|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
29-1173 |
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: 1977.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 29 PREFNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGKGLPPVAAYLTIDQIIETALKHNIDA 108
Cdd:COG1038 1 MKKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 109 IHPGYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIIL 188
Cdd:COG1038 81 IHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 189 KAAYGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQK 268
Cdd:COG1038 161 KAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 269 VVEIAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAE 348
Cdd:COG1038 241 VVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 349 GKSLDDLKL---SQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSASAFAGSVISPHYDSLMVKVI 425
Cdd:COG1038 321 GYSLDDPEIgipSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 426 ASARNHPNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEHPELFQFKPSQNRAQKLLNYLGEVKVN 505
Cdd:COG1038 401 AWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 506 GPTTPlATDLKPAVVSPPIPYIPAGAKPPTGLRDVLVQRGPTEFAKEVRSRPGCMITDTTFRDAHQSLLATRVRTYDMAA 585
Cdd:COG1038 481 GPPGV-KGRPKPDFPKPKLPKVDLGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 586 ISPFVAQSFNGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLRGANAMGYSNYPDNVIYKFCELAVKN 665
Cdd:COG1038 560 IAPATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 666 GMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTGDVTDKSRDKYDLKYYLNLADQLVKAQAHILSIKDMAGVLKP 745
Cdd:COG1038 640 GIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKP 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 746 EAAKLLIGALRDKFpDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGMTSQPSMGAIVASLQGTKHDTGLSLD 825
Cdd:COG1038 720 YAAYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLD 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 826 DISKYSAYWESTRQLYAPFEcaTTMKSGNADVYKHEIPGGQYTNLQFQAFSLGLGPQFDEVKRMYREANLVLGDIIKVTP 905
Cdd:COG1038 799 ALQELSNYWEAVRKYYAPFE--SGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTP 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 906 SSKIVGDLAQFMVQNNLTRETLVDRADDLSFPKSVVDFMQGNVGQPPYGFPEPLRTKVLRGKPKVDGRPGENAKPVDLDA 985
Cdd:COG1038 877 SSKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDA 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 986 VKVELEEKHGRTLSEEDVMSYSMFPTVFDEFETFRQQYGPVDKLPTRLFLTGLEIAEEVDVEIESGKTLAIQLLAEGKLN 1065
Cdd:COG1038 957 LRAELEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPD 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1066 KRGEREVFFDLNGQMRSIFVVDKEASKEIVTRPRALPGVRGHIGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVI 1145
Cdd:COG1038 1037 EDGMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTI 1116
|
1130 1140
....*....|....*....|....*...
gi 1845978298 1146 DSPIAGTVKAIHAPQGTKCSAGDLVVEV 1173
Cdd:COG1038 1117 TAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
28-1175 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 1864.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 28 KPREFNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGKGLPPVAAYLTIDQIIETALKHNID 107
Cdd:PRK12999 1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 108 AIHPGYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPII 187
Cdd:PRK12999 81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 188 LKAAYGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQ 267
Cdd:PRK12999 161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 268 KVVEIAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIA 347
Cdd:PRK12999 241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 348 EGKSLDDL---KLSQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSASAFAGSVISPHYDSLMVKV 424
Cdd:PRK12999 321 EGATLHDLeigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 425 IASARNHPNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEHPELFQFKPSQNRAQKLLNYLGEVKV 504
Cdd:PRK12999 401 TAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 505 NGPttPLATDLKPAVVSPPIPYIPAGAKPPTGLRDVLVQRGPTEFAKEVRSRPGCMITDTTFRDAHQSLLATRVRTYDMA 584
Cdd:PRK12999 481 NGF--PGVKKKPPVFPDPRLPKVDLSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 585 AISPFVAQSFNGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLRGANAMGYSNYPDNVIYKFCELAVK 664
Cdd:PRK12999 559 RIAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 665 NGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTGDVTDKSRDKYDLKYYLNLADQLVKAQAHILSIKDMAGVLK 744
Cdd:PRK12999 639 AGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLK 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 745 PEAAKLLIGALRDKFpDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGMTSQPSMGAIVASLQGTKHDTGLSL 824
Cdd:PRK12999 719 PAAAYELVSALKEEV-DLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDL 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 825 DDISKYSAYWESTRQLYAPFEcaTTMKSGNADVYKHEIPGGQYTNLQFQAFSLGLGPQFDEVKRMYREANLVLGDIIKVT 904
Cdd:PRK12999 798 DAIRKLSPYWEAVRPYYAPFE--SGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVT 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 905 PSSKIVGDLAQFMVQNNLTRETLVDRADDLSFPKSVVDFMQGNVGQPPYGFPEPLRTKVLRGKPKVDGRPGENAKPVDLD 984
Cdd:PRK12999 876 PSSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFE 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 985 AVKVELEEKHGRTLSEEDVMSYSMFPTVFDEFETFRQQYGPVDKLPTRLFLTGLEIAEEVDVEIESGKTLAIQLLAEGKL 1064
Cdd:PRK12999 956 AERAELEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEP 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1065 NKRGEREVFFDLNGQMRSIFVVDKEASKEIVTRPRALPGVRGHIGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMV 1144
Cdd:PRK12999 1036 DEDGMRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETT 1115
|
1130 1140 1150
....*....|....*....|....*....|.
gi 1845978298 1145 IDSPIAGTVKAIHAPQGTKCSAGDLVVEVEP 1175
Cdd:PRK12999 1116 ITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
34-1174 |
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: 1757.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 34 KVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGKG--LPPVAAYLTIDQIIETALKHNIDAIHP 111
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 112 GYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIILKAA 191
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 192 YGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKVVE 271
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 272 IAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGKS 351
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 352 LDDLKL---SQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSASAFAGSVISPHYDSLMVKVIASA 428
Cdd:TIGR01235 321 LPTPQLgvpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 429 RNHPNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEHPELFQFKPSQNRAQKLLNYLGEVKVNGpT 508
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNG-H 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 509 TPLATDLKPAVVSPPIPYIPAGAKP-PTGLRDVLVQRGPTEFAKEVRSRPGCMITDTTFRDAHQSLLATRVRTYDMAAIS 587
Cdd:TIGR01235 480 PEAKDKLKPLENAPRVVVLYADQNPvPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 588 PFVAQSFNGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLRGANAMGYSNYPDNVIYKFCELAVKNGM 667
Cdd:TIGR01235 560 PTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGI 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 668 DVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTGDVTDKSRDKYDLKYYLNLADQLVKAQAHILSIKDMAGVLKPEA 747
Cdd:TIGR01235 640 DIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAA 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 748 AKLLIGALRDKFpDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGMTSQPSMGAIVASLQGTKHDTGLSLDDI 827
Cdd:TIGR01235 720 AKLLIKALREKT-DLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWI 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 828 SKYSAYWESTRQLYAPFECatTMKSGNADVYKHEIPGGQYTNLQFQAFSLGLGPQFDEVKRMYREANLVLGDIIKVTPSS 907
Cdd:TIGR01235 799 RELSAYWEAVRNLYAAFES--DLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSS 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 908 KIVGDLAQFMVQNNLTRETLVDRADDLSFPKSVVDFMQGNVGQPPYGFPEPLRTKVLRGKPKVDGRPGENAKPVDLDAVK 987
Cdd:TIGR01235 877 KVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIR 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 988 VELEEKHGRTLSEEDVMSYSMFPTVFDEFETFRQQYGPVDKLPTRLFLTGLEIAEEVDVEIESGKTLAIQLLAEGKLNKR 1067
Cdd:TIGR01235 957 KDLQEKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQ 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1068 GEREVFFDLNGQMRSIFVVDKEASKEIVTRPRALPGVRGHIGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDS 1147
Cdd:TIGR01235 1037 GEREVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQA 1116
|
1130 1140
....*....|....*....|....*..
