|
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: 790.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 1 MMINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIH 80
Cdd:TIGR02279 1 ALTNVVTVAVIGAGAMGAGIAQVAASAGHQVLLYDIRAEALARAIAGIEARLNSLVTKGKLTAEECERTLKRLIPVTDLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 81 ALAAANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLA 160
Cdd:TIGR02279 81 ALADAGLVIEAIVENLEVKKALFAQLEELCPADTIIASNTSSLSITAIAAGLARPERVAGLHFFNPAPVMALVEVVSGLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 161 TAAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQD 240
Cdd:TIGR02279 161 TAAEVAEQLYETALAWGKQPVHCHSTPGFIVNRVARPYYAEALRALEEQVAAPAVLDAALRDGAGFPMGPFELTDLIGHD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 241 VNFAVTCSVFNAFWQERRFLPSLVQQELVIGGRLGKKSGLGVYDWRAEREAVVGLEAVSDSFSP---------------- 304
Cdd:TIGR02279 241 VNFAVTCSVFNAFWQDRRFLPSLVQQELVIAGRLGRKSGLGVYDYREEAEAVVPLEAVSDSFSPrvtvvgdigaaaplla 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 305 ------MKVEKKSD-GVTEIDDVLLIETQGETAQALAIRLARP-----VVVIDKMAGKVVTIAAAAVNPDSATRKAIYYL 372
Cdd:TIGR02279 321 rleaagIKVEKKSGmGVTQIGDALLALTDGRTAQARAIELARPnlvlfDLVLDYSTGKRIAIAAAAVNPDSATRKAIYYL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 373 QQQGKTVLQIADYPGMLIWRTVAMIINEALDALQKGVASEQDIDTAMRLGVNYPYGPLAWGAQLGWQRILRLLENLQHHY 452
Cdd:TIGR02279 401 QQAGKKVLQIADYPGLLILRTVAMLANEAADAVLQGVASAQDIDTAMRLGVNYPYGPLAWAAQLGWQRILRVLENLQHHY 480
|
490 500
....*....|....*....|...
gi 519083257 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: 728.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 1 MMINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIH 80
Cdd:PRK08268 3 ALPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAALARLRPVEALA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 81 ALAAANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLA 160
Cdd:PRK08268 83 DLADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSGLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 161 TAAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQD 240
Cdd:PRK08268 163 TDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLIGLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 241 VNFAVTCSVFNAFWQERRFLPSLVQQELVIGGRLGKKSGLGVYDWRAEREAVVGLEAVSDSFSPMKV------------- 307
Cdd:PRK08268 243 VNHAVMESVYRQFYQEPRFRPSLIQQELVAAGRLGRKSGQGFYRYADGAKQPPAEAAPPAALPPVWVsadvegdlaalar 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 308 --------EKKSDGVTEIDDVLLIETQGETAQALAIRL--ARPVVVIDKMAG----KVVTIAAAAVNPDSATRKAIYYLQ 373
Cdd:PRK08268 323 llerlgatIETGEGPSADGLVLLAPTGGDTTTAAAREGldAARVVLIDLLLDyaaaKRRTLMAAPATSPAARDAAHALFQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 374 QQGKTVLQIADYPGMLIWRTVAMIINEALDALQKGVASEQDIDTAMRLGVNYPYGPLAWGAQLGWQRILRLLENLQHHYG 453
Cdd:PRK08268 403 QDGKAVSVIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWGDRLGAARILRVLENLQALYG 482
|
490 500
....*....|....*....|..
