|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-1150 |
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: 2267.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1 MPISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPHlerdlgPIESYLAIDEIIRVAKL 80
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKG------PVDAYLDIEEIIRVAKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 81 SGADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIG 160
Cdd:COG1038 76 KGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 161 YPVMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQ 240
Cdd:COG1038 156 YPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 241 RRNQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDAnTGKFYFIEVNPRIQVEHTVTEVVTGIDIVKA 320
Cdd:COG1038 236 RRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDD-DGNFYFIEVNPRIQVEHTVTEEVTGIDIVQS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 321 QIHILDGHAIGTPESGVPKQADIRLNGHALQCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDGGTAYSGAIITRYYDP 400
Cdd:COG1038 315 QILIAEGYSLDDPEIGIPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 401 LLVKVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFIDTTPELFQQVKRQDRATKLLTYL 480
Cdd:COG1038 395 LLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 481 ADVTVNGHPEVKGRPKPpaDAAEPVVPYID--ADIKPGTKQLLDELGPKKFGDWMRNEKRILMTDTTMRDGHQSLLATRV 558
Cdd:COG1038 475 GDVTVNGPPGVKGRPKP--DFPKPKLPKVDlgAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 559 RTHDIARIADTYARALPNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQMLLRGANGVGYKNYPDNVVKYF 638
Cdd:COG1038 553 RTRDMLKIAPATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAF 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 639 VRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTGDLLNSARPKYDLKYYTALAAELEKAGAHIIAVKD 718
Cdd:COG1038 633 VKEAAEAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKD 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 719 MAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAFSGNTSQPCLGSIVEALRGSERD 798
Cdd:COG1038 713 MAGLLKPYAAYKLVKALKEEVDLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERD 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 799 PGLDPHWIRRLSFYWEAVRTQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLETRWHEVAQAYADANQMFGDIV 878
Cdd:COG1038 793 TGLDLDALQELSNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIV 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 879 KVTPSSKVVGDMALMMVSQDLSVAEVENPAKDIAFPDSVVSMLKGDLGQPPGGWPEALQKKVLKGEEPYTAVPGSLLPPA 958
Cdd:COG1038 873 KVTPSSKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPV 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 959 DLDAERKVIEEKLGREVSDFEFASYLMYPKVFTDYALAADMYGPVSVIPTPQYFYGLPAGEELFLDLEKGKTLVIVNQAL 1038
Cdd:COG1038 953 DFDALRAELEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAI 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1039 GHTDDKGMVTVFFELNGQPRRIKVPDRAHgASGSAVRRKAETGNTAQLGAPMPGVISQVSVSAGQTVKSGDVLLSIEAMK 1118
Cdd:COG1038 1033 GEPDEDGMRTVFFELNGQPREVRVRDRSV-KVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMK 1111
|
1130 1140 1150
....*....|....*....|....*....|..
gi 1059519736 1119 METALHADRDGTIAEVLVRIGDQIDAKDLLIV 1150
Cdd:COG1038 1112 METTITAPRDGTVKEVLVKEGDQVEAGDLLIE 1143
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-1152 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 2181.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1 MPISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPHlerdlgPIESYLAIDEIIRVAKL 80
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKH------PVRAYLDIDEIIRVAKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 81 SGADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIG 160
Cdd:PRK12999 77 AGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 161 YPVMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQ 240
Cdd:PRK12999 157 YPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 241 RRNQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANtGKFYFIEVNPRIQVEHTVTEVVTGIDIVKA 320
Cdd:PRK12999 237 RRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDAD-GNFYFIEVNPRIQVEHTVTEEVTGIDIVQS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 321 QIHILDGHAIGTPESGVPKQADIRLNGHALQCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDGGTAYSGAIITRYYDP 400
Cdd:PRK12999 316 QILIAEGATLHDLEIGIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 401 LLVKVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFIDTTPELFQQVKRQDRATKLLTYL 480
Cdd:PRK12999 396 LLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 481 ADVTVNGHPEVKGRPKppaDAAEPVVPYIDAD--IKPGTKQLLDELGPKKFGDWMRNEKRILMTDTTMRDGHQSLLATRV 558
Cdd:PRK12999 476 ADVTVNGFPGVKKKPP---VFPDPRLPKVDLSapPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 559 RTHDIARIADTYARALPNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQMLLRGANGVGYKNYPDNVVKYF 638
Cdd:PRK12999 553 RTKDLLRIAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAF 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 639 VRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTGDLLNSARPKYDLKYYTALAAELEKAGAHIIAVKD 718
Cdd:PRK12999 633 VREAAAAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKD 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 719 MAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAFSGNTSQPCLGSIVEALRGSERD 798
Cdd:PRK12999 713 MAGLLKPAAAYELVSALKEEVDLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERD 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 799 PGLDPHWIRRLSFYWEAVRTQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLETRWHEVAQAYADANQMFGDIV 878
Cdd:PRK12999 793 TGLDLDAIRKLSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIV 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 879 KVTPSSKVVGDMALMMVSQDLSVAEVENPAKDIAFPDSVVSMLKGDLGQPPGGWPEALQKKVLKGEEPYTAVPGSLLPPA 958
Cdd:PRK12999 873 KVTPSSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPV 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 959 DLDAERKVIEEKLGREVSDFEFASYLMYPKVFTDYALAADMYGPVSVIPTPQYFYGLPAGEELFLDLEKGKTLVIVNQAL 1038
Cdd:PRK12999 953 DFEAERAELEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAI 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1039 GHTDDKGMVTVFFELNGQPRRIKVPDRAHgASGSAVRRKAETGNTAQLGAPMPGVISQVSVSAGQTVKSGDVLLSIEAMK 1118
Cdd:PRK12999 1033 GEPDEDGMRTVYFELNGQPREVQVRDRSV-KSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMK 1111
|
1130 1140 1150
....*....|....*....|....*....|....
gi 1059519736 1119 METALHADRDGTIAEVLVRIGDQIDAKDLLIVYS 1152
Cdd:PRK12999 1112 METTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
5-1151 |
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: 1992.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 5 KILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPhlerDLGPIESYLAIDEIIRVAKLSGAD 84
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGP----DLGPIEAYLSIDEIIRVAKLNGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 85 AIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIGYPVM 164
Cdd:TIGR01235 77 AIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 165 LKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQRRNQ 244
Cdd:TIGR01235 157 IKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 245 KVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANtGKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQIHI 324
Cdd:TIGR01235 237 KVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDND-GKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 325 LDGHAIGTPESGVPKQADIRLNGHALQCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDGGTAYSGAIITRYYDPLLVK 404
Cdd:TIGR01235 316 ADGASLPTPQLGVPNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 405 VTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFIDTTPELFQQVKRQDRATKLLTYLADVT 484
Cdd:TIGR01235 396 VSAWASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 485 VNGHPEVKGRPKPPADAAEPVVPYID-ADIKPGTKQLLDELGPKKFGDWMRNEKRILMTDTTMRDGHQSLLATRVRTHDI 563
Cdd:TIGR01235 476 VNGHPEAKDKLKPLENAPRVVVLYADqNPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 564 ARIADTYARALPNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQMLLRGANGVGYKNYPDNVVKYFVRQAA 643
Cdd:TIGR01235 556 AKIAPTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 644 QGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTGDLLNSARPKYDLKYYTALAAELEKAGAHIIAVKDMAGLL 723
Cdd:TIGR01235 636 QGGIDIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLL 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 724 KPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAFSGNTSQPCLGSIVEALRGSERDPGLDP 803
Cdd:TIGR01235 716 KPAAAKLLIKALREKTDLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNV 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 804 HWIRRLSFYWEAVRTQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLETRWHEVAQAYADANQMFGDIVKVTPS 883
Cdd:TIGR01235 796 AWIRELSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPS 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 884 SKVVGDMALMMVSQDLSVAEVENPAKDIAFPDSVVSMLKGDLGQPPGGWPEALQKKVLKGEEPYTAVPGSLLPPADLDAE 963
Cdd:TIGR01235 876 SKVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAI 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 964 RKVIEEKLGREVSDFEFASYLMYPKVFTDYALAADMYGPVSVIPTPQYFYGLPAGEELFLDLEKGKTLVIVNQALGHTDD 1043
Cdd:TIGR01235 956 RKDLQEKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDS 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1044 KGMVTVFFELNGQPRRIKVPDRAHGASgSAVRRKAETGNTAQLGAPMPGVISQVSVSAGQTVKSGDVLLSIEAMKMETAL 1123
Cdd:TIGR01235 1036 QGEREVFFELNGQPRRIKVPDRSHKAE-AAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAI 1114
|
1130 1140
....*....|....*....|....*...
