|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
4-601 |
0e+00 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 1213.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 4 QPKKIAITDVVLRDAHQSLFATRLRLEDMLPIAKELDEIGYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQ 83
Cdd:PRK14040 1 MSKPLAITDVVLRDAHQSLFATRLRLDDMLPIAAKLDKVGYWSLESWGGATFDACIRFLGEDPWERLRELKKAMPNTPQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 84 MLLRGQNLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYTTSPVHTLETWLDV 163
Cdd:PRK14040 81 MLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYTTSPVHTLQTWVDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 164 TEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYGH 243
Cdd:PRK14040 161 AKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRVDVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAISSMSMTYGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 244 PATEAIVATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNLESQLKQQNAADKLDL 323
Cdd:PRK14040 241 SATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNMESQLKEQGAADKLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 324 VLKEIPEVRKDLGYIPLVTPTSQIVGTQAVINVLMGGRYKNIAKETAGILKGEYGRTPTPVNAELQARVLEGNEPITDRP 403
Cdd:PRK14040 321 VLAEIPRVREDLGFIPLVTPTSQIVGTQAVLNVLTGERYKTITKETAGVLKGEYGATPAPVNAELQARVLEGAEPITCRP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 404 ADHLAPEMDKLLAEVKQQAVEKGITLTKDEIDDALIVALFPQIGWKFLENRGNPAAFEPAPTLETAKAVeskveKPASSV 483
Cdd:PRK14040 401 ADLLAPELDKLEAELRRQAQEKGITLAENAIDDVLTYALFPQIGLKFLENRHNPAAFEPVPQAEAAQPA-----AKAEPA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 484 GAAVYTVELEGKAFVVKVSEGGDISNIAPVTAPTPVANLAPQATASGSGEPVNAPMAGNIIKVVVAEGQQVAEGDVLLIL 563
Cdd:PRK14040 476 GSETYTVEVEGKAYVVKVSEGGDISQITPAAPAAAPAAAAAAAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLIL 555
|
570 580 590
....*....|....*....|....*....|....*...
gi 737548984 564 EAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQIV 601
Cdd:PRK14040 556 EAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
10-597 |
0e+00 |
|
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate decarboxylase alpha subunit and its equivalents in archaea. The oxaloacetate decarboxylase Na+ pump is the paradigm of the family of Na+ transport decarboxylases that present in bacteria and archaea. It a multi subunit enzyme consisting of a peripheral alpha-subunit and integral membrane subunits beta and gamma. The energy released by the decarboxylation reaction of oxaloacetate is coupled to Na+ ion pumping across the membrane. [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Other]
Pssm-ID: 273447 [Multi-domain] Cd Length: 582 Bit Score: 968.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 10 ITDVVLRDAHQSLFATRLRLEDMLPIAKELDEIGYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQMLLRGQ 89
Cdd:TIGR01108 1 ITDVVLRDAHQSLFATRMRTEDMLPIAEKLDDVGYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLRGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 90 NLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYTTSPVHTLETWLDVTEQLLE 169
Cdd:TIGR01108 81 NLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYTTSPVHTLETYLDLAEELLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 170 IGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYGHPATEAI 249
Cdd:TIGR01108 161 MGVDSICIKDMAGILTPKAAYELVSALKKRFGLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGTSHPPTETM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 250 VATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNLESQLKQQNAADKLDLVLKEIP 329
Cdd:TIGR01108 241 VAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFEGQLKGPDSRILVAQVPGGMLSNLESQLKEQNALDKLDEVLEEIP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 330 EVRKDLGYIPLVTPTSQIVGTQAVINVLMGGRYKNIAKETAGILKGEYGRTPTPVNAELQARVLEGNEPITD-RPADHLA 408
Cdd:TIGR01108 321 RVREDLGYPPLVTPTSQIVGTQAVLNVLTGERYKTITKETKGYLKGEYGRTPAPINAELQRKILGDEKPIVDcRPADLLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 409 PEMDKLLAEVKQQAVEkgitltKDEIDDALIVALFPQIGWKFLENRGNPAAFEPAPT-----LETAKAVESKVEKPASsv 483
Cdd:TIGR01108 401 PELDKLRAEVREAGAE------KNSIEDVLTYALFPQVGLKFLENRHNPAAFEPKPEekvieQEHAQVVGKYEETHAS-- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 484 gaAVYTVELEGKAFVVKVSEGGDISNIAP-VTAPTPVANLAPQAtasGSGEPVNAPMAGNIIKVVVAEGQQVAEGDVLLI 562
Cdd:TIGR01108 473 --GSYTVEVEGKAFVVKVSPGGDVSQITAsAPANTSGGTVAAKA---GAGTPVTAPIAGSIVKVKVSEGQTVAEGEVLLI 547
|
570 580 590
....*....|....*....|....*....|....*
gi 737548984 563 LEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTL 597
Cdd:TIGR01108 548 LEAMKMETEIKAAAAGTVREILVKVGDAVSVGQVL 582
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
6-600 |
0e+00 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 875.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 6 KKIAITDVVLRDAHQSLFATRLRLEDMLPIAKELDEIGYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQML 85
Cdd:PRK09282 2 KKVKITDTTLRDAHQSLLATRMRTEDMLPIAEKLDKVGFWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 86 LRGQNLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYTTSPVHTLETWLDVTE 165
Cdd:PRK09282 82 LRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYTTSPVHTIEKYVELAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 166 QLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYGHPA 245
Cdd:PRK09282 162 ELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEVDLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISPLAFGTSQPP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 246 TEAIVATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNLESQLKQQNAADKLDLVL 325
Cdd:PRK09282 242 TESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTIVDTRVLIHQVPGGMISNLVSQLKEQNALDKLDEVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 326 KEIPEVRKDLGYIPLVTPTSQIVGTQAVINVLMGGRYKNIAKETAGILKGEYGRTPTPVNAELQARVLEGNEPITDRPAD 405