gi 1845978298 1148 PIAGTVKAIHAPQGTKCSAGDLVVEVE 1174
Cdd:TIGR01235 1117 PKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
32-492 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 689.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 32 FNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGkGLPPVAAYLTIDQIIETALKHNIDAIHP 111
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIG-PAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 112 GYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIILKAA 191
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 192 YggggrgirrVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKVVE 271
Cdd:COG4770 161 AggggkgmrvVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 272 IAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGKS 351
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 352 LDdlkLSQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSAsAFAGSVISPHYDSLMVKVIASARNH 431
Cdd:COG4770 321 LP---FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSMIAKLIVWGPDR 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 432 PNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEHPELFQFKPSQNRA 492
Cdd:COG4770 397 EEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
32-479 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 580.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 32 FNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGkglPPVAA--YLTIDQIIETALKHNIDAI 109
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIG---PAPSKksYLNIPAIISAAEITGADAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 110 HPGYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIILK 189
Cdd:PRK08591 79 HPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 190 AAYGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKV 269
Cdd:PRK08591 159 ATAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 270 VEIAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEG 349
Cdd:PRK08591 239 LEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 350 kslDDLKLSQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSAsAFAGSVISPHYDSLMVKVIASAR 429
Cdd:PRK08591 319 ---EPLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHGE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1845978298 430 NHPNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEH 479
Cdd:PRK08591 395 TREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
32-482 |
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 1845978298 32 FNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGKGlPPVAAYLTIDQIIETALKHNIDAIHP 111
Cdd:PRK08654 2 FKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPA-PPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 112 GYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIILKAA 191
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 192 YGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKVVE 271
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 272 IAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDqKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGks 351
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAG-- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 352 lDDLKLSQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSaSAFAGSVISPHYDSLMVKVIASARNH 431
Cdd:PRK08654 318 -EELSFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDS-GVHMGYEIPPYYDSMISKLIVWGRTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 432 PNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEHPEL 482
Cdd:PRK08654 396 EEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
32-479 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 562.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 32 FNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGKglPPVA-AYLTIDQIIETALKHNIDAIH 110
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGG--PRVQeSYLNLEKIIEIAKKTGAEAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 111 PGYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIILKA 190
Cdd:PRK06111 80 PGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 191 AYGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKVV 270
Cdd:PRK06111 160 SAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 271 EIAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGK 350
Cdd:PRK06111 240 EEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 351 SlddLKLSQETIQTTGSAIQCRVTTEDPaKGFQPDSGRIEVFRSGEGMGIRLDSASAfAGSVISPHYDSLMVKVIASARN 430
Cdd:PRK06111 320 K---LSFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMIAKLIAHGET 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1845978298 431 HPNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEH 479
Cdd:PRK06111 395 REEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQ 443
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
32-485 |
5.59e-178 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 531.21 E-value: 5.59e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 32 FNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGKGlpPVAAYLTIDQIIETALKHNIDAIHP 111
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD--PLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 112 GYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIILKAA 191
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 192 YGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKVVE 271
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 272 IAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGKS 351
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 352 lddLKLSQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSAsAFAGSVISPHYDSLMVKVIASARNH 431
Cdd:PRK07178 320 ---LSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTA-IYTGYTIPPYYDSMCAKLIVWALTW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1845978298 432 PNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEHPELFQF 485
Cdd:PRK07178 396 EEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNY 449
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
561-1175 |
1.09e-164 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 500.91 E-value: 1.09e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 561 ITDTTFRDAHQSLLATRVRTYDMAAIspfvAQSFN--GLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCL 638
Cdd:PRK09282 6 ITDTTLRDAHQSLLATRMRTEDMLPI----AEKLDkvGFWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 639 LRGANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYT-GDVtdksrdkYDLK 717
Cdd:PRK09282 82 LRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYTtSPV-------HTIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 718 YYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFpDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSM 797
Cdd:PRK09282 155 KYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEV-DLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 798 SGMTSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLYAPFECATTMksGNADVYKHEIPGGQYTNLQFQafsl 877
Cdd:PRK09282 234 AFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTI--VDTRVLIHQVPGGMISNLVSQ---- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 878 gLGPQ---------FDEVKRMYREanlvLGDIIKVTPSSKIVGDLAqfmVQNNLT--RETLVdraddlsfPKSVVDFMQG 946
Cdd:PRK09282 308 -LKEQnaldkldevLEEIPRVRED----LGYPPLVTPTSQIVGTQA---VLNVLTgeRYKVI--------TKEVKDYVKG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 947 NVGQPPYGFPEPLRTKVLRGKPKVDGRPGENAKPvDLDAVKVELEEKhgRTLSEEDVMSYSMFPTVFDEFETFRQQY--G 1024
Cdd:PRK09282 372 LYGRPPAPINEELRKKIIGDEEPITCRPADLLEP-ELEKARKEAEEL--GKSEKEDVLTYALFPQIAKKFLEEREAGelK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1025 PVDKLPTRLFLTGLEIAEEVDVEIEsGKTLAIQLlaEGKlNKRGEREVFFDLNGQMRSIFVvdkEASKEIVTRPRALPGV 1104
Cdd:PRK09282 449 PEPEPKEAAAAGAEGIPTEFKVEVD-GEKYEVKI--EGV-KAEGKRPFYLRVDGMPEEVVV---EPLKEIVVGGRPRASA 521
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 1105 RGHIGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVEP 1175
Cdd:PRK09282 522 PGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
32-478 |
1.36e-163 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 492.69 E-value: 1.36e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 32 FNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGKGLPPvAAYLTIDQIIETALKHNIDAIHP 111
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSK-DSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 112 GYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIILKAA 191
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 192 YGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKVVE 271
