|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-1151 |
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: 2281.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1 MQIKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGPHlerdlgPIESYLSIDEVIRVAKL 80
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKG------PVDAYLDIEEIIRVAKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 81 SGADAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVG 160
Cdd:COG1038 76 KGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 161 FPVMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQ 240
Cdd:COG1038 156 YPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 241 RRNQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDaDTGAFYFIEVNPRIQVEHTVTEEVTGVDIVKA 320
Cdd:COG1038 236 RRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVD-DDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 321 QIHILEGKKIGDKASGVPAQADIRLNGDALQCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDGGTAYSGAVITRFYDP 400
Cdd:COG1038 315 QILIAEGYSLDDPEIGIPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 401 LLEKVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFIDETPELFTQMKRQDRATKLLNYL 480
Cdd:COG1038 395 LLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 481 ADVTVNGHPEARGRALPnaEAAAPSVPYVD--QPVPDGSRQAFDRLGPDGFAKWMREQERVLVTDTTMRDAHQSLLATRM 558
Cdd:COG1038 475 GDVTVNGPPGVKGRPKP--DFPKPKLPKVDlgAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 559 RTFDMARIAGVYARALPELLSLECWGGATFDVSMRFLTEDPWERLSRIREGAPNLLLQMLLRGANGVGYTNYPDNVVQHF 638
Cdd:COG1038 553 RTRDMLKIAPATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAF 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 639 VKQAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTGDLLDPDRAKYDLKYYVGLAGELEAAGANIIAIKD 718
Cdd:COG1038 633 VKEAAEAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKD 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 719 MAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDAAMDALSGNTSQPCLGSIVEALKGDARD 798
Cdd:COG1038 713 MAGLLKPYAAYKLVKALKEEVDLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERD 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 799 TGLDREWVRRISFYWEAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLETRWHEVARAYHDVNMMFGDIV 878
Cdd:COG1038 793 TGLDLDALQELSNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIV 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 879 KVTPSSKVVGDMALMMVSQDLTVADVQSPDKDIAFPDSVVSMLHGDLGQPPAGWPRALQKKVLKNSEPITVRPGSLLEPA 958
Cdd:COG1038 873 KVTPSSKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPV 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 959 DLEQDRRALEEKLGREVSEFEFSSWLMYPKVFTDFASASENYGPVSVLPTPVYFYGMQPEDEIFVDIERGKTLVIRCLAV 1038
Cdd:COG1038 953 DFDALRAELEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAI 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1039 GDVDEKGMVTVFFELNGQPRRVKVPDrAHGASAAAARRKAEAGNEAHMGAPMPGVVSTLAVSPGQTVKSGDVILSIEAMK 1118
Cdd:COG1038 1033 GEPDEDGMRTVFFELNGQPREVRVRD-RSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMK 1111
|
1130 1140 1150
....*....|....*....|....*....|...
gi 1998276639 1119 METALHAERDGTIAEVLVKAGDQIDAKDLLVVF 1151
Cdd:COG1038 1112 METTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-1153 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 2192.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1 MQIKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGPHlerdlgPIESYLSIDEVIRVAKL 80
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKH------PVRAYLDIDEIIRVAKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 81 SGADAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVG 160
Cdd:PRK12999 77 AGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 161 FPVMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQ 240
Cdd:PRK12999 157 YPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 241 RRNQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtGAFYFIEVNPRIQVEHTVTEEVTGVDIVKA 320
Cdd:PRK12999 237 RRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDAD-GNFYFIEVNPRIQVEHTVTEEVTGIDIVQS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 321 QIHILEGKKIGDKASGVPAQADIRLNGDALQCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDGGTAYSGAVITRFYDP 400
Cdd:PRK12999 316 QILIAEGATLHDLEIGIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 401 LLEKVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFIDETPELFTQMKRQDRATKLLNYL 480
Cdd:PRK12999 396 LLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 481 ADVTVNGHPEARGRALPNAEAAAPSVPYvDQPVPDGSRQAFDRLGPDGFAKWMREQERVLVTDTTMRDAHQSLLATRMRT 560
Cdd:PRK12999 476 ADVTVNGFPGVKKKPPVFPDPRLPKVDL-SAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 561 FDMARIAGVYARALPELLSLECWGGATFDVSMRFLTEDPWERLSRIREGAPNLLLQMLLRGANGVGYTNYPDNVVQHFVK 640
Cdd:PRK12999 555 KDLLRIAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 641 QAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTGDLLDPDRAKYDLKYYVGLAGELEAAGANIIAIKDMA 720
Cdd:PRK12999 635 EAAAAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMA 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 721 GLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDAAMDALSGNTSQPCLGSIVEALKGDARDTG 800
Cdd:PRK12999 715 GLLKPAAAYELVSALKEEVDLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTG 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 801 LDREWVRRISFYWEAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLETRWHEVARAYHDVNMMFGDIVKV 880
Cdd:PRK12999 795 LDLDAIRKLSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKV 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 881 TPSSKVVGDMALMMVSQDLTVADVQSPDKDIAFPDSVVSMLHGDLGQPPAGWPRALQKKVLKNSEPITVRPGSLLEPADL 960
Cdd:PRK12999 875 TPSSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDF 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 961 EQDRRALEEKLGREVSEFEFSSWLMYPKVFTDFASASENYGPVSVLPTPVYFYGMQPEDEIFVDIERGKTLVIRCLAVGD 1040
Cdd:PRK12999 955 EAERAELEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGE 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1041 VDEKGMVTVFFELNGQPRRVKVPDrAHGASAAAARRKAEAGNEAHMGAPMPGVVSTLAVSPGQTVKSGDVILSIEAMKME 1120
Cdd:PRK12999 1035 PDEDGMRTVYFELNGQPREVQVRD-RSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKME 1113
|
1130 1140 1150
....*....|....*....|....*....|...
gi 1998276639 1121 TALHAERDGTIAEVLVKAGDQIDAKDLLVVFGD 1153
Cdd:PRK12999 1114 TTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
5-1152 |
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: 1916.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 5 KILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGPhlerDLGPIESYLSIDEVIRVAKLSGAD 84
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGP----DLGPIEAYLSIDEIIRVAKLNGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 85 AIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGFPVM 164
Cdd:TIGR01235 77 AIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 165 LKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQRRNQ 244
Cdd:TIGR01235 157 IKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 245 KVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtGAFYFIEVNPRIQVEHTVTEEVTGVDIVKAQIHI 324
Cdd:TIGR01235 237 KVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDND-GKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 325 LEGKKIGDKASGVPAQADIRLNGDALQCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDGGTAYSGAVITRFYDPLLEK 404
Cdd:TIGR01235 316 ADGASLPTPQLGVPNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 405 VTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFIDETPELFTQMKRQDRATKLLNYLADVT 484
Cdd:TIGR01235 396 VSAWASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 485 VNGHPEARGRALPNAEAAAPSVPYVDQ-PVPDGSRQAFDRLGPDGFAKWMREQERVLVTDTTMRDAHQSLLATRMRTFDM 563
Cdd:TIGR01235 476 VNGHPEAKDKLKPLENAPRVVVLYADQnPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 564 ARIAGVYARALPELLSLECWGGATFDVSMRFLTEDPWERLSRIREGAPNLLLQMLLRGANGVGYTNYPDNVVQHFVKQAA 643
Cdd:TIGR01235 556 AKIAPTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 644 DGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTGDLLDPDRAKYDLKYYVGLAGELEAAGANIIAIKDMAGLL 723
Cdd:TIGR01235 636 QGGIDIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLL 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 724 KPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDAAMDALSGNTSQPCLGSIVEALKGDARDTGLDR 803
Cdd:TIGR01235 716 KPAAAKLLIKALREKTDLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNV 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 804 EWVRRISFYWEAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLETRWHEVARAYHDVNMMFGDIVKVTPS 883
Cdd:TIGR01235 796 AWIRELSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPS 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 884 SKVVGDMALMMVSQDLTVADVQSPDKDIAFPDSVVSMLHGDLGQPPAGWPRALQKKVLKNSEPITVRPGSLLEPADLEQD 963
Cdd:TIGR01235 876 SKVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAI 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 964 RRALEEKLGREVSEFEFSSWLMYPKVFTDFASASENYGPVSVLPTPVYFYGMQPEDEIFVDIERGKTLVIRCLAVGDVDE 1043
Cdd:TIGR01235 956 RKDLQEKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDS 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1044 KGMVTVFFELNGQPRRVKVPDrAHGASAAAARRKAEAGNEAHMGAPMPGVVSTLAVSPGQTVKSGDVILSIEAMKMETAL 1123
Cdd:TIGR01235 1036 QGEREVFFELNGQPRRIKVPD-RSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAI 1114
|
1130 1140
....*....|....*....|....*....
