|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
57-501 |
2.11e-130 |
|
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: 385.69 E-value: 2.11e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 57 KILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKNIKLGSLIALMVEEGED 136
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 137 ----WKHVEIPKDVSAPPPVPKPPAPPQPSPQTQTPCPARKERT---------VGTPPRLRLSPAARNILEKHSLDASQG 203
Cdd:TIGR01349 81 vadaFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEpsspaplsdKESGDRIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 204 TATGPRGVFTKEDALRLVELKQmgKIAEFRPAPGPPSTLSAPVPPQPtaglsyprpmippvsipgqpnaaGTFTEIPASN 283
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSP--ASANQQAAATTPATYPAAAPVST-----------------------GSYEDVPLSN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 284 IRKVIAKRLTESKSTVPHAYATANCDLGAVLKVRRDLVK---DDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKHLP 360
Cdd:TIGR01349 216 IRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmasEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 361 SVDISVAVATDKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACI 440
Cdd:TIGR01349 296 NVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2029126870 441 LAVGRFRPVLKLTEDEEGNPQVRqhQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:TIGR01349 376 LAVGAVEDVAVVDNDEEKGFAVA--SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
55-501 |
9.20e-128 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 377.98 E-value: 9.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 55 PIKILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIALMVEEG 134
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 135 EdwkhVEIPKDVSAPPPVPKPPAPPQPSPQTQTPCPARKERTVGTPPRLRLSPAARNILEKHSLDASQGTATGPRGVFTK 214
Cdd:PRK11856 81 E----AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 215 EDalrlVElkqmgKIAEFRPAPGPPSTLSAPVPPQPtaglsyprpmippvsipgqpnAAGTFTEIPASNIRKVIAKRLTE 294
Cdd:PRK11856 157 ED----VE-----AAAAAAAPAAAAAAAAAAAPPAA---------------------AAEGEERVPLSGMRKAIAKRMVE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 295 SKSTVPHAYATANCDLGAVLKVRRDLVKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKHLPSVDISVAVATDKGL 374
Cdd:PRK11856 207 SKREIPHFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 375 ITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKl 452
Cdd:PRK11856 287 IVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV- 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2029126870 453 tedeegNPQVRQHQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:PRK11856 366 ------DGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
292-501 |
2.34e-78 |
|
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: 243.99 E-value: 2.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 292 LTESKSTVPHAYATANCDLGAVLKVRRDL----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPK--HLPSVDIS 365
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 366 VAVATDKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 445
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2029126870 446 --FRPVLKltedeegNPQVRQHQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:pfam00198 161 irKRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
56-130 |
1.00e-27 |
|
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: 105.56 E-value: 1.00e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2029126870 56 IKILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIALM 130
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
55-131 |
1.22e-24 |
|
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: 97.06 E-value: 1.22e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2029126870 55 PIKILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIALMV 131
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
57-501 |
2.11e-130 |
|
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: 385.69 E-value: 2.11e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 57 KILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKNIKLGSLIALMVEEGED 136
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 137 ----WKHVEIPKDVSAPPPVPKPPAPPQPSPQTQTPCPARKERT---------VGTPPRLRLSPAARNILEKHSLDASQG 203
Cdd:TIGR01349 81 vadaFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEpsspaplsdKESGDRIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 204 TATGPRGVFTKEDALRLVELKQmgKIAEFRPAPGPPSTLSAPVPPQPtaglsyprpmippvsipgqpnaaGTFTEIPASN 283
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSP--ASANQQAAATTPATYPAAAPVST-----------------------GSYEDVPLSN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 284 IRKVIAKRLTESKSTVPHAYATANCDLGAVLKVRRDLVK---DDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKHLP 360
