|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-415 |
1.62e-167 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 476.21 E-value: 1.62e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIETADEKT 81
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 82 NETTEEIQAKVDEHTQ-KSTKKASATVEQTFTAKQNQPRNNGRFSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVI 160
Cdd:PRK11856 84 AAAAAEAAPEAPAPEPaPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 161 ENGGTTAQSdkqvqtkSTSVDTSSNQSSEDNSEnsTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTRNHYKN 240
Cdd:PRK11856 164 AAAAPAAAA-------AAAAAAAPPAAAAEGEE--RVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 241 sfknkEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVPVIKHADEKSIKGIAREINTL 320
Cdd:PRK11856 235 -----IGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 321 ATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVINDMIAIRSMVNLCISIDHRILDGL 400
Cdd:PRK11856 310 AEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGA 389
|
410
....*....|....*
gi 446328983 401 QTGKFMNHIKQRIEQ 415
Cdd:PRK11856 390 DAARFLKALKELLEN 404
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
2-419 |
1.09e-101 |
|
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).
Pssm-ID: 200219 [Multi-domain] Cd Length: 579 Bit Score: 313.87 E-value: 1.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKI------- 74
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgdanaap 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 75 ------------ETADEKTNETTEEIQAKVDEHTQKStKKASATVEQTFTAKQNQPRNNGRFSPVVFKLASEHDIDLSQV 142
Cdd:TIGR02927 208 aepaeeeapapsEAGSEPAPDPAARAPHAAPDPPAPA-PAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLSTV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 143 VGSGFEGRVTKKDIMSVIENGGTTAQSD-KQVQTKSTSVDTSSNQSSEDNS---ENSTIPVNGVRKAIAQNMVNSVTEIP 218
Cdd:TIGR02927 287 KGTGVGGRIRKQDVLAAAKAAEEARAAAaAPAAAAAPAAPAAAAKPAEPDTaklRGTTQKMNRIRQITADKTIESLQTSA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 219 HAWMMIEVDATNLVNTRNHYKNSFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSW--QGNEIVLHKDINISIAVADENK 296
Cdd:TIGR02927 367 QLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDTPRG 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 297 LYVPVIKHADEKSIKGIAREINTLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVI 376
Cdd:TIGR02927 447 LLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVI 526
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446328983 377 -----NDMIAIRSMVNLCISIDHRILDGLQTGKFMNHIKQRIEQYTLE 419
Cdd:TIGR02927 527 kdedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDFE 574
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
210-418 |
7.41e-96 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 286.36 E-value: 7.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 210 MVNSVTEIPHAWMMIEVDATNLVNTRNHYKNSFKnKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGN--EIVLHKDINI 287
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAA-DEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 288 SIAVADENKLYVPVIKHADEKSIKGIAREINTLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVE 367
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446328983 368 SIVKKPVVINDMIAIRSMVNLCISIDHRILDGLQTGKFMNHIKQRIEQYTL 418
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPEL 210
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1-74 |
8.58e-29 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 107.49 E-value: 8.58e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446328983 1 MEITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKI 74
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
2-74 |
1.00e-28 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 107.46 E-value: 1.00e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKI 74
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-415 |
1.62e-167 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 476.21 E-value: 1.62e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIETADEKT 81
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 82 NETTEEIQAKVDEHTQ-KSTKKASATVEQTFTAKQNQPRNNGRFSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVI 160
Cdd:PRK11856 84 AAAAAEAAPEAPAPEPaPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 161 ENGGTTAQSdkqvqtkSTSVDTSSNQSSEDNSEnsTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTRNHYKN 240
Cdd:PRK11856 164 AAAAPAAAA-------AAAAAAAPPAAAAEGEE--RVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 241 sfknkEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVPVIKHADEKSIKGIAREINTL 320
Cdd:PRK11856 235 -----IGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 321 ATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVINDMIAIRSMVNLCISIDHRILDGL 400
Cdd:PRK11856 310 AEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGA 389
|
410
....*....|....*
gi 446328983 401 QTGKFMNHIKQRIEQ 415
Cdd:PRK11856 390 DAARFLKALKELLEN 404
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-415 |
5.59e-118 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 354.51 E-value: 5.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGEsVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIET---AD 78