gi 1998276639 1124 HAERDGTIAEVLVKAGDQIDAKDLLVVFG 1152
Cdd:TIGR01235 1115 QAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
3-473 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 702.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 3 IKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGPhlerdlgPIESYLSIDEVIRVAKLSG 82
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAP-------AAESYLNIDAIIAAAKATG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 83 ADAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGFP 162
Cdd:COG4770 75 ADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 163 VMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQRR 242
Cdd:COG4770 155 VLIKASAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 243 NQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtGAFYFIEVNPRIQVEHTVTEEVTGVDIVKAQI 322
Cdd:COG4770 235 HQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDAD-GNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 323 HILEGKKIGDKasgvpaQADIRLNGDALQCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDGGtAYSGAVITRFYDPLL 402
Cdd:COG4770 314 RIAAGEPLPFT------QEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSMI 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276639 403 EKVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFIDETPELFTQMKRQDRA 473
Cdd:COG4770 387 AKLIVWGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
2-459 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 606.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 2 QIKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGPhlerdlgPIESYLSIDEVIRVAKLS 81
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAP-------SKKSYLNIPAIISAAEIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 82 GADAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGF 161
Cdd:PRK08591 74 GADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 162 PVMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQR 241
Cdd:PRK08591 154 PVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 242 RNQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtGAFYFIEVNPRIQVEHTVTEEVTGVDIVKAQ 321
Cdd:PRK08591 234 RHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKN-GEFYFIEMNTRIQVEHPVTEMITGVDLVKEQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 322 IHILEGKKIGDKasgvpaQADIRLNGDALQCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDGGtAYSGAVITRFYDPL 401
Cdd:PRK08591 313 IRIAAGEPLSIK------QEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSM 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276639 402 LEKVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFIDE 459
Cdd:PRK08591 386 IGKLIVHGETREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEK 443
|
|
| 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: 578.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 4 KKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGPhlerdlgPIESYLSIDEVIRVAKLSGA 83
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAP-------PSKSYLNIERIIDVAKKAGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 84 DAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGFPV 163
Cdd:PRK08654 76 DAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 164 MLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQRRN 243
Cdd:PRK08654 156 IIKASAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 244 QKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMdaDTGAFYFIEVNPRIQVEHTVTEEVTGVDIVKAQIH 323
Cdd:PRK08654 236 QKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY--SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 324 ILEGKKIGDKasgvpaQADIRLNGDALQCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDGGTaYSGAVITRFYDPLLE 403
Cdd:PRK08654 314 IAAGEELSFK------QEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGV-HMGYEIPPYYDSMIS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276639 404 KVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFIDETPELFTQMKR 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: 547.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 3 IKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGPhlerdlgPIESYLSIDEVIRVAKLSG 82
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPR-------VQESYLNLEKIIEIAKKTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 83 ADAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGFP 162
Cdd:PRK06111 75 AEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 163 VMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQRR 242
Cdd:PRK06111 155 VMLKASAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 243 NQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtGAFYFIEVNPRIQVEHTVTEEVTGVDIVKAQI 322
Cdd:PRK06111 235 HQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQ-KNFYFLEMNTRLQVEHPVTEEITGIDLVEQQL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 323 HILEGKKIGDKasgvpaQADIRLNGDALQCRITTEDPeQNFIPDYGRITAYRGATGFGIRLDGGTAySGAVITRFYDPLL 402
Cdd:PRK06111 314 RIAAGEKLSFT------QDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMI 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276639 403 EKVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFI 457
Cdd:PRK06111 386 AKLIAHGETREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-463 |
2.58e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 536.61 E-value: 2.58e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 3 IKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGPhlerdlgpIESYLSIDEVIRVAKLSG 82
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP--------LAGYLNPRRLVNLAVETG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 83 ADAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGFP 162
Cdd:PRK07178 74 CDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 163 VMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQRR 242
Cdd:PRK07178 154 VMLKATSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 243 NQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtGAFYFIEVNPRIQVEHTVTEEVTGVDIVKAQI 322
Cdd:PRK07178 234 NQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDAD-GEVYFMEMNTRVQVEHTITEEITGIDIVREQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 323 HIlegkkigdkASGVP---AQADIRLNGDALQCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDGGTaYSGAVITRFYD 399
Cdd:PRK07178 313 RI---------ASGLPlsyKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAI-YTGYTIPPYYD 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276639 400 PLLEKVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFIDETPEL 463
Cdd:PRK07178 383 SMCAKLIVWALTWEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPEL 446
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
3-459 |
8.99e-175 |
|
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: 521.24 E-value: 8.99e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 3 IKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGPhlerdlgPIESYLSIDEVIRVAKLSG 82
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAP-------SAKSYLNIPNIISAAEITG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 83 ADAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGFP 162
Cdd:TIGR00514 75 ADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 163 VMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQRR 242
Cdd:TIGR00514 155 VIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 243 NQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtGAFYFIEVNPRIQVEHTVTEEVTGVDIVKAQI 322
Cdd:TIGR00514 235 HQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKN-GEFYFMEMNTRIQVEHPVTEMITGVDLIKEQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 323 HILEGKKIGDKasgvpaQADIRLNGDALQCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDgGTAYSGAVITRFYDPLL 402
Cdd:TIGR00514 314 RIAAGEPLSLK------QEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWD-SHVYSGYTVPPYYDSMI 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276639 403 EKVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFIDE 459
Cdd:TIGR00514 387 GKLITYGKTREVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-459 |
5.34e-173 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 516.57 E-value: 5.34e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 3 IKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGphlerdlGPIESYLSIDEVIRVAKLSG 82
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPA-------SSKDSYLNIQNIISATVLTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 83 ADAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGFP 162
Cdd:PRK05586 75 AQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 163 VMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQRR 242
Cdd:PRK05586 155 VMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 243 NQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtGAFYFIEVNPRIQVEHTVTEEVTGVDIVKAQI 322
Cdd:PRK05586 235 NQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKD-GNFYFMEMNTRIQVEHPITEMITGVDLVKEQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 323 HILEGKKIGDKasgvpaQADIRLNGDALQCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDgGTAYSGAVITRFYDPLL 402
Cdd:PRK05586 314 KIAYGEKLSIK------QEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVD-SAVYSGYTIPPYYDSMI 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276639 403 EKVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFIDE 459
Cdd:PRK05586 387 GKLIVYGKDREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
538-1150 |
3.11e-170 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 514.78 E-value: 3.11e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 538 RVLVTDTTMRDAHQSLLATRMRTFDMARIAgvyaralpELL------SLECWGGATFDVSMRFLTEDPWERLSRIREGAP 611
Cdd:PRK09282 3 KVKITDTTLRDAHQSLLATRMRTEDMLPIA--------EKLdkvgfwSLEVWGGATFDVCIRYLNEDPWERLRKLKKALP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 612 NLLLQMLLRGANGVGYTNYPDNVVQHFVKQAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTgdlLDPdr 691
Cdd:PRK09282 75 NTPLQMLLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT---TSP-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 692 aKYDLKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDA 771
Cdd:PRK09282 150 -VHTIEKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEVDLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 772 AMDALSGNTSQPCLGSIVEALKGDARDTGLDREWVRRISFYWEAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQA 851
Cdd:PRK09282 229 AISPLAFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTIVDTRVLIHQVPGGMISNLVSQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 852 RSLGLETRWHEVARAYHDVNMMFGDIVKVTPSSKVVGDMALMMVsqdLTVADVqspdKDIafPDSVVSMLHGDLGQPPAG 931
Cdd:PRK09282 309 KEQNALDKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNV---LTGERY----KVI--TKEVKDYVKGLYGRPPAP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 932 WPRALQKKVLKNSEPITVRPGSLLEPaDLEQDRRALEEKLGREVSefEFSSWLMYPKVFTDFASASENY----GPVSVLP 1007
Cdd:PRK09282 380 INEELRKKIIGDEEPITCRPADLLEP-ELEKARKEAEELGKSEKE--DVLTYALFPQIAKKFLEEREAGelkpEPEPKEA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1008 TPVYFYGMQPEDEIFVDierGKTLVIRclaVGDVDEKGMVTVFFELNGQPRRVKVPdrahGASAAAARRKAEAGNEAHMG 1087
Cdd:PRK09282 457 AAAGAEGIPTEFKVEVD---GEKYEVK---IEGVKAEGKRPFYLRVDGMPEEVVVE----PLKEIVVGGRPRASAPGAVT 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276639 1088 APMPGVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLVV 1150