Cdd:TIGR01349 216 IRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmasEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 361 SVDISVAVATDKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACI 440
Cdd:TIGR01349 296 NVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2029126870 441 LAVGRFRPVLKLTEDEEGNPQVRqhQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:TIGR01349 376 LAVGAVEDVAVVDNDEEKGFAVA--SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
55-501 |
9.20e-128 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 377.98 E-value: 9.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 55 PIKILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIALMVEEG 134
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 135 EdwkhVEIPKDVSAPPPVPKPPAPPQPSPQTQTPCPARKERTVGTPPRLRLSPAARNILEKHSLDASQGTATGPRGVFTK 214
Cdd:PRK11856 81 E----AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 215 EDalrlVElkqmgKIAEFRPAPGPPSTLSAPVPPQPtaglsyprpmippvsipgqpnAAGTFTEIPASNIRKVIAKRLTE 294
Cdd:PRK11856 157 ED----VE-----AAAAAAAPAAAAAAAAAAAPPAA---------------------AAEGEERVPLSGMRKAIAKRMVE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 295 SKSTVPHAYATANCDLGAVLKVRRDLVKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKHLPSVDISVAVATDKGL 374
Cdd:PRK11856 207 SKREIPHFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 375 ITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKl 452
Cdd:PRK11856 287 IVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV- 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2029126870 453 tedeegNPQVRQHQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:PRK11856 366 ------DGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
57-501 |
8.08e-104 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 321.03 E-value: 8.08e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 57 KILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKNIKLGSLIALMVEEGED 136
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEED 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 137 WKHVE-----IPKDVSAPPPVPKPPAPPQPSPQTQTPCPARKERTVGTPP----RLRLSPAARNILEKHSLDASQGTATG 207
Cdd:PLN02744 194 IGKFKdykpsSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPssgdRIFASPLARKLAEDNNVPLSSIKGTG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 208 PRGVFTKEDALRLveLKQMGKiaefrPAPGPPSTlsapvpPQPTAGLSYprpmippvsipgqpnaagtfTEIPASNIRKV 287
Cdd:PLN02744 274 PDGRIVKADIEDY--LASGGK-----GATAPPST------DSKAPALDY--------------------TDIPNTQIRKV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 288 IAKRLTESKSTVPHAYATANCDLGAVLKVRRDL-----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKHLPSV 362
Cdd:PLN02744 321 TASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLnslqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNV 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 363 DISVAVATDKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNL-GMFGIDEFTAVINPPQACIL 441
Cdd:PLN02744 401 NINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAIL 480
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2029126870 442 AVG----RFRPvlkltedEEGNPQVRQHQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:PLN02744 481 AVGsaekRVIP-------GSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESM 537
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
292-501 |
2.34e-78 |
|
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: 243.99 E-value: 2.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 292 LTESKSTVPHAYATANCDLGAVLKVRRDL----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPK--HLPSVDIS 365
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 366 VAVATDKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 445
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2029126870 446 --FRPVLKltedeegNPQVRQHQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:pfam00198 161 irKRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
56-502 |
7.54e-67 |
|
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: 220.76 E-value: 7.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 56 IKILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIAlMVEEGE 135
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLA-ILEEGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 136 DwkhveipkdvsappPVPKPPAPPQPSPQTQTPCPARKERTVgTPPRLRLSPAARNILEKHSLDASQGTATGPRGVFTKE 215
Cdd:TIGR01347 79 D--------------ATAAPPAKSGEEKEETPAASAAAAPTA-AANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 216 DALrlvelkqmgKIAEFRPAPGPPstlsaPVPPQPTAGLSYPRPMippvsipgqpnaagtfTEIPASNIRKVIAKRLTES 295
Cdd:TIGR01347 144 DII---------KKTEAPASAQPP-----AAAAAAAAPAAATRPE----------------ERVKMTRLRQRIAERLKEA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 296 KSTVPHAYATANCDLGAVLKVRRD-----LVKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKHLPSVDISVAVAT 370
Cdd:TIGR01347 194 QNSTAMLTTFNEVDMSAVMELRKRykeefEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVST 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 371 DKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RP 448
Cdd:TIGR01347 274 DRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIkeRP 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2029126870 449 VLKltedeegNPQVRQHQLITVTMSSDSRMVDDELATKFLETFKANLENPMRLA 502
Cdd:TIGR01347 354 VAV-------NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
56-501 |
6.57e-66 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 218.17 E-value: 6.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 56 IKILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAkNIKLGSLIALMVEEGE 135
Cdd:PRK05704 3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 136 DWKHVEIPKDVSAPPPVPkppappqpspqtqtpcPARKERTVGTPPRLRLSPAARNILEKHSLDASQGTATGPRGVFTKE 215
Cdd:PRK05704 82 AGAAAAAAAAAAAAAAAP----------------AQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 216 DALrlvelkqmGKIAEFRPAPGPPSTLSAPVPPQPTAGLSYPR-PMippvsipgqpnaagtfteipaSNIRKVIAKRLTE 294
Cdd:PRK05704 146 DVL--------AALAAAAAAPAAPAAAAPAAAPAPLGARPEERvPM---------------------TRLRKTIAERLLE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 295 SKSTvphayaTA------NCDLGAVLKVRRDLvKD------DIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKHLPSV 362
Cdd:PRK05704 197 AQNT------TAmlttfnEVDMTPVMDLRKQY-KDafekkhGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYY 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 363 DISVAVATDKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILA 442
Cdd:PRK05704 270 DIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILG 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2029126870 443 VGRF--RPVLKltedeegNPQVRQHQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:PRK05704 350 MHKIkeRPVAV-------NGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERL 403
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
70-502 |
5.11e-64 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 217.00 E-value: 5.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 70 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIALMveEGEDWKHVEIPKDVSAP 149
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVVI--EVAAAAPAAAAAPAAAA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 150 PPVPKPPAPPQPSPQTQTPCPARKERTVGTPPRLRLSPAARNILEKHSLDASQGTATGPRGVFTKEDALRLVELKQMGKI 229
Cdd:PRK11855 210 PAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 230 AEfRPAPGPPSTLSAPVPPQPTAGLSyprpmippvsipgqpnAAGTFTEIPASNIRKVIAKRLTESKSTVPHAYATANCD 309
Cdd:PRK11855 290 AA-AAAAAAAGGGGLGLLPWPKVDFS----------------KFGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEAD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 310 LGAVLKVRRDL----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGpKHL---PSVDISVAVATDKGLITPIIKDA 382
Cdd:PRK11855 353 ITDLEALRKQLkkeaEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDG-DELtykKYFNIGFAVDTPNGLVVPVIKDV 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 383 AAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRfrpVLKLTEDEEGNPQV 462
Cdd:PRK11855 432 DKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGK---SQMKPVWDGKEFVP 508
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2029126870 463 RqhQLITVTMSSDSRMVDDELATKFLETFKANLENPMRLA 502
Cdd:PRK11855 509 R--LMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
70-501 |
3.79e-48 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 175.96 E-value: 3.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 70 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIALMVEEGEDWKHVEIPKDVSAP 149
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRFEVEGAAPAAAPAKQEAAAP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 150 PPVPKPPAPPQPSPQTQtpcPARKERTVGTPPRLRLSPAARNILEKHSLDASQGTATGPRGVFTKEDALRLVelKQMGKI 229
Cdd:PRK11854 298 APAAAKAEAPAAAPAAK---AEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYV--KDAVKR 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 230 AEFRPAPGPPSTLSAPVPPQPTAglsyprpmippvsipgQPNAAGTFTEIPASNIRKVIAKRLTESKSTVPHAYATANCD 309
Cdd:PRK11854 373 AEAAPAAAAAGGGGPGLLPWPKV----------------DFSKFGEIEEVELGRIQKISGANLHRNWVMIPHVTQFDKAD 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 310 LGAVLKVRRD------LVKDDIKVSVNDFIIRAAAVTLKQMPGVNVTW--DGEGPKHLPSVDISVAVATDKGLITPIIKD 381
Cdd:PRK11854 437 ITELEAFRKQqnaeaeKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 382 AAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVlklTEDEEGN 459
Cdd:PRK11854 517 VNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKsaMEPV---WNGKEFA 593