Cdd:PRK11855 121 EVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVaaaAP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 79 EKTNETTEEIQAKVDEHTQKSTKKASATVEQTFTAKQNQPRNNGRFSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMS 158
Cdd:PRK11855 200 AAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 159 VIENGGTTAQSDKQVQTKSTS----------VDTSSNQSSEdnsensTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDA 228
Cdd:PRK11855 280 FVKGAMSAAAAAAAAAAAAGGgglgllpwpkVDFSKFGEIE------TKPLSRIKKISAANLHRSWVTIPHVTQFDEADI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 229 TNLVNTRNHYKNSFKnKEGYNLTFFAFFVKAVADALKAYPLLNSS--WQGNEIVLHKDINISIAVADENKLYVPVIKHAD 306
Cdd:PRK11855 354 TDLEALRKQLKKEAE-KAGVKLTMLPFFIKAVVAALKEFPVFNASldEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVD 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 307 EKSIKGIAREINTLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVINDMIAIRSMV 386
Cdd:PRK11855 433 KKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLML 512
|
410 420
....*....|....*....|....*....
gi 446328983 387 NLCISIDHRILDGLQTGKFMNHIKQRIEQ 415
Cdd:PRK11855 513 PLSLSYDHRVIDGATAARFTNYLKQLLAD 541
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
2-415 |
1.73e-112 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 336.04 E-value: 1.73e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIETADEKT 81
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 82 NETTEEIQAKVDEHTQKSTKKASATVEQTFTAkqnqprnngrfSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVIe 161
Cdd:PRK05704 84 AAAAAAAAAAAAAAAPAQAQAAAAAEQSNDAL-----------SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAAL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 162 nggttAQSDKQVQTKSTSVDTSSNQSSEDNSEnSTIPVNGVRKAIAQNMVNSVTEiphAWMMI---EVDATNLVNTRNHY 238
Cdd:PRK05704 152 -----AAAAAAPAAPAAAAPAAAPAPLGARPE-ERVPMTRLRKTIAERLLEAQNT---TAMLTtfnEVDMTPVMDLRKQY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 239 KNSFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVPVIKHADEKSIKGIAREIN 318
Cdd:PRK05704 223 KDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 319 TLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVINDMIAIRSMVNLCISIDHRILD 398
Cdd:PRK05704 303 ELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIID 382
|
410
....*....|....*..
gi 446328983 399 GLQTGKFMNHIKQRIEQ 415
Cdd:PRK05704 383 GKEAVGFLVTIKELLED 399
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
2-419 |
1.09e-101 |
|
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).
Pssm-ID: 200219 [Multi-domain] Cd Length: 579 Bit Score: 313.87 E-value: 1.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKI------- 74
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgdanaap 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 75 ------------ETADEKTNETTEEIQAKVDEHTQKStKKASATVEQTFTAKQNQPRNNGRFSPVVFKLASEHDIDLSQV 142
Cdd:TIGR02927 208 aepaeeeapapsEAGSEPAPDPAARAPHAAPDPPAPA-PAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLSTV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 143 VGSGFEGRVTKKDIMSVIENGGTTAQSD-KQVQTKSTSVDTSSNQSSEDNS---ENSTIPVNGVRKAIAQNMVNSVTEIP 218
Cdd:TIGR02927 287 KGTGVGGRIRKQDVLAAAKAAEEARAAAaAPAAAAAPAAPAAAAKPAEPDTaklRGTTQKMNRIRQITADKTIESLQTSA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 219 HAWMMIEVDATNLVNTRNHYKNSFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSW--QGNEIVLHKDINISIAVADENK 296
Cdd:TIGR02927 367 QLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDTPRG 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 297 LYVPVIKHADEKSIKGIAREINTLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVI 376
Cdd:TIGR02927 447 LLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVI 526
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446328983 377 -----NDMIAIRSMVNLCISIDHRILDGLQTGKFMNHIKQRIEQYTLE 419
Cdd:TIGR02927 527 kdedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDFE 574
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-414 |
1.76e-101 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 315.02 E-value: 1.76e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGesVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIETADEKT 81
Cdd:PRK11854 208 DVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 82 NETTEEIQAKVDEHTQKSTKKASATVEQTFTAKQNQPRNNG--RFSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSV 159
Cdd:PRK11854 286 AAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAyvHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAY 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 160 IENGGTTAQSDKQVQTKSTSVDTSSNQSSEDNS---ENSTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTRN 236
Cdd:PRK11854 366 VKDAVKRAEAAPAAAAAGGGGPGLLPWPKVDFSkfgEIEEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 237 HY-KNSFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSW--QGNEIVLHKDINISIAVADENKLYVPVIKHADEKSIKGI 313
Cdd:PRK11854 446 QQnAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 314 AREINTLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVINDMIAIRSMVNLCISID 393
Cdd:PRK11854 526 SRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYD 605
|
410 420
....*....|....*....|.
