|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
41-769 |
0e+00 |
|
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: 1138.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 41 RHVKnppqTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVKVSPSPVDPI 120
Cdd:COG1038 423 RGVK----TNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVNGPPGVKGRPKPDFPKPKL 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 121 VPVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFNNLFSIENWG 200
Cdd:COG1038 499 PKVDLGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKIAPATARLLPQLFSLEMWG 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 201 GATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLL 280
Cdd:COG1038 579 GATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEAGIDVFRIFDSLNWVENMRV 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 281 GMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPL 360
Cdd:COG1038 659 AIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKPYAAYKLVKALKEEV-DLPI 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 361 HIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAF 440
Cdd:COG1038 738 HLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLDALQELSNYWEAVRKYYAPF 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 441 DctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSR 520
Cdd:COG1038 818 E--SGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPSSKVVGDMALFMVQNGLTP 895
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 521 AEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELEKDLIDRHGEEVTPEDVL 600
Cdd:COG1038 896 EDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDALRAELEEKLGREPSDRDVL 975
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 601 SAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFELNGQLRSIL 680
Cdd:COG1038 976 SYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDEDGMRTVFFELNGQPREVR 1055
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 681 VKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTL 760
Cdd:COG1038 1056 VRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQV 1135
|
....*....
gi 1958642584 761 EGDDLILEI 769
Cdd:COG1038 1136 EAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
41-770 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 1070.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 41 RHVKnppqTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGPttPIPVKVSPSPVDPI 120
Cdd:PRK12999 424 RGVK----TNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTVNGF--PGVKKKPPVFPDPR 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 121 V-PVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFNNLFSIENW 199
Cdd:PRK12999 498 LpKVDLSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLLRIAPATARLLPNLFSLEMW 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 200 GGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNML 279
Cdd:PRK12999 578 GGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAAAGIDVFRIFDSLNWVENMR 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 280 LGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLP 359
Cdd:PRK12999 658 VAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLKPAAAYELVSALKEEV-DLP 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 360 LHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAA 439
Cdd:PRK12999 737 IHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDLDAIRKLSPYWEAVRPYYAP 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 440 FdcTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLS 519
Cdd:PRK12999 817 F--ESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVTPSSKVVGDMALFMVQNGLT 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 520 RAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELEKDLIDRHGEEVTPEDV 599
Cdd:PRK12999 895 PEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFEAERAELEEKLGREVTDRDV 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 600 LSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFELNGQLRSI 679
Cdd:PRK12999 975 LSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEPDEDGMRTVYFELNGQPREV 1054
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 680 LVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMT 759
Cdd:PRK12999 1055 QVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQ 1134
|
730
....*....|.
gi 1958642584 760 LEGDDLILEIE 770
Cdd:PRK12999 1135 VEAGDLLVELE 1145
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
48-770 |
0e+00 |
|
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: 1054.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 48 QTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGpTTPIPVKVSP--SPVDPIVPVVP 125
Cdd:TIGR01235 423 KTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNG-HPEAKDKLKPleNAPRVVVLYAD 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 126 IGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFNNLFSIENWGGATFD 205
Cdd:TIGR01235 502 QNPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIAPTTSHALPNLFSLECWGGATFD 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 206 VAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAA 285
Cdd:TIGR01235 582 VAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGIDIFRVFDSLNWVENMRVGMDAV 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 286 GSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTH 365
Cdd:TIGR01235 662 AEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAAAKLLIKALREKT-DLPIHFHTH 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 366 DTSGSGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTat 445
Cdd:TIGR01235 741 DTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWIRELSAYWEAVRNLYAAFESD-- 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 446 MKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEA 525