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2029126870 460 PQvrqhQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:PRK11854 594 PR----LMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRL 631
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
58-501 |
7.29e-48 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 170.63 E-value: 7.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 58 ILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKniklgslialmVEEGEDW 137
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDT-----------VEVGAPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 138 khVEIPKDVSAPPPvpkppappqpspqtqtpcPARKERTVGTPPRLRLSPAARNIlekhsldASQGTATgprgvftkeda 217
Cdd:PTZ00144 116 --SEIDTGGAPPAA------------------APAAAAAAKAEKTTPEKPKAAAP-------TPEPPAA----------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 218 lrlvelkqmgkiaefrPAPGPPSTLSAPVPPQptaglsYPRPMIPPVSIPGQPNaagtfTEIPASNIRKVIAKRLTESKS 297
Cdd:PTZ00144 158 ----------------SKPTPPAAAKPPEPAP------AAKPPPTPVARADPRE-----TRVPMSRMRQRIAERLKASQN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 298 TvphaYA---TAN-CDLGAVLKVRRDL-----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKHLPSVDISVAV 368
Cdd:PTZ00144 211 T----CAmltTFNeCDMSALMELRKEYkddfqKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 369 ATDKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACIL---AVGR 445
Cdd:PTZ00144 287 ATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILgmhAIKK 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2029126870 446 fRPVLKltedeegNPQVRQHQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:PTZ00144 367 -RPVVV-------GNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARM 414
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
68-501 |
5.50e-46 |
|
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: 168.51 E-value: 5.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 68 ERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIalMVEEGEDWKHVEIPKDVS 147
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLI--LTLSVAGSTPATAPAPAS 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 148 APPPVPKPPAPPQPSPQTQTPCPARKERTVGTPPRL-----RLSPAARNILEKHSLDASQGTATGPRGVFTKEDALRLVE 222
Cdd:TIGR01348 205 AQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNpakvdHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVK 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 223 lKQMGKiaefrpapgppstlsAPVPPQPTAGlsyPRPMIPPVsipgqPNAA----GTFTEIPASNIRKVIAKRLTESKST 298
Cdd:TIGR01348 285 -EPSVR---------------AQAAAASAAG---GAPGALPW-----PNVDfskfGEVEEVDMSRIRKISGANLTRNWTM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 299 VPHAYATANCDLGAVLKVRRDL----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWD--GEGPKHLPSVDISVAVATDK 372
Cdd:TIGR01348 341 IPHVTHFDKADITEMEAFRKQQnaavEKEGVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPN 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 373 GLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVL 450
Cdd:TIGR01348 421 GLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKsgMEPVW 500
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2029126870 451 KLTEDEEGNpqvrqhqLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:TIGR01348 501 NGKEFEPRL-------MLPLSLSYDHRVIDGADAARFTTYICESLADIRRL 544
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
72-501 |
8.30e-44 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 159.88 E-value: 8.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 72 IVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLG-SLIALMVEEGEDWKHVEIPKDVSAPP 150
Cdd:PLN02528 15 LLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGeTLLKIMVEDSQHLRSDSLLLPTDSSN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 151 PVPKPPAPpqpspqtqtpcpARKERTVGTpprlRLSPAARNILEKHSLDASQGTATGPRGVFTKEDALRLveLKQMGKIA 230
Cdd:PLN02528 94 IVSLAESD------------ERGSNLSGV----LSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKY--AAQKGVVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 231 EfrpapgPPSTLSAPVPPQptaGLSYPRPMIPPvsipGQPNAAGTfteIPASNIRKVIAKRLTESKStVPHAYATA--NC 308
Cdd:PLN02528 156 D------SSSAEEATIAEQ---EEFSTSVSTPT----EQSYEDKT---IPLRGFQRAMVKTMTAAAK-VPHFHYVEeiNV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 309 DlgAVLKVRRDL----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPK--HLPSVDISVAVATDKGLITPIIKDA 382
Cdd:PLN02528 219 D--ALVELKASFqennTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEirLKGSHNIGVAMATEHGLVVPNIKNV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 383 AAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEEGNPQv 462
Cdd:PLN02528 297 QSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPA- 375
|
410 420 430
....*....|....*....|....*....|....*....