gi 1059519736 1124 HADRDGTIAEVLVRIGDQIDAKDLLIVY 1151
Cdd:TIGR01235 1115 QAPKDGTIKEVLVKAGEQIDAKDLLLVL 1142
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
2-473 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 678.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 2 PISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPhlerdlgPIESYLAIDEIIRVAKLS 81
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAP-------AAESYLNIDAIIAAAKAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 82 GADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIGY 161
Cdd:COG4770 74 GADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 162 PVMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQR 241
Cdd:COG4770 154 PVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 242 RNQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANtGKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQ 321
Cdd:COG4770 234 RHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDAD-GNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 322 IHILDGHAIGtpesgvPKQADIRLNGHALQCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDGGtAYSGAIITRYYDPL 401
Cdd:COG4770 313 IRIAAGEPLP------FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSM 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1059519736 402 LVKVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFIDTT-PELFQQVKRQDRA 473
Cdd:COG4770 386 IAKLIVWGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERElAELLAAAAPEELA 458
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
3-458 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 584.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 3 ISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPhlerdlgPIESYLAIDEIIRVAKLSG 82
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAP-------SKKSYLNIPAIISAAEITG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 83 ADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIGYP 162
Cdd:PRK08591 75 ADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 163 VMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQRR 242
Cdd:PRK08591 155 VIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 243 NQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANtGKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQI 322
Cdd:PRK08591 235 HQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKN-GEFYFIEMNTRIQVEHPVTEMITGVDLVKEQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 323 HILDGHAIGTpesgvpKQADIRLNGHALQCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDGGtAYSGAIITRYYDPLL 402
Cdd:PRK08591 314 RIAAGEPLSI------KQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMI 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1059519736 403 VKVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFID 458
Cdd:PRK08591 387 GKLIVHGETREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLE 442
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
4-469 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 558.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 4 SKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPhlerdlgPIESYLAIDEIIRVAKLSGA 83
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAP-------PSKSYLNIERIIDVAKKAGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 84 DAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIGYPV 163
Cdd:PRK08654 76 DAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 164 MLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQRRN 243
Cdd:PRK08654 156 IIKASAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 244 QKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDanTGKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQIH 323
Cdd:PRK08654 236 QKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 324 ILDGHAIGTpesgvpKQADIRLNGHALQCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDGGTaYSGAIITRYYDPLLV 403
Cdd:PRK08654 314 IAAGEELSF------KQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGV-HMGYEIPPYYDSMIS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1059519736 404 KVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFIDTTPELFQQVKR 469
Cdd:PRK08654 387 KLIVWGRTREEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILEEMKR 452
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
3-457 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 540.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 3 ISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPhlerdlgPIESYLAIDEIIRVAKLSG 82
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPR-------VQESYLNLEKIIEIAKKTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 83 ADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIGYP 162
Cdd:PRK06111 75 AEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 163 VMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQRR 242
Cdd:PRK06111 155 VMLKASAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 243 NQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDaNTGKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQI 322
Cdd:PRK06111 235 HQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVD-EQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 323 HILDGHAIGTpesgvpKQADIRLNGHALQCRITTEDPeQNFIPDYGRITAYRSAAGFGIRLDGGTAySGAIITRYYDPLL 402
Cdd:PRK06111 314 RIAAGEKLSF------TQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMI 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1059519736 403 VKVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFI 457
Cdd:PRK06111 386 AKLIAHGETREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-472 |
1.16e-173 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 519.27 E-value: 1.16e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 3 ISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPhlerdlgpIESYLAIDEIIRVAKLSG 82
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP--------LAGYLNPRRLVNLAVETG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 83 ADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIGYP 162
Cdd:PRK07178 74 CDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 163 VMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQRR 242
Cdd:PRK07178 154 VMLKATSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 243 NQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANtGKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQI 322
Cdd:PRK07178 234 NQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDAD-GEVYFMEMNTRVQVEHTITEEITGIDIVREQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 323 HIldghAIGTPESgvPKQADIRLNGHALQCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDGGTaYSGAIITRYYDPLL 402
Cdd:PRK07178 313 RI----ASGLPLS--YKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAI-YTGYTIPPYYDSMC 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1059519736 403 VKVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFIDTTPELFQ-QVKRQDR 472
Cdd:PRK07178 386 AKLIVWALTWEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNySIKRKPE 456
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-457 |
1.74e-169 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 507.33 E-value: 1.74e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 3 ISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESyqVGRGPHLERDlgpieSYLAIDEIIRVAKLSG 82
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEA--VCIGPASSKD-----SYLNIQNIISATVLTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 83 ADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIGYP 162
Cdd:PRK05586 75 AQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 163 VMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQRR 242
Cdd:PRK05586 155 VMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 243 NQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANtGKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQI 322
Cdd:PRK05586 235 NQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKD-GNFYFMEMNTRIQVEHPITEMITGVDLVKEQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 323 HILDGHAIGTpesgvpKQADIRLNGHALQCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDgGTAYSGAIITRYYDPLL 402
Cdd:PRK05586 314 KIAYGEKLSI------KQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVD-SAVYSGYTIPPYYDSMI 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1059519736 403 VKVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFI 457
Cdd:PRK05586 387 GKLIVYGKDREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFI 441
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
3-459 |
1.36e-168 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 505.07 E-value: 1.36e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 3 ISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPhlerdlgPIESYLAIDEIIRVAKLSG 82
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAP-------SAKSYLNIPNIISAAEITG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 83 ADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIGYP 162
Cdd:TIGR00514 75 ADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 163 VMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQRR 242
Cdd:TIGR00514 155 VIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 243 NQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANtGKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQI 322
Cdd:TIGR00514 235 HQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKN-GEFYFMEMNTRIQVEHPVTEMITGVDLIKEQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 323 HIldghAIGTPESgvPKQADIRLNGHALQCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDgGTAYSGAIITRYYDPLL 402
Cdd:TIGR00514 314 RI----AAGEPLS--LKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWD-SHVYSGYTVPPYYDSMI 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1059519736 403 VKVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFIDT 459
Cdd:TIGR00514 387 GKLITYGKTREVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
537-1150 |
3.57e-164 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 498.98 E-value: 3.57e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 537 KRILMTDTTMRDGHQSLLATRVRTHDIARIADTYARAlpNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQ 616
Cdd:PRK09282 2 KKVKITDTTLRDAHQSLLATRMRTEDMLPIAEKLDKV--GFWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 617 MLLRGANGVGYKNYPDNVVKYFVRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTgdllnsARPKYDL 696
Cdd:PRK09282 80 MLLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT------TSPVHTI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 697 KYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAF 776
Cdd:PRK09282 154 EKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEVDLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 777 SGNTSQPCLGSIVEALRGSERDPGLDPHWIRRLSFYWEAVRTQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGL 856
Cdd:PRK09282 234 AFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTIVDTRVLIHQVPGGMISNLVSQLKEQNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 857 ETRWHEVAQAYADANQMFGDIVKVTPSSKVVGDMALMMVSQDLSVAEVENPAKDiafpdsvvsMLKGDLGQPPGGWPEAL 936
Cdd:PRK09282 314 LDKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTGERYKVITKEVKD---------YVKGLYGRPPAPINEEL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 937 QKKVLKGEEPYTAVPGSLLPPaDLDAERKVIEEKLGREVSDfeFASYLMYPKV---FTDYALAADMYGPVSVIPTPQY-F 1012
Cdd:PRK09282 385 RKKIIGDEEPITCRPADLLEP-ELEKARKEAEELGKSEKED--VLTYALFPQIakkFLEEREAGELKPEPEPKEAAAAgA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1013 YGLPAGEELFLDLEKgktlviVNQALGHTDDKGMVTVFFELNGQPRRIKVPdrAHGASGSAVRRKAETGNTAQlgAPMPG 1092