gi 519083257 454 EERYRPCSLLRQRALLESGYES 475
Cdd:PRK08268 483 DPRYRPSPWLRRRAALGLSLRS 504
|
|
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
4-285 |
2.56e-138 |
|
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: 398.71 E-value: 2.56e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 4 NVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHALA 83
Cdd:COG1250 1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARITPTTDLAALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 84 AANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAA 163
Cdd:COG1250 81 DADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 164 EVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVNF 243
Cdd:COG1250 161 ETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLVGLDTAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 519083257 244 AVTCSVFNAFwQERRFLPSLVQQELVIGGRLGKKSGLGVYDW 285
Cdd:COG1250 241 AVLEVLYEAL-GDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
|
|
| PRK05808 |
PRK05808 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
3-285 |
2.59e-98 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 180269 [Multi-domain] Cd Length: 282 Bit Score: 296.87 E-value: 2.59e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 3 INVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHAL 82
Cdd:PRK05808 1 MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARITGTTDLDDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 83 AAANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATA 162
Cdd:PRK05808 81 KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 163 AEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVN 242
Cdd:PRK05808 161 DATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIGLDTC 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 519083257 243 FAVTCSVFNAFwQERRFLPSLVQQELVIGGRLGKKSGLGVYDW 285
Cdd:PRK05808 241 LAIMEVLYEGF-GDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
|
|
| PLN02545 |
PLN02545 |
3-hydroxybutyryl-CoA dehydrogenase |
2-292 |
3.90e-94 |
|
3-hydroxybutyryl-CoA dehydrogenase
Pssm-ID: 215300 [Multi-domain] Cd Length: 295 Bit Score: 286.63 E-value: 3.90e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 2 MINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHA 81
Cdd:PLN02545 1 MAEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATLGRIRCTTNLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 82 LAAANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLAT 161
Cdd:PLN02545 81 LRDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 162 AAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDV 241
Cdd:PLN02545 161 SDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIGLDT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 519083257 242 NFAVTcSVFNAFWQERRFLPSLVQQELVIGGRLGKKSGLGVYDWRAEREAV 292
Cdd:PLN02545 241 CLSIM-KVLHEGLGDSKYRPCPLLVQYVDAGRLGRKSGRGVYHYDGKKRGD 290
|
|
| PRK07530 |
PRK07530 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
2-288 |
4.29e-93 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181018 [Multi-domain] Cd Length: 292 Bit Score: 283.82 E-value: 4.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 2 MINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHA 81
Cdd:PRK07530 1 MMAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARQVAKGKISEEARAAALARISTATDLED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 82 LAAANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLAT 161
Cdd:PRK07530 81 LADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIRGIAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 162 AAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDv 241
Cdd:PRK07530 161 DEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIYTLYEGVGSVEAIDTAMKLGANHPMGPLELADFIGLD- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 519083257 242 nfavTC-SVFNAFWQ-----ERRFLPSLVQqeLVIGGRLGKKSGLGVYDWRAE 288
Cdd:PRK07530 240 ----TClSIMQVLHDgladsKYRPCPLLVK--YVEAGWLGRKTGRGFYDYRGE 286
|
|
| PRK07819 |
PRK07819 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
1-285 |
3.04e-83 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181133 [Multi-domain] Cd Length: 286 Bit Score: 258.38 E-value: 3.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 1 MMINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIH 80
Cdd:PRK07819 1 MSDAIQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERAVSRGKLTERERDAALARLRFTTDLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 81 ALAAANLVIEAASERLEVKKALFEQLAEVCP-PQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGL 159
Cdd:PRK07819 81 DFADRQLVIEAVVEDEAVKTEIFAELDKVVTdPDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 160 ATAAEVV---EQLCELTLswGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDL 236