Cdd:TIGR01235 819 LKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSSKVVGDMALFMVSNDLTVDDVVE 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 526 QAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELEKDLIDRHGEEVTPEDVLSAAMY 605
Cdd:TIGR01235 899 PAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIRKDLQEKHEREVSDFDVASYAMY 978
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 606 PDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFELNGQLRSILVKDTQ 685
Cdd:TIGR01235 979 PKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQGEREVFFELNGQPRRIKVPDRS 1058
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 686 AMKEMHFHPKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDL 765
Cdd:TIGR01235 1059 HKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDL 1138
|
....*
gi 1958642584 766 ILEIE 770
Cdd:TIGR01235 1139 LLVLE 1143
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
157-440 |
1.32e-167 |
|
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: 483.86 E-value: 1.32e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 157 LMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFnnLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 236
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 237 GANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDvadpsrTKYSLEYYM 316
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 317 GLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPdLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGM 396
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958642584 397 TSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAF 440
Cdd:cd07937 232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
159-770 |
3.83e-160 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 477.03 E-value: 3.83e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 159 DTTFRDAHQSLLATRVRTHDLKKIAP------YvahnfnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQ 232
Cdd:PRK09282 8 DTTLRDAHQSLLATRMRTEDMLPIAEkldkvgF--------WSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 233 MLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysL 312
Cdd:PRK09282 80 MLLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT---TSPVHT---I 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 313 EYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDS 392
Cdd:PRK09282 154 EKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEV-DLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 393 MSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMksGNSDVYENEIPGGQYTNLHFQAHS 472
Cdd:PRK09282 233 LAFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTI--VDTRVLIHQVPGGMISNLVSQLKE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 473 MGLGSKFKEVKK--AYVEANqmLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGYIGIPHGG 550
Cdd:PRK09282 311 QNALDKLDEVLEeiPRVRED--LGYPPLVTPTSQIVGTQAVLNVLTG-ERYK--------VITKEVKDYVKGLYGRPPAP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 551 FPEPFRSKVLKDLPRIEGRPGASLPPlnlkELEKdlIDRHGEE---VTPEDVLSAAMYPDV----FAQFKDFTATFGPLD 623
Cdd:PRK09282 380 INEELRKKIIGDEEPITCRPADLLEP----ELEK--ARKEAEElgkSEKEDVLTYALFPQIakkfLEEREAGELKPEPEP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 624 SLNTRlfLQGPKIAEEFEVELErGKTLHIKALAVSdlnRAGQRQVFFELNGQLRSILVkdtQAMKEMHFHPKALKDVKGQ 703
Cdd:PRK09282 454 KEAAA--AGAEGIPTEFKVEVD-GEKYEVKIEGVK---AEGKRPFYLRVDGMPEEVVV---EPLKEIVVGGRPRASAPGA 524
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642584 704 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 770
Cdd:PRK09282 525 VTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
155-612 |
3.63e-135 |
|
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: 410.82 E-value: 3.63e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 155 LLLMDTTFRDAHQSLLATRVRTHDLKKIAPY-VAHNFnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQM 233
Cdd:COG5016 4 VKITDTTLRDGHQSLFATRMRTEDMLPIAEKlDEAGF---WSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 234 LLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVAdpsrtkYSLE 313
Cdd:COG5016 81 LLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYTISPV------HTVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 314 YYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSM 393
Cdd:COG5016 155 YYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEAL-DIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 394 SGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMKsgNSDVYENEIPGGQYTNLHFQAHSM 473
Cdd:COG5016 234 AGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGV--DPRVLVHQVPGGMLSNLVSQLKEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 474 GLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGYIGIPHGGFPE 553
Cdd:COG5016 312 GALDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG-ERYK--------MITKEVKDYVLGYYGKTPAPIDP 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642584 554 PFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIdrhgeEVTPEDVLSAAMYPDVFAQF 612
Cdd:COG5016 383 EVRKKALGDEEPITCRPADLLEP-ELEKLRKEGL-----AKSDEDVLTYALFPQVAIKF 435
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
159-760 |
9.16e-130 |
|
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: 398.39 E-value: 9.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 159 DTTFRDAHQSLLATRVRTHDLKKIAPyvAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGA 238
Cdd:TIGR01108 3 DVVLRDAHQSLFATRMRTEDMLPIAE--KLDDVGYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLRGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 239 NAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEYYMGL 318
Cdd:TIGR01108 81 NLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT---TSPVHT---LETYLDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 319 AEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMTS 398