Cdd:PRK09282 462 EGIPTEFKVEVDGEK------YEVKIEGVKAEGKRPFYLRVDGMPEEVVVE--PLKEIVVGGRPRASAPGAVT--SPMPG 531
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1059519736 1093 VISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLIV 1150
Cdd:PRK09282 532 TVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLME 589
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
542-823 |
8.63e-164 |
|
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: 485.78 E-value: 8.63e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 542 TDTTMRDGHQSLLATRVRTHDIARIADTYARALpnLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQMLLRG 621
Cdd:cd07937 2 TDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 622 ANGVGYKNYPDNVVKYFVRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTGDllnsarPKYDLKYYTA 701
Cdd:cd07937 80 QNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 702 LAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAFSGNTS 781
Cdd:cd07937 154 LAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVGLPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGGTS 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1059519736 782 QPCLGSIVEALRGSERDPGLDPHWIRRLSFYWEAVRTQYAAF 823
Cdd:cd07937 234 QPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-473 |
2.58e-160 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 484.26 E-value: 2.58e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1 MPISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGrGPHLERdlgpieSYLAIDEIIRVAKL 80
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIG-PSHAAK------SYLNPAAILAAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 81 SGADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIG 160
Cdd:PRK12833 76 CGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 161 YPVMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHgNVVHLFERDCSIQ 240
Cdd:PRK12833 156 YPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 241 RRNQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANTGKFYFIEVNPRIQVEHTVTEVVTGIDIVKA 320
Cdd:PRK12833 235 RRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 321 QIHILDGHAIGTpesgvpKQADIRLNGHALQCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDgGTAYSGAIITRYYDP 400
Cdd:PRK12833 315 MLRIADGEPLRF------AQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVD-SLLYPGYRVPPFYDS 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1059519736 401 LLVKVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFIDT-TPELFQQVKRQDRA 473
Cdd:PRK12833 388 LLAKLIVHGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEAwLAEWRAALDAAASA 461
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
541-1148 |
1.13e-150 |
|
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: 463.49 E-value: 1.13e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 541 MTDTTMRDGHQSLLATRVRTHDIARIADTYARAlpNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQMLLR 620
Cdd:TIGR01108 1 ITDVVLRDAHQSLFATRMRTEDMLPIAEKLDDV--GYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 621 GANGVGYKNYPDNVVKYFVRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTgdllnsARPKYDLKYYT 700
Cdd:TIGR01108 79 GQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT------TSPVHTLETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 701 ALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAFSGNT 780
Cdd:TIGR01108 153 DLAEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRFGLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 781 SQPCLGSIVEALRGSERDPGLDPHWIRRLSFYWEAVRTQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLETRW 860
Cdd:TIGR01108 233 SHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFEGQLKGPDSRILVAQVPGGMLSNLESQLKEQNALDKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 861 HEVAQAYADANQMFGDIVKVTPSSKVVGDMALMMVSQDLSVAEVENPAKDIafpdsvvsmLKGDLGQPPGGWPEALQKKV 940
Cdd:TIGR01108 313 DEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTGERYKTITKETKGY---------LKGEYGRTPAPINAELQRKI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 941 LKGEEP-YTAVPGSLLPPaDLDAERKVIEEKLGREVSDFEFASYLMYPKVFTDYalAADMYGPVSVIPTPQyfyglpage 1019
Cdd:TIGR01108 384 LGDEKPiVDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQVGLKF--LENRHNPAAFEPKPE--------- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1020 elfldlEKGKTLVIVNQALGHTDDKGMVTVFFELNGQPRRIKV----------PDRAHGASGSAVRRKAETGNTaqLGAP 1089
Cdd:TIGR01108 452 ------EKVIEQEHAQVVGKYEETHASGSYTVEVEGKAFVVKVspggdvsqitASAPANTSGGTVAAKAGAGTP--VTAP 523
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1059519736 1090 MPGVISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLL 1148
Cdd:TIGR01108 524 IAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAVSVGQVL 582
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
3-459 |
1.60e-150 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 459.28 E-value: 1.60e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 3 ISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPhlerdlgpIESYLAIDEIIRVAKLSG 82
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDP--------IKGYLDVKRIVEIAKACG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 83 ADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAE-IHRLAAEIGY 161
Cdd:PRK08463 74 ADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEeIKIFARKIGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 162 PVMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQR 241
Cdd:PRK08463 154 PVILKASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 242 RNQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANTgKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQ 321
Cdd:PRK08463 234 RHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYN-RFYFMEMNTRIQVEHGVTEEITGIDLIVRQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 322 IHILDGHAIGTpesgvpKQADIRLNGHALQCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDgGTAYSGAIITRYYDPL 401
Cdd:PRK08463 313 IRIAAGEILDL------EQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVD-SHIYKDYTIPPYYDSM 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1059519736 402 LVKVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFIDT 459
Cdd:PRK08463 386 LAKLIVKATSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIET 443
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
537-993 |
4.87e-150 |
|
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: 460.51 E-value: 4.87e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 537 KRILMTDTTMRDGHQSLLATRVRTHDIARIADTYARAlpNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQ 616
Cdd:COG5016 2 KKVKITDTTLRDGHQSLFATRMRTEDMLPIAEKLDEA--GFWSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 617 MLLRGANGVGYKNYPDNVVKYFVRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTGDllnsarPKYDL 696
Cdd:COG5016 80 MLLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYTIS------PVHTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 697 KYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAF 776
Cdd:COG5016 154 EYYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEALDIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 777 SGNTSQPCLGSIVEALRGSERDPGLDPHWIRRLSFYWEAVRTQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGL 856
Cdd:COG5016 234 AGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGVDPRVLVHQVPGGMLSNLVSQLKEQGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 857 ETRWHEVAQAYADANQMFGDIVKVTPSSKVVGDMALMMVsqdLSVAEVENPakdiafPDSVVSMLKGDLGQPPGGWPEAL 936
Cdd:COG5016 314 LDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNV---LTGERYKMI------TKEVKDYVLGYYGKTPAPIDPEV 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1059519736 937 QKKVLKGEEPYTAVPGSLLPPaDLDAERKVieeklGREVSDFEFASYLMYPKVFTDY 993
Cdd:COG5016 385 RKKALGDEEPITCRPADLLEP-ELEKLRKE-----GLAKSDEDVLTYALFPQVAIKF 435
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-459 |
2.32e-143 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 439.18 E-value: 2.32e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1 MPISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGrGPHLErdlgpiESYLAIDEIIRVAKL 80
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIG-GAKSS------ESYLNIPAIISAAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 81 SGADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIG 160
Cdd:PRK08462 75 FEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 161 YPVMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQ 240
Cdd:PRK08462 155 YPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 241 RRNQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANTgKFYFIEVNPRIQVEHTVTEVVTGIDIVKA 320
Cdd:PRK08462 235 RRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNL-DFYFMEMNTRLQVEHTVSEMVSGLDLIEW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 321 QIHILDGHAIgtpesgvPKQADIRLNGHALQCRITTEDPEQnFIPDYGRITAYRSAAGFGIRLDgGTAYSGAIITRYYDP 400
Cdd:PRK08462 314 MIKIAEGEEL-------PSQESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPGGRNVRMD-SHAYAGYVVPPYYDS 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1059519736 401 LLVKVTASGSTPQEAISRMDRALREFRIRGVATNLTFLEAIIGHPSFRDNSYTTRFIDT 459
Cdd:PRK08462 385 MIGKLIVWGEDRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
537-1149 |
2.06e-125 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 397.38 E-value: 2.06e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 537 KRILMTDTTMRDGHQSLLATRVRTHDIARIADTYARAlpNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQ 616
Cdd:PRK14040 3 KPLAITDVVLRDAHQSLFATRLRLDDMLPIAAKLDKV--GYWSLESWGGATFDACIRFLGEDPWERLRELKKAMPNTPQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 617 MLLRGANGVGYKNYPDNVVKYFVRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTgdllnsARPKYDL 696
Cdd:PRK14040 81 MLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT------TSPVHTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 697 KYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAF 776
Cdd:PRK14040 155 QTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRVDVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAISSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 777 SGNTSQPCLGSIVEALRGSERDPGLDPHWIRRLSFYWEAVRTQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGL 856
Cdd:PRK14040 235 SMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNMESQLKEQGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 857 ETRWHEVAQAYADANQMFGDIVKVTPSSKVVGDMALMMVsqdLSVAEVENPAKDIAfpdsvvSMLKGDLGQPPGGWPEAL 936
Cdd:PRK14040 315 ADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQAVLNV---LTGERYKTITKETA------GVLKGEYGATPAPVNAEL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 937 QKKVLKGEEPYTAVPGSLLPP--ADLDAE--RKVIEE--KLGREVSDfEFASYLMYPKV---FTDYALAADMYGPV-SVI 1006
Cdd:PRK14040 386 QARVLEGAEPITCRPADLLAPelDKLEAElrRQAQEKgiTLAENAID-DVLTYALFPQIglkFLENRHNPAAFEPVpQAE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1007 PTPQYFYGLPAGEELFLDLEKGKTLVI-VNQAlghtddkgmvtvffelnGQPRRIKvPDRAHGASGSAVRRKAETGNTAQ 1085
Cdd:PRK14040 465 AAQPAAKAEPAGSETYTVEVEGKAYVVkVSEG-----------------GDISQIT-PAAPAAAPAAAAAAAPAAAAGEP 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1059519736 1086 LGAPMPGVISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLI 1149
Cdd:PRK14040 527 VTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
537-993 |