gi 2029126870 463 rqhQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:PLN02528 376 ---SIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELL 411
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
58-496 |
4.12e-43 |
|
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: 160.95 E-value: 4.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 58 ILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEE------GAKNIKLGSLIALMV 131
Cdd:TIGR02927 129 VKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEddtvevGTVLAIIGDANAAPA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 132 EEGEDWKHVEIPKDVSAPPPVPKPPAPPQPSPQTQTPCPARKERTVGTPPRLR------LSPAARNILEKHSLDASQGTA 205
Cdd:TIGR02927 209 EPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSgdsgpyVTPLVRKLAKDKGVDLSTVKG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 206 TGPRGVFTKEDALRLVELKQMGKIAEFRPAPgppstlsAPVPPQPTAGLSYPRPMIPPVSipgqpnaaGTfTEiPASNIR 285
Cdd:TIGR02927 289 TGVGGRIRKQDVLAAAKAAEEARAAAAAPAA-------AAAPAAPAAAAKPAEPDTAKLR--------GT-TQ-KMNRIR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 286 KVIAKRLTESKSTVPHAYATANCDLGAVLKVRRD-----LVKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPK--H 358
Cdd:TIGR02927 352 QITADKTIESLQTSAQLTQVHEVDMTRVAALRARakndfLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEvtY 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 359 LPSVDISVAVATDKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQA 438
Cdd:TIGR02927 432 HDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQA 511
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2029126870 439 CILAVGRFRPVLKLTEDEEGNPQVRQHQLITVTMSSDSRMVDDELATKFLETFKANLE 496
Cdd:TIGR02927 512 AILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
183-501 |
1.36e-41 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 151.98 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 183 LRLSPAARNILEKHSLDASQGTATGPRGVFTKEDALRLVElkqmgkiaefrpapgppstlsapvPPQPTAGLSYPRPMIP 262
Cdd:PRK14843 49 VRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLP------------------------ENIENDSIKSPAQIEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 263 PVSIPGQPNAAGTFTEIPASNIRKVIAKRLTESKSTVPHAYATANCDLGAVLKVRRDLVkDDI------KVSVNDFIIRA 336
Cdd:PRK14843 105 VEEVPDNVTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVL-EPImeatgkKTTVTDLLSLA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 337 AAVTLKQMPGVNVTWDGEGPKHLPS--VDISVAVATDKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGG 414
Cdd:PRK14843 184 VVKTLMKHPYINASLTEDGKTIITHnyVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 415 SFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegNPQVRQHQLITVTMSSDSRMVDDELATKFLETFK 492
Cdd:PRK14843 264 TFTISNLGMFGVQSFGPIINQPNSAILGVSSTieKPVVV-------NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLK 336
|
....*....
gi 2029126870 493 ANLENPMRL 501
Cdd:PRK14843 337 ELIETPISM 345
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
54-501 |
1.08e-37 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 144.13 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 54 DPIKILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGaKNIKLGSLIALMVEE 133
Cdd:PLN02226 90 DTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEG-DTVEPGTKVAIISKS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 134 GEDWKHVeipkdvsapppvpkppappqpspqtqtpCPARK--ERTVGTPprlrlSPAARNILEkhsldasqgtatgPRgv 211
Cdd:PLN02226 169 EDAASQV----------------------------TPSQKipETTDPKP-----SPPAEDKQK-------------PK-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 212 ftkedalrlvelKQMGKIAEFRPAPGPPStlsapvPPQPTAglsyPRPMIPPVSIPgqpnaagtfTEIPASNIRKVIAKR 291
Cdd:PLN02226 201 ------------VESAPVAEKPKAPSSPP------PPKQSA----KEPQLPPKERE---------RRVPMTRLRKRVATR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 292 LTESKSTVPHAYATANCDLGAVLKVRRD-----LVKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKHLPSVDISV 366
Cdd:PLN02226 250 LKDSQNTFALLTTFNEVDMTNLMKLRSQykdafYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 367 AVATDKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF 446
Cdd:PLN02226 330 AVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSI 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2029126870 447 --RPVLKltedeegNPQVRQHQLITVTMSSDSRMVDDELATKFLETFKANLENPMRL 501
Cdd:PLN02226 410 vsRPMVV-------GGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRL 459
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
55-136 |
2.90e-32 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 128.50 E-value: 2.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 55 PIKILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKNIKLGSLIALMVEEG 134
Cdd:PRK11892 2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEG 81
|
..