Cdd:PRK07819 161 VTSEATVaraEEFASDVL--GKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 519083257 237 IGQDVNFAVTCSVFNAFWQERRFLPSLVQQeLVIGGRLGKKSGLGVYDW 285
Cdd:PRK07819 239 VGLDTVKAIADSMYEEFKEPLYAPPPLLLR-MVEAGLLGKKSGRGFYTY 286
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
7-186 |
1.01e-82 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 253.23 E-value: 1.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 7 TVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHALAAAN 86
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARISFTTDLAAAVDAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 87 LVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAAEVV 166
Cdd:pfam02737 81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160
|
170 180
....*....|....*....|
gi 519083257 167 EQLCELTLSWGKQPVRCHST 186
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVKDT 180
|
|
| PRK09260 |
PRK09260 |
3-hydroxyacyl-CoA dehydrogenase; |
5-288 |
2.08e-77 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 236434 [Multi-domain] Cd Length: 288 Bit Score: 243.54 E-value: 2.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 5 VQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHALAA 84
Cdd:PRK09260 1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGKLTEAARQAALARLSYSLDLKAAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 85 -ANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAA 163
Cdd:PRK09260 81 dADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLETSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 164 EVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVNF 243
Cdd:PRK09260 161 ETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLVGLDTRL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 519083257 244 AVTCSVFNAFWQERRFLPSLVQqeLVIGGRLGKKSGLGVYDWRAE 288
Cdd:PRK09260 241 NNLKYLHETLGEKYRPAPLLEK--YVKAGRLGRKTGRGVYDYTNR 283
|
|
| PRK06130 |
PRK06130 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
2-296 |
1.42e-64 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 235707 [Multi-domain] Cd Length: 311 Bit Score: 211.17 E-value: 1.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 2 MINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNsrVTRGKLTAETCERTLKRLIPVTDihA 81
Cdd:PRK06130 1 MNPIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALG--VYAPLGIASAGMGRIRMEAGLAA--A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 82 LAAANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLAT 161
Cdd:PRK06130 77 VSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 162 AAEVVEQLCELTLSWGKQPVRCH-STPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPM---GPLELTDLI 237
Cdd:PRK06130 157 SPQTVATTMALLRSIGKRPVLVKkDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQRDMN 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 519083257 238 GQDVNFAVTCSVFNAFwqERRFLPSLVQQELVIGGRLGKKSGLGVYDWRAEREAVVGLE 296
Cdd:PRK06130 237 GLDVHLAVASYLYQDL--ENRTTPSPLLEEKVEAGELGAKSGQGFYAWPPERREEVLAD 293
|
|
| PRK06035 |
PRK06035 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
4-277 |
1.51e-58 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 180361 [Multi-domain] Cd Length: 291 Bit Score: 194.71 E-value: 1.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 4 NVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHAR---LNSRVTRGKLTAETCERTLKRLIPVTDIH 80
Cdd:PRK06035 2 DIKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKGKMSEDEAKAIMARIRTSTSYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 81 ALAAANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLA 160
Cdd:PRK06035 82 SLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVRAAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 161 TAAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQD 240
Cdd:PRK06035 162 TSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELMDIIGID 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 519083257 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 |
3.40e-53 |
|
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: 190.82 E-value: 3.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 5 VQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHALAA 84
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLDYSGFKN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 85 ANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAAE 164
Cdd:TIGR02441 415 ADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDGTSKD 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 165 VVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVaAPEVIDaALRDGAGFPMGPLELTDLIGQDVNFA 244