Cdd:PRK09282 322 EEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTGERYKVITKEVKDYVKGLYGRPPAPINEELRKKIIGDEEPITCRPAD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 406 HLAPEMDKLLAEVKQQAvekgitltKDEIDDALIVALFPQIGWKFLENRGNPAAFEPAPTLETAKAVESKVekpassvgA 485
Cdd:PRK09282 402 LLEPELEKARKEAEELG--------KSEKEDVLTYALFPQIAKKFLEEREAGELKPEPEPKEAAAAGAEGI--------P 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 486 AVYTVELEGKAFVVKVsEGGDISNIAP------------VTAPTPVANLAPQATASGSGePVNAPMAGNIIKVVVAEGQQ 553
Cdd:PRK09282 466 TEFKVEVDGEKYEVKI-EGVKAEGKRPfylrvdgmpeevVVEPLKEIVVGGRPRASAPG-AVTSPMPGTVVKVKVKEGDK 543
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 737548984 554 VAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK09282 544 VKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
5-555 |
0e+00 |
|
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate/oxaloacetate carboxyltransferase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 444040 [Multi-domain] Cd Length: 540 Bit Score: 832.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 5 PKKIAITDVVLRDAHQSLFATRLRLEDMLPIAKELDEIGYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQM 84
Cdd:COG5016 1 MKKVKITDTTLRDGHQSLFATRMRTEDMLPIAEKLDEAGFWSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 85 LLRGQNLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYTTSPVHTLETWLDVT 164
Cdd:COG5016 81 LLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYTISPVHTVEYYVELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 165 EQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYGHP 244
Cdd:COG5016 161 KELEDMGADSICIKDMAGLLTPYRAYELVKALKEALDIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPLAGGTSQP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 245 ATEAIVATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNLESQLKQQNAADKLDLV 324
Cdd:COG5016 241 PTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGVDPRVLVHQVPGGMLSNLVSQLKEQGALDRLDEV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 325 LKEIPEVRKDLGYIPLVTPTSQIVGTQAVINVLMGGRYKNIAKETAGILKGEYGRTPTPVNAELQARVLEGNEPITDRPA 404
Cdd:COG5016 321 LEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTGERYKMITKEVKDYVLGYYGKTPAPIDPEVRKKALGDEEPITCRPA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 405 DHLAPEMDKLLAEVkqqavekgitLTKDEiDDALIVALFPQIGWKFLENRGNPAAFEPAPTLETAKAVESKVEKPASSVG 484
Cdd:COG5016 401 DLLEPELEKLRKEG----------LAKSD-EDVLTYALFPQVAIKFLKGRAAGEARPDAPLAELAAVEEVVVVAEGVVVV 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737548984 485 AAVYTVELEGKAFVVKVSEGGDISNIAPVTAPTPVANLAPQATASGSGEPVNAPMAGNIIKVVVAEGQQVA 555
Cdd:COG5016 470 VVVGGGAEGVVVVVVGVPGAGAVAVVAAAAAVAAAAAAAAAAAAAAAGAAVKKVVAVGGAVVVGVEVVVVV 540
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
6-457 |
0e+00 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 651.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 6 KKIAITDVVLRDAHQSLFATRLRLEDMLPIAKELDEIGYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQML 85
Cdd:PRK12331 2 TKIKITETVLRDGQQSLIATRMTTEEMLPILEKLDNAGYHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 86 LRGQNLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYTTSPVHTLETWLDVTE 165
Cdd:PRK12331 82 LRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYTTSPVHTIDYFVKLAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 166 QLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYGHPA 245
Cdd:PRK12331 162 EMQEMGADSICIKDMAGILTPYVAYELVKRIKEAVTVPLEVHTHATSGIAEMTYLKAIEAGADIIDTAISPFAGGTSQPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 246 TEAIVATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKfEGQL----KGVDSRILVAQVPGGMLTNLESQLKQQNAADKL 321
Cdd:PRK12331 242 TESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYRE-EGILnpkvKDVEPKTLIYQVPGGMLSNLLSQLKEQGAEDKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 322 DLVLKEIPEVRKDLGYIPLVTPTSQIVGTQAVINVLMGGRYKNIAKETAGILKGEYGRTPTPVNAELQARVLEGNEPITD 401
Cdd:PRK12331 321 EEVLKEVPKVRADLGYPPLVTPLSQMVGTQALMNVISGERYKMVPNEIKDYVRGLYGRPPAPIAEEIKKKIIGDEEVITC 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 737548984 402 RPADHLAPEMDKLLAEVKQQAvekgitltkDEIDDALIVALFPQIGWKFLENRGNP 457
Cdd:PRK12331 401 RPADLIEPQLEKLREEIAEYA---------ESEEDVLSYALFPQQAKDFLGRREDP 447
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
5-505 |
0e+00 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 616.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 5 PKKIAITDVVLRDAHQSLFATRLRLEDMLPIAKELDEIGYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQM 84
Cdd:PRK12330 2 PRKIGVTELALRDAHQSLMATRMAMEDMVGACEDIDNAGYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 85 LLRGQNLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYTTSPVHTLETWLDVT 164
Cdd:PRK12330 82 LLRGQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYTVSPIHTVEGFVEQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 165 EQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRY--DIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYG 242
Cdd:PRK12330 162 KRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgeDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSMSLGPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 243 HPATEAIVATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNLESQLKQQNAADKLD 322
Cdd:PRK12330 242 HNPTESLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTTGVETEIFKSQIPGGMLSNMESQLKQQGAGDRMD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 323 LVLKEIPEVRKDLGYIPLVTPTSQIVGTQAVINVLMgGRYKNIAKETAGILKGEYGRTPTPVNAEL--QARVLEGNEPIT 400
Cdd:PRK12330 322 EVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVFNVLM-GRYKVLTGEFADLMLGYYGETPGERNPEVveQAKKQAKKEPIT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 401 DRPADHLAPEMDKLLAEVKQQAVEKGitltKDEidDALIVALFPQIGWKFLENRGN-PAAFEPAPtlETAKAVESKVEKP 479
Cdd:PRK12330 401 CRPADLLEPEWDKLRAEALALEGCDG----SDE--DVLTYALFPQVAPKFFATRAEgPKNVGKDP--AQGAAEAAAAAGH 472
|
490 500
....*....|....*....|....*..