Cdd:PRK09282 527 SPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLME 589
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
541-823 |
5.79e-161 |
|
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: 478.46 E-value: 5.79e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 541 VTDTTMRDAHQSLLATRMRTFDMARIAGVYARALpeLLSLECWGGATFDVSMRFLTEDPWERLSRIREGAPNLLLQMLLR 620
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 621 GANGVGYTNYPDNVVQHFVKQAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTGDlldpdrAKYDLKYYV 700
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 701 GLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDAAMDALSGNT 780
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVGLPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGGT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1998276639 781 SQPCLGSIVEALKGDARDTGLDREWVRRISFYWEAVRNQYAAF 823
Cdd:cd07937 233 SQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-458 |
8.45e-160 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 483.10 E-value: 8.45e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1 MQIKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGrGPHLERdlgpieSYLSIDEVIRVAKL 80
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIG-PSHAAK------SYLNPAAILAAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 81 SGADAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVG 160
Cdd:PRK12833 76 CGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 161 FPVMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHgNAVHLFERDCSIQ 240
Cdd:PRK12833 156 YPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 241 RRNQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADTGAFYFIEVNPRIQVEHTVTEEVTGVDIVKA 320
Cdd:PRK12833 235 RRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 321 QIHILEGKKIGdkasgvPAQADIRLNGDALQCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDgGTAYSGAVITRFYDP 400
Cdd:PRK12833 315 MLRIADGEPLR------FAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVD-SLLYPGYRVPPFYDS 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276639 401 LLEKVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFID 458
Cdd:PRK12833 388 LLAKLIVHGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
2-459 |
2.29e-153 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 466.98 E-value: 2.29e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 2 QIKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGPhlerdlgpIESYLSIDEVIRVAKLS 81
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDP--------IKGYLDVKRIVEIAKAC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 82 GADAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDD-MAKVAEMAEEVG 160
Cdd:PRK08463 73 GADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSEsMEEIKIFARKIG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 161 FPVMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQ 240
Cdd:PRK08463 153 YPVILKASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 241 RRNQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDaDTGAFYFIEVNPRIQVEHTVTEEVTGVDIVKA 320
Cdd:PRK08463 233 RRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD-DYNRFYFMEMNTRIQVEHGVTEEITGIDLIVR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 321 QIHILEGkKIGDKasgvpAQADIRLNGDALQCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDgGTAYSGAVITRFYDP 400
Cdd:PRK08463 312 QIRIAAG-EILDL-----EQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVD-SHIYKDYTIPPYYDS 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276639 401 LLEKVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFIDE 459
Cdd:PRK08463 385 MLAKLIVKATSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIET 443
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
541-1148 |
4.28e-149 |
|
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: 459.64 E-value: 4.28e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 541 VTDTTMRDAHQSLLATRMRTFDMARIAGVYARAlpELLSLECWGGATFDVSMRFLTEDPWERLSRIREGAPNLLLQMLLR 620
Cdd:TIGR01108 1 ITDVVLRDAHQSLFATRMRTEDMLPIAEKLDDV--GYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 621 GANGVGYTNYPDNVVQHFVKQAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTgdlLDPdraKYDLKYYV 700
Cdd:TIGR01108 79 GQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT---TSP---VHTLETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 701 GLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDAAMDALSGNT 780
Cdd:TIGR01108 153 DLAEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRFGLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 781 SQPCLGSIVEALKGDARDTGLDREWVRRISFYWEAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLETRW 860
Cdd:TIGR01108 233 SHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFEGQLKGPDSRILVAQVPGGMLSNLESQLKEQNALDKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 861 HEVARAYHDVNMMFGDIVKVTPSSKVVGDMALMMVSQDLTVADVQSPDKDIafpdsvvsmLHGDLGQPPAGWPRALQKKV 940
Cdd:TIGR01108 313 DEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTGERYKTITKETKGY---------LKGEYGRTPAPINAELQRKI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 941 LKNSEPI-TVRPGSLLEPaDLEQDRRALEEKLGREVSEFEFSSWLMYPKVFTDFASASENYGPVSVLPT---------PV 1010
Cdd:TIGR01108 384 LGDEKPIvDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQVGLKFLENRHNPAAFEPKPEekvieqehaQV 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1011 YFYGMQPEDE--IFVDIErGKTLVIRCLAVGDVDEKGMVTVffelNGQPRRVKVPdrahgasaaaarrkaEAGNEAHMGA 1088
Cdd:TIGR01108 463 VGKYEETHASgsYTVEVE-GKAFVVKVSPGGDVSQITASAP----ANTSGGTVAA---------------KAGAGTPVTA 522
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1089 PMPGVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLL 1148
Cdd:TIGR01108 523 PIAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAVSVGQVL 582
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
538-1119 |
6.74e-148 |
|
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: 454.74 E-value: 6.74e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 538 RVLVTDTTMRDAHQSLLATRMRTFDMARIAgvyaralpELL------SLECWGGATFDVSMRFLTEDPWERLSRIREGAP 611
Cdd:COG5016 3 KVKITDTTLRDGHQSLFATRMRTEDMLPIA--------EKLdeagfwSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 612 NLLLQMLLRGANGVGYTNYPDNVVQHFVKQAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTgdlLDPdr 691
Cdd:COG5016 75 NTPLQMLLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYT---ISP-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 692 aKYDLKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDA 771
Cdd:COG5016 150 -VHTVEYYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEALDIPIELHTHATSGLAPATYLKAIEAGVDIIDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 772 AMDALSGNTSQPCLGSIVEALKGDARDTGLDREWVRRISFYWEAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQA 851
Cdd:COG5016 229 AISPLAGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGVDPRVLVHQVPGGMLSNLVSQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 852 RSLGLETRWHEVARAYHDVNMMFGDIVKVTPSSKVVGDMALMMVsqdLTvadvQSPDKDIafPDSVVSMLHGDLGQPPAG 931
Cdd:COG5016 309 KEQGALDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNV---LT----GERYKMI--TKEVKDYVLGYYGKTPAP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 932 WPRALQKKVLKNSEPITVRPGSLLEPaDLEQDRraleeKLGREVSEFEFSSWLMYPKVFTDFASASENYGPVSVLPtpvy 1011
Cdd:COG5016 380 IDPEVRKKALGDEEPITCRPADLLEP-ELEKLR-----KEGLAKSDEDVLTYALFPQVAIKFLKGRAAGEARPDAP---- 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1012 fygmqpedeifvdiERGKTLVIrclAVGDVDEKGMVTVFFELNGQPRRVKVPDRAHGASAAAARRKAEAGNEAHMGAPMP 1091
Cdd:COG5016 450 --------------LAELAAVE---EVVVVAEGVVVVVVVGGGAEGVVVVVVGVPGAGAVAVVAAAAAVAAAAAAAAAAA 512
|
570 580
....*....|....*....|....*...
gi 1998276639 1092 GVVSTLAVSPGQTVKSGDVILSIEAMKM 1119
Cdd:COG5016 513 AAAAGAAVKKVVAVGGAVVVGVEVVVVV 540
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-459 |
1.09e-144 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 443.03 E-value: 1.09e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1 MQIKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGrGPHLErdlgpiESYLSIDEVIRVAKL 80
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIG-GAKSS------ESYLNIPAIISAAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 81 SGADAIHPGYGLLSESPEFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVG 160
Cdd:PRK08462 75 FEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 161 FPVMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQ 240
Cdd:PRK08462 155 YPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 241 RRNQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADTGaFYFIEVNPRIQVEHTVTEEVTGVDIVKA 320
Cdd:PRK08462 235 RRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLD-FYFMEMNTRLQVEHTVSEMVSGLDLIEW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 321 QIHILEGKKIgdkasgvPAQADIRLNGDALQCRITTEDPEQnFIPDYGRITAYRGATGFGIRLDgGTAYSGAVITRFYDP 400
Cdd:PRK08462 314 MIKIAEGEEL-------PSQESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPGGRNVRMD-SHAYAGYVVPPYYDS 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276639 401 LLEKVTAWAPTPEEAIARMDRALREFRIRGVATNLTFLEAIISHPKFRDASYTTRFIDE 459
Cdd:PRK08462 385 MIGKLIVWGEDRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
541-1149 |
3.94e-130 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 410.09 E-value: 3.94e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 541 VTDTTMRDAHQSLLATRMRTFDMARIAgvyaralPEL-----LSLECWGGATFDVSMRFLTEDPWERLSRIREGAPNLLL 615
Cdd:PRK14040 7 ITDVVLRDAHQSLFATRLRLDDMLPIA-------AKLdkvgyWSLESWGGATFDACIRFLGEDPWERLRELKKAMPNTPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 616 QMLLRGANGVGYTNYPDNVVQHFVKQAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTgdlLDPdraKYD 695
Cdd:PRK14040 80 QMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT---TSP---VHT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 696 LKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDAAMDA 775
Cdd:PRK14040 154 LQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRVDVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAISS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 776 LSGNTSQPCLGSIVEALKGDARDTGLDREWVRRISFYWEAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLG 855
Cdd:PRK14040 234 MSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNMESQLKEQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 856 LETRWHEVARAYHDVNMMFGDIVKVTPSSKVVGDMALMMVsqdLTVADVQSPDKDIAfpdsvvSMLHGDLGQPPAGWPRA 935
Cdd:PRK14040 314 AADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQAVLNV---LTGERYKTITKETA------GVLKGEYGATPAPVNAE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 936 LQKKVLKNSEPITVRPGSLLEP--ADLEQDRRALEEKLGREVSEFEFSSWLMY---PKVFTDFAsasENYG-PVSVLPTP 1009
Cdd:PRK14040 385 LQARVLEGAEPITCRPADLLAPelDKLEAELRRQAQEKGITLAENAIDDVLTYalfPQIGLKFL---ENRHnPAAFEPVP 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1010 vyfygmQPEDEifvdiergktlviRCLAVGDVDEKGMVTVffELNGQPRRVKV----------PDRAHGASAAAARRKAE 1079
Cdd:PRK14040 462 ------QAEAA-------------QPAAKAEPAGSETYTV--EVEGKAYVVKVseggdisqitPAAPAAAPAAAAAAAPA 520
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1080 AGNEAHMGAPMPGVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLV 1149
Cdd:PRK14040 521 AAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
538-993 |