Cdd:TIGR01108 155 AEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRF-GLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 399 QPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSK 478
Cdd:TIGR01108 234 HPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFE--GQLKGPDSRILVAQVPGGMLSNLESQLKEQNALDK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 479 FKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGYIGIPHGGFPEPFRSK 558
Cdd:TIGR01108 312 LDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG-ERYK--------TITKETKGYLKGEYGRTPAPINAELQRK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 559 VLKDL-PRIEGRPGASLPPlNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLntrlfLQGPKIA 637
Cdd:TIGR01108 383 ILGDEkPIVDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQVGLKFLENRHNPAAFEPK-----PEEKVIE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 638 EEfevelergktlHIKAlAVSDLNRAGQRQVFFELNGQLRSILVKD-------TQAMKEMHFHPKALKDVK--GQIGAPM 708
Cdd:TIGR01108 457 QE-----------HAQV-VGKYEETHASGSYTVEVEGKAFVVKVSPggdvsqiTASAPANTSGGTVAAKAGagTPVTAPI 524
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642584 709 PGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKV------HVTKDMTL 760
Cdd:TIGR01108 525 AGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREIlvkvgdAVSVGQVL 582
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
155-763 |
2.40e-105 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 334.98 E-value: 2.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 155 LLLMDTTFRDAHQSLLATRVRTHDLKKIAP------YvahnfnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPN 228
Cdd:PRK14040 5 LAITDVVLRDAHQSLFATRLRLDDMLPIAAkldkvgY--------WSLESWGGATFDACIRFLGEDPWERLRELKKAMPN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 229 IPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRT 308
Cdd:PRK14040 77 TPQQMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT---TSPVHT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 309 kysLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDV 388
Cdd:PRK14040 154 ---LQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRV-DVPLHLHCHATTGLSTATLLKAIEAGIDGVDT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 389 AVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHF 468
Cdd:PRK14040 230 AISSMSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFE--GQLKGVDSRILVAQVPGGMLTNMES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 469 QAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGyigiPH 548
Cdd:PRK14040 308 QLKEQGAADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQAVLNVLTG-ERYK--------TITKETAGVLKG----EY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 549 GGFPEPF----RSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRHGE------EVTPEDVLSAAMYPDV---FAQFKDF 615
Cdd:PRK14040 375 GATPAPVnaelQARVLEGAEPITCRPADLLAP-ELDKLEAELRRQAQEkgitlaENAIDDVLTYALFPQIglkFLENRHN 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 616 TATFGPLDSL-NTRLFLQGPKIAEE-FEVELErGKTLHIKalaVSDlnragqrqvffelNGQLRSILVKDTQAMKEMHFH 693
Cdd:PRK14040 454 PAAFEPVPQAeAAQPAAKAEPAGSEtYTVEVE-GKAYVVK---VSE-------------GGDISQITPAAPAAAPAAAAA 516
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 694 PKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTkdmtlEGD 763
Cdd:PRK14040 517 AAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVK-----EGD 581
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
157-612 |
1.05e-100 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 318.18 E-value: 1.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 157 LMDTTFRDAHQSLLATRVRTHDLKKIApyvaHNFNNL--FSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQML 234
Cdd:PRK12331 6 ITETVLRDGQQSLIATRMTTEEMLPIL----EKLDNAgyHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 235 LRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEY 314
Cdd:PRK12331 82 LRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT---TSPVHT---IDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 315 YMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTsgSGVAAM--LACAQAGADVVDVAVDS 392
Cdd:PRK12331 156 FVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAV-TVPLEVHTHAT--SGIAEMtyLKAIEAGADIIDTAISP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 393 MSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLY-AAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAH 471
Cdd:PRK12331 233 FAGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYrEEGILNPKVKDVEPKTLIYQVPGGMLSNLLSQLK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 472 SMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEAeaqaeelsFPRSVVEFLQGYIGIPHGGF 551
Cdd:PRK12331 313 EQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALMNVISG-ERYKM--------VPNEIKDYVRGLYGRPPAPI 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642584 552 PEPFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRHGEEvtpEDVLSAAMYPDVFAQF 612
Cdd:PRK12331 384 AEEIKKKIIGDEEVITCRPADLIEP-QLEKLREEIAEYAESE---EDVLSYALFPQQAKDF 440
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
453-653 |
3.76e-98 |
|
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: 302.07 E-value: 3.76e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 453 VYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSF 532
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 533 PRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQF 612
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958642584 613 KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIK 653
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
156-770 |
1.31e-93 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 304.34 E-value: 1.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 156 LLMDTTFRDAHQSLLATRVRTHDLKKIAPYVahNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLL 235