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 272 IAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGKS 351
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 352 LDdlkLSQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSAsAFAGSVISPHYDSLMVKVIASARNH 431
Cdd:PRK05586 321 LS---IKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSA-VYSGYTIPPYYDSMIGKLIVYGKDR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1845978298 432 PNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDE 478
Cdd:PRK05586 397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
561-844 |
2.45e-162 |
|
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: 482.32 E-value: 2.45e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 561 ITDTTFRDAHQSLLATRVRTYDMAAISPFVAQsfNGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLR 640
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDE--AGFFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 641 GANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTGDvtdksrDKYDLKYYL 720
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 721 NLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFPdIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGM 800
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1845978298 801 TSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLYAPF 844
Cdd:cd07937 232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
32-482 |
2.70e-162 |
|
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: 489.66 E-value: 2.70e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 32 FNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGKGlPPVAAYLTIDQIIETALKHNIDAIHP 111
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPA-PSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 112 GYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIILKAA 191
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 192 YGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKVVE 271
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 272 IAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGks 351
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAG-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 352 lDDLKLSQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSAsAFAGSVISPHYDSLMVKVIASARNH 431
Cdd:TIGR00514 319 -EPLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSH-VYSGYTVPPYYDSMIGKLITYGKTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 432 PNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEHPEL 482
Cdd:TIGR00514 397 EVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
29-477 |
4.37e-155 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 471.55 E-value: 4.37e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 29 PREFNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGkglPPVAA--YLTIDQIIETALKHNI 106
Cdd:PRK12833 2 PSRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIG---PSHAAksYLNPAAILAAARQCGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 107 DAIHPGYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPI 186
Cdd:PRK12833 79 DAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 187 ILKAAYGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHgNIVHLYERDCSVQRRH 266
Cdd:PRK12833 159 MIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 267 QKVVEIAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVD-QKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIR 345
Cdd:PRK12833 238 QKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 346 IAEGKSLDdlkLSQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSaSAFAGSVISPHYDSLMVKVI 425
Cdd:PRK12833 318 IADGEPLR---FAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDS-LLYPGYRVPPFYDSLLAKLI 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1845978298 426 ASARNHPNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFID 477
Cdd:PRK12833 394 VHGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
30-479 |
1.78e-153 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 466.14 E-value: 1.78e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 30 REFNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGkGLPPVAAYLTIDQIIETALKHNIDAI 109
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIG-GAKSSESYLNIPAIISAAEIFEADAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 110 HPGYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIILK 189
Cdd:PRK08462 81 FPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 190 AAYGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKV 269
Cdd:PRK08462 161 AAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 270 VEIAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEG 349
Cdd:PRK08462 241 IEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 350 KSLddlkLSQETIQTTGSAIQCRVTTEDPAKgFQPDSGRIEVFRSGEGMGIRLDSaSAFAGSVISPHYDSLMVKVIASAR 429
Cdd:PRK08462 321 EEL----PSQESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPGGRNVRMDS-HAYAGYVVPPYYDSMIGKLIVWGE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1845978298 430 NHPNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEH 479
Cdd:PRK08462 395 DRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
32-479 |
1.24e-149 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 457.74 E-value: 1.24e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 32 FNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGKGlpPVAAYLTIDQIIETALKHNIDAIHP 111
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTD--PIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 112 GYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGT-PGPITTADEAVEFAKQYGTPIILKA 190
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTeKLNSESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 191 AYGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKVV 270
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 271 EIAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGK 350
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 351 SLDdlkLSQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSaSAFAGSVISPHYDSLMVKVIASARN 430
Cdd:PRK08463 320 ILD---LEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDS-HIYKDYTIPPYYDSMLAKLIVKATS 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1845978298 431 HPNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEH 479
Cdd:PRK08463 396 YDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETH 444
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
561-1127 |
2.14e-133 |
|
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: 416.99 E-value: 2.14e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 561 ITDTTFRDAHQSLLATRVRTYDMAAISPFVAQSfnGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLR 640
Cdd:COG5016 6 ITDTTLRDGHQSLFATRMRTEDMLPIAEKLDEA--GFWSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQMLLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 641 GANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYT-GDVtdksrdkYDLKYY 719
Cdd:COG5016 84 GQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYTiSPV-------HTVEYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 720 LNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFpDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSG 799
Cdd:COG5016 157 VELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEAL-DIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPLAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 800 MTSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLYAPFEcaTTMKSGNADVYKHEIPGGQYTNLQFQAFSLGL 879
Cdd:COG5016 236 GTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFE--PEATGVDPRVLVHQVPGGMLSNLVSQLKEQGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 880 GPQFDEV----KRMYREanlvLGDIIKVTPSSKIVGDLAqfmVQNNLTRE--TLVdraddlsfPKSVVDFMQGNVGQPPY 953
Cdd:COG5016 314 LDRLDEVleeiPRVRED----LGYPPLVTPTSQIVGTQA---VLNVLTGEryKMI--------TKEVKDYVLGYYGKTPA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 954 GFPEPLRTKVLRGKPKVDGRPGENAKPvdldavkvELEE--KHGRTLSEEDVMSYSMFPTVFDEFETFRQQYGPVDKLPT 1031
Cdd:COG5016 379 PIDPEVRKKALGDEEPITCRPADLLEP--------ELEKlrKEGLAKSDEDVLTYALFPQVAIKFLKGRAAGEARPDAPL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1032 RlfltGLEIAEEVDVEIESGKTLAIqllAEGKLNKRGEREVFFDLNGQMRSIFVVDKEASKEIVTRPRALPGVRGHIGAP 1111
Cdd:COG5016 451 A----ELAAVEEVVVVAEGVVVVVV---VGGGAEGVVVVVVGVPGAGAVAVVAAAAAVAAAAAAAAAAAAAAAGAAVKKV 523
|
570
....*....|....*.
gi 1845978298 1112 MPGDVLELKIKEGDKV 1127
Cdd:COG5016 524 VAVGGAVVVGVEVVVV 539
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