2.10e-118 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 373.65 E-value: 2.10e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 538 RVLVTDTTMRDAHQSLLATRMRTFDMARIAgvyaralpELL------SLECWGGATFDVSMRFLTEDPWERLSRIREGAP 611
Cdd:PRK12331 3 KIKITETVLRDGQQSLIATRMTTEEMLPIL--------EKLdnagyhSLEMWGGATFDACLRFLNEDPWERLRKIRKAVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 612 NLLLQMLLRGANGVGYTNYPDNVVQHFVKQAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTgdlLDPdr 691
Cdd:PRK12331 75 KTKLQMLLRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT---TSP-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 692 aKYDLKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDA 771
Cdd:PRK12331 150 -VHTIDYFVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAVTVPLEVHTHATSGIAEMTYLKAIEAGADIIDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 772 AMDALSGNTSQPCLGSIVEALKGDARDTGLDREWVRRISFYWEAVRNQYAAfESDL----KGPASEVYLHEMPGGQFTNL 847
Cdd:PRK12331 229 AISPFAGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYRE-EGILnpkvKDVEPKTLIYQVPGGMLSNL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 848 KEQARSLGLETRWHEVARAYHDVNMMFGDIVKVTPSSKVVGDMALMmvsqdltvaDVQSPDKDIAFPDSVVSMLHGDLGQ 927
Cdd:PRK12331 308 LSQLKEQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALM---------NVISGERYKMVPNEIKDYVRGLYGR 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276639 928 PPAGWPRALQKKVLKNSEPITVRPGSLLEPaDLEQDRRALEEKLGrevSEFEFSSWLMYPKVFTDF 993
Cdd:PRK12331 379 PPAPIAEEIKKKIIGDEEVITCRPADLIEP-QLEKLREEIAEYAE---SEEDVLSYALFPQQAKDF 440
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
538-1149 |
1.55e-109 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 355.18 E-value: 1.55e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 538 RVLVTDTTMRDAHQSLLATRMRTFDMARIAGVYARAlpELLSLECWGGATFDVSMRFLTEDPWERLSRIREGAPNLLLQM 617
Cdd:PRK14042 3 KTFITDVTLRDAHQCLIATRMRTEDMLPICNKMDDV--GFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 618 LLRGANGVGYTNYPDNVVQHFVKQAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTGDLLdpdrakYDLK 697
Cdd:PRK14042 81 LLRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYTTSPV------HTLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 698 YYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDAAMDALS 777
Cdd:PRK14042 155 NFLELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 778 GNTSQPCLGSIVEALKGDARDTGLDREWVRRISFYWEAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLE 857
Cdd:PRK14042 235 GGASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 858 TRWHEVARAYHDVNMMFGDIVKVTPSSKVVGDMAlmmvsqdltVADVQSPDKDIAFPDSVVSMLHGDLGQPPAGWPRALQ 937
Cdd:PRK14042 315 DKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQA---------VINVLTGERYKTITNEVKLYCQGKYGTPPGKISSALR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 938 KKVLKNSEPITVRPGSLLePADLEQdrraleekLGREVSEFEFSS-----WLMYPKVFTDFASASENYgpvSVLPTPVYF 1012
Cdd:PRK14042 386 KKAIGRTEVIEVRPGDLL-PNELDQ--------LQNEISDLALSDedvllYAMFPEIGRQFLEQRKNN---QLIPEPLLT 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1013 YGMQPEDEIFVDIE---RGKTLVIRCLAVGDVdEKGMVTVFFELNGQPRRVKVPDRAHGASAAAARRKAEAGnEAHMGAP 1089
Cdd:PRK14042 454 QSSAPDNSVMSEFDiilHGESYHVKVAGYGMI-EHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIG-PGDITVA 531
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1090 MPGVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLV 1149
Cdd:PRK14042 532 IPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLI 591
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
834-1034 |
5.83e-100 |
|
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: 314.78 E-value: 5.83e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 834 VYLHEMPGGQFTNLKEQARSLGLETRWHEVARAYHDVNMMFGDIVKVTPSSKVVGDMALMMVSQDLTVADVQSPDKDIAF 913
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 914 PDSVVSMLHGDLGQPPAGWPRALQKKVLKNSEPITVRPGSLLEPADLEQDRRALEEKLGREVSEFEFSSWLMYPKVFTDF 993
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1998276639 994 ASASENYGPVSVLPTPVYFYGMQPEDEIFVDIERGKTLVIR 1034
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
538-967 |
9.88e-100 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 324.43 E-value: 9.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 538 RVLVTDTTMRDAHQSLLATRMRTFDMARIAGVYARAlpELLSLECWGGATFDVSMRFLTEDPWERLSRIREGAPNLLLQM 617
Cdd:PRK14041 2 KVMFVDTTLRDGHQSLIATRMRTEDMLPALEAFDRM--GFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 618 LLRGANGVGYTNYPDNVVQHFVKQAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTgdlLDPdraKYDLK 697
Cdd:PRK14041 80 LLRGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT---VSP---VHTLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 698 YYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDAAMDALS 777
Cdd:PRK14041 154 YYLEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKFGVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 778 GNTSQPCLGSIVEALKGDARDTGLDREWVRRISFYWEAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLE 857
Cdd:PRK14041 234 MGTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYDVGMKSPDSRILVSQIPGGMYSNLVKQLKEQKML 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 858 TRWHEVARAYHDVNMMFGDIVKVTPSSKVVGDMALMMVSQDLTVADVQSPDKDiafpdsvvsMLHGDLGQPPAGWPRALQ 937
Cdd:PRK14041 314 HKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQAVLNVLTGERYKRVTNETKN---------YVKGLYGRPPAPIDEELM 384
|
410 420 430
....*....|....*....|....*....|
gi 1998276639 938 KKVLKNSEPITVRPGSLLEPaDLEQDRRAL 967
Cdd:PRK14041 385 KKILGDEKPIDCRPADLLEP-ELEKARKEL 413
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
541-1010 |
1.65e-95 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 314.01 E-value: 1.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 541 VTDTTMRDAHQSLLATRMRTFDMARI------AGVYaralpellSLECWGGATFDVSMRFLTEDPWERLSRIREGAPNLL 614
Cdd:PRK12330 7 VTELALRDAHQSLMATRMAMEDMVGAcedidnAGYW--------SVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 615 LQMLLRGANGVGYTNYPDNVVQHFVKQAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTGDLLdpdrakY 694
Cdd:PRK12330 79 LQMLLRGQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYTVSPI------H 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 695 DLKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREA--TDLPLHFHTHDTSGISAATVLAAVESGVDAVDAA 772
Cdd:PRK12330 153 TVEGFVEQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEAcgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 773 MDALSGNTSQPCLGSIVEALKGDARDTGLDREWVRRISFYWEAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQAR 852
Cdd:PRK12330 233 ISSMSLGPGHNPTESLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTTGVETEIFKSQIPGGMLSNMESQLK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 853 SLGLETRWHEVARAYHDVNMMFGDIVKVTPSSKVVGDMA----LMMVSQDLT--VADVqspdkdiafpdsvvsMLhGDLG 926
Cdd:PRK12330 313 QQGAGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAvfnvLMGRYKVLTgeFADL---------------ML-GYYG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 927 QPPAGWPRALQKKVLKNS--EPITVRPGSLLEP--ADLEQDRRALEeklGREVSEFEFSSWLMYPKVFTDFAsASENYGP 1002
Cdd:PRK12330 377 ETPGERNPEVVEQAKKQAkkEPITCRPADLLEPewDKLRAEALALE---GCDGSDEDVLTYALFPQVAPKFF-ATRAEGP 452
|
....*...
gi 1998276639 1003 VSVLPTPV 1010
Cdd:PRK12330 453 KNVGKDPA 460
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
536-957 |
3.17e-84 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 282.01 E-value: 3.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 536 QERVLVTDTTMRDAHQSLLATRMRTFDMARIAGVYARAlpELLSLECWGGATFDVSMRFLTEDPWERLSRIREGAPNLLL 615
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDMLPVLTILDKI--GYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 616 QMLLRGANGVGYTNYPDNVVQHFVKQAADGGIDLFRVFDCLNWVENMRVAMDAVRSEGKLCEATICYTGDLLdpdrakYD 695
Cdd:PRK12581 88 QMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYTTSPV------HT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 696 LKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDAAMDA 775
Cdd:PRK12581 162 LNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIKAMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALSP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 776 LSGNTSQPCLGSIVEALKGDARDTGLDREWVRRISFYWEAVRNQYAA---FESDLKGPASEVYLHEMPGGQFTNLKEQAR 852
Cdd:PRK12581 242 FSEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYLAdgiLDPSLLFPDPRTLQYQVPGGMLSNMLSQLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 853 SLGLETRWHEVARAYHDVNMMFGDIVKVTPSSKVVGDMALMMVsqdLTVADVQSPDKDIAfpdsvvSMLHGDLGQPPAGW 932
Cdd:PRK12581 322 QANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNV---ILGKPYQMVSKEIK------QYLAGDYGKTPAPV 392
|
410 420
....*....|....*....|....*
gi 1998276639 933 PRALQKKVLKNSEPITVRPGSLLEP 957
Cdd:PRK12581 393 NEDLKRSQIGSAPVTTNRPADQLSP 417
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
124-331 |
1.26e-79 |
|
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: 259.54 E-value: 1.26e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 124 KVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGFPVMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKD 203
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 204 EVYLEKLVERARHVEVQVLGDTHGNAVHLFERDCSIQRRNQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVE 283
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276639 284 FLMDADTGAFYFIEVNPRIQVEHTVTEEVTGVDIVKAQIHILEGKKIG 331
Cdd:pfam02786 162 FALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
542-814 |
3.37e-67 |
|
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: 226.95 E-value: 3.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 542 TDTTMRDAHQSLLATrMRTFDMARIAgvyaRALPELL--SLECWGGATFDVSmrFLTEDPWERLSRIREGAPNLLLQMLL 619
Cdd:cd03174 1 TDTTLRDGLQSEGAT-FSTEDKLEIA----EALDEAGvdSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 620 RGangvgytnypdnvVQHFVKQAADGGIDLFRVFDCLN--------------WVENMRVAMDAVRSEGKLCEATICYTGd 685
Cdd:cd03174 74 RN-------------REKGIERALEAGVDEVRIFDSASethsrknlnksreeDLENAEEAIEAAKEAGLEVEGSLEDAF- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 686 lldpdRAKYDLKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREAT-DLPLHFHTHDTSGISAATVLAAVES 764
Cdd:cd03174 140 -----GCKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALpDVPLGLHTHNTLGLAVANSLAALEA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1998276639 765 GVDAVDAAMDALSGNTSQPCLGSIVEALKGDARDTGLDREWVRRISFYWE 814
Cdd:cd03174 215 GADRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
71-330 |
7.26e-61 |
|
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: 208.96 E-value: 7.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 71 IDEVIRVAKLSGADAIhpgyglLSES----PEFADACAENGITfiGPKPETMRRLGNKVAARNLAIEVGVPVvPATEPLp 146
Cdd:COG0439 6 IAAAAELARETGIDAV------LSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFALV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 147 DDMAKVAEMAEEVGFPVMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFGKDEVYLEKLVErARHVEVQVLGDtH 226
Cdd:COG0439 76 DSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLE-GREYSVEGLVR-D 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 227 GNAVHlferdCSIQRRNQK---VVER---APAPyLNDEKRAELCGYALKIAEATDYI-GAGTVEFLMDADtGAFYFIEVN 299
Cdd:COG0439 154 GEVVV-----CSITRKHQKppyFVELgheAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPD-GEPYLIEIN 226
|
250 260 270
....*....|....*....|....*....|...