3.01e-111 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 354.78 E-value: 3.01e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 537 KRILMTDTTMRDGHQSLLATRVRTHDIARIADTYARAlpNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQ 616
Cdd:PRK12331 2 TKIKITETVLRDGQQSLIATRMTTEEMLPILEKLDNA--GYHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 617 MLLRGANGVGYKNYPDNVVKYFVRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTgdllnsARPKYDL 696
Cdd:PRK12331 80 MLLRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT------TSPVHTI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 697 KYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAF 776
Cdd:PRK12331 154 DYFVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAVTVPLEVHTHATSGIAEMTYLKAIEAGADIIDTAISPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 777 SGNTSQPCLGSIVEALRGSERDPGLDPHWIRRLSFYWEAVRTQYAAfESDL----KGPASEVYLHEMPGGQFTNLKEQAR 852
Cdd:PRK12331 234 AGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYRE-EGILnpkvKDVEPKTLIYQVPGGMLSNLLSQLK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 853 SLGLETRWHEVAQAYADANQMFGDIVKVTPSSKVVGDMALMMVSQDLSVAEVENPAKDiafpdsvvsMLKGDLGQPPGGW 932
Cdd:PRK12331 313 EQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALMNVISGERYKMVPNEIKD---------YVRGLYGRPPAPI 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1059519736 933 PEALQKKVLKGEEPYTAVPGSLLPPaDLDAERKVIEEKLGrevSDFEFASYLMYPKVFTDY 993
Cdd:PRK12331 384 AEEIKKKIIGDEEVITCRPADLIEP-QLEKLREEIAEYAE---SEEDVLSYALFPQQAKDF 440
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
538-1149 |
5.81e-102 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 334.77 E-value: 5.81e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 538 RILMTDTTMRDGHQSLLATRVRTHDIARIADTYARAlpNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQM 617
Cdd:PRK14042 3 KTFITDVTLRDAHQCLIATRMRTEDMLPICNKMDDV--GFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 618 LLRGANGVGYKNYPDNVVKYFVRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTgdllnsARPKYDLK 697
Cdd:PRK14042 81 LLRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT------TSPVHTLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 698 YYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAFS 777
Cdd:PRK14042 155 NFLELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 778 GNTSQPCLGSIVEALRGSERDPGLDPHWIRRLSFYWEAVRTQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLE 857
Cdd:PRK14042 235 GGASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 858 TRWHEVAQAYADANQMFGDIVKVTPSSKVVGDMALMMVSQDLSVAEVENPAKdiafpdsvvSMLKGDLGQPPGGWPEALQ 937
Cdd:PRK14042 315 DKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQAVINVLTGERYKTITNEVK---------LYCQGKYGTPPGKISSALR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 938 KKVLKGEEPYTAVPGSLLpPADLDaerkvieeKLGREVSDFEFAS-----YLMYPKVFTDYalaADMYGPVSVIPTPQYF 1012
Cdd:PRK14042 386 KKAIGRTEVIEVRPGDLL-PNELD--------QLQNEISDLALSDedvllYAMFPEIGRQF---LEQRKNNQLIPEPLLT 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1013 YGLPAGEELFLDLE---KGKTLVIVNQALGHTdDKGMVTVFFELNGQPRRIKV--PDRAHGASGSAVRRKAETGNtaqLG 1087
Cdd:PRK14042 454 QSSAPDNSVMSEFDiilHGESYHVKVAGYGMI-EHGQQSCFLWVDGVPEEVVVqhSELHDKIERSSVNNKIGPGD---IT 529
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1059519736 1088 APMPGVISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLI 1149
Cdd:PRK14042 530 VAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLI 591
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
537-989 |
1.30e-101 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 329.44 E-value: 1.30e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 537 KRILMTDTTMRDGHQSLLATRVRTHDIARIADTYARAlpNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQ 616
Cdd:PRK14041 1 MKVMFVDTTLRDGHQSLIATRMRTEDMLPALEAFDRM--GFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 617 MLLRGANGVGYKNYPDNVVKYFVRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTgdllnsARPKYDL 696
Cdd:PRK14041 79 MLLRGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT------VSPVHTL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 697 KYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAF 776
Cdd:PRK14041 153 EYYLEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKFGVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 777 SGNTSQPCLGSIVEALRGSERDPGLDPHWIRRLSFYWEAVRTQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGL 856
Cdd:PRK14041 233 SMGTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYDVGMKSPDSRILVSQIPGGMYSNLVKQLKEQKM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 857 ETRWHEVAQAYADANQMFGDIVKVTPSSKVVGDMALMMVSQDLSVAEVENPAKDiafpdsvvsMLKGDLGQPPGGWPEAL 936
Cdd:PRK14041 313 LHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQAVLNVLTGERYKRVTNETKN---------YVKGLYGRPPAPIDEEL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1059519736 937 QKKVLKGEEPYTAVPGSLLPPaDLDAERKvieeKLGREV-SDFEFASYLMYPKV 989
Cdd:PRK14041 384 MKKILGDEKPIDCRPADLLEP-ELEKARK----ELGILAeTDEDLLIYVILGEV 432
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
834-1034 |
3.01e-101 |
|
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: 318.25 E-value: 3.01e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 834 VYLHEMPGGQFTNLKEQARSLGLETRWHEVAQAYADANQMFGDIVKVTPSSKVVGDMALMMVSQDLSVAEVENPAKDIAF 913
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 914 PDSVVSMLKGDLGQPPGGWPEALQKKVLKGEEPYTAVPGSLLPPADLDAERKVIEEKLGREVSDFEFASYLMYPKVFTDY 993
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1059519736 994 ALAADMYGPVSVIPTPQYFYGLPAGEELFLDLEKGKTLVIV 1034
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
537-1009 |
7.80e-87 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 290.12 E-value: 7.80e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 537 KRILMTDTTMRDGHQSLLATRVRTHDIARIADTYARAlpNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQ 616
Cdd:PRK12330 3 RKIGVTELALRDAHQSLMATRMAMEDMVGACEDIDNA--GYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 617 MLLRGANGVGYKNYPDNVVKYFVRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTgdllnsARPKYDL 696
Cdd:PRK12330 81 MLLRGQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT------VSPIHTV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 697 KYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETG--LPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMD 774
Cdd:PRK12330 155 EGFVEQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACGedTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAIS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 775 AFSGNTSQPCLGSIVEALRGSERDPGLDPHWIRRLSFYWEAVRTQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSL 854
Cdd:PRK12330 235 SMSLGPGHNPTESLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTTGVETEIFKSQIPGGMLSNMESQLKQQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 855 GLETRWHEVAQAYADANQMFGDIVKVTPSSKVVGDMA---LMMVSQDLSVAEvenpakdiaFPDsvvsMLKGDLGQPPGG 931
Cdd:PRK12330 315 GAGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAvfnVLMGRYKVLTGE---------FAD----LMLGYYGETPGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 932 W-PEALQK-KVLKGEEPYTAVPGSLLPP--ADLDAERKVIEeklGREVSDFEFASYLMYPKVFTDYaLAADMYGPVSVIP 1007
Cdd:PRK12330 382 RnPEVVEQaKKQAKKEPITCRPADLLEPewDKLRAEALALE---GCDGSDEDVLTYALFPQVAPKF-FATRAEGPKNVGK 457
|
..
gi 1059519736 1008 TP 1009
Cdd:PRK12330 458 DP 459
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
536-989 |
5.98e-82 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 275.84 E-value: 5.98e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 536 EKRILMTDTTMRDGHQSLLATRVRTHDIARIADTYARAlpNLFSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLL 615
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDMLPVLTILDKI--GYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 616 QMLLRGANGVGYKNYPDNVVKYFVRQAAQGGIDLFRVFDCLNWVDNMRVSMDAVIEENKLCEAVICYTgdllnsARPKYD 695
Cdd:PRK12581 88 QMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT------TSPVHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 696 LKYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDA 775
Cdd:PRK12581 162 LNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIKAMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALSP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 776 FSGNTSQPCLGSIVEALRGSERDPGLDPHWIRRLSFYWEAVRTQYAA---FESDLKGPASEVYLHEMPGGQFTNLKEQAR 852
Cdd:PRK12581 242 FSEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYLAdgiLDPSLLFPDPRTLQYQVPGGMLSNMLSQLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 853 SLGLETRWHEVAQAYADANQMFGDIVKVTPSSKVVGDMALMMVSqdlsvaeVENPAKDIAfpDSVVSMLKGDLGQPPGGW 932
Cdd:PRK12581 322 QANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVI-------LGKPYQMVS--KEIKQYLAGDYGKTPAPV 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1059519736 933 PEALQKKVLKGEEPYTAVPGSLLPPadldaERKVIEEKLGREV-SDFEFASYLMYPKV 989
Cdd:PRK12581 393 NEDLKRSQIGSAPVTTNRPADQLSP-----EFEVLKAEVADLAqTDEDVLTYALFPSV 445
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
124-328 |
7.89e-76 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 249.14 E-value: 7.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 124 KVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKD 203
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 204 EVYLEKLVERARHVESQVLGDTHGNVVHLFERDCSIQRRNQKVVERAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVE 283
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1059519736 284 YLMDANTGKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQIHILDGH 328
Cdd:pfam02786 162 FALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGY 206
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
542-814 |
1.72e-70 |
|
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: 236.20 E-value: 1.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 542 TDTTMRDGHQSLLATRvRTHDIARIADTYARAlpNLFSLECWGGATFDVSmrFLTEDPWERLALVREGAPNLLLQMLLRG 621
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEA--GVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 622 angvgyknypdnvVKYFVRQAAQGGIDLFRVFDCLN--------------WVDNMRVSMDAVIEENKLCEAVICYTGdll 687
Cdd:cd03174 76 -------------REKGIERALEAGVDEVRIFDSASethsrknlnksreeDLENAEEAIEAAKEAGLEVEGSLEDAF--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 688 nsaRPKYDLKYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETG-LPIHFHTHDTSGIAAATVLAAVEAGV 766
Cdd:cd03174 140 ---GCKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPdVPLGLHTHNTLGLAVANSLAALEAGA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1059519736 767 DAVDAAMDAFSGNTSQPCLGSIVEALRGSERDPGLDPHWIRRLSFYWE 814
Cdd:cd03174 217 DRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
71-330 |
6.39e-54 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 189.31 E-value: 6.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 71 IDEIIRVAKLSGADAIhpgyglLSESPEFVDA----CNDAGLIfiGPKSDTMRQLGNKVAARNLAISVGVPVvPATNPLp 146
Cdd:COG0439 6 IAAAAELARETGIDAV------LSESEFAVETaaelAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFALV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 147 DDEAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAAFGKDEVYLEKLVErARHVESQVLGDtH 226
Cdd:COG0439 76 DSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLE-GREYSVEGLVR-D 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 227 GNVVHlferdCSIQRRNQK---VVER---APAPyLNEVQRQELADYSLRIAKATSYI-GAGTVEYLMDANtGKFYFIEVN 299
Cdd:COG0439 154 GEVVV-----CSITRKHQKppyFVELgheAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPD-GEPYLIEIN 226
|
250 260 270
....*....|....*....|....*....|...