Cdd:PRK14042 5 FITDVTLRDAHQCLIATRMRTEDMLPICNKM--DDVGFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSMLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 236 RGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvadpSRTKYSLEYY 315
Cdd:PRK14042 83 RGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT------TSPVHTLDNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 316 MGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRdRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSG 395
Cdd:PRK14042 157 LELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLK-QATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 396 MTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMKSGNSDVYenEIPGGQYTNLHFQAHSMGL 475
Cdd:PRK14042 236 GASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLY--QVPGGMISNLYNQLKEQNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 476 GSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlsraeaeaqAEELSFPRSVVEFLQGYIGIPHGGFPEPF 555
Cdd:PRK14042 314 LDKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQAVINVLTG---------ERYKTITNEVKLYCQGKYGTPPGKISSAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 556 RSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRhgeEVTPEDVLSAAMYPDVFAQFKDFTATFGPL-DSLNTRLFLQGP 634
Cdd:PRK14042 385 RKKAIGRTEVIEVRPGDLLPN-ELDQLQNEISDL---ALSDEDVLLYAMFPEIGRQFLEQRKNNQLIpEPLLTQSSAPDN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 635 KIAEEFEVELErGKTLHIKaLAVSDLNRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVID 714
Cdd:PRK14042 461 SVMSEFDIILH-GESYHVK-VAGYGMIEHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPGSIIA 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642584 715 VKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 770
Cdd:PRK14042 539 IHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
156-645 |
2.38e-93 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 299.39 E-value: 2.38e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 156 LLMDTTFRDAHQSLLATRVRTHDLKKIAPyvAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLL 235
Cdd:PRK14041 4 MFVDTTLRDGHQSLIATRMRTEDMLPALE--AFDRMGFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQMLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 236 RGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEYY 315
Cdd:PRK14041 82 RGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT---VSPVHT---LEYY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 316 MGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSG 395
Cdd:PRK14041 156 LEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 396 MTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGL 475
Cdd:PRK14041 235 GTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYD--VGMKSPDSRILVSQIPGGMYSNLVKQLKEQKM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 476 GSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEaqaeelsfpRSVVEFLQGYIGIPHGGFPEPF 555
Cdd:PRK14041 313 LHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQAVLNVLTGERYKRVT---------NETKNYVKGLYGRPPAPIDEEL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 556 RSKVLKDLPRIEGRPGASLPPlnlkELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFkdftatfgpldsLNTRlFLQGPK 635
Cdd:PRK14041 384 MKKILGDEKPIDCRPADLLEP----ELEKARKELGILAETDEDLLIYVILGEVGKKF------------LKKK-YEEKIG 446
|
490
....*....|
gi 1958642584 636 IAEEFEVELE 645
Cdd:PRK14041 447 VDFNLLEELS 456
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
163-612 |
5.19e-84 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 275.87 E-value: 5.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 163 RDAHQSLLATRVRTHDLKKI------APYvahnfnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 236
Cdd:PRK12330 13 RDAHQSLMATRMAMEDMVGAcedidnAGY--------WSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQMLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 237 GANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEYYM 316
Cdd:PRK12330 85 GQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT---VSPIHT---VEGFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 317 GLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRF-PDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMS- 394
Cdd:PRK12330 159 EQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSMSl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 395 GMTSQPSMgALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATmkSGNSDVYENEIPGGQYTNLHFQAHSMG 474
Cdd:PRK12330 239 GPGHNPTE-SLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTT--GVETEIFKSQIPGGMLSNMESQLKQQG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 475 LGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlsraeaeaqaeelSFPRSVVEF---LQGYIGIPhggf 551
Cdd:PRK12330 316 AGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVFNVLMG-------------RYKVLTGEFadlMLGYYGET---- 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642584 552 PEPFRSKVLKDLPR------IEGRPGASLPPlNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQF 612
Cdd:PRK12330 379 PGERNPEVVEQAKKqakkepITCRPADLLEP-EWDKLRAEALALEGCDGSDEDVLTYALFPQVAPKF 444
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
158-431 |
7.04e-75 |
|
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: 243.52 E-value: 7.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 158 MDTTFRDAHQSLLATRvRTHDLKKIAPYVAHNfnNLFSIENWGGATFDVAmrFLYECPWRRLQELRELIPNIPFQMLLRG 237
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEA--GVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 238 anavgytnypdnvVFKFCEVAKENGMDVFRIFDSLNY--------------LPNMLLGMEAAGSAGGVVEAAISYTgdva 303
Cdd:cd03174 76 -------------REKGIERALEAGVDEVRIFDSASEthsrknlnksreedLENAEEAIEAAKEAGLEVEGSLEDA---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 304 dpSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGA 383
Cdd:cd03174 139 --FGCKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958642584 384 DVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWE 431