gi 1998276639 300 PRIQVEH--TVTEEVTGVDIVKAQIHILEGKKI 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 |
1.07e-53 |
|
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: 182.30 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 3 IKKILVANRSEIAIRVFRAANELDIRTVAIWAEEDKYSLHRFKADESYQVGRGPhlerdlgPIESYLSIDEVIRVAKLSG 82
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGP-------ASESYLNIDAIIDAAKETG 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1998276639 83 ADAIHPGYGLLSESPEFADACAENGITFIGPKPET 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 |
8.36e-49 |
|
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: 168.36 E-value: 8.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 351 QCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDGGtAYSGAVITRFYDPLLEKVTAWAPTPEEAIARMDRALREFRIRG 430
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSG-VYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 1998276639 431 VATNLTFLEAIISHPKFRDASYTTRFID 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 |
7.64e-44 |
|
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: 154.19 E-value: 7.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 351 QCRITTEDPEQNFIPDYGRITAYRGATGFGIRLDGGtAYSGAVITRFYDPLLEKVTAWAPTPEEAIARMDRALREFRIRG 430
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 1998276639 431 VATNLTFLEAIISHPKFRDASYTTRFIDE 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 |
1.54e-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: 113.21 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 538 RVLVTDTTMRDAHQSLlATRMRTFDMARIAgvyaralpelLSLECWGGATFDVSMRFLTEDPWERLSRIREGAPNLLLQM 617
Cdd:pfam00682 1 AVAICDTTLRDGEQAL-GVAFSIDEKLAIA----------RALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 618 LLRGAngvgytnypDNVVQHFVKQAADGGIDLFRVFD-------------CLNWV-ENMRVAMDAVRSEGKLCEaticyt 683
Cdd:pfam00682 70 LCRAR---------EHDIKAAVEALKGAGAVRVHVFIatsdlhrkyklgkDREEVaKRAVAAVKAARSRGIDVE------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 684 gdLLDPDRAKYDLKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATD--LPLHFHTHDTSGISAATVLAA 761
Cdd:pfam00682 135 --FSPEDASRTDPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPnkAIISVHCHNDLGMAVANSLAA 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1998276639 762 VESGVDAVDAAMDALSGNTSQPCLGSIVEALKGDARDTGLDREWVRRIS 810
Cdd:pfam00682 213 VEAGADRVDGTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIA 261
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1085-1151 |
5.75e-25 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 99.03 E-value: 5.75e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276639 1085 HMGAPMPGVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLVVF 1151
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
20-363 |
6.15e-17 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 84.21 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 20 RAANELDIRTVAIWAEEDKYSLH-RFkADESYQVgrgPHLERDLgpiESYlsIDEVIRVAKLSGADAIHPGygllseSPE 98
Cdd:COG3919 22 RSLGEAGVRVIVVDRDPLGPAARsRY-VDEVVVV---PDPGDDP---EAF--VDALLELAERHGPDVLIPT------GDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 99 FADACAEN------GITFIGPKPETMRRLGNKVAARNLAIEVGVPVvPATEpLPDDMAKVAEMAEEVGFPVMLKASWG-- 170
Cdd:COG3919 87 YVELLSRHrdeleeHYRLPYPDADLLDRLLDKERFYELAEELGVPV-PKTV-VLDSADDLDALAEDLGFPVVVKPADSvg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 171 ------GGGRGMRVIRSRDDLEnevtEAKREARAAFGkdEVYLEKLVERARHVEVQVLG--DTHGNAVHLFerdcSIQRR 242
Cdd:COG3919 165 ydelsfPGKKKVFYVDDREELL----ALLRRIAAAGY--ELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF----TGRKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 243 NQKVVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADTGAFYFIEVNPRI--QVEHTVteeVTGVDIVKA 320
Cdd:COG3919 235 RHYPPAGGNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFwrSLYLAT---AAGVNFPYL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1998276639 321 QIHILEGKKIGDKASGVPAQADIRLNGDALQCRITTEDPEQNF 363
Cdd:COG3919 312 LYDDAVGRPLEPVPAYREGVLWRVLPGDLLLRYLRDGELRKRL 354
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
105-332 |
8.11e-17 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 86.18 E-value: 8.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 105 ENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATepLPDDMAKVAEMAEEVGFPVMLKASWGGGGRGMRVIRSRDD 184
Cdd:PRK12815 652 EAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGL--TATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPA 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 185 LENEVTEakrearAAFGKDEVYLEKLVErARHVEVQVLGDthGNAVHL---FERdcsiqrrnqkvVERA----------- 250
Cdd:PRK12815 730 LEAYLAE------NASQLYPILIDQFID-GKEYEVDAISD--GEDVTIpgiIEH-----------IEQAgvhsgdsiavl 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 251 PAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADTgaFYFIEVNPRiqVEHTV--TEEVTGVDIVKAQIHILEGK 328
Cdd:PRK12815 790 PPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDE--IYVLEVNPR--ASRTVpfVSKATGVPLAKLATKVLLGK 865
|
....
gi 1998276639 329 KIGD 332
Cdd:PRK12815 866 SLAE 869
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1088-1150 |
1.32e-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: 77.63 E-value: 1.32e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1088 APMPGVV-------STLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLVV 1150
Cdd:COG0511 65 SPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFV 134
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
100-330 |
8.09e-16 |
|
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: 82.74 E-value: 8.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 100 ADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVP---ATeplpdDMAKVAEMAEEVGFPVMLKASWGGGGRGM 176
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKwktAT-----SVEEAVEFASEIGYPVLVRPSYVLGGRAM 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 177 RVIRSRDDLENEVTEAKrearAAFGKDEVYLEKLVERARHVEVQVLGDtHGNAV--HLFERdcsiqrrnqkvVERA---- 250
Cdd:TIGR01369 721 EIVYNEEELRRYLEEAV----AVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVLipGIMEH-----------IEEAgvhs 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 251 -------PAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADTgaFYFIEVNPRIQVEHTVTEEVTGVDIVKAQIH 323
Cdd:TIGR01369 785 gdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGE--VYVIEVNPRASRTVPFVSKATGVPLAKLAVR 862
|
....*..
gi 1998276639 324 ILEGKKI 330
Cdd:TIGR01369 863 VMLGKKL 869
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
73-320 |
5.01e-15 |
|
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: 76.90 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 73 EVIRVAKLSGADAI-----HPGYGLlsespEFADACAENGITFIGPkPETMRRLGNKVAARNLAIEVGVPVvPATEPLPD 147
Cdd:COG0189 47 ELYRGEDLSEFDAVlpridPPFYGL-----ALLRQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPV-PPTLVTRD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 148 DmAKVAEMAEEVGFPVMLKASWGGGGRGMRVIRSRDDLenevtEAKREARAAFGKDEVYLEKLVERARHVE--VQVLGdt 225
Cdd:COG0189 120 P-DDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDAL-----ESILEALTELGSEPVLVQEFIPEEDGRDirVLVVG-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 226 hGNAVHLFER-----DCSIQRRNQKVVERAPAPylndekrAELCGYALKIAEATDYIGAGtVEFLMDADtgAFYFIEVNP 300
Cdd:COG0189 192 -GEPVAAIRRipaegEFRTNLARGGRAEPVELT-------DEERELALRAAPALGLDFAG-VDLIEDDD--GPLVLEVNV 260
|
250 260
....*....|....*....|
gi 1998276639 301 RIQVEHtvTEEVTGVDIVKA 320
Cdd:COG0189 261 TPGFRG--LERATGVDIAEA 278
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
100-301 |
5.42e-15 |
|
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: 79.54 E-value: 5.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 100 ADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVP---ATeplpdDMAKVAEMAEEVGFPVMLKASWGGGGRGM 176
Cdd:COG0458 91 EEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKsgtAT-----SVEEALAIAEEIGYPVIVRPSYVLGGRGM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 177 RVIRSRDDLENEVTEAKRearaAFGKDEVYLEKLVERARHVEVQVLGDTHGNAV------HlFER------DcSIqrrnq 244
Cdd:COG0458 166 GIVYNEEELEEYLERALK----VSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIivgimeH-IEPagvhsgD-SI----- 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276639 245 kVVerAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLmdADTGAFYFIEVNPR 301
Cdd:COG0458 235 -CV--APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFA--VDDGRVYVIEVNPR 286
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
113-301 |
8.63e-15 |
|
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: 77.42 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 113 PKPETMRRLGNKVAARNLAIEVGVPVVP-ATeplPDDMAKVAEMAEEVGFPVMLKASWGG-GGRGMRVIRSRDDLEnevt 190
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAPfAA---VDSLEDLEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADLE---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 191 eakrEARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVH--LFErdcSIQRRNQKVVERAPAPyLNDEKRAELCGYAL 268
Cdd:COG0026 152 ----AAWAALGGGPCILEEFVPFERELSVIVARSPDGEVATypVVE---NVHRNGILDESIAPAR-ISEALAAEAEEIAK 223
|
170 180 190
....*....|....*....|....*....|...
gi 1998276639 269 KIAEATDYIGAGTVEFLMDADtGAFYFIEVNPR 301
Cdd:COG0026 224 RIAEALDYVGVLAVEFFVTKD-GELLVNEIAPR 255
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
44-301 |
1.62e-14 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 76.08 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 44 FKADESYQVgrgPHLERdlgpiESYlsIDEVIRVAKLSGADAIHPGY----GLLSESpefADACAENGITFIGPKPETMR 119
Cdd:PRK12767 41 YFADKFYVV---PKVTD-----PNY--IDRLLDICKKEKIDLLIPLIdpelPLLAQN---RDRFEEIGVKVLVSSKEVIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 120 RLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGFPVMLKASWGGGGRGMRVIRSRDDLENEVTEAKrearaa 199
Cdd:PRK12767 108 ICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVP------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 200 fgkdEVYLEKLVErARHVEVQVLGDTHGNAVHlferdcSIQRRNQKV----VERAPApylndEKRAELCGYALKIAEATD 275
Cdd:PRK12767 182 ----NLIIQEFIE-GQEYTVDVLCDLNGEVIS------IVPRKRIEVrageTSKGVT-----VKDPELFKLAERLAEALG 245
|
250 260
....*....|....*....|....*.
