGkLTAETCERTLkRLIPVTDIHALAAADL 87
Cdd:PRK06522 3 IAILGAGAIGGLFGAALAQAGHDVTLVARRGAHL--------DALN---ENG-LRLEDGEITV-PVLAADDPAELGPQDL 69
|
90 100 110
....*....|....*....|....*....|.
gi 446896099 88 VIeaaserLEVK----KALFAQLAEVCPPQT 114
Cdd:PRK06522 70 VI------LAVKayqlPAALPSLAPLLGPDT 94
|
|
| YdfG |
COG4221 |
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ... |
2-52 |
6.77e-03 |
|
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 443365 [Multi-domain] Cd Length: 240 Bit Score: 38.24 E-value: 6.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446896099 2 MINVQTVAVI--GSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARL 52
Cdd:COG4221 1 MSDKGKVALItgASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRA 53
|
|
| AspD |
COG1712 |
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism]; |
7-93 |
8.31e-03 |
|
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];
Pssm-ID: 441318 [Multi-domain] Cd Length: 263 Bit Score: 37.86 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446896099 7 TVAVIGSGTMGAGIAEVAASHGHQVL-LYDISAEALTRAIDGIHARlnsrvkrgkltaetcertlkrliPVTDIHALAAA 85
Cdd:COG1712 2 RIGLIGCGAIGSEVAEALADAGVELVaVYDRDPERAEALLASLGAR-----------------------VVSDVDELLAA 58
|
90
....*....|
gi 446896099 86 --DLVIEAAS 93
Cdd:COG1712 59 dpDLVVEAAS 68
|
|
| PRK11036 |
PRK11036 |
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM; |
12-51 |
8.85e-03 |
|
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
Pssm-ID: 182918 Cd Length: 255 Bit Score: 38.02 E-value: 8.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446896099 12 GSGTMGAGIAEVaashGHQVLLYDISAEALTRAIDGIHAR 51
Cdd:PRK11036 54 GEGQTAIKLAEL----GHQVILCDLSAEMIQRAKQAAEAK 89
|
|
| |