Cdd:TIGR02441 495 TLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGV-DPKKLD-KLTTKFGFPVGAATLADEVGVDVAEH 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 245 VTCSVFNAFwQERRFLPSL-VQQELVIGGRLGKKSGLGVYDWraeREAVVGLEAVsdsfspmkvekkSDGVTEIddvlli 323
Cdd:TIGR02441 573 VAEDLGKAF-GERFGGGSAeLLSELVKAGFLGRKSGKGIFIY---QEGKKGSKKV------------NSDADEI------ 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 324 etqgetaqalairlarpvvvidkMAGKVVTIAAAAVNPDSatrkaiyylqqqgktvLQIadypgmliwRTVAMIINEALD 403
Cdd:TIGR02441 631 -----------------------LAQYKLPPKAEVSSPED----------------IQI---------RLVSRFVNEAVL 662
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 519083257 404 ALQKGV-ASEQDIDTAMRLGVNYPY---GPLAWGAQLGWQRILRLLENLQHHYGEErYRPCSLLRQRA 467
Cdd:TIGR02441 663 CLEEGIlASPSEGDIGAVFGLGFPPflgGPFRFVDLYGADKLVDKMEKYAAAYGVQ-FTPCQLLLDHA 729
|
|
| fadJ |
PRK11154 |
fatty acid oxidation complex subunit alpha FadJ; |
5-467 |
1.60e-50 |
|
fatty acid oxidation complex subunit alpha FadJ;
Pssm-ID: 236864 [Multi-domain] Cd Length: 708 Bit Score: 182.79 E-value: 1.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 5 VQTVAVIGSGTMGAGIAEV-AASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHALA 83
Cdd:PRK11154 309 VNKVGVLGGGLMGGGIAYVtATKAGLPVRIKDINPQGINHALKYSWDLLDKKVKRRHLKPSERDKQMALISGTTDYRGFK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 84 AANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAA 163
Cdd:PRK11154 389 HADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVIPHAKTSA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 164 EVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAApEVIDAALRDgAGFPMGPLELTDLIGQDVNF 243
Cdd:PRK11154 469 ETIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLEGEPI-EHIDAALVK-FGFPVGPITLLDEVGIDVGT 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 244 AVTCSVFNAFWQerRFLPSLVQQELVIGGRLGKKSGLGVYDWRAEREavvgleavsdsfspmKVEKKSDgvTEIDDVLLI 323
Cdd:PRK11154 547 KIIPILEAALGE--RFSAPAAFDKLLNDDRKGRKNGRGFYLYGQKGK---------------KSKKQVD--ESVYPLLGI 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 324 ETQGETAQAlairlarpvvvidkmagkvvtiaaaavnpdsatrkaiyylqqqgktvlQIADypgmliwRTVAMIINEALD 403
Cdd:PRK11154 608 TPQSRLSAN------------------------------------------------EIAE-------RCVMLMLNEAVR 632
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 519083257 404 ALQKGV-ASEQDIDTAMRLGVNYPY---GPLAWGAQLGWQRILRLLENLQHHYGeERYRPCSLLRQRA 467
Cdd:PRK11154 633 CLDEGIiRSARDGDIGAVFGIGFPPflgGPFRYMDSLGAGEVVAILERLAAQYG-DRFTPCERLVEMA 699
|
|
| PRK08293 |
PRK08293 |
3-hydroxyacyl-CoA dehydrogenase; |
4-286 |
1.16e-48 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 181359 [Multi-domain] Cd Length: 287 Bit Score: 168.58 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 4 NVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAE-TCERTLKRLIPVTDIHAL 82
Cdd:PRK08293 2 DIKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATKEaPAEAALNRITLTTDLAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 83 AA-ANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLAT 161
Cdd:PRK08293 82 VKdADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 162 AAEVVEQLCELTLSWGKQPVRCH-STPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQD 240
Cdd:PRK08293 162 DPEVFDTVVAFAKAIGMVPIVLKkEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIVGLD 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 519083257 241 vnfavTCSVFNAFWQERRFLPSLVQ-----QELVIGGRLGKKSGLGVYDWR 286
Cdd:PRK08293 242 -----TAYNITSNWAEATDDENAKKaaallKEYIDKGKLGVATGEGFYNYP 287
|
|
| fadB |
PRK11730 |
fatty acid oxidation complex subunit alpha FadB; |
5-467 |
3.27e-48 |
|
fatty acid oxidation complex subunit alpha FadB;
Pssm-ID: 183293 [Multi-domain] Cd Length: 715 Bit Score: 176.59 E-value: 3.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 5 VQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHALAA 84
Cdd:PRK11730 313 VKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDLGMTEAAKLLNKQVERGKIDGAKMAGVLSSIRPTLDYAGFER 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 85 ANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAAE 164
Cdd:PRK11730 393 VDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKTSDE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 165 VVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSeAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVnfA 244
Cdd:PRK11730 473 TIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFA-GFSQLLRDGADFRQIDKVMEKQFGWPMGPAYLLDVVGIDT--A 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 245 VTC-SVFNAFWQER--RFLPSLVQQeLVIGGRLGKKSGLGVYDWRAEREAvvgleavsdsfSPMKVekksdgVTEIDDVL 321