gi 1998276639 276 YIGAGTVEFLMDADTgaFYFIEVNPR 301
Cdd:PRK12767 246 ARGPLNIQCFVTDGE--PYLFEINPR 269
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1085-1151 |
1.18e-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: 66.85 E-value: 1.18e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276639 1085 HMGAPMPGVVSTLA-----VSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLVVF 1151
Cdd:pfam00364 2 EIKSPMIGESVREGvvewlVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
107-300 |
2.08e-13 |
|
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: 72.45 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 107 GITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGFPVMLKASWGGGGRGMRVIRSRDDLE 186
Cdd:COG1181 79 GIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 187 NEVTEAKREARAAfgkdevylekLVERA---RHVEVQVLGDTHGNAVHLFErdcsIQRRN-----------QKVVERAPA 252
Cdd:COG1181 159 AALEEAFKYDDKV----------LVEEFidgREVTVGVLGNGGPRALPPIE----IVPENgfydyeakytdGGTEYICPA 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276639 253 PyLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtGAFYFIEVNP 300
Cdd:COG1181 225 R-LPEELEERIQELALKAFRALGCRGYARVDFRLDED-GEPYLLEVNT 270
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1088-1152 |
3.90e-13 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 68.35 E-value: 3.90e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276639 1088 APMPGVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLVVFG 1152
Cdd:PRK05641 89 APMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIELG 153
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
104-302 |
4.77e-13 |
|
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: 73.88 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 104 AENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVvPATEpLPDDMAKVAEMAEEVGFPVMLKASWGGGGRGMRVIRSRD 183
Cdd:TIGR01369 108 EKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPV-PESE-IAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNRE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 184 DLEnevtEAKREARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNA-------------VHLFErdcSIqrrnqkVVerA 250
Cdd:TIGR01369 186 ELK----EIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCitvcnmenfdpmgVHTGD---SI------VV--A 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276639 251 PAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADTGAFYFIEVNPRI 302
Cdd:TIGR01369 251 PSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRV 302
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
113-301 |
2.65e-12 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 69.80 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 113 PKPETMRRLGNKVAARNLAIEVGVPVVPATepLPDDMAKVAEMAEEVGFPVMLKASWGG-GGRGMRVIRSRDDLEnevte 191
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFA--VVDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLE----- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 192 akrEARAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVH--LFErdcSIQRRNQKVVERAPAPyLNDEKRAELCGYALK 269
Cdd:PRK06019 163 ---AAWALLGSVPCILEEFVPFEREVSVIVARGRDGEVVFypLVE---NVHRNGILRTSIAPAR-ISAELQAQAEEIASR 235
|
170 180 190
....*....|....*....|....*....|..
gi 1998276639 270 IAEATDYIGAGTVEFLMDADtGAFYFIEVNPR 301
Cdd:PRK06019 236 IAEELDYVGVLAVEFFVTGD-GELLVNEIAPR 266
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
71-427 |
1.19e-11 |
|
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: 67.64 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 71 IDEVIRVAKLSGADAIHPGYGLLSEsPEFADACAENGItFIGPKPETMRRLGNKVA-ARNLAiEVGVPVvPATEPLPDDm 149
Cdd:COG2232 62 PAALLELAAADDPDGLVYGSGFENF-PELLERLARRLP-LLGNPPEVVRRVKDPLRfFALLD-ELGIPH-PETRFEPPP- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 150 akvaemaeeVGFPVMLKASWGGGGRGMRVIRSrddlenevteakrearAAFGKDEVYLEKLVErARHVEVQVLGDTHGNA 229
Cdd:COG2232 137 ---------DPGPWLVKPIGGAGGWHIRPADS----------------EAPPAPGRYFQRYVE-GTPASVLFLADGSDAR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 230 VHLFERdcsiqrrnQKVVERAPAPY----------LNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtgAFYFIEVN 299
Cdd:COG2232 191 VLGFNR--------QLIGPAGERPFryggnigplaLPPALAEEMRAIAEALVAALGLVGLNGVDFILDGD--GPYVLEVN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 300 PRIQVEHTVTEEVTGVDIVKAQIHILEGkKIGDKASGVPAQADIRlngdalqcRITtedpeqnFIPDYGRITAyrgatgf 379
Cdd:COG2232 261 PRPQASLDLYEDATGGNLFDAHLRACRG-ELPEVPRPKPRRVAAK--------AIL-------YAPRDLTIPD------- 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1998276639 380 GIRLDGGTA---YSGAVITRfYDPLLeKVTAWAPTPEEAIARMDRALREFR 427
Cdd:COG2232 318 DLSWPPWVAdipAPGTRIEK-GEPVC-TVLAEGPTAEAARALLERRAEEVR 366
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
107-319 |
1.10e-10 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 66.15 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 107 GITFIGPKPETMRRLGNKVAARNLAIEVGVPVvPATEPLpDDMAKVAEMAEEVGFPVMLKASWGGGGRGMRVIRSRDDLE 186
Cdd:PRK12815 112 GVELLGTNIEAIQKGEDRERFRALMKELGEPV-PESEIV-TSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 187 NEVTEAKREARAafgkDEVYLEKLVERARHVEVQVLGDTHGNAVHLferdCS--------IQRRNQKVVerAPAPYLNDE 258
Cdd:PRK12815 190 QLFKQGLQASPI----HQCLLEESIAGWKEIEYEVMRDRNGNCITV----CNmenidpvgIHTGDSIVV--APSQTLTDD 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276639 259 KRAELCGYALKIAEATDYIGAGTVEFLMDADTGAFYFIEVNPRIQVEHTVTEEVTGVDIVK 319
Cdd:PRK12815 260 EYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAK 320
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1092-1151 |
4.14e-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: 57.07 E-value: 4.14e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1092 GVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLVVF 1151
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
154-332 |
1.71e-09 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 62.42 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 154 EMAEEVGFPVMLKASWGGGGRGMRVIRSRDDLENEVTEAKRearaAFGKDEVYLEKLVERARHVEVQVLGDthGNAVHL- 232
Cdd:PRK05294 698 EVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVK----VSPDHPVLIDKFLEGAIEVDVDAICD--GEDVLIg 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 233 -----FER------D--CSIqrrnqkvveraPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADTgaFYFIEVN 299
Cdd:PRK05294 772 gimehIEEagvhsgDsaCSL-----------PPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDE--VYVIEVN 838
|
170 180 190
....*....|....*....|....*....|....*
gi 1998276639 300 PRiqVEHTV--TEEVTGVDIVKAQIHILEGKKIGD 332
Cdd:PRK05294 839 PR--ASRTVpfVSKATGVPLAKIAARVMLGKKLAE 871
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
134-300 |
2.40e-09 |
|
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: 58.48 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 134 VGVPVVP------ATEPLpDDMAKVAEMAEEVGFPVMLKASWGGGGRGMRVIRSRDDLENEVteakreaRAAFGKDE-VY 206
Cdd:pfam07478 5 AGLPVVPfvtftrADWKL-NPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAI-------EEAFQYDEkVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 207 LEKLVErARHVEVQVLGDTHGNAVHLFER---------DCSIQRRNQKVVERAPapyLNDEKRAELCGYALKIAEATDYI 277
Cdd:pfam07478 77 VEEGIE-GREIECAVLGNEDPEVSPVGEIvpsggfydyEAKYIDDSAQIVVPAD---LEEEQEEQIQELALKAYKALGCR 152
|
170 180
....*....|....*....|...