gi 1059519736 300 PRIQVEH--TVTEVVTGIDIVKAQIHILDGHAI 330
Cdd:COG0439 227 ARLGGEHipPLTELATGVDLVREQIRLALGEPR 259
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
3-117 |
5.03e-51 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 174.98 E-value: 5.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 3 ISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPhlerdlgPIESYLAIDEIIRVAKLSG 82
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGP-------ASESYLNIDAIIDAAKETG 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1059519736 83 ADAIHPGYGLLSESPEFVDACNDAGLIFIGPKSDT 117
Cdd:pfam00289 74 ADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
351-458 |
1.04e-47 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses 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: 214878 [Multi-domain] Cd Length: 107 Bit Score: 165.28 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 351 QCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDGGtAYSGAIITRYYDPLLVKVTASGSTPQEAISRMDRALREFRIRG 430
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSG-VYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 1059519736 431 VATNLTFLEAIIGHPSFRDNSYTTRFID 458
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
351-459 |
4.15e-42 |
|
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: 149.18 E-value: 4.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 351 QCRITTEDPEQNFIPDYGRITAYRSAAGFGIRLDGGtAYSGAIITRYYDPLLVKVTASGSTPQEAISRMDRALREFRIRG 430
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 1059519736 431 VATNLTFLEAIIGHPSFRDNSYTTRFIDT 459
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
538-810 |
3.20e-27 |
|
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: 112.05 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 538 RILMTDTTMRDGHQSLlATRVRTHDIARIADtyaralpnlfSLECWGGATFDVSMRFLTEDPWERLALVREGAPNLLLQM 617
Cdd:pfam00682 1 AVAICDTTLRDGEQAL-GVAFSIDEKLAIAR----------ALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 618 LLRGAngvgyknypDNVVKYFVRQAAQGGIDLFRVFDC---LNWVDNMRVSMDAVIEE-NKLCEAVICYTGDLLNSAR-- 691
Cdd:pfam00682 70 LCRAR---------EHDIKAAVEALKGAGAVRVHVFIAtsdLHRKYKLGKDREEVAKRaVAAVKAARSRGIDVEFSPEda 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 692 PKYDLKYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREET--GLPIHFHTHDTSGIAAATVLAAVEAGVDAV 769
Cdd:pfam00682 141 SRTDPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVpnKAIISVHCHNDLGMAVANSLAAVEAGADRV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1059519736 770 DAAMDAFSGNTSQPCLGSIVEALRGSERDPGLDPHWIRRLS 810
Cdd:pfam00682 221 DGTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIA 261
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1085-1150 |
1.39e-24 |
|
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: 97.87 E-value: 1.39e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1059519736 1085 QLGAPMPGVISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLIV 1150
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVV 66
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1088-1150 |
6.86e-16 |
|
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: 75.32 E-value: 6.86e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1088 APMPGVI-------SQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLIV 1150
Cdd:COG0511 65 SPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFV 134
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
20-302 |
5.45e-15 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 78.43 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 20 RAANELGLKTVAIWAEEDKLALH-RFkADESYQVgrgPHLERDLgpiESYlaIDEIIRVAKLSGADAIHPgygllsespe 98
Cdd:COG3919 22 RSLGEAGVRVIVVDRDPLGPAARsRY-VDEVVVV---PDPGDDP---EAF--VDALLELAERHGPDVLIP---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 99 fvdaCNDAGLIFIG--------------PKSDTMRQLGNKVAARNLAISVGVPVvPATNpLPDDEAEIHRLAAEIGYPVM 164
Cdd:COG3919 83 ----TGDEYVELLSrhrdeleehyrlpyPDADLLDRLLDKERFYELAEELGVPV-PKTV-VLDSADDLDALAEDLGFPVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 165 LKASWG--------GGGRGMRAIRDPKDLLREVtegkrEAMAAFGkDEVYLEKLVERArhvESQVLG-----DTHGNVVH 231
Cdd:COG3919 157 VKPADSvgydelsfPGKKKVFYVDDREELLALL-----RRIAAAG-YELIVQEYIPGD---DGEMRGltayvDRDGEVVA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1059519736 232 LFERdcsiqrrnQKVVERAPA---PYLNE-VQRQELADYSLRIAKATSYIGAGTVEYLMDANTGKFYFIEVNPRI 302
Cdd:COG3919 228 TFTG--------RKLRHYPPAggnSAAREsVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRF 294
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
115-319 |
2.31e-14 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 77.23 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 115 SDTMRQLGNKVAARNLAISVgvpvvpatnplpdDEAEihRLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLLREVTEGKR 194
Cdd:COG0458 119 KELLDKLGIPQPKSGTATSV-------------EEAL--AIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLERALK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 195 eamaAFGKDEVYLEKLVERARHVESQVLGDTHGNVV------HlFER------DcSIqrrnqkVVerAPAPYLNEVQRQE 262
Cdd:COG0458 184 ----VSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIivgimeH-IEPagvhsgD-SI------CV--APPQTLSDKEYQR 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1059519736 263 LADYSLRIAKATSYIGAGTVEYLMDanTGKFYFIEVNPRiqVEHTVTEV--VTGIDIVK 319
Cdd:COG0458 250 LRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPR--ASRSSPFAskATGYPIAK 304
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
105-340 |
3.83e-14 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 77.32 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 105 DAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATnpLPDDEAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKD 184
Cdd:PRK12815 652 EAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGL--TATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPA 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 185 LLREVTEgkreamAAFGKDEVYLEKLVErARHVESQVLGDthGNVVHL---FERdcsiqrrnqkvVERA----------- 250
Cdd:PRK12815 730 LEAYLAE------NASQLYPILIDQFID-GKEYEVDAISD--GEDVTIpgiIEH-----------IEQAgvhsgdsiavl 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 251 PAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDanTGKFYFIEVNPRiqVEHTVTEV--VTGIDIVKAQIHILDGH 328
Cdd:PRK12815 790 PPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLA--NDEIYVLEVNPR--ASRTVPFVskATGVPLAKLATKVLLGK 865
|
250
....*....|..
gi 1059519736 329 AIGtpESGVPKQ 340
Cdd:PRK12815 866 SLA--ELGYPNG 875
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
148-327 |
5.19e-14 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 76.96 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 148 DEAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLLREVtegkREAMAAFGKDEVYLEKLVERARHVESQVLGDtHG 227
Cdd:TIGR01369 692 SVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYL----EEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GE 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 228 NVV--HLFERdcsiqrrnqkvVERA-----------PAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANTgkFY 294
Cdd:TIGR01369 767 EVLipGIMEH-----------IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGE--VY 833
|
170 180 190
....*....|....*....|....*....|....*
gi 1059519736 295 FIEVNPRiqVEHTVTEV--VTGIDIVKAQIHILDG 327
Cdd:TIGR01369 834 VIEVNPR--ASRTVPFVskATGVPLAKLAVRVMLG 866
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1088-1149 |
1.46e-13 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 69.51 E-value: 1.46e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1059519736 1088 APMPGVISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLI 1149
Cdd:PRK05641 89 APMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1085-1150 |
2.55e-13 |
|
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: 66.08 E-value: 2.55e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1059519736 1085 QLGAPMPGV-----ISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLIV 1150
Cdd:pfam00364 2 EIKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAK 72
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
111-302 |
1.93e-12 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 71.95 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 111 IGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEihRLAAEIGYPVMLKASW--GGGGRGmraIRDPKDLLRE 188
Cdd:TIGR01369 115 LGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEAL--AAAKEIGYPVIVRPAFtlGGTGGG---IAYNREELKE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 189 VTEGkreAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNV-------------VHLFErdcSIqrrnqkVVerAPAPYL 255
Cdd:TIGR01369 190 IAER---ALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCitvcnmenfdpmgVHTGD---SI------VV--APSQTL 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1059519736 256 NEVQRQELADYSLRIAKATSYIGAGTVEYLMDANTGKFYFIEVNPRI 302
Cdd:TIGR01369 256 TDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRV 302
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
20-427 |
1.53e-10 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 64.17 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 20 RAANELGLKTVAI--WAEEDKLALhrfkADESYQVGRGPHlERDLGPIEsylaiDEIIRVAKLSGADAIHPGYGLLSEsP 97
Cdd:COG2232 19 QSARRAGYRVYAVdlFADLDTRAL----AERWVRLDAESC-GFDLEDLP-----AALLELAAADDPDGLVYGSGFENF-P 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 98 EFVDACNdAGLIFIGPKSDTMRQLGNKVA-ARNLAiSVGVPVvPATNPLPDDEAeihrlaaeigYPVMLKASWGGGGRGM 176
Cdd:COG2232 88 ELLERLA-RRLPLLGNPPEVVRRVKDPLRfFALLD-ELGIPH-PETRFEPPPDP----------GPWLVKPIGGAGGWHI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 177 RAIRDPkdllrevtegkreamaAFGKDEVYLEKLVErARHVESQVLGDTHGNVVHLFERdcsiqrrnQKVVERAPAPY-- 254
Cdd:COG2232 155 RPADSE----------------APPAPGRYFQRYVE-GTPASVLFLADGSDARVLGFNR--------QLIGPAGERPFry 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 255 --------LNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANtgKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQIHILD 326
Cdd:COG2232 210 ggnigplaLPPALAEEMRAIAEALVAALGLVGLNGVDFILDGD--GPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 327 GHAIGTPESgVPKQADIRLNGHAlqcrittedPEQNFIPDygritayrsaagfGIRLDGGTA---YSGAIITRyYDPlLV 403
Cdd:COG2232 288 GELPEVPRP-KPRRVAAKAILYA---------PRDLTIPD-------------DLSWPPWVAdipAPGTRIEK-GEP-VC 342
|
410 420
....*....|....*....|....