gi 737548984 480 ASSV-GAAVYTVELEGKAFVVKVSEGG 505
Cdd:PRK12330 473 AGAItGPITYKVTVGGRSHKVTVAPAK 499
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
6-454 |
0e+00 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 570.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 6 KKIAITDVVLRDAHQSLFATRLRLEDMLPIAKELDEIGYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQML 85
Cdd:PRK14041 1 MKVMFVDTTLRDGHQSLIATRMRTEDMLPALEAFDRMGFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 86 LRGQNLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYTTSPVHTLETWLDVTE 165
Cdd:PRK14041 81 LRGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYTVSPVHTLEYYLEFAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 166 QLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYGHPA 245
Cdd:PRK14041 161 ELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKFGVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFSMGTSQPP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 246 TEAIVATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNLESQLKQQNAADKLDLVL 325
Cdd:PRK14041 241 FESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYDVGMKSPDSRILVSQIPGGMYSNLVKQLKEQKMLHKLDKVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 326 KEIPEVRKDLGYIPLVTPTSQIVGTQAVINVLMGGRYKNIAKETAGILKGEYGRTPTPVNAELQARVLEGNEPITDRPAD 405
Cdd:PRK14041 321 EEVPRVRKDLGYPPLVTPTSQIVGVQAVLNVLTGERYKRVTNETKNYVKGLYGRPPAPIDEELMKKILGDEKPIDCRPAD 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 737548984 406 HLAPEMDKLLAEVkqqavekGITLTKDEidDALIVALFPQIGWKFLENR 454
Cdd:PRK14041 401 LLEPELEKARKEL-------GILAETDE--DLLIYVILGEVGKKFLKKK 440
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
7-600 |
0e+00 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 531.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 7 KIAITDVVLRDAHQSLFATRLRLEDMLPIAKELDEIGYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQMLL 86
Cdd:PRK14042 3 KTFITDVTLRDAHQCLIATRMRTEDMLPICNKMDDVGFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSMLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 87 RGQNLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYTTSPVHTLETWLDVTEQ 166
Cdd:PRK14042 83 RGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYTTSPVHTLDNFLELGKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 167 LLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYGHPAT 246
Cdd:PRK14042 163 LAEMGCDSIAIKDMAGLLTPTVTVELYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSGGASHPPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 247 EAIVATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNLESQLKQQNAADKLDLVLK 326
Cdd:PRK14042 243 EALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNALDKMDAVHK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 327 EIPEVRKDLGYIPLVTPTSQIVGTQAVINVLMGGRYKNIAKETAGILKGEYGRTPTPVNAELQARVLEGNEPITDRPADH 406
Cdd:PRK14042 323 EIPRVRKDLGYPPLVTPTSQVVGTQAVINVLTGERYKTITNEVKLYCQGKYGTPPGKISSALRKKAIGRTEVIEVRPGDL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 407 LAPEMDKLLAEVKQQAVEKgitltkdeiDDALIVALFPQIGWKFLENRGNPAAFePAPTLETAKAveskvekPASSVgAA 486
Cdd:PRK14042 403 LPNELDQLQNEISDLALSD---------EDVLLYAMFPEIGRQFLEQRKNNQLI-PEPLLTQSSA-------PDNSV-MS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 487 VYTVELEGKAFVVKVSEGGDIS----------NIAPVTAPTPVANLAPQATAS------GSGEpVNAPMAGNIIKVVVAE 550
Cdd:PRK14042 465 EFDIILHGESYHVKVAGYGMIEhgqqscflwvDGVPEEVVVQHSELHDKIERSsvnnkiGPGD-ITVAIPGSIIAIHVSA 543
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 737548984 551 GQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK14042 544 GDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
10-284 |
0e+00 |
|
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163675 Cd Length: 275 Bit Score: 515.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 10 ITDVVLRDAHQSLFATRLRLEDMLPIAKELDEIGYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQMLLRGQ 89
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAGFFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLRGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 90 NLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYTTSPVHTLETWLDVTEQLLE 169
Cdd:cd07937 81 NLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGSPVHTLEYYVKLAKELED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 170 IGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYGHPATEAI 249
Cdd:cd07937 161 MGADSICIKDMAGLLTPYAAYELVKALKKEVGLPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGGTSQPSTESM 240
|
250 260 270
....*....|....*....|....*....|....*
gi 737548984 250 VATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKF 284
Cdd:cd07937 241 VAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
6-600 |
2.49e-171 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 517.00 E-value: 2.49e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 6 KKIAITDVVLRDAHQSLFATRLRLEDMLPIAKELDEI--GYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQ 83
Cdd:PRK12999 531 KRVLLTDTTFRDAHQSLLATRVRTKDLLRIAPATARLlpNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQ 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 84 MLLRGQNLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYT------TSPVHTL 157