561-1168 |
1.69e-130 |
|
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate decarboxylase alpha subunit and its equivalents in archaea. The oxaloacetate decarboxylase Na+ pump is the paradigm of the family of Na+ transport decarboxylases that present in bacteria and archaea. It a multi subunit enzyme consisting of a peripheral alpha-subunit and integral membrane subunits beta and gamma. The energy released by the decarboxylation reaction of oxaloacetate is coupled to Na+ ion pumping across the membrane. [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Other]
Pssm-ID: 273447 [Multi-domain] Cd Length: 582 Bit Score: 411.11 E-value: 1.69e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 561 ITDTTFRDAHQSLLATRVRTYDMAAISPFVAQSfnGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLR 640
Cdd:TIGR01108 1 ITDVVLRDAHQSLFATRMRTEDMLPIAEKLDDV--GYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 641 GANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTgdvtdkSRDKYDLKYYL 720
Cdd:TIGR01108 79 GQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT------TSPVHTLETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 721 NLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFpDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGM 800
Cdd:TIGR01108 153 DLAEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRF-GLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 801 TSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLYAPFEcaTTMKSGNADVYKHEIPGGQYTNLQFQAFSLGLG 880
Cdd:TIGR01108 232 TSHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFE--GQLKGPDSRILVAQVPGGMLSNLESQLKEQNAL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 881 PQFDEVkrmYREANLV---LGDIIKVTPSSKIVGDLAqfmVQNNLTREtlvdRADDLSfpKSVVDFMQGNVGQPPYGFPE 957
Cdd:TIGR01108 310 DKLDEV---LEEIPRVredLGYPPLVTPTSQIVGTQA---VLNVLTGE----RYKTIT--KETKGYLKGEYGRTPAPINA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 958 PLRTKVLRG-KPKVDGRPGENAKPvDLDAVKVELEEKHGRTLSEEDVMSYSMFPTVFDEFETFRQQYGPVDKLPTRLFLT 1036
Cdd:TIGR01108 378 ELQRKILGDeKPIVDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQVGLKFLENRHNPAAFEPKPEEKVIE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1037 GlEIAEEVDVEIESGKTLAIQLLAEGKLnkrgerevfFDLNGQMRSIFVVDKEASKEIVTRPR--ALPGVRGHIGAPMPG 1114
Cdd:TIGR01108 457 Q-EHAQVVGKYEETHASGSYTVEVEGKA---------FVVKVSPGGDVSQITASAPANTSGGTvaAKAGAGTPVTAPIAG 526
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1845978298 1115 DVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGD 1168
Cdd:TIGR01108 527 SIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAVSVGQ 580
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
561-1168 |
6.98e-116 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 372.34 E-value: 6.98e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 561 ITDTTFRDAHQSLLATRVRTYDMAAISPFVAQSfnGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLR 640
Cdd:PRK14040 7 ITDVVLRDAHQSLFATRLRLDDMLPIAAKLDKV--GYWSLESWGGATFDACIRFLGEDPWERLRELKKAMPNTPQQMLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 641 GANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTgdvtdkSRDKYDLKYYL 720
Cdd:PRK14040 85 GQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT------TSPVHTLQTWV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 721 NLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFpDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGM 800
Cdd:PRK14040 159 DLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRV-DVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAISSMSMT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 801 TSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLYAPFECAttMKSGNADVYKHEIPGGQYTNLQFQAFSLGLG 880
Cdd:PRK14040 238 YGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFEGQ--LKGVDSRILVAQVPGGMLTNMESQLKEQGAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 881 PQFDEV----KRMyREAnlvLGDIIKVTPSSKIVGDLAqfmVQNNLTREtlvdRADDLSfpKSVVDFMQGNVGQPPYGFP 956
Cdd:PRK14040 316 DKLDEVlaeiPRV-RED---LGFIPLVTPTSQIVGTQA---VLNVLTGE----RYKTIT--KETAGVLKGEYGATPAPVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 957 EPLRTKVLRGKPKVDGRPGENAKPvDLDAVKVELEEK---HGRTLSEE---DVMSYSMFPTV---F-------DEFEtfr 1020
Cdd:PRK14040 383 AELQARVLEGAEPITCRPADLLAP-ELDKLEAELRRQaqeKGITLAENaidDVLTYALFPQIglkFlenrhnpAAFE--- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1021 qqygPV----DKLPTRLFLTGLEIAEEVDVEiesGKTLAIQlLAEGklnkrgerevffdlnGQMRSIFVVDKEASKEIVT 1096
Cdd:PRK14040 459 ----PVpqaeAAQPAAKAEPAGSETYTVEVE---GKAYVVK-VSEG---------------GDISQITPAAPAAAPAAAA 515
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845978298 1097 RPRALPGVRGHIGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGD 1168
Cdd:PRK14040 516 AAAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGD 587
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
561-1016 |
7.77e-108 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 345.92 E-value: 7.77e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 561 ITDTTFRDAHQSLLATRVRTYDMAAISPFVAQSfnGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLR 640
Cdd:PRK12331 6 ITETVLRDGQQSLIATRMTTEEMLPILEKLDNA--GYHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQMLLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 641 GANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTgdvtdkSRDKYDLKYYL 720
Cdd:PRK12331 84 GQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT------TSPVHTIDYFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 721 NLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFpDIPIHVHTHDTSgaGVAAM--LECAKAGADVVDAAVDSMS 798
Cdd:PRK12331 158 KLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAV-TVPLEVHTHATS--GIAEMtyLKAIEAGADIIDTAISPFA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 799 GMTSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLY-APFECATTMKSGNADVYKHEIPGGQYTNLQFQAFSL 877
Cdd:PRK12331 235 GGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYrEEGILNPKVKDVEPKTLIYQVPGGMLSNLLSQLKEQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 878 GLGPQFDEVKRMYREANLVLGDIIKVTPSSKIVGDLAqfmVQNNLT--RETLVdraddlsfPKSVVDFMQGNVGQPPYGF 955
Cdd:PRK12331 315 GAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQA---LMNVISgeRYKMV--------PNEIKDYVRGLYGRPPAPI 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 956 PEPLRTKVLRGKPKVDGRPGENAKPvDLDAVKVELEEkhgRTLSEEDVMSYSMFPTVFDEF 1016
Cdd:PRK12331 384 AEEIKKKIIGDEEVITCRPADLIEP-QLEKLREEIAE---YAESEEDVLSYALFPQQAKDF 440
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
857-1057 |
1.95e-102 |
|
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: 321.71 E-value: 1.95e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 857 VYKHEIPGGQYTNLQFQAFSLGLGPQFDEVKRMYREANLVLGDIIKVTPSSKIVGDLAQFMVQNNLTRETLVDRADDLSF 936
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 937 PKSVVDFMQGNVGQPPYGFPEPLRTKVLRGKPKVDGRPGENAKPVDLDAVKVELEEKHGRTLSEEDVMSYSMFPTVFDEF 1016
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1845978298 1017 ETFRQQYGPVDKLPTRLFLTGLEIAEEVDVEIESGKTLAIQ 1057
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
561-1174 |
2.73e-92 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 308.96 E-value: 2.73e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 561 ITDTTFRDAHQSLLATRVRTYDMAAISPFVAQSfnGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLR 640
Cdd:PRK14042 6 ITDVTLRDAHQCLIATRMRTEDMLPICNKMDDV--GFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSMLLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 641 GANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTgdvtdkSRDKYDLKYYL 720
Cdd:PRK14042 84 GQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT------TSPVHTLDNFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 721 NLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRdKFPDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGM 800
Cdd:PRK14042 158 ELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLK-QATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 801 TSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLYAPFEcaTTMKSGNADVYKHEIPGGQYTNLQFQAFSLGLG 880
Cdd:PRK14042 237 ASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFE--SEAQNIDPRVQLYQVPGGMISNLYNQLKEQNAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 881 PQFDEVKRMYREANLVLGDIIKVTPSSKIVGDLAqfmVQNNLTRETLVDRADDLSFpksvvdFMQGNVGQPPYGFPEPLR 960
Cdd:PRK14042 315 DKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQA---VINVLTGERYKTITNEVKL------YCQGKYGTPPGKISSALR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 961 TKVLRGKPKVDGRPGEnAKPVDLDAVKVELEEkhgRTLSEEDVMSYSMFPTVFDEFETFRQ--QYGPvDKLPTRLFLTGL 1038