Cdd:PRK11730 550 HHAqAVMAEGFPDRmkKDYRDAIDV-LFEAKRFGQKNGKGFYRYEEDKKG-----------KPKKE------VDPAVYEL 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 322 LIETQGETaqalaiRLARPVVVIDKMagkvvtiaaaavnpdsatrkaiyylqqqgktvlqiadypgmliwrtvaMI--IN 399
Cdd:PRK11730 612 LAPVVQPK------REFSDEEIIARM------------------------------------------------MIpmIN 637
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519083257 400 EALDALQKG-VASEQDIDTAMRLGVNYPY---GPLAWGAQLGWQRILRLLENLQHHyGeERYRPCSLLRQRA 467
Cdd:PRK11730 638 EVVRCLEEGiVASPAEADMALVYGLGFPPfrgGAFRYLDTLGVANYVALADKYAHL-G-PLYQVPEGLREMA 707
|
|
| PRK08269 |
PRK08269 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
16-287 |
5.23e-45 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181340 [Multi-domain] Cd Length: 314 Bit Score: 159.84 E-value: 5.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 16 MGAGIAEVAASHGHQVLLYDI---SAEA----LTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTD---IHALAAA 85
Cdd:PRK08269 1 MGQGIALAFAFAGHDVTLIDFkprDAAGwralDAEARAEIERTLAALVALGRIDAAQADAVLARIAVVARdgaADALADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 86 NLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAAEV 165
Cdd:PRK08269 81 DLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATDPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 166 VEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFP---MGPLELTDLIGQDVN 242
Cdd:PRK08269 161 VDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRfavLGLLEFIDWGGCDIL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 519083257 243 FAVTCSVFNAFWQErRFLPSLVQQELVIGGRLGKKSGLGVYDWRA 287
Cdd:PRK08269 241 YYASRYLAGEIGPD-RFAPPAIVVRNMEEGRDGLRTGAGFYDYAG 284
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
8-236 |
1.50e-40 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 147.50 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 8 VAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDI-HALAAAN 86
Cdd:PRK06129 5 VAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEAPDAVLARIRVTDSLaDAVADAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 87 LVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLATAAEVV 166
Cdd:PRK06129 85 YVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTAPATL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 519083257 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 |
1.67e-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: 129.64 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 188 GFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVNFAVTCsVFNAFWQERRFLPSLVQQE 267
Cdd:pfam00725 1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILE-VLAEEFGDRAYRPPPLLEK 79
|
90
....*....|....*...
gi 519083257 268 LVIGGRLGKKSGLGVYDW 285
Cdd:pfam00725 80 LVEAGRLGRKTGKGFYKY 97
|
|
| PRK07066 |
PRK07066 |
L-carnitine dehydrogenase; |
4-225 |
1.29e-24 |
|
L-carnitine dehydrogenase;
Pssm-ID: 168796 [Multi-domain] Cd Length: 321 Bit Score: 103.76 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 4 NVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISaealtraiDGIHARLNSRVT-------RGKLTAETcerTLKRLIPV 76
Cdd:PRK07066 6 DIKTFAAIGSGVIGSGWVARALAHGLDVVAWDPA--------PGAEAALRANVAnawpaleRQGLAPGA---SPARLRFV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 77 TDIHA-LAAANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEV 155
Cdd:PRK07066 75 ATIEAcVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519083257 156 VSGLATAAEVVEQLCELTLSWGKQPVRCH-STPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAG 225
Cdd:PRK07066 155 LGGERTAPEAVDAAMGIYRALGMRPLHVRkEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAG 225
|
|
| PRK07531 |
PRK07531 |
carnitine 3-dehydrogenase; |
2-225 |
3.47e-18 |
|
carnitine 3-dehydrogenase;
Pssm-ID: 236044 [Multi-domain] Cd Length: 495 Bit Score: 87.10 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 2 MINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEAlTRAIDGIHArlNSRVTRGKLTAETCERTLKRLIPVTDIHA 81
Cdd:PRK07531 1 MTMIMKAACIGGGVIGGGWAARFLLAGIDVAVFDPHPEA-ERIIGEVLA--NAERAYAMLTDAPLPPEGRLTFCASLAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 82 LAAANLVIEAASERLEVKKALFEQLAEVCPPQTLLTTNTSSISITAIAAEVKNPERVAGLHFFNPAPVMKLVEVVSGLAT 161
Cdd:PRK07531 78 VAGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVELVGGGKT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519083257 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 |
7.47e-16 |
|
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: 73.02 E-value: 7.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 392 RTVAMIINEALDALQKGVASEQDIDTAMRLGVNYPYGPLAWGAQLGWQRILRLLENLQHHYGEERYRPCSLLRQraLLES 471
Cdd:pfam00725 6 RLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAEEFGDRAYRPPPLLEK--LVEA 83
|
..