gi 1059519736 404 KVTASGSTPQEAISRMDRALREFR 427
Cdd:COG2232 343 TVLAEGPTAEAARALLERRAEEVR 366
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1085-1150 |
2.64e-10 |
|
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: 57.45 E-value: 2.64e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1059519736 1085 QLGAPMP------GVISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLIV 1150
Cdd:cd06663 1 TILIPDLaqhlgdGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVK 72
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
73-320 |
5.40e-10 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 61.88 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 73 EIIRVAKLSGADAI-----HPGYGLlsespEFVDACNDAGLIFIGPkSDTMRQLGNKVAARNLAISVGVPVvPATNPLPD 147
Cdd:COG0189 47 ELYRGEDLSEFDAVlpridPPFYGL-----ALLRQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPV-PPTLVTRD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 148 DEaEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLLREVtegkrEAMAAFGKDEVYLEKLVErarhvESQ------- 220
Cdd:COG0189 120 PD-DLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESIL-----EALTELGSEPVLVQEFIP-----EEDgrdirvl 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 221 VLGdthGNVVHLFER-----DCSIQRRNQKVVERAPAPylnevqrQELADYSLRIAKATSYIGAGtVEYLMDAntGKFYF 295
Cdd:COG0189 189 VVG---GEPVAAIRRipaegEFRTNLARGGRAEPVELT-------DEERELALRAAPALGLDFAG-VDLIEDD--DGPLV 255
|
250 260
....*....|....*....|....*
gi 1059519736 296 IEVNPRIQVEHtvTEVVTGIDIVKA 320
Cdd:COG0189 256 LEVNVTPGFRG--LERATGVDIAEA 278
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
113-301 |
1.50e-09 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 61.24 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 113 PKSDTMRQLGNKVAARNLAISVGVPVVP-ATnplPDDEAEIHRLAAEIGYPVMLKASWGG-GGRGMRAIRDPKDLlrevt 190
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAPfAA---VDSLEDLEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADL----- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 191 egkREAMAAFGKDEVYLEKLVERARHVeSQVLG-DTHGNVVH--LFErdcSIQRRNQKVVERAPAPyLNEVQRQELADYS 267
Cdd:COG0026 151 ---EAAWAALGGGPCILEEFVPFEREL-SVIVArSPDGEVATypVVE---NVHRNGILDESIAPAR-ISEALAAEAEEIA 222
|
170 180 190
....*....|....*....|....*....|....
gi 1059519736 268 LRIAKATSYIGAGTVEYLMDANtGKFYFIEVNPR 301
Cdd:COG0026 223 KRIAEALDYVGVLAVEFFVTKD-GELLVNEIAPR 255
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
147-302 |
1.73e-09 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 62.29 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 147 DDEAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLLREVTEGKREAMAafgkDEVYLEKLVERARHVESQVLGDTH 226
Cdd:PRK12815 150 TSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPI----HQCLLEESIAGWKEIEYEVMRDRN 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 227 GNVVHLferdCS--------IQRRNQKVVerAPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANTGKFYFIEV 298
Cdd:PRK12815 226 GNCITV----CNmenidpvgIHTGDSIVV--APSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEV 299
|
....
gi 1059519736 299 NPRI 302
Cdd:PRK12815 300 NPRV 303
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1088-1149 |
1.97e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 56.74 E-value: 1.97e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1059519736 1088 APMPGVISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLI 1149
Cdd:PRK06549 66 SPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
695-810 |
2.06e-09 |
|
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: 59.44 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 695 DLKYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMD 774
Cdd:cd07939 137 DPDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAATDLPLEFHAHNDLGLATANTLAAVRAGATHVSVTVN 216
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1059519736 775 AF---SGNTSqpcLGSIVEALRGSE-RDPGLDPHWIRRLS 810
Cdd:cd07939 217 GLgerAGNAA---LEEVVMALKHLYgRDTGIDTTRLPELS 253
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
703-780 |
2.78e-09 |
|
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: 59.43 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 703 AAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREE-TGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAA---MDAFSG 778
Cdd:cd07943 147 AKLMESYGADCVYVTDSAGAMLPDDVRERVRALREAlDPTPVGFHGHNNLGLAVANSLAAVEAGATRIDGSlagLGAGAG 226
|
..
gi 1059519736 779 NT 780
Cdd:cd07943 227 NT 228
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
123-300 |
4.52e-09 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 59.35 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 123 NKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLlrevtegkREAMA-AFG 201
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEEL--------AAALEeAFK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 202 KDEVYlekLVERA---RHVESQVLGDTHGNVVHLFErdcsIQRRN-----------QKVVERAPAPyLNEVQRQELADYS 267
Cdd:COG1181 167 YDDKV---LVEEFidgREVTVGVLGNGGPRALPPIE----IVPENgfydyeakytdGGTEYICPAR-LPEELEERIQELA 238
|
170 180 190
....*....|....*....|....*....|...
gi 1059519736 268 LRIAKATSYIGAGTVEYLMDANtGKFYFIEVNP 300
Cdd:COG1181 239 LKAFRALGCRGYARVDFRLDED-GEPYLLEVNT 270
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
44-301 |
7.80e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 58.74 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 44 FKADESYQVgrgPHLERdlgpiESYlaIDEIIRVAKLSGADAIHPGY----GLLSE---------------SPEFVDACN 104
Cdd:PRK12767 41 YFADKFYVV---PKVTD-----PNY--IDRLLDICKKEKIDLLIPLIdpelPLLAQnrdrfeeigvkvlvsSKEVIEICN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 105 DaglifigpksdtmrqlgnKVAARNLAISVGVPVVPATNPLPDDEAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKD 184
Cdd:PRK12767 111 D------------------KWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 185 LLREVTEGKreamaafgkdEVYLEKLVErARHVESQVLGDTHGNVVHlferdcSIQRRNQKV----VERAPApylneVQR 260
Cdd:PRK12767 173 LEFLLEYVP----------NLIIQEFIE-GQEYTVDVLCDLNGEVIS------IVPRKRIEVrageTSKGVT-----VKD 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1059519736 261 QELADYSLRIAKATSYIGAGTVEYLMDAntGKFYFIEVNPR 301
Cdd:PRK12767 231 PELFKLAERLAEALGARGPLNIQCFVTD--GEPYLFEINPR 269
|
|
| PRK08195 |
PRK08195 |
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated |
701-780 |
2.04e-08 |
|
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
Pssm-ID: 181282 [Multi-domain] Cd Length: 337 Bit Score: 57.54 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 701 ALAAE---LEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGL--PIHFHTHDTSGIAAATVLAAVEAGVDAVDAA--- 772
Cdd:PRK08195 145 KLAEQaklMESYGAQCVYVVDSAGALLPEDVRDRVRALRAALKPdtQVGFHGHNNLGLGVANSLAAVEAGATRIDGSlag 224
|
....*...
gi 1059519736 773 MDAFSGNT 780
Cdd:PRK08195 225 LGAGAGNT 232
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
147-301 |
2.11e-08 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 54.95 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 147 DDEAEIHRLAAEIGYPVMLKASWGG-GGRGMRAIRDPKDLlrevtegkREAMAAFGKDEVYLEKLV----ERARHVESQV 221
Cdd:pfam02222 14 ESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADL--------PQAWEELGDGPVIVEEFVpfdrELSVLVVRSV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 222 LGDTHG-NVVHlferdcSIQRRNQKVVERAPAPYLNEVQrQELADYSLRIAKATSYIGAGTVEyLMDANTGKFYFIEVNP 300
Cdd:pfam02222 86 DGETAFyPVVE------TIQEDGICRLSVAPARVPQAIQ-AEAQDIAKRLVDELGGVGVFGVE-LFVTEDGDLLINELAP 157
|
.
gi 1059519736 301 R 301
Cdd:pfam02222 158 R 158
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
701-773 |
2.16e-08 |
|
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: 56.63 E-value: 2.16e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1059519736 701 ALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETG-LPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAM 773
Cdd:cd07938 153 EVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFPdEKLALHFHDTRGQALANILAALEAGVRRFDSSV 226
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
149-320 |
2.77e-08 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 58.18 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 149 EAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLLREVtegkREAMAAFGKDEVYLEKLVERARHVESQVLGDtHGN 228
Cdd:PRK05294 693 VEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYM----REAVKVSPDHPVLIDKFLEGAIEVDVDAICD-GED 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 229 VV------HLfER------D--CSIqrrnqkvveraPAPYLNEVQRQELADYSLRIAKATSYIGagtveyLMdaNT---- 290
Cdd:PRK05294 768 VLiggimeHI-EEagvhsgDsaCSL-----------PPQTLSEEIIEEIREYTKKLALELNVVG------LM--NVqfav 827
|
170 180 190
....*....|....*....|....*....|....
gi 1059519736 291 --GKFYFIEVNPRiqVEHTVTEV--VTGIDIVKA 320
Cdd:PRK05294 828 kdDEVYVIEVNPR--ASRTVPFVskATGVPLAKI 859
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
695-810 |
6.35e-08 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 56.34 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 695 DLKYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMD 774
Cdd:PRK11858 143 DLDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELVEAVDIPIEVHCHNDFGMATANALAGIEAGAKQVHTTVN 222
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1059519736 775 AF---SGNTSqpcLGSIVEALR---GSerDPGLDPHWIRRLS 810
Cdd:PRK11858 223 GLgerAGNAA---LEEVVMALKylyGI--DLGIDTERLYELS 259
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
695-781 |
9.09e-08 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 56.10 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 695 DLKYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMD 774
Cdd:PRK09389 141 DLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSELVKGPVSIHCHNDFGLAVANTLAALAAGADQVHVTIN 220
|
90
....*....|
gi 1059519736 775 AF---SGNTS 781
Cdd:PRK09389 221 GIgerAGNAS 230
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
149-301 |
9.09e-08 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 56.71 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 149 EAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLLREVTegkrEAMAAFGKDEVYLEKLVERARHVESQVLGDTHGN 228
Cdd:PLN02735 726 EADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLE----TAVEVDPERPVLVDKYLSDATEIDVDALADSEGN 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 229 VV-------------HLFERDCSIqrrnqkvveraPAPYLNEVQRQELADYSLRIAKATSYIGAGTVEYLMDANtGKFYF 295
Cdd:PLN02735 802 VViggimehieqagvHSGDSACSL-----------PTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPS-GEVYI 869
|
....*.