Cdd:PRK14042 386 KKAIGRTEVIEVRPGD-LLPNELDQLQNEISD---LALSDEDVLLYAMFPEIGRQFLEQRKnnQLIP-EPLLTQSSAPDN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1039 EIAEEVDVeIESGKTLAIQLLAEGKLnKRGEREVFFDLNGQMRSIFVVDKEASKEIVTRPRALPGVRGHIGAPMPGDVLE 1118
Cdd:PRK14042 461 SVMSEFDI-ILHGESYHVKVAGYGMI-EHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPGSIIA 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1845978298 1119 LKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVE 1174
Cdd:PRK14042 539 IHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
561-1025 |
1.90e-91 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 303.22 E-value: 1.90e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 561 ITDTTFRDAHQSLLATRVRTYDMAAISPFVAQSfnGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLR 640
Cdd:PRK12330 7 VTELALRDAHQSLMATRMAMEDMVGACEDIDNA--GYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQMLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 641 GANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTgdvtdkSRDKYDLKYYL 720
Cdd:PRK12330 85 GQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT------VSPIHTVEGFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 721 NLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKF-PDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMS- 798
Cdd:PRK12330 159 EQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSMSl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 799 GMTSQPSMgAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLYAPFECATTmkSGNADVYKHEIPGGQYTNLQFQAFSLG 878
Cdd:PRK12330 239 GPGHNPTE-SLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTT--GVETEIFKSQIPGGMLSNMESQLKQQG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 879 LGPQFDEVkrmYREANLVLGD---IIKVTPSSKIVGDLAQFMV----QNNLTREtlvdraddlsfpksVVDFMQGNVGQP 951
Cdd:PRK12330 316 AGDRMDEV---LEEVPRVRKDagyPPLVTPSSQIVGTQAVFNVlmgrYKVLTGE--------------FADLMLGYYGET 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845978298 952 PyGFPEPLRTKVLR---GKPKVDGRPGENAKPvDLDAVKVELEEKHGRTLSEEDVMSYSMFPTVFDEFETFRQQyGP 1025
Cdd:PRK12330 379 P-GERNPEVVEQAKkqaKKEPITCRPADLLEP-EWDKLRAEALALEGCDGSDEDVLTYALFPQVAPKFFATRAE-GP 452
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
560-1016 |
2.48e-89 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 296.31 E-value: 2.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 560 MITDTTFRDAHQSLLATRVRTYDMAAISPFVAQSfnGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLL 639
Cdd:PRK14041 4 MFVDTTLRDGHQSLIATRMRTEDMLPALEAFDRM--GFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQMLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 640 RGANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTGDVTdksrdkYDLKYY 719
Cdd:PRK14041 82 RGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYTVSPV------HTLEYY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 720 LNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFpDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSG 799
Cdd:PRK14041 156 LEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 800 MTSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLYAPFECAttMKSGNADVYKHEIPGGQYTNLQFQAFSLGL 879
Cdd:PRK14041 235 GTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYDVG--MKSPDSRILVSQIPGGMYSNLVKQLKEQKM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 880 GPQFDEVKRMYREANLVLGDIIKVTPSSKIVGDLAqfmVQNNLTREtlvdRADDLSfpKSVVDFMQGNVGQPPYGFPEPL 959
Cdd:PRK14041 313 LHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQA---VLNVLTGE----RYKRVT--NETKNYVKGLYGRPPAPIDEEL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1845978298 960 RTKVLRGKPKVDGRPGENAKPvDLDAVKVELEEKhgrTLSEEDVMSYSMFPTVFDEF 1016
Cdd:PRK14041 384 MKKILGDEKPIDCRPADLLEP-ELEKARKELGIL---AETDEDLLIYVILGEVGKKF 436
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
146-353 |
8.40e-83 |
|
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: 268.40 E-value: 8.40e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 146 DKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIILKAAYGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGD 225
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 226 GSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKVVEIAPAPALPEGVREKILADALRLARHVGYQNAGTV 305
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1845978298 306 EFLVDQK-GNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGKSLD 353
Cdd:pfam02786 161 EFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
562-835 |
6.98e-74 |
|
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: 245.83 E-value: 6.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 562 TDTTFRDAHQSLLATRvRTYDMAAISPFVAQSfnGLFSLENWGGATFDVSmrFLHECPWERLQTLRKLIPNIPFQCLLRG 641
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEA--GVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 642 AnamgysnypdnviYKFCELAVKNGMDVFRVFDSLNY--------------LPNLLVGMEAVGKAGGVVEAAIAYTgdvt 707
Cdd:cd03174 76 R-------------EKGIERALEAGVDEVRIFDSASEthsrknlnksreedLENAEEAIEAAKEAGLEVEGSLEDA---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 708 dkSRDKYDLKYYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFPDIPIHVHTHDTSGAGVAAMLECAKAGA 787
Cdd:cd03174 139 --FGCKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1845978298 788 DVVDAAVDSMSGMTSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWE 835
Cdd:cd03174 217 DRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
561-1029 |
1.85e-73 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 252.35 E-value: 1.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 561 ITDTTFRDAHQSLLATRVRTYDMAAISPFVAQSfnGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLR 640
Cdd:PRK12581 15 ITETVLRDGHQSLMATRLSIEDMLPVLTILDKI--GYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRLQMLLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 641 GANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTgdvtdkSRDKYDLKYYL 720
Cdd:PRK12581 93 GQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT------TSPVHTLNYYL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 721 NLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRdKFPDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGM 800
Cdd:PRK12581 167 SLVKELVEMGADSICIKDMAGILTPKAAKELVSGIK-AMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALSPFSEG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 801 TSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLY-APFECATTMKSGNADVYKHEIPGGQYTNLQFQAFSLGL 879
Cdd:PRK12581 246 TSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYlADGILDPSLLFPDPRTLQYQVPGGMLSNMLSQLKQANA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 880 GPQFDEVKRMYREANLVLGDIIKVTPSSKIVGDLAQFMVQNNLTRETLvdraddlsfPKSVVDFMQGNVGQPPYGFPEPL 959
Cdd:PRK12581 326 ESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVILGKPYQMV---------SKEIKQYLAGDYGKTPAPVNEDL 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 960 RTKVLRGKPKVDGRPGENAKPvDLDAVKVELEEkhgRTLSEEDVMSYSMFPTVFDEFETFRQQYGPVDKL 1029
Cdd:PRK12581 397 KRSQIGSAPVTTNRPADQLSP-EFEVLKAEVAD---LAQTDEDVLTYALFPSVAKPFLTTKYQTDDVIKV 462
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
94-350 |
8.14e-57 |
|
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: 197.40 E-value: 8.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 94 IDQIIETALKHNIDAIHPGYGFLSERsdFAAACQNAGIvfIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPgpITTAD 173
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVET--AAELAEELGL--PGPSPEAIRAMRDKVLMREALAAAGVPVPGFAL--VDSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 174 EAVEFAKQYGTPIILKAAYGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERpRHIEVQLLGdHHGNIV 253
Cdd:COG0439 80 EALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV-RDGEVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 254 HlyerdCSVQRRHQK---VVE---IAPAPaLPEGVREKILADALRLARHVGYQN-AGTVEFLVDQKGNYYFIEVNARLQV 326
Cdd:COG0439 158 V-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYLIEINARLGG 231
|
250 260
....*....|....*....|....*.
gi 1845978298 327 EH--TVTEEITGVDLVQAQIRIAEGK 350
Cdd:COG0439 232 EHipPLTELATGVDLVREQIRLALGE 257
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
32-140 |
1.71e-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: 181.92 E-value: 1.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 32 FNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGKGlPPVAAYLTIDQIIETALKHNIDAIHP 111
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPG-PASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*....