gi 1998276639 278 GAGTVEFLMDADtGAFYFIEVNP 300
Cdd:pfam07478 153 GLARVDFFLTED-GEIVLNEVNT 174
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
688-810 |
3.36e-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: 59.06 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 688 DPDRAkyDLKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVD 767
Cdd:cd07939 132 DASRA--DPDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAATDLPLEFHAHNDLGLATANTLAAVRAGAT 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1998276639 768 AVDAAMDAL---SGNTSqpcLGSIVEALKG-DARDTGLDREWVRRIS 810
Cdd:cd07939 210 HVSVTVNGLgerAGNAA---LEEVVMALKHlYGRDTGIDTTRLPELS 253
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1086-1149 |
5.56e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 55.59 E-value: 5.56e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276639 1086 MGAPMPGVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLV 1149
Cdd:PRK06549 64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
147-301 |
6.35e-09 |
|
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: 56.49 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 147 DDMAKVAEMAEEVGFPVMLKASWGG-GGRGMRVIRSRDDLEnevteakrEARAAFGKDEVYLEKLVERARHVEVQVLGDT 225
Cdd:pfam02222 14 ESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP--------QAWEELGDGPVIVEEFVPFDRELSVLVVRSV 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276639 226 HGnAVHLFERDCSIQRRNQKVVERAPAPYLND-EKRAELcgYALKIAEATDYIGAGTVEFLMdADTGAFYFIEVNPR 301
Cdd:pfam02222 86 DG-ETAFYPVVETIQEDGICRLSVAPARVPQAiQAEAQD--IAKRLVDELGGVGVFGVELFV-TEDGDLLINELAPR 158
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1088-1149 |
9.85e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 52.87 E-value: 9.85e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276639 1088 APMPGVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLV 1149
Cdd:PRK08225 6 ASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLL 67
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
105-317 |
1.59e-08 |
|
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: 57.36 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 105 ENGITFIGPkPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVaeMAEEVGFPVMLKASWGGGGRGMRVIRSRDD 184
Cdd:TIGR00768 71 SLGVPVINS-SDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALK--LIEEIGFPVVLKPVFGSWGRGVSLARDRQA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 185 LENeVTEAKREARAAFGkdEVYLEKLVERA--RHVEVQVLGDThgnAVHLFERDCSIQRRNQKVVERAPAPYLNDEKRAE 262
Cdd:TIGR00768 148 AES-LLEHFEQLNGPQN--LFLVQEYIKKPggRDIRVFVVGDE---VVAAIYRITSGHWRSNLARGGKAEPCSLTEEIEE 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276639 263 LcgyALKIAEATDyIGAGTVEFLMDADtgAFYFIEVNPriQVEHTVTEEVTGVDI 317
Cdd:TIGR00768 222 L---AIKAAKALG-LDVAGVDLLESED--GLLVNEVNA--NPEFKNSVKTTGVNI 268
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
706-780 |
3.63e-08 |
|
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: 55.97 E-value: 3.63e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276639 706 LEAAGANIIAIKDMAGLLKPGAARVLFKALREATDL-PLHFHTHDTSGISAATVLAAVESGVDAVDAA---MDALSGNT 780
Cdd:cd07943 150 MESYGADCVYVTDSAGAMLPDDVRERVRALREALDPtPVGFHGHNNLGLAVANSLAAVEAGATRIDGSlagLGAGAGNT 228
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
659-781 |
4.81e-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: 55.86 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 659 VENMRVAMDAVRSEGKLCEATI-----C-YTGDLlDPDRAkydlkyyVGLAGELEAAGANIIAIKDMAGLLKPGAARVLF 732
Cdd:cd07938 113 LERFEPVAELAKAAGLRVRGYVstafgCpYEGEV-PPERV-------AEVAERLLDLGCDEISLGDTIGVATPAQVRRLL 184
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276639 733 KALREAT-DLPLHFHTHDTSGISAATVLAAVESGVDAVDAAM---------DALSGNTS 781
Cdd:cd07938 185 EAVLERFpDEKLALHFHDTRGQALANILAALEAGVRRFDSSVgglggcpfaPGATGNVA 243
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
688-810 |
7.35e-08 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 56.49 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 688 DPDRAkyDLKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVD 767
Cdd:PRK09389 136 DASRA--DLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSELVKGPVSIHCHNDFGLAVANTLAALAAGAD 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1998276639 768 AVDAAMDAL---SGNTSqpcLGSIVEALK-GDARDTGLDREWVRRIS 810
Cdd:PRK09389 214 QVHVTINGIgerAGNAS---LEEVVMALKhLYDVETGIKLEELYELS 257
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1092-1151 |
4.74e-07 |
|
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: 48.14 E-value: 4.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1092 GVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLVVF 1151
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK08195 |
PRK08195 |
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated |
706-780 |
5.54e-07 |
|
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
Pssm-ID: 181282 [Multi-domain] Cd Length: 337 Bit Score: 52.91 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 706 LEAAGANIIAIKDMAGLLKPGAARVLFKALREA--TDLPLHFHTHDTSGISAATVLAAVESGVDAVDAA---MDALSGNT 780
Cdd:PRK08195 153 MESYGAQCVYVVDSAGALLPEDVRDRVRALRAAlkPDTQVGFHGHNNLGLGVANSLAAVEAGATRIDGSlagLGAGAGNT 232
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1088-1150 |
6.39e-07 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 47.88 E-value: 6.39e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276639 1088 APMPGVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLVV 1150
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAV 69
|
|
| PRK06524 |
PRK06524 |
biotin carboxylase-like protein; Validated |
98-326 |
1.15e-06 |
|
biotin carboxylase-like protein; Validated
Pssm-ID: 180605 [Multi-domain] Cd Length: 493 Bit Score: 52.44 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 98 EFADACAENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMAKVAEMAEEVGF--PVMLKASWGGGGRG 175
Cdd:PRK06524 117 ETEALARQAGLEVMHPPAELRHRLDSKIVTTRLANEAGVPSVPHVLGRVDSYDELSALAHGAGLgdDLVVQTPYGDSGST 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 176 MRVIRSRDDLenevteaKREARAAFGKDEVyleKLVERARHVEVQVLG--DTHGNAVHLFERD--------------CSi 239
Cdd:PRK06524 197 TFFVRGQRDW-------DKYAGGIVGQPEI---KVMKRIRNVEVCIEAcvTRHGTVIGPAMTSlvgypeltpyrggwCG- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 240 qrrNQkvVERAPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADTGAFYFIEVNPRIQVEHTVTEEVTGV--DI 317
Cdd:PRK06524 266 ---ND--IWPGALPPAQTRKAREMVRKLGDVLSREGYRGYFEVDLLHDLDADELYLGEVNPRLSGASPMTNLTTEAyaDM 340
|
....*....
gi 1998276639 318 VKAQIHILE 326
Cdd:PRK06524 341 PLFLFHLLE 349
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
104-301 |
2.61e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 52.02 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 104 AENGITFIGPKPETMRRLGNKVAARNLAIEVGVPVVP---ATeplpdDMAKVAEMAEEVGFPVMLKASWGGGGRGMRVIR 180
Cdd:PRK05294 109 EKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRsgiAH-----SMEEALEVAEEIGYPVIIRPSFTLGGTGGGIAY 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 181 SRDDLENEVTEAKREARAafgkDEVYLEKLVERARHVEVQVLGDTHGNA-------------VHLFErdcSIqrrnqkVV 247
Cdd:PRK05294 184 NEEELEEIVERGLDLSPV----TEVLIEESLLGWKEYEYEVMRDKNDNCiivcsienidpmgVHTGD---SI------TV 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276639 248 erAPAPYLNDEKRAELCGYALKIAEATDYI-GAGTVEFLMDADTGAFYFIEVNPR 301
Cdd:PRK05294 251 --APAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPR 303
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
695-793 |
2.65e-06 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 50.94 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 695 DLKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVDAAMD 774
Cdd:PRK11858 143 DLDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELVEAVDIPIEVHCHNDFGMATANALAGIEAGAKQVHTTVN 222
|
90 100
....*....|....*....|..
gi 1998276639 775 AL---SGNTSqpcLGSIVEALK 793
Cdd:PRK11858 223 GLgerAGNAA---LEEVVMALK 241
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
154-301 |
3.63e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 51.32 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 154 EMAEEVGFPVMLKASWGGGGRGMRVIRSRDDLenevteaKREARAAFGKD---EVYLEKLVERARHVEVQVLGDTHGNAV 230
Cdd:PLN02735 731 AIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKL-------KTYLETAVEVDperPVLVDKYLSDATEIDVDALADSEGNVV 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 231 -------------HLFERDCSIqrrnqkvveraPAPYLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtGAFYFIE 297
Cdd:PLN02735 804 iggimehieqagvHSGDSACSL-----------PTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPS-GEVYIIE 871
|
....
gi 1998276639 298 VNPR 301
Cdd:PLN02735 872 ANPR 875
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
695-793 |
7.25e-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: 48.98 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 695 DLKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREAT---DLPLHFHTHDTSGISAATVLAAVESGVDAVDA 771
Cdd:cd07940 141 DLDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVpniKVPISVHCHNDLGLAVANSLAAVEAGARQVEC 220
|
90 100
....*....|....*....|....*
gi 1998276639 772 AMDAL---SGNTSqpcLGSIVEALK 793
Cdd:cd07940 221 TINGIgerAGNAA---LEEVVMALK 242
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
70-322 |
9.79e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 49.85 E-value: 9.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 70 SIDEVIR-VAKLSGADaihpgyGLLSESPEFADACAE--NGITFIGPKPETMRRLGNKVA-ARNLAiEVGVPVvPATEPL 145
Cdd:PRK02186 57 DPDRIHRfVSSLDGVA------GIMSSSEYFIEVASEvaRRLGLPAANTEAIRTCRDKKRlARTLR-DHGIDV-PRTHAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 146 PDDmAKVAEMAEEVGFPVMLKASWGGGGRGMRVIRSRDDLENEVTEAKREARAAFgkdevYLEKLVERARHvEVQVLGDT 225
Cdd:PRK02186 129 ALR-AVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTRAA-----LVQAYVEGDEY-SVETLTVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 226 HGNAV------HLFERDCSIQrrnqkVVERAPAPyLNDEKRAELCGYALKIAEATDY-IGAGTVEFLMDADTGAfyFIEV 298
Cdd:PRK02186 202 RGHQVlgitrkHLGPPPHFVE-----IGHDFPAP-LSAPQRERIVRTVLRALDAVGYaFGPAHTELRVRGDTVV--IIEI 273
|
250 260
....*....|....*....|....*....