Cdd:PRK12999 611 MLLRGSNAVGYTNYPDNVVRAFVREAAAAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTgdildpARAKYDL 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 158 ETWLDVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSM 237
Cdd:PRK12999 691 DYYVDLAKELEKAGAHILAIKDMAGLLKPAAAYELVSALKEEVDLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASM 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 238 SGTYGHPATEAIVATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNLESQLKQQNA 317
Cdd:PRK12999 771 SGLTSQPSLNSIVAALEGTERDTGLDLDAIRKLSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSNLKQQARALGL 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 318 ADKLDLVLKEIPEVRKDLGYIPLVTPTSQIVG-------TQAVI--NVLMGGRYKNIAKETAGILKGEYGRTPTPVNAEL 388
Cdd:PRK12999 851 GDRFEEVKEMYAAVNRMFGDIVKVTPSSKVVGdmalfmvQNGLTpeDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPL 930
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 389 QARVLEGNEPITDRPADHLAPeMDklLAEVKQQAVEKGITLTKDEidDALIVALFPQIGWKFLENR---GNPAAFePAPT 465
Cdd:PRK12999 931 QKKVLKGEEPITVRPGELLEP-VD--FEAERAELEEKLGREVTDR--DVLSYLLYPKVFEDYIKHReeyGDVSVL-PTPT 1004
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 466 ----LETAKAVESKVEKPAS------SVGAA-------VYtVELEGKAFVVKVseggdisniaPVTAPTPVANLAPQATA 528
Cdd:PRK12999 1005 ffygLRPGEEIEVEIEPGKTliikleAIGEPdedgmrtVY-FELNGQPREVQV----------RDRSVKSTVAAREKADP 1073
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737548984 529 SGSGEpVNAPMAGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK12999 1074 GNPGH-VGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
6-454 |
2.88e-168 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 487.32 E-value: 2.88e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 6 KKIAITDVVLRDAHQSLFATRLRLEDMLPIAKELDEIGYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQML 85
Cdd:PRK12581 11 QQVAITETVLRDGHQSLMATRLSIEDMLPVLTILDKIGYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRLQML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 86 LRGQNLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYTTSPVHTLETWLDVTE 165
Cdd:PRK12581 91 LRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYTTSPVHTLNYYLSLVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 166 QLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYGHPA 245
Cdd:PRK12581 171 ELVEMGADSICIKDMAGILTPKAAKELVSGIKAMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALSPFSEGTSQPA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 246 TEAIVATLQGTPYDTGLAIPQIERIAAHFREVRKKY---AKFEGQLKGVDSRILVAQVPGGMLTNLESQLKQQNAADKLD 322
Cdd:PRK12581 251 TESMYLALKEAGYDITLDETLLEQAANHLRQARQKYladGILDPSLLFPDPRTLQYQVPGGMLSNMLSQLKQANAESKLE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 323 LVLKEIPEVRKDLGYIPLVTPTSQIVGTQAVINVLMGGRYKNIAKETAGILKGEYGRTPTPVNAELQARVLEGNEPITDR 402
Cdd:PRK12581 331 EVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVILGKPYQMVSKEIKQYLAGDYGKTPAPVNEDLKRSQIGSAPVTTNR 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 737548984 403 PADHLAPEMDKLLAEVKQQAvekgitlTKDEidDALIVALFPQIGWKFLENR 454
Cdd:PRK12581 411 PADQLSPEFEVLKAEVADLA-------QTDE--DVLTYALFPSVAKPFLTTK 453
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
6-600 |
2.81e-162 |
|
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: 493.44 E-value: 2.81e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 6 KKIAITDVVLRDAHQSLFATRLRLEDMLPIAKELDEI--GYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQ 83
Cdd:COG1038 531 KKVLLTDTTFRDAHQSLLATRVRTRDMLKIAPATARLlpQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQ 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 84 MLLRGQNLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYT------TSPVHTL 157
Cdd:COG1038 611 MLLRGSNAVGYTNYPDNVVRAFVKEAAEAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTgdildpKRTKYTL 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 158 ETWLDVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSM 237
Cdd:COG1038 691 DYYVDLAKELEKAGAHILAIKDMAGLLKPYAAYKLVKALKEEVDLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASM 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 238 SGTYGHPATEAIVATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNLESQLKQQNA 317
Cdd:COG1038 771 SGLTSQPSLNSLVAALEGTERDTGLDLDALQELSNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSNLRQQARALGL 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 318 ADKLDLVLKEIPEVRKDLGYIPLVTPTSQIVGTQAVINVLMGGRYKNIAKETAGI---------LKGEYGRTPTPVNAEL 388
Cdd:COG1038 851 GDRWEEVKEMYAAVNRLFGDIVKVTPSSKVVGDMALFMVQNGLTPEDVYEKGKDLdfpdsvvsfFKGELGQPPGGFPEEL 930
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 389 QARVLEGNEPITDRPADHLAPEmDklLAEVKQQAVEKGITLTKDEidDALIVALFPQIGWKFLENR---GNPAAFePAPT 465
Cdd:COG1038 931 QKKVLKGRKPITVRPGELLPPV-D--FDALRAELEEKLGREPSDR--DVLSYLLYPKVFEDYAKHReeyGDVSVL-PTPT 1004
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 466 ----LETAKAVEskvekpassvgaavytVELE-GKAFVVKVSEGGDIS-------------NIAPVTAP----TPVANLA 523
Cdd:COG1038 1005 ffygLRPGEEIE----------------VEIEeGKTLIIKLLAIGEPDedgmrtvffelngQPREVRVRdrsvKVTVASR 1068