gi 446328983 394 HRILDGLQTGKFMNHIKQRIE 414
Cdd:PRK11854 606 HRVIDGADGARFITIINDRLS 626
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
2-414 |
4.76e-101 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 306.66 E-value: 4.76e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIETADEKT 81
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 82 NETTEEIQAKVDEHTQKSTKKASATVEQTFTAkqnqprnngrfSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVIE 161
Cdd:TIGR01347 82 AAPPAKSGEEKEETPAASAAAAPTAAANRPSL-----------SPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 162 NGGTTAQSdkqvqtkstSVDTSSNQSSEDNSENSTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTRNHYKNS 241
Cdd:TIGR01347 151 APASAQPP---------AAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 242 FKNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVPVIKHADEKSIKGIAREINTLA 321
Cdd:TIGR01347 222 FEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 322 TKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVINDMIAIRSMVNLCISIDHRILDGLQ 401
Cdd:TIGR01347 302 KKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKE 381
|
410
....*....|...
gi 446328983 402 TGKFMNHIKQRIE 414
Cdd:TIGR01347 382 AVTFLVTIKELLE 394
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
210-418 |
7.41e-96 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 286.36 E-value: 7.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 210 MVNSVTEIPHAWMMIEVDATNLVNTRNHYKNSFKnKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGN--EIVLHKDINI 287
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAA-DEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 288 SIAVADENKLYVPVIKHADEKSIKGIAREINTLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVE 367
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446328983 368 SIVKKPVVINDMIAIRSMVNLCISIDHRILDGLQTGKFMNHIKQRIEQYTL 418
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPEL 210
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
3-414 |
1.17e-84 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 265.01 E-value: 1.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 3 ITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIETADEKTN 82
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 83 ETTEEIQAKVDEHTQKSTKKASATVEQTFTAKQNQPrnngrfspvvfklasehdidlsqvvgsgfegrvtkkdimsvien 162
Cdd:PTZ00144 127 AAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTP-------------------------------------------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 163 ggttAQSDKQVQTKSTSVDTSSNQSSEDNSENStIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTRNHYKNSF 242
Cdd:PTZ00144 163 ----PAAAKPPEPAPAAKPPPTPVARADPRETR-VPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 243 KNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVPVIKHADEKSIKGIAREINTLAT 322
Cdd:PTZ00144 238 QKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 323 KARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVINDMIAIRSMVNLCISIDHRILDGLQT 402
Cdd:PTZ00144 318 KARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDA 397
|
410
....*....|..