Cdd:cd03174 217 DRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
152-633 |
9.84e-67 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 228.85 E-value: 9.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 152 HQGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVahNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPF 231
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDMLPVLTIL--DKIGYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 232 QMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvadpSRTKYS 311
Cdd:PRK12581 88 QMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT------TSPVHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 312 LEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRdRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVD 391
Cdd:PRK12581 162 LNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIK-AMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 392 SMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAfDCT--ATMKSGNSDVYENEIPGGQYTNLHFQ 469
Cdd:PRK12581 241 PFSEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYLA-DGIldPSLLFPDPRTLQYQVPGGMLSNMLSQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 470 AHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEaqaeelsfpRSVVEFLQGYIGIPHG 549
Cdd:PRK12581 320 LKQANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVILGKPYQMVS---------KEIKQYLAGDYGKTPA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 550 GFPEPFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRhgeEVTPEDVLSAAMYPDVFAQFkdFTATFGPLDSLNTRL 629
Cdd:PRK12581 391 PVNEDLKRSQIGSAPVTTNRPADQLSP-EFEVLKAEVADL---AQTDEDVLTYALFPSVAKPF--LTTKYQTDDVIKVTA 464
|
....
gi 1958642584 630 FLQG 633
Cdd:PRK12581 465 FIKA 468
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
157-429 |
2.06e-30 |
|
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: 120.91 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 157 LMDTTFRDAHQSLlATRVRTHDLKKIAPyvahnfnnlfSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 236
Cdd:pfam00682 4 ICDTTLRDGEQAL-GVAFSIDEKLAIAR----------ALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 237 GAnavgytnypDNVVFKFCEVAKENGMDVFRIFDSLNYLP-NMLLGM---EAAGSAGGVVEAAISYTGDVA----DPSRT 308
Cdd:pfam00682 73 AR---------EHDIKAAVEALKGAGAVRVHVFIATSDLHrKYKLGKdreEVAKRAVAAVKAARSRGIDVEfspeDASRT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 309 kySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPD-LPLHIHTHDTSGSGVAAMLACAQAGADVVD 387
Cdd:pfam00682 144 --DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVD 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958642584 388 VAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEY 429
Cdd:pfam00682 222 GTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANL 263
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
703-769 |
5.30e-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: 98.64 E-value: 5.30e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642584 703 QIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 769
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
703-769 |
3.69e-19 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 82.26 E-value: 3.69e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642584 703 QIGAPMPGKVID-----VKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 769
Cdd:pfam00364 2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
702-770 |
2.95e-14 |
|
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: 70.31 E-value: 2.95e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642584 702 GQIGAPMPGKV-------IDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 770
Cdd:COG0511 61 GAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
704-766 |
1.36e-12 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 65.22 E-value: 1.36e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642584 704 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLE-GDDLI 766
Cdd:PRK06549 64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNpGDGLI 127
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
702-766 |
3.10e-11 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 62.19 E-value: 3.10e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642584 702 GQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLE-GDDLI 766
Cdd:PRK05641 85 NVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDtGQPLI 150
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
282-390 |
2.11e-10 |
|
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: 62.02 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 282 MEAAGSAGGVVEAAIS------YTGDVaDPSRTkysleyyMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRF 355
Cdd:cd07938 120 AELAKAAGLRVRGYVStafgcpYEGEV-PPERV-------AEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERF 191
|
90 100 110
....*....|....*....|....*....|....*
gi 1958642584 356 PDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAV 390
Cdd:cd07938 192 PDEKLALHFHDTRGQALANILAALEAGVRRFDSSV 226
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
703-770 |
3.49e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 56.72 E-value: 3.49e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642584 703 QIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTK-DMTLEGDDLiLEIE 770
Cdd:PRK08225 3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEgDFVNEGDVL-LEIE 70
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
291-390 |
1.75e-09 |
|
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439889 [Multi-domain] Cd Length: 452 Bit Score: 60.57 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 291 VVEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHD 366
Cdd:COG0119 124 AVKYAKEHGLEVEfsaeDATRT--DPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHN 201
|
90 100
....*....|....*....|....