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 737548984 524 PQATASGSGEpVNAPMAGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:COG1038 1069 EKADPGNPGH-IGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
4-600 |
7.70e-133 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 416.54 E-value: 7.70e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 4 QPKKIAITDVVLRDAHQSLFATRLRLEDMLPIAKELDEI--GYWSLEAWGGATFDACIRFLGEDPWVRLRELKKAMPKTP 81
Cdd:TIGR01235 527 NQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIAPTTSHAlpNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNIL 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 82 LQMLLRGQNLLGYRHYADDVVDRFVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTLSYT------TSPVH 155
Cdd:TIGR01235 607 FQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGIDIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTgdildpARPKY 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 156 TLETWLDVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAIS 235
Cdd:TIGR01235 687 DLKYYTNLAVELEKAGAHILGIKDMAGLLKPAAAKLLIKALREKTDLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVD 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 236 SMSGTYGHPATEAIVATLQGTPYDTGLAIPQIERIAAHFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNLESQLKQQ 315
Cdd:TIGR01235 767 SMSGLTSQPSLGAIVAALEGSERDPGLNVAWIRELSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQFQARSL 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 316 NAADKLDLVLKEIPEVRKDLGYIPLVTPTSQIVGTQA---------VINVLMGGRYKNIAKETAGILKGEYGRTPTPVNA 386
Cdd:TIGR01235 847 GLGDRWHEVKQAYREANQMFGDIVKVTPSSKVVGDMAlfmvsndltVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPE 926
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 387 ELQARVLEGNEPITDRPADHLAP-EMDKLLAEVKQQavekgitLTKDEID-DALIVALFPQIGWKFLENRGN--PAAFEP 462
Cdd:TIGR01235 927 PLQKKVLKGEKPITVRPGSLLEPaDLDAIRKDLQEK-------HEREVSDfDVASYAMYPKVFTDFAKARDTygPVSVLP 999
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 463 APT----LETAKAVESKVEKPAS------------SVGAAVYTVELEGKAFVVKVSEGGDISNIApvtaptpvanLAPQA 526
Cdd:TIGR01235 1000 TPAffygLADGEEIEVDIEKGKTliiklqavgatdSQGEREVFFELNGQPRRIKVPDRSHKAEAA----------VRRKA 1069
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737548984 527 TaSGSGEPVNAPMAGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:TIGR01235 1070 D-PGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVL 1142
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
11-276 |
2.42e-85 |
|
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163674 [Multi-domain] Cd Length: 265 Bit Score: 267.01 E-value: 2.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 11 TDVVLRDAHQSLFATRlRLEDMLPIAKELDEIGYWSLEAWGGATFDACirFLGEDPWVRLRELKKAMPKTPLQMLLRGQn 90
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEAGVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRNR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 91 llgyrhyaddvvDRFVERAVANGMSVFRVFDAMNDP--------------RNMKQALQAVRKNGGHAQGTLSYTTSPVHT 156
Cdd:cd03174 77 ------------EKGIERALEAGVDEVRIFDSASEThsrknlnksreedlENAEEAIEAAKEAGLEVEGSLEDAFGCKTD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 157 LETWLDVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRY-DIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAIS 235
Cdd:cd03174 145 PEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALpDVPLGLHTHNTLGLAVANSLAALEAGADRVDGSVN 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 737548984 236 SMSGTYGHPATEAIVATLQGTPYDTGLAIPQIERIAAHFRE 276
Cdd:cd03174 225 GLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVEE 265
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
7-272 |
4.12e-73 |
|
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.
Pssm-ID: 459902 [Multi-domain] Cd Length: 264 Bit Score: 234.93 E-value: 4.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 7 KIAITDVVLRDAHQSLfATRLRLEDMLPIAKELDEIGYWSLEAWggatfdacIRFLGEDPWVRLRELKKAMPKTPLQmll 86
Cdd:pfam00682 1 AVAICDTTLRDGEQAL-GVAFSIDEKLAIARALDAAGVDEIEVG--------FPAASEDDFEVVRAIAKVIPHARIL--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 87 rgqnllGYRHYADDVVDRFVERAVANGMSVFRVFDAMND--------------PRNMKQALQAVRKNGghAQGTLSYTTS 152
Cdd:pfam00682 69 ------VLCRAREHDIKAAVEALKGAGAVRVHVFIATSDlhrkyklgkdreevAKRAVAAVKAARSRG--IDVEFSPEDA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 153 PVHTLETWLDVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYD--IQLHLHCHATTGMSEMALLKAIEAGVDGV 230
Cdd:pfam00682 141 SRTDPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPnkAIISVHCHNDLGMAVANSLAAVEAGADRV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 737548984 231 DTAISSMSGTYGHPATEAIVATLQGTPYDTGLAIPQIERIAA 272
Cdd:pfam00682 221 DGTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIAN 262
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
295-499 |
4.99e-73 |
|
Conserved carboxylase domain; This domain represents a conserved region in pyruvate carboxylase (PYC), oxaloacetate decarboxylase alpha chain (OADA), and transcarboxylase 5s subunit. The domain is found adjacent to the HMGL-like domain (pfam00682) and often close to the biotin_lipoyl domain (pfam00364) of biotin requiring enzymes.