gi 446328983 403 GKFMNHIKQRIE 414
Cdd:PTZ00144 398 VTFLKKIKDLIE 409
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-414 |
1.85e-84 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 265.12 E-value: 1.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAG-QTVAIDTIICKIET---- 76
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEeked 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 77 -ADEKTNETTEEIQAKVDEHTQKS-------TKKASATVEQTFTAKQNQPRN----NGRF--SPVVFKLASEHDIDLSQV 142
Cdd:TIGR01349 81 vADAFKNYKLESSASPAPKPSEIAptappsaPKPSPAPQKQSPEPSSPAPLSdkesGDRIfaSPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 143 VGSGFEGRVTKKDIMSVIENGGTTAQSdkqvQTKSTSVDTSSNQSSEDNSENSTIPVNGVRKAIAQNMVNSVTEIPHAWM 222
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPASANQ----QAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 223 MIEVDATNLVNTRNHYKNSfkNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVPVI 302
Cdd:TIGR01349 237 SIECNVDKLLALRKELNAM--ASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 303 KHADEKSIKGIAREINTLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVIND---M 379
Cdd:TIGR01349 315 RNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDeekG 394
|
410 420 430
....*....|....*....|....*....|....*
gi 446328983 380 IAIRSMVNLCISIDHRILDGLQTGKFMNHIKQRIE 414
Cdd:TIGR01349 395 FAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLE 429
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-414 |
1.15e-70 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 232.46 E-value: 1.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGeSVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIETAD--- 78
Cdd:TIGR01348 118 EVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGstp 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 79 --EKTNETTEEiQAKVDEHTQKSTKKASATVEQTFTAKQNQPRNNGRF----SPVVFKLASEHDIDLSQVVGSGFEGRVT 152
Cdd:TIGR01348 197 atAPAPASAQP-AAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAKvdhaAPAVRRLAREFGVDLSAVKGTGIKGRIL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 153 KKDIMSVIengGTTAQsdkqvQTKSTSVDTSS---------NQSSEDNSENSTIPVNGVRKAIAQNMVNSVTEIPHAWMM 223
Cdd:TIGR01348 276 REDVQRFV---KEPSV-----RAQAAAASAAGgapgalpwpNVDFSKFGEVEEVDMSRIRKISGANLTRNWTMIPHVTHF 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 224 IEVDATNLVNTRNHYkNSFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQ--GNEIVLHKDINISIAVADENKLYVPV 301
Cdd:TIGR01348 348 DKADITEMEAFRKQQ-NAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPV 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 302 IKHADEKSIKGIAREINTLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVINDMIA 381
Cdd:TIGR01348 427 IKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFE 506
|
410 420 430
....*....|....*....|....*....|...
gi 446328983 382 IRSMVNLCISIDHRILDGLQTGKFMNHIKQRIE 414
Cdd:TIGR01348 507 PRLMLPLSLSYDHRVIDGADAARFTTYICESLA 539
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
1-414 |
3.13e-69 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 228.20 E-value: 3.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 1 MEITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEIL-------VEAGQTVAIdTI--- 70
Cdd:PLN02744 113 QEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVkgdgakeIKVGEVIAI-TVeee 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 71 --ICKIE----------TADEKTNETTEEIQAKVDEHTQKSTKKASATVEQtftakqnqPRNNGRF--SPVVFKLASEHD 136
Cdd:PLN02744 192 edIGKFKdykpsssaapAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAP--------PSSGDRIfaSPLARKLAEDNN 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 137 IDLSQVVGSGFEGRVTKKDIMSVIENGGTTAQSDKQVQTKSTSVDTSSnqssednsenstIPVNGVRKAIAQNMVNSVTE 216
Cdd:PLN02744 264 VPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPALDYTD------------IPNTQIRKVTASRLLQSKQT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 217 IPHAWMMIEVDATNLVNTRNHYkNSFKNKEG-YNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADEN 295