gi 519083257 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 |
8.23e-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: 8.23e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519083257 325 TQGETAQALAIRLARPVVVIDKM----AGKVVTIAAAAVNPDSATRKAIYYLQQQGKTVLQIADYP 386
Cdd:pfam18321 4 TDGRTATQRAAELGRPVVLFDLAldydSATRLAVAPAAQCSPQALAQAVALLQALGKAVLVLADAP 69
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
7-149 |
1.42e-04 |
|
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: 42.07 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 7 TVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAID-GIharlnsrvtRGKLTAETCERTLKRLIpvTDIHALAAA 85
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAaGA---------IAAASPAEFVAGLDVVI--TMVPAGAAV 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519083257 86 NLVIEAaserlevkkalfEQLAEVCPPQTLL--TTNTSSISITAIAAEVKNpervAGLHFFNpAPV 149
Cdd:pfam03446 70 DAVIFG------------EGLLPGLKPGDIIidGSTSSPEDARRRAKELKE----KGLHFLD-APV 118
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
7-72 |
5.57e-04 |
|
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: 40.18 E-value: 5.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519083257 7 TVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRaidgIHARLNSRVTRGKLTAETCERTLKR 72
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQ----LESLLGARFTTLYSQAELLEEAVKE 83
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
6-116 |
1.03e-03 |
|
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: 41.18 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 6 QTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEaltrAIDGIHA-RLNSRVTRG-KLTaetcertlKRLIPVTDI-HAL 82
Cdd:COG0240 1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPE----VAEEINEtRENPRYLPGvKLP--------ENLRATSDLeEAL 68
|
90 100 110
....*....|....*....|....*....|....*
gi 519083257 83 AAANLVIEA-ASERLevkKALFEQLAEVCPPQTLL 116
Cdd:COG0240 69 AGADLVLLAvPSQAL---REVLEQLAPLLPPGAPV 100
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
7-46 |
1.33e-03 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 40.48 E-value: 1.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 519083257 7 TVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAID 46
Cdd:COG2084 3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVA 42
|
|
| YqeC |
COG1023 |
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; |
8-50 |
1.97e-03 |
|
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
Pssm-ID: 440646 [Multi-domain] Cd Length: 300 Bit Score: 40.07 E-value: 1.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 519083257 8 VAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTR-AIDGIHA 50
Cdd:COG1023 3 IGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAAlAAEGATG 46
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
7-89 |
2.19e-03 |
|
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: 40.29 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 7 TVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEaltrAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIH-ALAAA 85
Cdd:TIGR03026 2 KIAVIGLGYVGLPLAALLADLGHDVTGVDIDQE----KVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEeAIRDA 77
|
....
gi 519083257 86 NLVI 89
Cdd:TIGR03026 78 DVII 81
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
8-33 |
4.20e-03 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 38.61 E-value: 4.20e-03
10 20
....*....|....*....|....*.
gi 519083257 8 VAVIGSGTMGAGIAEVAASHGHQVLL 33
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAGHEVVI 26
|
|
| ApbA |
pfam02558 |
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ... |
8-114 |
6.89e-03 |
|
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: 37.21 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083257 8 VAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHarlnsrvtrgkLTAETCERTLKRLIPVTDIHALAAANL 87
Cdd:pfam02558 1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELAAIKKNGLR-----------LTSPGGERIVPPPAVTSASESLGPIDL 69
|
90 100 110
....*....|....*....|....*....|.
gi 519083257 88 VIeaaserLEVK----KALFEQLAEVCPPQT 114
Cdd:pfam02558 70 VI------VTVKayqtEEALEDIAPLLGPNT 94
|
|
| YdfG |
COG4221 |
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ... |
2-52 |
7.01e-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: 7.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 519083257 2 MINVQTVAVI--GSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARL 52
Cdd:COG4221 1 MSDKGKVALItgASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRA 53
|
|
| PRK11036 |
PRK11036 |
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM; |
12-51 |
9.25e-03 |
|
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
Pssm-ID: 182918 Cd Length: 255 Bit Score: 38.02 E-value: 9.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 519083257 12 GSGTMGAGIAEVaashGHQVLLYDISAEALTRAIDGIHAR 51
Cdd:PRK11036 54 GEGQTAIKLAEL----GHQVILCDLSAEMIQRAKQAAEAK 89
|
|
| |