gi 1958642584 367 TSGSGVAAMLACAQAGADVVDVAV 390
Cdd:COG0119 202 DLGLAVANSLAAVEAGADQVEGTI 225
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
304-390 |
8.38e-07 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 52.25 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 304 DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRfPDLPLHIHTHDTSGSGVAAMLACAQAGA 383
Cdd:PRK09389 136 DASRA--DLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSEL-VKGPVSIHCHNDFGLAVANTLAALAAGA 212
|
....*..
gi 1958642584 384 DVVDVAV 390
Cdd:PRK09389 213 DQVHVTI 219
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
703-769 |
1.30e-06 |
|
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: 46.60 E-value: 1.30e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642584 703 QIGAPM-PGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 769
Cdd:COG0508 9 DLGESMtEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
292-390 |
2.04e-06 |
|
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: 50.14 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 292 VEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFP--DLPLHIHTH 365
Cdd:cd07940 120 VEYAKSHGLDVEfsaeDATRT--DLDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPniKVPISVHCH 197
|
90 100
....*....|....*....|....*
gi 1958642584 366 DTSGSGVAAMLACAQAGADVVDVAV 390
Cdd:cd07940 198 NDLGLAVANSLAAVEAGARQVECTI 222
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
315-396 |
8.90e-06 |
|
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: 47.88 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 315 YMGLAEELVR-------AGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVD 387
Cdd:cd07943 136 HMASPEELAEqaklmesYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRID 215
|
....*....
gi 1958642584 388 VavdSMSGM 396
Cdd:cd07943 216 G---SLAGL 221
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
706-769 |
2.26e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 42.87 E-value: 2.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642584 706 APMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 769
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
309-431 |
5.60e-05 |
|
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: 45.83 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 309 KYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDV 388
Cdd:cd07945 143 RDSPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVLAAVKAGIKGLHT 222
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958642584 389 AVDSMSGMTSQPSMGALVACTKG-TPLDTEVPLERVFDYSEYWE 431
Cdd:cd07945 223 TVNGLGERAGNAPLASVIAVLKDkLKVKTNIDEKRLNRASRLVE 266
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
304-390 |
8.41e-05 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 45.55 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 304 DPSRTKYS-LEYYMGLAEElvrAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAG 382
Cdd:PRK11858 138 DASRTDLDfLIEFAKAAEE---AGADRVRFCDTVGILDPFTMYELVKELVEAV-DIPIEVHCHNDFGMATANALAGIEAG 213
|
....*...
gi 1958642584 383 ADVVDVAV 390
Cdd:PRK11858 214 AKQVHTTV 221
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
704-770 |
1.05e-04 |
|
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: 45.64 E-value: 1.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642584 704 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 770
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
47-75 |
1.26e-04 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 41.71 E-value: 1.26e-04
10 20
....*....|....*....|....*....