gi 1845978298 112 GYGFLSERSDFAAACQNAGIVFIGPSPDV 140
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
370-477 |
1.92e-47 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 164.51 E-value: 1.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 370 QCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSAsAFAGSVISPHYDSLMVKVIASARNHPNAAAKMIRALKKFRIRG 449
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSG-VYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 1845978298 450 VKTNIPFLLNVLRQPSFLDASVDTYFID 477
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
370-478 |
3.61e-41 |
|
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: 146.87 E-value: 3.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 370 QCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSAsAFAGSVISPHYDSLMVKVIASARNHPNAAAKMIRALKKFRIRG 449
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 1845978298 450 VKTNIPFLLNVLRQPSFLDASVDTYFIDE 478
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
561-833 |
5.41e-35 |
|
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: 134.78 E-value: 5.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 561 ITDTTFRDAHQSLlATRVRTYDMAAISPfvaqsfnglfSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLR 640
Cdd:pfam00682 4 ICDTTLRDGEQAL-GVAFSIDEKLAIAR----------ALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 641 GAnamgysnypDNVIYKFCELAVKNGMDVFRVFDSLNYL---PNLLVGM-EAVGKAGGVVEAAIAYTGDVTDKSRD--KY 714
Cdd:pfam00682 73 AR---------EHDIKAAVEALKGAGAVRVHVFIATSDLhrkYKLGKDReEVAKRAVAAVKAARSRGIDVEFSPEDasRT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 715 DLKYYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFPD-IPIHVHTHDTSGAGVAAMLECAKAGADVVDAA 793
Cdd:pfam00682 144 DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVDGT 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1845978298 794 VDSMSGMTSQPSMGAIVASLQGTKHDTGLSLDDISKYSAY 833
Cdd:pfam00682 224 VNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANL 263
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1107-1173 |
6.49e-23 |
|
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: 93.25 E-value: 6.49e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845978298 1107 HIGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEV 1173
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1107-1173 |
9.26e-16 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 73.02 E-value: 9.26e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845978298 1107 HIGAPMPGD-----VLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEV 1173
Cdd:pfam00364 2 EIKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
49-394 |
4.96e-15 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 78.43 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 49 RALTELNKTSVAIyAEQDKNSMHRLK-ADEAYLVGKGLPPVAAYltIDQIIETALKHNIDAIHPGY----GFLSERSDFA 123
Cdd:COG3919 22 RSLGEAGVRVIVV-DRDPLGPAARSRyVDEVVVVPDPGDDPEAF--VDALLELAERHGPDVLIPTGdeyvELLSRHRDEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 124 AAcqnaGIVFIGPSPDVMARMGDKVAARQAAIEAGVqVVPGTpGPITTADEAVEFAKQYGTPIILKAAYGGGGRGIRR-- 201
Cdd:COG3919 99 EE----HYRLPYPDADLLDRLLDKERFYELAEELGV-PVPKT-VVLDSADDLDALAEDLGFPVVVKPADSVGYDELSFpg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 202 ------VDKLEEVEEAFRRsyseaqAAFGDGSLFVEKFVERPRHIEVQLLG--DHHGNIVHLyerdCSVQRRHQKVVEIA 273
Cdd:COG3919 173 kkkvfyVDDREELLALLRR------IAAAGYELIVQEYIPGDDGEMRGLTAyvDRDGEVVAT----FTGRKLRHYPPAGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 274 PaPALPEGVR-EKILADALRLARHVGYQNAGTVEFLVDQK-GNYYFIEVNARL--QVEHTVteeITGVDLVQAQIRIAEG 349
Cdd:COG3919 243 N-SAARESVDdPELEEAARRLLEALGYHGFANVEFKRDPRdGEYKLIEINPRFwrSLYLAT---AAGVNFPYLLYDDAVG 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1845978298 350 KSLddlklsqETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRS 394
Cdd:COG3919 319 RPL-------EPVPAYREGVLWRVLPGDLLLRYLRDGELRKRLRE 356
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1108-1168 |
1.12e-14 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 71.77 E-value: 1.12e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 1108 IGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGD 1168
Cdd:PRK06549 64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGD 124
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
129-414 |
1.31e-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: 75.81 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 129 AGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGtpGPITTADEAVEFAKQYGTPIILKAAYGGGGRGIRRVDKLEEV 208
Cdd:TIGR01369 652 AGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEEL 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 209 EEAFRrsysEAQAAFGDGSLFVEKFVERPRHIEVQLLGDH-----HGNIVHLyER------DCSVqrrhqkvveIAPAPA 277
Cdd:TIGR01369 730 RRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGeevliPGIMEHI-EEagvhsgDSTC---------VLPPQT 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 278 LPEGVREKILADALRLARHVGYQNAGTVEFLVDQkGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGKSLDDLKL 357
Cdd:TIGR01369 796 LSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGV 874
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845978298 358 SQETIQTTgsaiqcrVTTEDPAKGFQPDSGR-----IEVFRSGEGMGIRLDSASAFAGSVIS 414
Cdd:TIGR01369 875 GKEKEPKY-------VAVKEPVFSFSKLAGVdpvlgPEMKSTGEVMGIGRDLAEAFLKAQLS 929
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1107-1174 |
1.62e-13 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 66.35 E-value: 1.62e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845978298 1107 HIGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVE 1174
Cdd:PRK08225 3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
92-409 |
1.75e-13 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 75.39 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 92 LTIDQIIETALKHNIDAIHPGYGFLSErSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGtpGPITT 171
Cdd:PRK12815 617 LTLEDVLNVAEAENIKGVIVQFGGQTA-INLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATD 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 172 ADEAVEFAKQYGTPIILKAAYGGGGRGIRRVDKLEEVEEAFRRSYSeaqaafGDGSLFVEKFVErPRHIEVQLLGDHH-- 249
Cdd:PRK12815 694 EEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENAS------QLYPILIDQFID-GKEYEVDAISDGEdv 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 250 ---GNIVHLyERDCSvqrrHQ-KVVEIAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVdQKGNYYFIEVNARlq 325
Cdd:PRK12815 767 tipGIIEHI-EQAGV----HSgDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVLEVNPR-- 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 326 VEHTV--TEEITGVDLVQAQIRIAEGKSLDDLKLSQETIQTTGSaiqcrVTTEDPAKGFQ--PDSGRI---EVFRSGEGM 398
Cdd:PRK12815 839 ASRTVpfVSKATGVPLAKLATKVLLGKSLAELGYPNGLWPGSPF-----IHVKMPVFSYLkyPGVDNTlgpEMKSTGEVM 913
|
330
....*....|.