Pssm-ID: 460557 [Multi-domain] Cd Length: 201 Bit Score: 232.35 E-value: 4.99e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 295 ILVAQVPGGMLTNLESQLKQQNAADKLDLVLKEIPEVRKDLGYIPLVTPTSQIVGTQAVINVLMG---------GRYKNI 365
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNltpedvlgeGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 366 AKETAGILKGEYGRTPTPVNAELQARVLEGNEPITDRPADHLAP-EMDKLLAEVKqqavEKGITLTKDEidDALIVALFP 444
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPvDLEKLRKELE----EKAGRETTEE--DVLSYALYP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 737548984 445 QIGWKFLENRgnpAAFEPAPTLETAKAVESKVEkpassvgAAVYTVELEGKAFVV 499
Cdd:pfam02436 155 KVAEKFLKFR---EKYGDVSVLPTPVFFYGLEP-------GEEYEVEIEGGKYLI 199
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
487-600 |
8.40e-27 |
|
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: 105.75 E-value: 8.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 487 VYTVELEGKAFVVKVSEGGDISNiAPVTAPTPVANLA------PQATASGSGEPVNAPMAGNI-------IKVVVAEGQQ 553
Cdd:COG0511 10 LTELEVEEGEYKVRIKRGGAAAA-APVAAPAAAAPAAaapaaaAAAAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDK 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 737548984 554 VAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:COG0511 89 VKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
535-600 |
5.34e-25 |
|
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: 98.26 E-value: 5.34e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737548984 535 VNAPMAGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
488-600 |
1.39e-24 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 99.12 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 488 YTVELEGKAFVVKVSEGGDISN----IAPVTAPTPVAN--------LAPQATASGSGEPVNAPMAGNIIKVVVAEGQQVA 555
Cdd:PRK06549 5 FKITIDGKEYLVEMEEIGAPAQaaapAQPASTPVPVPTeaspqveaQAPQPAAAAGADAMPSPMPGTILKVLVAVGDQVT 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 737548984 556 EGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK06549 85 ENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITI 129
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
472-600 |
7.37e-23 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 95.31 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 472 VESKVEkpASSVGAAVYTVELEGKAFVVKVSEGG-DISNI-----APVTAPTPVANLAPQATASGSGEP---------VN 536
Cdd:PRK05641 11 VEYEVE--VEELGPGKFRVSFEGKTYEVEAKGLGiDLSAVqeqvpTPAPAPAPAVPSAPTPVAPAAPAPapasagenvVT 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737548984 537 APMAGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK05641 89 APMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
535-600 |
9.20e-17 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 74.82 E-value: 9.20e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737548984 535 VNAPMAGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK08225 4 VYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEI 69
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
533-600 |
4.43e-16 |
|
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: 73.02 E-value: 4.43e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737548984 533 EPVNAPMAG-----NIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:pfam00364 1 TEIKSPMIGesvreGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
461-600 |
2.17e-12 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 69.85 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 461 EPAPTLETAKAVeskVEKPASSVG------AAVYTVELEGKAFVVKVSEGGDISNIAPVTAPTP------------VANL 522
Cdd:PRK11855 33 QPLVTVETDKAT---MEIPSPAAGvvkeikVKVGDTVSVGGLLAVIEAAGAAAAAAAPAAAAAPaaaaaaapapaaAAPA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 523 APQATASGSGEPVNAP-----MAGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTL 597
Cdd:PRK11855 110 AAAAAAGGGVVEVKVPdigeiTEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLL 189
|
...
gi 737548984 598 MQI 600
Cdd:PRK11855 190 VVI 192
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
106-276 |
7.27e-12 |
|
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163676 Cd Length: 274 Bit Score: 66.26 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 106 VERAVANGMSVFRVF----DAMNDpRNM-----------KQALQAVRKNGGHAQGTLS------Y--TTSPvhtlETWLD 162
Cdd:cd07938 79 AERALAAGVDEVAVFvsasETFSQ-KNIncsiaeslerfEPVAELAKAAGLRVRGYVStafgcpYegEVPP----ERVAE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 163 VTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRY-DIQLHLHCHATTGMsemAL---LKAIEAGVDGVDtaiSSMS 238
Cdd:cd07938 154 VAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFpDEKLALHFHDTRGQ---ALaniLAALEAGVRRFD---SSVG 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 737548984 239 GTYGHP---------ATEAIVATLQGTPYDTGLAIPQIERIAAHFRE 276
Cdd:cd07938 228 GLGGCPfapgatgnvATEDLVYMLEGMGIETGIDLDKLLAAARWISE 274
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
447-598 |
1.19e-11 |
|
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: 67.21 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 447 GWKFLENRGNPAAFE-PAPTLETAKAVESKVEKpASSVGAAVYTVELEGKAfVVKVSEGGDISNIAPVTAPTPVAN--LA 523
Cdd:TIGR01348 30 GQSLITLESDKASMEvPSSAAGIIKEIKVKVGD-TLPVGGVIATLEVGAGA-QAQAEAKKEAAPAPTAGAPAPAAQaqAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 524 PQATASGSGEPVNAPMAG-----NIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLM 598
Cdd:TIGR01348 108 PAAGQSSGVQEVTVPDIGdiekvTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLIL 187
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
533-600 |
2.18e-11 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 59.82 E-value: 2.18e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737548984 533 EPVNAPMAGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK05889 3 EDVRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