gi 1958642584 47 PQTNIPFLQNVLNNQQFLAGIVDTQFIDE 75
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| DRE_TIM_LeuA3 |
cd07941 |
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ... |
348-386 |
3.16e-04 |
|
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel domain; Desulfobacterium autotrophicum LeuA3 is sequence-similar to alpha-isopropylmalate synthase (LeuA) but its exact function is unknown. Members of this family have an N-terminal TIM barrel domain that 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: 163679 Cd Length: 273 Bit Score: 43.21 E-value: 3.16e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1958642584 348 VSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVV 386
Cdd:cd07941 186 VKEVRERLPGVPLGIHAHNDSGLAVANSLAAVEAGATQV 224
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
291-390 |
3.38e-04 |
|
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: 43.26 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 291 VVEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHD 366
Cdd:cd07939 115 LVGRAKDRGLFVSvgaeDASRA--DPDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAAT-DLPLEFHAHN 191
|
90 100
....*....|....*....|....
gi 1958642584 367 TSGSGVAAMLACAQAGADVVDVAV 390
Cdd:cd07939 192 DLGLATANTLAAVRAGATHVSVTV 215
|
|
| PLN02746 |
PLN02746 |
hydroxymethylglutaryl-CoA lyase |
318-429 |
9.29e-04 |
|
hydroxymethylglutaryl-CoA lyase
Pssm-ID: 178347 Cd Length: 347 Bit Score: 42.08 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 318 LAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMT 397
Cdd:PLN02746 202 VAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTVDSSVAGLGGCP 281
|
90 100 110
....*....|....*....|....*....|....*...
gi 1958642584 398 SQPSMGALVACT------KGTPLDTEVPLERVFDYSEY 429
Cdd:PLN02746 282 YAKGASGNVATEdvvymlNGLGVSTNVDLGKLMAAGDF 319
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
704-770 |
1.12e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 42.12 E-value: 1.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642584 704 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 770
Cdd:PRK11855 10 IGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
710-770 |
1.32e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 42.12 E-value: 1.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642584 710 GKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 770
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
710-770 |
2.32e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 41.53 E-value: 2.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642584 710 GKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 770
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
49-79 |
2.83e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 41.12 E-value: 2.83e-03
10 20 30
....*....|....*....|....*....|.
gi 1958642584 49 TNIPFLQNVLNNQQFLAGIVDTQFIDENPEL 79
Cdd:PRK08654 416 TNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
|
|
| PLN03228 |
PLN03228 |
methylthioalkylmalate synthase; Provisional |
313-414 |
3.28e-03 |
|
methylthioalkylmalate synthase; Provisional
Pssm-ID: 178767 [Multi-domain] Cd Length: 503 Bit Score: 40.68 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 313 EYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFP---DLPLHIHTHDTSGSGVAAMLACAQAGADVVDVA 389
Cdd:PLN03228 239 EFLCKILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKANTPgidDIVFSVHCHNDLGLATANTIAGICAGARQVEVT 318
|
90 100
....*....|....*....|....*..
gi 1958642584 390 VDSMSGMTSQPSMGALVACTK--GTPL 414
Cdd:PLN03228 319 INGIGERSGNASLEEVVMALKcrGAYL 345
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
696-770 |
3.49e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 40.76 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642584 696 ALKDVKgqigapMP------GKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 769
Cdd:PRK11854 205 GVKDVN------VPdiggdeVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF 278
|
.
gi 1958642584 770 E 770
Cdd:PRK11854 279 E 279
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
48-81 |
4.56e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 40.09 E-value: 4.56e-03
10 20 30
....*....|....*....|....*....|....
gi 1958642584 48 QTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQ 81
Cdd:PRK07178 415 KTTIPYYQEILRNPEFRSGQFNTSFVESHPELTN 448
|
|
| PRK08195 |
PRK08195 |
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated |
317-390 |
4.82e-03 |
|
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
Pssm-ID: 181282 [Multi-domain] Cd Length: 337 Bit Score: 39.82 E-value: 4.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642584 317 GLAEE---LVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRF-PDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAV 390
Cdd:PRK08195 145 KLAEQaklMESYGAQCVYVVDSAGALLPEDVRDRVRALRAALkPDTQVGFHGHNNLGLGVANSLAAVEAGATRIDGSL 222
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
710-770 |
8.13e-03 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 39.39 E-value: 8.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642584 710 GKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTkdmtlEGD-----DLILEIE 770
Cdd:PRK11856 17 GEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVE-----EGDvvpvgSVIAVIE 77
|
|
| |