Cdd:PLN02744 332 IPHYYLTVDTRVDKLMALRSQL-NSLQEASGgKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTEN 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 296 KLYVPVIKHADEKSIKGIAREINTLATKARNKQLTTEDMQGGTFTVNNT-GTFGSVSSMGIINHPQAAILQVESIVKK-- 372
Cdd:PLN02744 411 GLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRvi 490
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446328983 373 PVVINDMIAIRSMVNLCISIDHRILDGLQTGKFMNHIKQRIE 414
Cdd:PLN02744 491 PGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIE 532
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
9-415 |
3.06e-67 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 219.59 E-value: 3.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 9 GESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIETADEKTNETTEEI 88
Cdd:PLN02528 7 GEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDSLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 89 QAKVDEHTQKS-TKKASATVEQTFTAkqnqprnngrfSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMS-VIENGGTT 166
Cdd:PLN02528 87 LPTDSSNIVSLaESDERGSNLSGVLS-----------TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKyAAQKGVVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 167 AQSDKQVQTKSTSVDTSSNQSSEDNS--ENSTIPVNGVRKAIAQNMVNSvTEIPHAWMMIEVDATNLVNTRNHYKNSfkN 244
Cdd:PLN02528 156 DSSSAEEATIAEQEEFSTSVSTPTEQsyEDKTIPLRGFQRAMVKTMTAA-AKVPHFHYVEEINVDALVELKASFQEN--N 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 245 KE-GYNLTFFAFFVKAVADALKAYPLLNSSWQG--NEIVLHKDINISIAVADENKLYVPVIKHADEKSIKGIAREINTLA 321
Cdd:PLN02528 233 TDpTVKHTFLPFLIKSLSMALSKYPLLNSCFNEetSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 322 TKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKP-VVINDMIAIRSMVNLCISIDHRILDGL 400
Cdd:PLN02528 313 HLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPrFVDDGNVYPASIMTVTIGADHRVLDGA 392
|
410
....*....|....*
gi 446328983 401 QTGKFMNHIKQRIEQ 415
Cdd:PLN02528 393 TVARFCNEWKSYVEK 407
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
125-415 |
1.53e-59 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 196.17 E-value: 1.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 125 SPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVIENGGTTAQSDKQV------QTKSTSVDTSSNQSSEDNSEnstiP 198
Cdd:PRK11857 5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAAsvssaqQAAKTAAPAAAPPKLEGKRE----K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 199 VNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTRNHYKNSFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSW--QG 276
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYdeAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 277 NEIVLHKDINISIAVADENKLYVPVIKHADEKSIKGIAREINTLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGII 356
Cdd:PRK11857 161 SELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446328983 357 NHPQAAILQVESIVKKPVVINDMIAIRSMVNLCISIDHRILDGLQTGKFMNHIKQRIEQ 415
Cdd:PRK11857 241 NYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEK 299
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
1-414 |
7.36e-57 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 193.82 E-value: 7.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 1 MEITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIETADEK 80
Cdd:PLN02226 92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 81 TNETTEEIQAKvdehtQKSTKKASATVEQtftakQNQPRNNGrfSPVVFKlasehdidlsqvvgsgfegrvtkkdimsvi 160
Cdd:PLN02226 172 ASQVTPSQKIP-----ETTDPKPSPPAED-----KQKPKVES--APVAEK------------------------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 161 enggttaqsdkqvqTKSTSVDTSSNQSSED-----NSENSTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTR 235
Cdd:PLN02226 210 --------------PKAPSSPPPPKQSAKEpqlppKERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 236 NHYKNSFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVPVIKHADEKSIKGIAR 315
Cdd:PLN02226 276 SQYKDAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 316 EINTLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIVKKPVVINDMIAIRSMVNLCISIDHR 395
Cdd:PLN02226 356 TINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHR 435
|
410
....*....|....*....