gi 1998276639 299 NPR-----IQVehtVTEEVTGVDIVKAQI 322
Cdd:PRK02186 274 NPRlaggmIPV---LLEEAFGVDLLDHVI 299
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
1099-1153 |
1.78e-05 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 43.85 E-value: 1.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276639 1099 VSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLVVFGD 1153
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
107-300 |
2.41e-05 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 47.81 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 107 GITFIGPKPE----TMrrlgNKVAARNLAIEVGVPVVPATEPLPDD--MAKVAEMAEEVGFPVMLKASWGGGGRGMRVIR 180
Cdd:PRK01966 107 GIPYVGCGVLasalSM----DKILTKRLLAAAGIPVAPYVVLTRGDweEASLAEIEAKLGLPVFVKPANLGSSVGISKVK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 181 SRDDLENEVTEAKREARaafgkdEVYLEKLVErARHVEVQVLGdthgnavhlFERDCS----IQRRN-----------QK 245
Cdd:PRK01966 183 NEEELAAALDLAFEYDR------KVLVEQGIK-GREIECAVLG---------NDPKASvpgeIVKPDdfydyeakyldGS 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276639 246 VVERAPAPyLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDADtGAFYFIEVNP 300
Cdd:PRK01966 247 AELIIPAD-LSEELTEKIRELAIKAFKALGCSGLARVDFFLTED-GEIYLNEINT 299
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
123-300 |
3.51e-05 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 48.27 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 123 NKVAARNLAIEVGVPVVPaTEPLPDDMAK------VAEMAEEVGFPVMLKASWGGGGRGMRVIRSRDDLENEVTEakrea 196
Cdd:PRK14573 568 DKVLTKRFASDVGVPVVP-YQPLTLAGWKrepelcLAHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISE----- 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 197 raAFGKD-EVYLEKLVERARHVEVQVLGDTHG----NAVHlferdcsiQRRNQKVVERAPAPY---------------LN 256
Cdd:PRK14573 642 --AFLYDtDVFVEESRLGSREIEVSCLGDGSSayviAGPH--------ERRGSGGFIDYQEKYglsgkssaqivfdldLS 711
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1998276639 257 DEKRAELCGYALKIAEATDYIGAGTVEFLMDaDTGAFYFIEVNP 300
Cdd:PRK14573 712 KESQEQVLELAERIYRLLQGKGSCRIDFFLD-EEGNFWLSEMNP 754
|
|
| PLN02746 |
PLN02746 |
hydroxymethylglutaryl-CoA lyase |
702-778 |
9.60e-05 |
|
hydroxymethylglutaryl-CoA lyase
Pssm-ID: 178347 Cd Length: 347 Bit Score: 45.94 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 702 LAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREATD---LPLHFHthDTSGISAATVLAAVESGVDAVDAAMDALSG 778
Cdd:PLN02746 202 VAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPvdkLAVHFH--DTYGQALANILVSLQMGISTVDSSVAGLGG 279
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
113-301 |
1.00e-04 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 46.59 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 113 PKPETMRRLGNKVAARNLAIEVGVPVVPATEPlpDDMAKVAEMAEEVGFPVMLKASWGG-GGRGMRVIRSRDDLEnevte 191
Cdd:PLN02948 111 PKSSTIRIIQDKYAQKVHFSKHGIPLPEFMEI--DDLESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTEEDLS----- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 192 akrEARAAFGKDE--VYLEKLVERARHVEVQVLGDTHGNAV--HLFErdcSIQRRNQKVVERAPAPYlnDEKRAELcgyA 267
Cdd:PLN02948 184 ---SAVAALGGFErgLYAEKWAPFVKELAVMVARSRDGSTRcyPVVE---TIHKDNICHVVEAPANV--PWKVAKL---A 252
|
170 180 190
....*....|....*....|....*....|....*...
gi 1998276639 268 LKIAE-ATDYI-GAGT--VEFLMDADtGAFYFIEVNPR 301
Cdd:PLN02948 253 TDVAEkAVGSLeGAGVfgVELFLLKD-GQILLNEVAPR 289
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
100-319 |
1.71e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 45.92 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 100 ADACAENGI------TFIGPKPETMRRLGNKVAARNLAIEVGVPVVPATepLPDDMAKVAEMAEEVG-FPVMLKASWGGG 172
Cdd:PLN02735 115 AVALAESGIlekygvELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSG--IATTLDECFEIAEDIGeFPLIIRPAFTLG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 173 GRGMRVIRSRDDLENEVTEAkreaRAAFGKDEVYLEKLVERARHVEVQVLGDTHGNAVHLferdCSIQRRNQKVVER--- 249
Cdd:PLN02735 193 GTGGGIAYNKEEFETICKAG----LAASITSQVLVEKSLLGWKEYELEVMRDLADNVVII----CSIENIDPMGVHTgds 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276639 250 ---APAPYLNDEKRAELCGYALKIA-EATDYIGAGTVEFLMDADTGAFYFIEVNPRIQVEHTVTEEVTGVDIVK 319
Cdd:PLN02735 265 itvAPAQTLTDKEYQRLRDYSVAIIrEIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
123-224 |
2.04e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.53 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 123 NKVAARNLAIEVGVPVvpatePL------PDDMAkvaEMAEEVGFPVMLKASWGGGGRGMRV-IRSRDDLEnevtEAKRE 195
Cdd:PRK14016 214 DKELTKRLLAAAGVPV-----PEgrvvtsAEDAW---EAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIE----AAYAV 281
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1998276639 196 ARaAFGKD---EVYLE-----------KLVERARHVEVQVLGD 224
Cdd:PRK14016 282 AS-KESSDvivERYIPgkdhrllvvggKLVAAARREPPHVIGD 323
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
695-810 |
8.10e-04 |
|
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: 43.23 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 695 DLKYYVGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALREAT-DLPLHFHTHDTSGISAATVLAAVESGVDAVDAAM 773
Cdd:COG0119 146 DPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVpDVILSVHCHNDLGLAVANSLAAVEAGADQVEGTI 225
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1998276639 774 DAL---SGNTSqpcLGSIVEALK---GdaRDTGLDREWVRRIS 810
Cdd:COG0119 226 NGIgerAGNAA---LEEVVMNLKlkyG--VDTGIDLSKLTELS 263
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
1088-1124 |
1.26e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 37.81 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1998276639 1088 APMPGVVSTLAVSPGQTVKSGDVILSIEAMKMETALH 1124
Cdd:pfam13533 7 SPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQ 43
|
|
| DRE_TIM_HCS |
cd07948 |
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ... |
706-770 |
1.46e-03 |
|
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: 41.93 E-value: 1.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276639 706 LEAAGANIIAIKDMAGLLKPGAARVLFKALREATDLPLHFHTHDTSGISAATVLAAVESGVDAVD 770
Cdd:cd07948 150 VDKLGVNRVGIADTVGIATPRQVYELVRTLRGVVSCDIEFHGHNDTGCAIANAYAALEAGATHID 214
|
|
| DRE_TIM_HOA_like |
cd07944 |
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ... |
631-771 |
1.47e-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: 41.78 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 631 PDNVVQHFVKQAADGGIDLFRVfdCLNwVENMRVAMDAVRS---EGKLCEATICYTgdlldpdrAKYDLKYYVGLAGELE 707
Cdd:cd07944 80 YGNDDIDLLEPASGSVVDMIRV--AFH-KHEFDEALPLIKAikeKGYEVFFNLMAI--------SGYSDEELLELLELVN 148
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276639 708 AAGANIIAIKDMAGLLKPGAARVLFKALREATD--LPLHFHTHDTSGISAATVLAAVESGVDAVDA 771
Cdd:cd07944 149 EIKPDVFYIVDSFGSMYPEDIKRIISLLRSNLDkdIKLGFHAHNNLQLALANTLEAIELGVEIIDA 214
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1086-1155 |
1.64e-03 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 42.55 E-value: 1.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 1086 MGAPMPGVVSTLAVSPGQTVKSGDVILSIEAMKMETALHAERDGTIAEVLVKAGDQIDAKDLLVVFGDGD 1155
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGA 77
|
|
| PRK05692 |
PRK05692 |
hydroxymethylglutaryl-CoA lyase; Provisional |
700-818 |
2.23e-03 |
|
hydroxymethylglutaryl-CoA lyase; Provisional
Pssm-ID: 180206 Cd Length: 287 Bit Score: 41.41 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 700 VGLAGELEAAGANIIAIKDMAGLLKPGAARVLFKALRE---ATDLPLHFHthDTSGISAATVLAAVESGVDAVDAAMDAL 776
Cdd:PRK05692 158 ADVAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAefpAERLAGHFH--DTYGQALANIYASLEEGITVFDASVGGL 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1998276639 777 ---------SGNTSQPclgSIVEALKGDARDTGLDREWVRRISFYWEAVRN 818
Cdd:PRK05692 236 ggcpyapgaSGNVATE---DVLYMLHGLGIETGIDLDKLVRAGQFIQSKLG 283
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
145-299 |
3.31e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 40.81 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 145 LPDDMAKVAE----MAEEVGFPVMLKASWGGGGRGMRVIRSRDDLENEVTEAKREAraafgkdEVYLEKLVErARHVEVQ 220
Cdd:PRK14569 111 MPTPMAKFLTdklvAEDEISFPVAVKPSSGGSSIATFKVKSIQELKHAYEEASKYG-------EVMIEQWVT-GKEITVA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 221 VLGDTHGNAVHLFERDCSIQRRNQ---KVVERAPAPyLNDEKRAELCGYALKIAEATDYIGAGTVEFLMDaDTGAFYFIE 297
Cdd:PRK14569 183 IVNDEVYSSVWIEPQNEFYDYESKysgKSIYHSPSG-LCEQKELEVRQLAKKAYDLLGCSGHARVDFIYD-DRGNFYIME 260
|
..
gi 1998276639 298 VN 299
Cdd:PRK14569 261 IN 262
|
|
| PRK00915 |
PRK00915 |
2-isopropylmalate synthase; Validated |
665-793 |
9.10e-03 |
|
2-isopropylmalate synthase; Validated
Pssm-ID: 234864 [Multi-domain] Cd Length: 513 Bit Score: 40.09 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 665 AMDAVRSE-GKLC---EATIcytgdlldpdrakydlkyyvglageleAAGANIIAIKDMAGLLKPGAARVLFKALRE--- 737
Cdd:PRK00915 140 AEDATRTDlDFLCrvvEAAI---------------------------DAGATTINIPDTVGYTTPEEFGELIKTLRErvp 192
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276639 738 -ATDLPLHFHTHDTSGISAATVLAAVESGVDAVDAAMDAL---SGNTSqpcLGSIVEALK 793
Cdd:PRK00915 193 nIDKAIISVHCHNDLGLAVANSLAAVEAGARQVECTINGIgerAGNAA---LEEVVMALK 249
|
|
| |