gi 1845978298 399 GIRLDSASAFA 409
Cdd:PRK12815 914 GIDKDLEEALY 924
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1108-1173 |
3.79e-12 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 65.27 E-value: 3.79e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845978298 1108 IGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEV 1173
Cdd:PRK05641 87 VTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
96-360 |
4.15e-12 |
|
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: 70.29 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 96 QIIEtalKHNIDAIHPGYG-----FLSErsDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGtpGPIT 170
Cdd:COG0458 64 DIIE---KEKPDGVIVQFGgqtalNLAV--ELEEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKS--GTAT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 171 TADEAVEFAKQYGTPIILKAAYGGGGRGIRRVDKLEEVEEAFRRsyseAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHG 250
Cdd:COG0458 137 SVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLER----ALKVSPDHPVLIDESLLGAKEIEVDVVRDGED 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 251 NIV------HLyER------DCSVqrrhqkvveIAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDqKGNYYFI 318
Cdd:COG0458 213 NVIivgimeHI-EPagvhsgDSIC---------VAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD-DGRVYVI 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1845978298 319 EVNARlqVEHTVT--EEITGVDLVQAQIRIAEGKSLDDLKLSQE 360
Cdd:COG0458 282 EVNPR--ASRSSPfaSKATGYPIAKIAAKLALGYTLDELGNDTG 323
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1106-1174 |
1.99e-11 |
|
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: 62.61 E-value: 1.99e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845978298 1106 GHIGAPMPGDV-------LELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVE 1174
Cdd:COG0511 61 GAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
75-356 |
4.47e-11 |
|
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: 67.33 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 75 ADEAYLvgkgLPPVAAYLTidQIIEtalKHNIDAIHPGYG---------FLSERsdfaAACQNAGIVFIGPSPDVMARMG 145
Cdd:TIGR01369 60 ADKVYI----EPLTPEAVE--KIIE---KERPDAILPTFGgqtalnlavELEES----GVLEKYGVEVLGTPVEAIKKAE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 146 DKVAARQAAIEAGVQVVPGtpGPITTADEAVEFAKQYGTPIILKAAYGGGGRGIRRVDKLEE----VEEAFRRSYSeaqa 221
Cdd:TIGR01369 127 DRELFREAMKEIGEPVPES--EIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREElkeiAERALSASPI---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 222 afgdGSLFVEKFVERPRHIEVQLLGDHHGNIVHLyerdCSVQR-----RH--QKVVeIAPAPALPEGVREKILADALRLA 294
Cdd:TIGR01369 201 ----NQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHtgDSIV-VAPSQTLTDKEYQMLRDASIKII 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845978298 295 RHVGYQNAGTVEFLVDQKGN-YYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGKSLDDLK 356
Cdd:TIGR01369 272 RELGIEGGCNVQFALNPDSGrYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDELK 334
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
686-794 |
9.57e-10 |
|
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163676 Cd Length: 274 Bit Score: 60.87 E-value: 9.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 686 MEAVGKAGGVVEAAIA------YTGDVtdksrdkyDLKYYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKF 759
Cdd:cd07938 120 AELAKAAGLRVRGYVStafgcpYEGEV--------PPERVAEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERF 191
|
90 100 110
....*....|....*....|....*....|....*
gi 1845978298 760 PDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAV 794
Cdd:cd07938 192 PDEKLALHFHDTRGQALANILAALEAGVRRFDSSV 226
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1114-1173 |
3.28e-09 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 54.33 E-value: 3.28e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1114 GDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEV 1173
Cdd:cd06849 15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
80-321 |
6.58e-09 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 58.58 E-value: 6.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 80 LVGKGLPPVAAYLTIDQIIETALKHNID----AIHPGYGflsERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAI 155
Cdd:COG1181 28 LDKAGYDVVPIGIDVEDLPAALKELKPDvvfpALHGRGG---EDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 156 EAGVQVVPG---TPGPITTADEAVEfakQYGTPIILKAA--------YggggrgirRVDKLEEVEEAFRRSYSEaqaafg 224
Cdd:COG1181 105 AAGLPTPPYvvlRRGELADLEAIEE---ELGLPLFVKPAregssvgvS--------KVKNAEELAAALEEAFKY------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 225 DGSLFVEKFVErPRHIEVQLLGDHH------GNIV---------HLYERDcsvqrrhqKVVEIAPAPaLPEGVREKILAD 289
Cdd:COG1181 168 DDKVLVEEFID-GREVTVGVLGNGGpralppIEIVpengfydyeAKYTDG--------GTEYICPAR-LPEELEERIQEL 237
|
250 260 270
....*....|....*....|....*....|..
gi 1845978298 290 ALRLARHVGYQNAGTVEFLVDQKGNYYFIEVN 321
Cdd:COG1181 238 ALKAFRALGCRGYARVDFRLDEDGEPYLLEVN 269
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
121-342 |
6.94e-09 |
|
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: 58.41 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 121 DFAAACQNAGIVFIgPSPDVMARMGDKVAARQAAIEAGVQVvpgtpgPIT----TADEAVEFAKQYGTPIILKAAYGGGG 196
Cdd:COG0189 72 ALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPV------PPTlvtrDPDDLRAFLEELGGPVVLKPLDGSGG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 197 RGirrVDKLEEVEEAfrRSYSEAQAAFGDGSLFVEKFV--ERPRHIEVQLLGdhhGNIVHLYER-----DCSVQRRHQKV 269
Cdd:COG0189 145 RG---VFLVEDEDAL--ESILEALTELGSEPVLVQEFIpeEDGRDIRVLVVG---GEPVAAIRRipaegEFRTNLARGGR 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845978298 270 VEIAPAPalpegvrEKILADALRLARHVGYQNAGtVEFLVDQKGnYYFIEVNARLQVEHtvTEEITGVDLVQA 342
Cdd:COG0189 217 AEPVELT-------DEERELALRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVTPGFRG--LERATGVDIAEA 278
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
136-321 |
1.41e-08 |
|
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: 58.16 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 136 PSPDVMARMGDKVAARQAAIEAGVQVVPGTPgpITTADEAVEFAKQYGTPIILKAA---------YggggrgirRVDKLE 206
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAPFAA--VDSLEDLEAAIAELGLPAVLKTRrggydgkgqV--------VIKSAA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 207 EVEEAFrrsyseaqAAFGDGSLFVEKFV--ERprhiEVQLLG--DHHGNIVHlY---ErdcSVQRRHQKVVEIAPApALP 279
Cdd:COG0026 149 DLEAAW--------AALGGGPCILEEFVpfER----ELSVIVarSPDGEVAT-YpvvE---NVHRNGILDESIAPA-RIS 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1845978298 280 EGVREKILADALRLARHVGYQnaGT--VEFLVDQKGNYYfieVN 321
Cdd:COG0026 212 EALAAEAEEIAKRIAEALDYV--GVlaVEFFVTKDGELL---VN 250
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1114-1174 |
2.74e-08 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 57.91 E-value: 2.74e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 1114 GDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVE 1174
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1108-1175 |
3.17e-08 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 57.91 E-value: 3.17e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845978298 1108 IGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVEP 1175
Cdd:PRK11855 10 IGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEA 77
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1108-1174 |
4.35e-08 |
|
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: 57.19 E-value: 4.35e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845978298 1108 IGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVE 1174
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1114-1173 |
4.65e-08 |
|
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: 51.22 E-value: 4.65e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1114 GDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEV 1173
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
687-833 |
1.74e-07 |
|
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439889 [Multi-domain] Cd Length: 452 Bit Score: 55.17 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 687 EAVGKAGGVVEAAIAYTGDVT----DKSRDkyDLKYYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFPDI 762
Cdd:COG0119 116 EVLEMAVEAVKYAKEHGLEVEfsaeDATRT--DPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDV 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845978298 763 PIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSM---SGMTsqpSMGAIVASLQgTKH--DTGLSLDDISKYSAY 833
Cdd:COG0119 194 ILSVHCHNDLGLAVANSLAAVEAGADQVEGTINGIgerAGNA---ALEEVVMNLK-LKYgvDTGIDLSKLTELSRL 265
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1114-1174 |
2.04e-07 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 55.39 E-value: 2.04e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 1114 GDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVE 1174
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE 279
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1114-1174 |
2.34e-07 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 55.01 E-value: 2.34e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 1114 GDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVE 1174
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFE 178
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1114-1175 |
1.09e-06 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 52.70 E-value: 1.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845978298 1114 GDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVEP 1175
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFES 76
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
136-313 |
1.42e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 52.08 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 136 PSPDVMARMGDKVAARQAAIEAGVQVVPGTPgpITTADEAVEFAKQYGTPIILKAA---YggggrgirrvD-----KLEE 207
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFAV--VDSAEDLEAALADLGLPAVLKTRrggY----------DgkgqwVIRS 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 208 VEEAfrrsySEAQAAFGDGSLFVEKFV--ERprhiEVQLLG--DHHGNIVH--LYErdcSVQRRHQKVVEIAPApALPEG 281
Cdd:PRK06019 158 AEDL-----EAAWALLGSVPCILEEFVpfER----EVSVIVarGRDGEVVFypLVE---NVHRNGILRTSIAPA-RISAE 224
|
170 180 190
....*....|....*....|....*....|....