461-600 |
2.62e-10 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 63.10 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 461 EPAPTLETAKAvesKVEKPASSVGaavytVELEGKAFVV-KVSEGGDISNI---------APVTAPTPVANLAPQATASG 530
Cdd:PRK11854 32 QSLITVEGDKA---SMEVPSPQAG-----VVKEIKVKVGdKVETGALIMIFesadgaadaAPAQAEEKKEAAPAAAPAAA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737548984 531 SGEPVNAPMAG----NIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK11854 104 AAKDVHVPDIGsdevEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVF 177
|
|
| PRK05692 |
PRK05692 |
hydroxymethylglutaryl-CoA lyase; Provisional |
161-280 |
7.54e-10 |
|
hydroxymethylglutaryl-CoA lyase; Provisional
Pssm-ID: 180206 Cd Length: 287 Bit Score: 60.29 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 161 LDVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDI-QLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSG 239
Cdd:PRK05692 158 ADVAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAeRLAGHFHDTYGQALANIYASLEEGITVFDASVGGLGG 237
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 737548984 240 T-Y-----GHPATEAIVATLQGTPYDTGLAIPQIERIAAHFREVRKK 280
Cdd:PRK05692 238 CpYapgasGNVATEDVLYMLHGLGIETGIDLDKLVRAGQFIQSKLGR 284
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
461-600 |
9.84e-10 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 61.56 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 461 EPAPTLETAKAvesKVEKPASSVGAAVYTVELEGKafvvKVSEGGDI-----SNIAPVTAPTPVANLAPQATASGSGEP- 534
Cdd:PRK11854 135 QSLITVEGDKA---SMEVPAPFAGTVKEIKVNVGD----KVSTGSLImvfevAGEAPAAAPAAAEAAAPAAAPAAAAGVk 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737548984 535 -VNAPMAG----NIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK11854 208 dVNVPDIGgdevEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF 278
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
541-601 |
8.25e-09 |
|
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: 52.38 E-value: 8.25e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737548984 541 GNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQIV 601
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
511-601 |
1.46e-08 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 56.39 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 511 APVTAPTPVANLAPQATASGSGEP-VNAPMAGNI-----------IKVvvaeGQQVAEGDVLLILEAMKMETQICAAKAG 578
Cdd:PLN02983 175 APASSPPPTPASPPPAKAPKSSHPpLKSPMAGTFyrspapgeppfVKV----GDKVQKGQVVCIIEAMKLMNEIEADQSG 250
|
90 100
....*....|....*....|...
gi 737548984 579 TVQGIKVKSGDVVGVGDTLMQIV 601
Cdd:PLN02983 251 TIVEILAEDGKPVSVDTPLFVIE 273
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
548-600 |
4.59e-08 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 50.40 E-value: 4.59e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 737548984 548 VAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
149-278 |
1.16e-07 |
|
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic TIM barrel domain; Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step of the citramalate pathway. Citramalate is only found in Leptospira interrogans and a few other microorganisms. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163683 [Multi-domain] Cd Length: 280 Bit Score: 53.53 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 149 YTTSPvhtlETWLDVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRY-DIQLHLHCHATTGMSEMALLKAIEAGV 227
Cdd:cd07945 142 MRDSP----DYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYpNLHFDFHAHNDYDLAVANVLAAVKAGI 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 737548984 228 DGVDTAISSMSGTYGHPATEAIVATLQG-TPYDTGL---AIPQIERIAAHFREVR 278
Cdd:cd07945 218 KGLHTTVNGLGERAGNAPLASVIAVLKDkLKVKTNIdekRLNRASRLVETFSGKR 272
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
8-262 |
3.42e-07 |
|
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF ) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163681 Cd Length: 263 Bit Score: 51.73 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 8 IAITDVVLRD-----AHQslfatrLRLEDMLPIAKELDEIGYWSLE-----AWGGATFdaCIRFLGEDPWVRLRELKKAM 77
Cdd:cd07943 1 VYIHDVTLRDgmhavRHQ------FTLEQVRAIARALDAAGVPLIEvghgdGLGGSSL--NYGFAAHTDEEYLEAAAEAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 78 PKTPLQMLLrgqnL--LGYRHYaddvvdrfVERAVANGMSVFRVFDAMNDPRNMKQALQAVRKNGGHAQGTL--SYTTSP 153
Cdd:cd07943 73 KQAKLGVLL----LpgIGTVDD--------LKMAADLGVDVVRVATHCTEADVSEQHIGAARKLGMDVVGFLmmSHMASP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 154 vhtlETWLDVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDI-QLHLHCHATTGMSEMALLKAIEAGVDGVDT 232
Cdd:cd07943 141 ----EELAEQAKLMESYGADCVYVTDSAGAMLPDDVRERVRALREALDPtPVGFHGHNNLGLAVANSLAAVEAGATRIDG 216
|
250 260 270
....*....|....*....|....*....|
gi 737548984 233 AISSMSGTYGHPATEAIVATLQGTPYDTGL 262
Cdd:cd07943 217 SLAGLGAGAGNTPLEVLVAVLERMGIETGI 246
|
|
| DRE_TIM_HCS |
cd07948 |
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ... |
152-234 |
7.87e-07 |
|
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel domain; Homocitrate synthase (HCS) catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate, the first step in the lysine biosynthesis pathway. This family includes the Yarrowia lipolytica LYS1 protein as well as the Saccharomyces cerevisiae LYS20 and LYS21 proteins. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163685 Cd Length: 262 Bit Score: 50.79 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 152 SPVHTLetwLDVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVD 231
Cdd:cd07948 138 SDLVDL---LRVYRAVDKLGVNRVGIADTVGIATPRQVYELVRTLRGVVSCDIEFHGHNDTGCAIANAYAALEAGATHID 214
|
...