gi 1059519736 296 IEVNPR 301
Cdd:PLN02735 870 IEANPR 875
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1088-1149 |
1.09e-07 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 49.79 E-value: 1.09e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1059519736 1088 APMPGVISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLI 1149
Cdd:PRK08225 6 ASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLL 67
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1088-1152 |
1.99e-07 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 49.42 E-value: 1.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1059519736 1088 APMPGVISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLIVYS 1152
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVIS 71
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
113-283 |
7.16e-07 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 52.85 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 113 PKSDTMRQLGNKVAARNLAISVGVPVVPATnpLPDDEAEIHRLAAEIGYPVMLKASWGG-GGRGMRAIRDPKDLlrevte 191
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFA--VVDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDL------ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 192 gkREAMAAFGKDEVYLEKLVERARHVeSQVL-GDTHGNVVH--LFErdcSIQRRNQKVVERAPAPYLNEVQRQelA-DYS 267
Cdd:PRK06019 162 --EAAWALLGSVPCILEEFVPFEREV-SVIVaRGRDGEVVFypLVE---NVHRNGILRTSIAPARISAELQAQ--AeEIA 233
|
170
....*....|....*.
gi 1059519736 268 LRIAKATSYIGAGTVE 283
Cdd:PRK06019 234 SRIAEELDYVGVLAVE 249
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
695-810 |
7.28e-07 |
|
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: 53.25 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 695 DLKYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREET-GLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAM 773
Cdd:COG0119 146 DPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVpDVILSVHCHNDLGLAVANSLAAVEAGADQVEGTI 225
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1059519736 774 DAF---SGNTSqpcLGSIVEALRGSE-RDPGLDPHWIRRLS 810
Cdd:COG0119 226 NGIgerAGNAA---LEEVVMNLKLKYgVDTGIDLSKLTELS 263
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
707-793 |
1.99e-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: 50.52 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 707 EKAGAHIIAVKDMAGLLKPAAAKVLFKALREETG---LPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAF---SGNT 780
Cdd:cd07940 153 IEAGATTINIPDTVGYLTPEEFGELIKKLKENVPnikVPISVHCHNDLGLAVANSLAAVEAGARQVECTINGIgerAGNA 232
|
90
....*....|...
gi 1059519736 781 SqpcLGSIVEALR 793
Cdd:cd07940 233 A---LEEVVMALK 242
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
128-301 |
4.19e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 51.25 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 128 RNLAISVGVPVVP---ATNPlpdDEAEihRLAAEIGYPVMLKASW--GGGGRGMraIRDPKDLLREVTEGkreaMAAFGK 202
Cdd:PRK05294 133 KEAMKKIGLPVPRsgiAHSM---EEAL--EVAEEIGYPVIIRPSFtlGGTGGGI--AYNEEELEEIVERG----LDLSPV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 203 DEVYLEKLVERARHVESQVLGDTHGNV-------------VHLFErdcSIqrrnqkVVerAPAPYLNEVQRQELADYSLR 269
Cdd:PRK05294 202 TEVLIEESLLGWKEYEYEVMRDKNDNCiivcsienidpmgVHTGD---SI------TV--APAQTLTDKEYQMLRDASIA 270
|
170 180 190
....*....|....*....|....*....|....*.
gi 1059519736 270 IAKAtsyI----GAGTVEYLMDANTGKFYFIEVNPR 301
Cdd:PRK05294 271 IIRE---IgvetGGCNVQFALNPKDGRYIVIEMNPR 303
|
|
| PRK06524 |
PRK06524 |
biotin carboxylase-like protein; Validated |
101-314 |
8.29e-06 |
|
biotin carboxylase-like protein; Validated
Pssm-ID: 180605 [Multi-domain] Cd Length: 493 Bit Score: 49.74 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 101 DACNDAGLIFIGPKSDTMRQLGNKVAARNLAISVGVPVVPATNPLPDDEAEIHRLA--AEIGYPVMLKASWGGGGRGMRA 178
Cdd:PRK06524 120 ALARQAGLEVMHPPAELRHRLDSKIVTTRLANEAGVPSVPHVLGRVDSYDELSALAhgAGLGDDLVVQTPYGDSGSTTFF 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 179 IRDPKDLlrevtegKREAMAAFGKDEVyleKLVERARHVESQVLG--DTHGNVVHLFERDCsiqrrnqkVVERAPAPYL- 255
Cdd:PRK06524 200 VRGQRDW-------DKYAGGIVGQPEI---KVMKRIRNVEVCIEAcvTRHGTVIGPAMTSL--------VGYPELTPYRg 261
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1059519736 256 ----NEVQRQELADYSLRIAKATS-----------YIGAGTVEYLMDANTGKFYFIEVNPRIQVEHTVTEVVTG 314
Cdd:PRK06524 262 gwcgNDIWPGALPPAQTRKAREMVrklgdvlsregYRGYFEVDLLHDLDADELYLGEVNPRLSGASPMTNLTTE 335
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1085-1150 |
1.04e-05 |
|
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: 44.67 E-value: 1.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1059519736 1085 QLGAPM-PGVISQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLIV 1150
Cdd:COG0508 9 DLGESMtEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAV 75
|
|
| DRE_TIM_HCS |
cd07948 |
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ... |
706-770 |
1.35e-05 |
|
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: 48.10 E-value: 1.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1059519736 706 LEKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGVDAVD 770
Cdd:cd07948 150 VDKLGVNRVGIADTVGIATPRQVYELVRTLRGVVSCDIEFHGHNDTGCAIANAYAALEAGATHID 214
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
1088-1150 |
3.02e-05 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 43.46 E-value: 3.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 1088 APMPGVI-------SQVSVSAGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVLVRIGDQIDAKDLLIV 1150
Cdd:PRK07051 8 SPLPGTFyrrpspdAPPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLAR 77
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
115-317 |
5.18e-05 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 46.57 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 115 SDTMRQLGNKVAARNLAISVGVPVvPATNpLPDDEAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDpKDLLREVTEGKR 194
Cdd:TIGR00768 80 SDAILNAGDKFLSHQLLAKAGIPL-PRTG-LAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARD-RQAAESLLEHFE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 195 EaMAAFGKdEVYLEKLVERA--RHVESQVLGDThgnVVHLFERDCSIQRRNQ----KVVERAPapyLNEvqrqELADYSL 268
Cdd:TIGR00768 157 Q-LNGPQN-LFLVQEYIKKPggRDIRVFVVGDE---VVAAIYRITSGHWRSNlargGKAEPCS---LTE----EIEELAI 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1059519736 269 RIAKATSyIGAGTVEYLMDANTgkFYFIEVNPriQVEHTVTEVVTGIDI 317
Cdd:TIGR00768 225 KAAKALG-LDVAGVDLLESEDG--LLVNEVNA--NPEFKNSVKTTGVNI 268
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
1082-1124 |
5.49e-05 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 41.66 E-value: 5.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1059519736 1082 NTAQLGAPMPGVISQVSVSAGQTVKSGDVLLSIEAMKMETALH 1124
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQ 43
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
72-341 |
1.64e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 45.99 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 72 DEIIR-VAKLSGADaihpgyGLLSESPEFVDACNDAGLIFIGPKSDT--MRQLGNKVA-ARNLAiSVGVPVvPATNPLPD 147
Cdd:PRK02186 59 DRIHRfVSSLDGVA------GIMSSSEYFIEVASEVARRLGLPAANTeaIRTCRDKKRlARTLR-DHGIDV-PRTHALAL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 148 DeAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLLREVtegkrEAMAAFGKDEVYLEKLVERARH-VESQVLGDTH 226
Cdd:PRK02186 131 R-AVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHC-----AALRRAGTRAALVQAYVEGDEYsVETLTVARGH 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 227 GNVVHLFERdcsiQRRNQKVVERA---PAPyLNEVQRQELADYSLRIAKATSY-IGAGTVEYLMDAntGKFYFIEVNPR- 301
Cdd:PRK02186 205 QVLGITRKH----LGPPPHFVEIGhdfPAP-LSAPQRERIVRTVLRALDAVGYaFGPAHTELRVRG--DTVVIIEINPRl 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1059519736 302 ----IQVehtVTEVVTGIDIVKaqiHILDGHAiGTPESGVPKQA 341
Cdd:PRK02186 278 aggmIPV---LLEEAFGVDLLD---HVIDLHL-GVAAFADPTAK 314
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
123-300 |
2.10e-04 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 45.58 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 123 NKVAARNLAISVGVPVVPaTNPLP------DDEAEIHRLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLLREVTEgkrea 196
Cdd:PRK14573 568 DKVLTKRFASDVGVPVVP-YQPLTlagwkrEPELCLAHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISE----- 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 197 maAFGKD-EVYLEKLVERARHVESQVLGDTHGN--VVHLFERDCSIQ------------RRNQKVVERAPAPYLNEVQRQ 261
Cdd:PRK14573 642 --AFLYDtDVFVEESRLGSREIEVSCLGDGSSAyvIAGPHERRGSGGfidyqekyglsgKSSAQIVFDLDLSKESQEQVL 719
|
170 180 190
....*....|....*....|....*....|....*....