gi 446328983 396 ILDGLQTGKFMNHIKQRIE 414
Cdd:PLN02226 436 LIDGREAVYFLRRVKDVVE 454
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
123-414 |
7.88e-51 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 174.71 E-value: 7.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 123 RFSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVIEnggttaqSDKQVQTKSTSVDTSSNQSSEDN----SENSTIP 198
Cdd:PRK14843 50 RISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLP-------ENIENDSIKSPAQIEKVEEVPDNvtpyGEIERIP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 199 VNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTRNHYKNSFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSW--QG 276
Cdd:PRK14843 123 MTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteDG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 277 NEIVLHKDINISIAVADENKLYVPVIKHADEKSIKGIAREINTLATKARNKQLTTEDMQGGTFTVNNTGTFGsVSSMG-I 355
Cdd:PRK14843 203 KTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFG-VQSFGpI 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446328983 356 INHPQAAILQVESIVKKPVVINDMIAIRSMVNLCISIDHRILDGLQTGKFMNHIKQRIE 414
Cdd:PRK14843 282 INQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIE 340
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1-74 |
8.58e-29 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 107.49 E-value: 8.58e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446328983 1 MEITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKI 74
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
2-74 |
1.00e-28 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 107.46 E-value: 1.00e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKI 74
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
2-74 |
3.42e-19 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 81.11 E-value: 3.42e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446328983 2 EITMPKLGESVHEGtIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKI 74
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
189-424 |
3.92e-19 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 90.33 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 189 EDNSENSTIPVNGVRKAIAQNMVNSVtEIPHAWMMIEVDATNLVNTR----NHY------KNSFKNKEGYnltffaffvk 258
Cdd:PRK12270 110 AAAVEDEVTPLRGAAAAVAKNMDASL-EVPTATSVRAVPAKLLIDNRivinNHLkrtrggKVSFTHLIGY---------- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 259 AVADALKAYPLLNSSWQgnEI------VLHKDINISIAVADENK-----LYVPVIKHADEKSIKGIAREINTLATKARNK 327
Cdd:PRK12270 179 ALVQALKAFPNMNRHYA--EVdgkptlVTPAHVNLGLAIDLPKKdgsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 328 QLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQVESIV-------KKPVVINDMiAIRSMVNLCISIDHRILDGL 400
Cdd:PRK12270 257 KLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEypaefqgASEERLAEL-GISKVMTLTSTYDHRIIQGA 335
|
250 260
....*....|....*....|....
gi 446328983 401 QTGKFMnhikQRIEQYTLENTNIY 424
Cdd:PRK12270 336 ESGEFL----RTIHQLLLGEDGFY 355
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
2-94 |
2.53e-17 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 83.07 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIetADEKT 81
Cdd:PRK14875 4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVV--ADAEV 81
|
90
....*....|...
gi 446328983 82 NEttEEIQAKVDE 94
Cdd:PRK14875 82 SD--AEIDAFIAP 92
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
2-74 |
8.38e-14 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 65.93 E-value: 8.38e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKI 74
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
2-105 |
1.79e-11 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 65.71 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 2 EITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAG-QTVAIDTIICKI----ET 76
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLleegES 83
|
90 100
....*....|....*....|....*....
gi 446328983 77 ADEKTNETTEEIQAKVDEHTQKSTKKASA 105
Cdd:PRK11892 84 ASDAGAAPAAAAEAAAAAPAAAAAAAAKK 112
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
125-156 |
5.76e-10 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 54.23 E-value: 5.76e-10
10 20 30
....*....|....*....|....*....|..
gi 446328983 125 SPVVFKLASEHDIDLSQVVGSGFEGRVTKKDI 156
Cdd:pfam02817 4 SPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
15-74 |
2.96e-09 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 52.80 E-value: 2.96e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328983 15 GTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKI 74
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
21-65 |
1.81e-06 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 47.20 E-value: 1.81e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 446328983 21 LVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTV 65
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPV 126
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
15-75 |
2.78e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 49.46 E-value: 2.78e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446328983 15 GTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIE 75
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
15-65 |
4.07e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 42.88 E-value: 4.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446328983 15 GTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTV 65
Cdd:PRK06549 70 GTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVV 120
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
22-69 |
7.64e-05 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 44.06 E-value: 7.64e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446328983 22 VSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVEAGQTVAIDT 69
Cdd:PLN02983 220 VKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDT 267
|
|
| PRK06748 |
PRK06748 |
hypothetical protein; Validated |
15-75 |
2.87e-03 |
|
hypothetical protein; Validated
Pssm-ID: 180678 [Multi-domain] Cd Length: 83 Bit Score: 36.77 E-value: 2.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446328983 15 GTIEQWLVSVGDHIDEYEPLCEVIT-DKVTAEVPSTISGTITEILVEAGQTVAIDTIICKIE 75
Cdd:PRK06748 13 GKVEKLFVRESSYVYEWEKLALIETiDKQKVEIKVGISGYIESLEVVEGQAIADQKLLITVR 74
|
|
| |