gi 737548984 232 TAI 234
Cdd:cd07948 215 TTV 217
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
540-600 |
8.90e-07 |
|
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: 46.67 E-value: 8.90e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737548984 540 AGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:cd06663 13 DGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
541-600 |
2.22e-06 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 50.59 E-value: 2.22e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 541 GNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVI 75
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
168-271 |
2.39e-06 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 50.32 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 168 LEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYGHPATE 247
Cdd:PRK09389 153 IEAGADRICFCDTVGILTPEKTYELFKRLSELVKGPVSIHCHNDFGLAVANTLAALAAGADQVHVTINGIGERAGNASLE 232
|
90 100
....*....|....*....|....*
gi 737548984 248 AIVATL-QGTPYDTGLAIPQIERIA 271
Cdd:PRK09389 233 EVVMALkHLYDVETGIKLEELYELS 257
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
169-232 |
5.08e-06 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 49.02 E-value: 5.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737548984 169 EIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDT 232
Cdd:PRK11858 156 EAGADRVRFCDTVGILDPFTMYELVKELVEAVDIPIEVHCHNDFGMATANALAGIEAGAKQVHT 219
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
169-272 |
8.03e-06 |
|
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163677 [Multi-domain] Cd Length: 259 Bit Score: 47.50 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 169 EIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMSGTYGHPATEA 248
Cdd:cd07939 150 EAGADRLRFADTVGILDPFTTYELIRRLRAATDLPLEFHAHNDLGLATANTLAAVRAGATHVSVTVNGLGERAGNAALEE 229
|
90 100
....*....|....*....|....*
gi 737548984 249 IVATL-QGTPYDTGLAIPQIERIAA 272
Cdd:cd07939 230 VVMALkHLYGRDTGIDTTRLPELSQ 254
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
541-600 |
1.04e-05 |
|
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: 48.33 E-value: 1.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 541 GNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:TIGR01348 14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATL 73
|
|
| DRE_TIM_HOA_like |
cd07944 |
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ... |
125-281 |
2.07e-05 |
|
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of bacterial enzymes is sequence-similar to 4-hydroxy-2-oxovalerate aldolase (HOA) but its exact function is unknown. This family includes the Bacteroides vulgatus Bvu_2661 protein and belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163682 Cd Length: 266 Bit Score: 46.40 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 125 DPRNMKQALQAVRKngGHAQGtlsYTTS--PVH----TLETWLDVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKK 198
Cdd:cd07944 104 HKHEFDEALPLIKA--IKEKG---YEVFfnLMAisgySDEELLELLELVNEIKPDVFYIVDSFGSMYPEDIKRIISLLRS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 199 RYD--IQLHLHCHATTGMSeMAL-LKAIEAGVDGVDTAISSMSGTYGHPATEAIVATL---QGTPYDTglaIPQIERIAA 272
Cdd:cd07944 179 NLDkdIKLGFHAHNNLQLA-LANtLEAIELGVEIIDATVYGMGRGAGNLPTELLLDYLnnkFGKKYNL---EPVLELIDE 254
|
....*....
gi 737548984 273 HFREVRKKY 281
Cdd:cd07944 255 YIAPLKKKY 263
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
534-577 |
1.18e-04 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 39.73 E-value: 1.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 737548984 534 PVNAPMAGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKA 577
Cdd:pfam13533 4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEA 47
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
541-600 |
2.07e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 44.22 E-value: 2.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 541 GNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKAGTVQGIKVKSGDVVGVGDTLMQI 600
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF 74
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
162-271 |
2.40e-04 |
|
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163678 Cd Length: 268 Bit Score: 43.21 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 162 DVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKR---YDIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMS 238
Cdd:cd07940 147 EVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENvpnIKVPISVHCHNDLGLAVANSLAAVEAGARQVECTINGIG 226
|
90 100 110
....*....|....*....|....*....|....*..
gi 737548984 239 GTYGHPATEAIVATL----QGTPYDTGLAIPQIERIA 271
Cdd:cd07940 227 ERAGNAALEEVVMALktryDYYGVETGIDTEELYETS 263
|
|
| PLN03228 |
PLN03228 |
methylthioalkylmalate synthase; Provisional |
163-254 |
7.79e-04 |
|
methylthioalkylmalate synthase; Provisional
Pssm-ID: 178767 [Multi-domain] Cd Length: 503 Bit Score: 42.22 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 163 VTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRY----DIQLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMS 238
Cdd:PLN03228 244 ILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKANTpgidDIVFSVHCHNDLGLATANTIAGICAGARQVEVTINGIG 323
|
90
....*....|....*.
gi 737548984 239 GTYGHPATEAIVATLQ 254
Cdd:PLN03228 324 ERSGNASLEEVVMALK 339
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
534-563 |
8.20e-04 |
|
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: 38.17 E-value: 8.20e-04
10 20 30
....*....|....*....|....*....|
gi 737548984 534 PVNAPMAGNIIKVVVAEGQQVAEGDVLLIL 563
Cdd:cd06850 38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PLN02746 |
PLN02746 |
hydroxymethylglutaryl-CoA lyase |
162-262 |
1.03e-03 |
|
hydroxymethylglutaryl-CoA lyase
Pssm-ID: 178347 Cd Length: 347 Bit Score: 41.70 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737548984 162 DVTEQLLEIGVNSLVIKDMSGILTPMAAYELVSEIKKRYDI-QLHLHCHATTGMSEMALLKAIEAGVDGVDTAISSMS-- 238
Cdd:PLN02746 201 YVAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVdKLAVHFHDTYGQALANILVSLQMGISTVDSSVAGLGgc 280
|
90 100
....*....|....*....|....*...
gi 737548984 239 ----GTYGHPATEAIVATLQGTPYDTGL 262
Cdd:PLN02746 281 pyakGASGNVATEDVVYMLNGLGVSTNV 308
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
520-577 |
2.78e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 40.31 E-value: 2.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737548984 520 ANLAPQATASGSGEP-----VNAPMAGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKA 577
Cdd:COG0845 6 GDVPETVEATGTVEArreveVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQA 68
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
534-577 |
6.22e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 39.26 E-value: 6.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 737548984 534 PVNAPMAGNIIKVVVAEGQQVAEGDVLLILEAMKMETQICAAKA 577
Cdd:COG1566 47 TVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEA 90
|
|
| |