gi 2029126870 135 ED 136
Cdd:PRK11892 82 ES 83
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
186-498 |
2.07e-31 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 122.98 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 186 SPAARNILEKHSLDASQGTATGPRGVFTKEDALRLVELKQMGkiaefrPAPGPPSTLSAPVPPQPTAglsyprpmiPPVS 265
Cdd:PRK11857 5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSA------PTPAEAASVSSAQQAAKTA---------APAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 266 IPGQPNAAGTfteiPASNIRKVIAKRLTESKSTVPHAYATANCDLGAVLKVRRDLVKD-----DIKVSVNDFIIRAAAVT 340
Cdd:PRK11857 70 APPKLEGKRE----KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlkteGVKLTFLPFIAKAILIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 341 LKQMPGVNVTWDgEGPKHL--PS-VDISVAVATDKGLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFS 417
Cdd:PRK11857 146 LKEFPIFAAKYD-EATSELvyPDtLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 418 ISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegNPQVRQHQLITVTMSSDSRMVDDELATKFLETFKANL 495
Cdd:PRK11857 225 ITNYGSVGSLYGVPVINYPELAIAGVGAIidKAIVK-------NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELL 297
|
...
gi 2029126870 496 ENP 498
Cdd:PRK11857 298 EKP 300
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
56-130 |
1.00e-27 |
|
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: 105.56 E-value: 1.00e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2029126870 56 IKILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIALM 130
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
55-131 |
1.22e-24 |
|
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: 97.06 E-value: 1.22e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2029126870 55 PIKILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIALMV 131
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
57-134 |
8.11e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 78.83 E-value: 8.11e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2029126870 57 KILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGaKNIKLGSLIALMVEEG 134
Cdd:PRK14875 4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEG-ETLPVGALLAVVADAE 80
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
58-130 |
5.14e-15 |
|
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: 69.94 E-value: 5.14e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2029126870 58 ILMPSLSPTMERGnIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIALM 130
Cdd:pfam00364 3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
58-119 |
1.07e-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: 69.01 E-value: 1.07e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2029126870 58 ILMPSLSPTMERGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAK 119
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
234-444 |
3.57e-12 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 69.15 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 234 PAPGPPSTLSAPVPPQPTAGLSYPRPMIPPVSIPGQPNAAGTFTEIPASNIR---KVIAKRLTESKStVPhaYATANCDL 310
Cdd:PRK12270 70 PAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRgaaAAVAKNMDASLE-VP--TATSVRAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126870 311 GAVLKVRRDLVKDD-------IKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKhlPSV----DISVAVATD-------K 372
Cdd:PRK12270 147 PAKLLIDNRIVINNhlkrtrgGKVSFTHLIGYALVQALKAFPNMNRHYAEVDGK--PTLvtpaHVNLGLAIDlpkkdgsR 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2029126870 373 GLITPIIKDAAAKDIREIADAVKVLSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVG 444
Cdd:PRK12270 225 QLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVG 296
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
70-128 |
4.13e-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: 4.13e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2029126870 70 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAkNIKLGSLIA 128
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGD-QVEAGQLLV 65
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
56-134 |
7.11e-06 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 48.46 E-value: 7.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2029126870 56 IKILMPSLSPTmeRGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIALMVEEG 134
Cdd:PRK11854 3 IEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDK-VETGALIMIFESAD 78
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
184-218 |
8.04e-05 |
|
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: 39.59 E-value: 8.04e-05
10 20 30
....*....|....*....|....*....|....*
gi 2029126870 184 RLSPAARNILEKHSLDASQGTATGPRGVFTKEDAL 218
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
70-130 |
1.24e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 41.60 E-value: 1.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2029126870 70 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAKnIKLGSLIALM 130
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ-VEAGDLLIEL 1144
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
63-117 |
3.15e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 40.21 E-value: 3.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2029126870 63 LSPTMeRGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEG 117
Cdd:PRK09282 525 VTSPM-PGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
78-135 |
5.92e-03 |
|
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: 37.18 E-value: 5.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2029126870 78 KEGEAVSAGDALCEIETDKAVVTLDANDDGILAKIVVEEGAkniklgslialMVEEGE 135
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQ-----------PVEYGQ 130
|
|
| |