gi 1059519736 262 ELADyslRIAKATSYIGAGTVEYLMDaNTGKFYFIEVNP 300
Cdd:PRK14573 720 ELAE---RIYRLLQGKGSCRIDFFLD-EEGNFWLSEMNP 754
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
113-301 |
2.12e-04 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 45.44 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 113 PKSDTMRQLGNKVAARNLAISVGVPVVPATNPlpDDEAEIHRLAAEIGYPVMLKASWGG-GGRGMRAIRDPKDLLrevte 191
Cdd:PLN02948 111 PKSSTIRIIQDKYAQKVHFSKHGIPLPEFMEI--DDLESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTEEDLS----- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 192 gkrEAMAAFGKDE--VYLEKLVERARHVESQVLGDTHGNVV--HLFErdcSIQRRNQKVVERAPAPYLNEVQRQELAdys 267
Cdd:PLN02948 184 ---SAVAALGGFErgLYAEKWAPFVKELAVMVARSRDGSTRcyPVVE---TIHKDNICHVVEAPANVPWKVAKLATD--- 254
|
170 180 190
....*....|....*....|....*....|....*...
gi 1059519736 268 lrIAKAT--SYIGAGT--VEyLMDANTGKFYFIEVNPR 301
Cdd:PLN02948 255 --VAEKAvgSLEGAGVfgVE-LFLLKDGQILLNEVAPR 289
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
133-300 |
2.56e-04 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 133 SVGVPVVP------ATNPLPDDEAEIHrLAAEIGYPVMLKASWGGGGRGMRAIRDPKDLlrevtegkREAM-AAFGKDE- 204
Cdd:pfam07478 4 AAGLPVVPfvtftrADWKLNPKEWCAQ-VEEALGYPVFVKPARLGSSVGVSKVESREEL--------QAAIeEAFQYDEk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 205 VYLEKLVErARHVESQVLGDTHGNVVHLFER---------DCSIQRRNQKVVERAPapyLNEVQRQELADYSLRIAKATS 275
Cdd:pfam07478 75 VLVEEGIE-GREIECAVLGNEDPEVSPVGEIvpsggfydyEAKYIDDSAQIVVPAD---LEEEQEEQIQELALKAYKALG 150
|
170 180
....*....|....*....|....*
gi 1059519736 276 YIGAGTVEYLMDAnTGKFYFIEVNP 300
Cdd:pfam07478 151 CRGLARVDFFLTE-DGEIVLNEVNT 174
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
1088-1135 |
5.94e-04 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 43.29 E-value: 5.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1059519736 1088 APMPGVISQVSVsaGQTVKSGDVLLSIEAMKMETALHADRDGTIAEVL 1135
Cdd:PLN02983 211 SPAPGEPPFVKV--GDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEIL 256
|
|
| DRE_TIM_HOA_like |
cd07944 |
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ... |
693-771 |
1.15e-03 |
|
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: 42.17 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 693 KYDLKYYTALAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREET--GLPIHFHTHDTSGIAAATVLAAVEAGVDAVD 770
Cdd:cd07944 134 GYSDEELLELLELVNEIKPDVFYIVDSFGSMYPEDIKRIISLLRSNLdkDIKLGFHAHNNLQLALANTLEAIELGVEIID 213
|
.
gi 1059519736 771 A 771
Cdd:cd07944 214 A 214
|
|
| DRE_TIM_LeuA3 |
cd07941 |
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ... |
690-766 |
1.63e-03 |
|
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: 41.67 E-value: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1059519736 690 ARPKYDLKyyTALAAEleKAGAHIIAVKDMAGLLKPAAAKVLFKALREET-GLPIHFHTHDTSGIAAATVLAAVEAGV 766
Cdd:cd07941 148 ANPEYALA--TLKAAA--EAGADWLVLCDTNGGTLPHEIAEIVKEVRERLpGVPLGIHAHNDSGLAVANSLAAVEAGA 221
|
|
| IspG |
COG0821 |
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism] ... |
704-769 |
1.65e-03 |
|
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism]; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440583 [Multi-domain] Cd Length: 363 Bit Score: 41.95 E-value: 1.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1059519736 704 AELEKAGAHI--IAVKDMAgllkpAAAKvlFKALREETGLP----IHFHTHdtsgIAaatvLAAVEAGVDAV 769
Cdd:COG0821 48 KALAEAGCEIvrVAVPDEE-----AAAA--LPEIKKQLPVPlvadIHFDYR----LA----LEAAEAGVDKL 104
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
151-319 |
1.86e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.46 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 151 EIHRLAAEIG-YPVMLKASWGGGGRGmRAIRDPKDLLREVTEGkreAMAAFGKDEVYLEKLVERARHVESQVLGDTHGNV 229
Cdd:PLN02735 170 ECFEIAEDIGeFPLIIRPAFTLGGTG-GGIAYNKEEFETICKA---GLAASITSQVLVEKSLLGWKEYELEVMRDLADNV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 230 VHLferdCSIQRRNQKVVER------APAPYLNEVQRQELADYSLRIAKATSY-IGAGTVEYLMDANTGKFYFIEVNPRI 302
Cdd:PLN02735 246 VII----CSIENIDPMGVHTgdsitvAPAQTLTDKEYQRLRDYSVAIIREIGVeCGGSNVQFAVNPVDGEVMIIEMNPRV 321
|
170
....*....|....*..
gi 1059519736 303 QVEHTVTEVVTGIDIVK 319
Cdd:PLN02735 322 SRSSALASKATGFPIAK 338
|
|
| PLN02746 |
PLN02746 |
hydroxymethylglutaryl-CoA lyase |
702-778 |
2.03e-03 |
|
hydroxymethylglutaryl-CoA lyase
Pssm-ID: 178347 Cd Length: 347 Bit Score: 41.70 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 702 LAAELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREET---GLPIHFHthDTSGIAAATVLAAVEAGVDAVDAAMDAFSG 778
Cdd:PLN02746 202 VAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVpvdKLAVHFH--DTYGQALANILVSLQMGISTVDSSVAGLGG 279
|
|
| PRK12344 |
PRK12344 |
putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional |
692-766 |
3.06e-03 |
|
putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional
Pssm-ID: 237068 [Multi-domain] Cd Length: 524 Bit Score: 41.61 E-value: 3.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1059519736 692 PKYDLKyyTALAAEleKAGAHIIAVKDMAGLLKPAAAKVLFKALREETGLPIHFHTHDTSGIAAATVLAAVEAGV 766
Cdd:PRK12344 157 PEYALA--TLKAAA--EAGADWVVLCDTNGGTLPHEVAEIVAEVRAAPGVPLGIHAHNDSGCAVANSLAAVEAGA 227
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1080-1123 |
3.35e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 3.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1059519736 1080 TGNTAQLGAPMPGVISQVSVSAGQTVKSGDVLLSIEAMKMETAL 1123
Cdd:COG1566 42 EARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAAL 85
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
1082-1123 |
3.76e-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: 40.70 E-value: 3.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1059519736 1082 NTAQLGAPMPGVISQVSVSAGQTVKSGDVLLSIEAMKMETAL 1123
Cdd:COG0845 22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAAL 63
|
|
| ispG |
PRK00366 |
flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase; |
704-769 |
3.97e-03 |
|
flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase;
Pssm-ID: 234737 [Multi-domain] Cd Length: 360 Bit Score: 40.83 E-value: 3.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1059519736 704 AELEKAGAHI--IAVKDMAgllkpaAAKVLfKALREETGLP----IHFHTHdtsgiaaaTVLAAVEAGVDAV 769
Cdd:PRK00366 49 KRLARAGCEIvrVAVPDME------AAAAL-PEIKKQLPVPlvadIHFDYR--------LALAAAEAGADAL 105
|
|
| PLN03228 |
PLN03228 |
methylthioalkylmalate synthase; Provisional |
705-793 |
4.42e-03 |
|
methylthioalkylmalate synthase; Provisional
Pssm-ID: 178767 [Multi-domain] Cd Length: 503 Bit Score: 41.06 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059519736 705 ELEKAGAHIIAVKDMAGLLKPAAAKVLFKALREET----GLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAMDAF---S 777
Cdd:PLN03228 247 EAIKAGATSVGIADTVGINMPHEFGELVTYVKANTpgidDIVFSVHCHNDLGLATANTIAGICAGARQVEVTINGIgerS 326
|
90
....*....|....*.
gi 1059519736 778 GNTSqpcLGSIVEALR 793
Cdd:PLN03228 327 GNAS---LEEVVMALK 339
|
|
| PRK00915 |
PRK00915 |
2-isopropylmalate synthase; Validated |
708-769 |
6.96e-03 |
|
2-isopropylmalate synthase; Validated
Pssm-ID: 234864 [Multi-domain] Cd Length: 513 Bit Score: 40.48 E-value: 6.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1059519736 708 KAGAHIIAVKDMAGLLKPAAAKVLFKALREET----GLPIHFHTHDTSGIAAATVLAAVEAGVDAV 769
Cdd:PRK00915 160 DAGATTINIPDTVGYTTPEEFGELIKTLRERVpnidKAIISVHCHNDLGLAVANSLAAVEAGARQV 225
|
|
| |