gi 1845978298 282 VREKILADALRLARHVGYqnAGT--VEFLVDQKG 313
Cdd:PRK06019 225 LQAQAEEIASRIAEELDY--VGVlaVEFFVTGDG 256
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
687-794 |
1.98e-06 |
|
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163678 Cd Length: 268 Bit Score: 50.91 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 687 EAVGKAGGVVEAAIAYTGDVT----DKSRDkyDLKYYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFPDI 762
Cdd:cd07940 111 EVLERAVEAVEYAKSHGLDVEfsaeDATRT--DLDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPNI 188
|
90 100 110
....*....|....*....|....*....|....
gi 1845978298 763 --PIHVHTHDTSGAGVAAMLECAKAGADVVDAAV 794
Cdd:cd07940 189 kvPISVHCHNDLGLAVANSLAAVEAGARQVECTI 222
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1108-1163 |
6.05e-06 |
|
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: 45.13 E-value: 6.05e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845978298 1108 IGAPMP------GDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTK 1163
Cdd:cd06663 2 ILIPDLaqhlgdGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1110-1170 |
7.11e-06 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 44.80 E-value: 7.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 1110 APMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLV 1170
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLI 67
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
75-323 |
9.09e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 49.11 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 75 ADEAYLVgkglPPVAAYLTIDQIIETALKHNIDAIHPGY----GFLSE-RSDFAAAcqnaGIVFIGPSPDVMARMGDKVA 149
Cdd:PRK12767 43 ADKFYVV----PKVTDPNYIDRLLDICKKEKIDLLIPLIdpelPLLAQnRDRFEEI----GVKVLVSSKEVIEICNDKWL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 150 ARQAAIEAGVQVVPG-TPGPITTADEAvEFAKQYGTPIILKAAYGGGGRGIRRVDKLEEVEEAFrrSYSEAqaafgdgsL 228
Cdd:PRK12767 115 TYEFLKENGIPTPKSyLPESLEDFKAA-LAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLL--EYVPN--------L 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 229 FVEKFVErprHIE--VQLLGDHHGNIVHlyerdcSVQRRHQKVV--EIAPAPALPEGVREKILADALRLARHVGYQNagt 304
Cdd:PRK12767 184 IIQEFIE---GQEytVDVLCDLNGEVIS------IVPRKRIEVRagETSKGVTVKDPELFKLAERLAEALGARGPLN--- 251
|
250
....*....|....*....
gi 1845978298 305 VEFLVDqKGNYYFIEVNAR 323
Cdd:PRK12767 252 IQCFVT-DGEPYLFEINPR 269
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1114-1174 |
1.13e-05 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 49.02 E-value: 1.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 1114 GDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVE 1174
Cdd:PRK11856 17 GEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIE 77
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
722-800 |
1.44e-05 |
|
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF ) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163681 Cd Length: 263 Bit Score: 47.88 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 722 LADQ---LVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFPDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAavdSMS 798
Cdd:cd07943 143 LAEQaklMESYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRIDG---SLA 219
|
..
gi 1845978298 799 GM 800
Cdd:cd07943 220 GL 221
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
183-321 |
1.56e-05 |
|
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: 47.31 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 183 GTPIILKAAYGGGGRGIRRVDKLEEVEEAFRRsyseaqAAFGDGSLFVEKFVErPRHIEVQLLGDHHGNIVHLYER--DC 260
Cdd:pfam07478 36 GYPVFVKPARLGSSVGVSKVESREELQAAIEE------AFQYDEKVLVEEGIE-GREIECAVLGNEDPEVSPVGEIvpSG 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845978298 261 SVQRRHQKVVE-----IAPAPaLPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVN 321
Cdd:pfam07478 109 GFYDYEAKYIDdsaqiVVPAD-LEEEQEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVN 173
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1108-1174 |
3.10e-05 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 47.95 E-value: 3.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845978298 1108 IGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVE 1174
Cdd:TIGR01348 124 IGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
133-321 |
3.80e-05 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 47.89 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 133 FIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVE-----FAKQYGTPIILKAAYGGGGRGIRRVDKLEE 207
Cdd:PRK14573 555 YTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQPLTLAGWKREPElclahIVEAFSFPMFVKTAHLGSSIGVFEVHNVEE 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 208 VEEAFrrsyseAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGN--IVHLYERdC------SVQRRH----QKVVEIAPA 275
Cdd:PRK14573 635 LRDKI------SEAFLYDTDVFVEESRLGSREIEVSCLGDGSSAyvIAGPHER-RgsggfiDYQEKYglsgKSSAQIVFD 707
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1845978298 276 PALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVN 321
Cdd:PRK14573 708 LDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMN 753
|
|
| PRK08195 |
PRK08195 |
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated |
721-827 |
8.11e-05 |
|
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
Pssm-ID: 181282 [Multi-domain] Cd Length: 337 Bit Score: 46.36 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 721 NLADQ---LVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKF-PDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDS 796
Cdd:PRK08195 145 KLAEQaklMESYGAQCVYVVDSAGALLPEDVRDRVRALRAALkPDTQVGFHGHNNLGLGVANSLAAVEAGATRIDGSLAG 224
|
90 100 110
....*....|....*....|....*....|....
gi 1845978298 797 M---SGMTsqpSMGAIVASLQGTKHDTGLSLDDI 827
Cdd:PRK08195 225 LgagAGNT---PLEVLVAVLDRMGWETGVDLYKL 255
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
695-829 |
8.37e-05 |
|
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic TIM barrel domain; Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step of the citramalate pathway. Citramalate is only found in Leptospira interrogans and a few other microorganisms. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163683 [Multi-domain] Cd Length: 280 Bit Score: 45.83 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 695 VVEAAIA-------YTGDVTDKSRDKYDlkYYLNLADQLVKaqahiLSIK-----DMAGVLKPEAAKLLIGALRDKFPDI 762
Cdd:cd07945 120 VIEYAIKngievniYLEDWSNGMRDSPD--YVFQLVDFLSD-----LPIKrimlpDTLGILSPFETYTYISDMVKRYPNL 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845978298 763 PIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGMTSQPSMGAIVASLQG-TKHDTGL---SLDDISK 829
Cdd:cd07945 193 HFDFHAHNDYDLAVANVLAAVKAGIKGLHTTVNGLGERAGNAPLASVIAVLKDkLKVKTNIdekRLNRASR 263
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
124-414 |
8.58e-05 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 47.08 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 124 AACQNAGIVFIGPSPDVMARMGDKvaARQAAI--EAGVQVVPGtpGPITTADEAVEFAKQYGTPIILKAAYGGGGRGIRR 201
Cdd:PLN02735 680 SASGNGNVKIWGTSPDSIDAAEDR--ERFNAIlnELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEI 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 202 VDKleevEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIV-------------HLYERDCSVqrrhqk 268
Cdd:PLN02735 756 VYS----DDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVViggimehieqagvHSGDSACSL------ 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 269 vveiaPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAE 348
Cdd:PLN02735 826 -----PTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMS 900
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845978298 349 GKSLDDLKLSQETIqTTGSAIQCRVTTEDPAKGFQPDSGRiEVFRSGEGMGIRLDSASAFAGSVIS 414
Cdd:PLN02735 901 GKSLKDLGFTEEVI-PAHVSVKEAVLPFDKFQGCDVLLGP-EMRSTGEVMGIDYEFSKAFAKAQIA 964
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
123-362 |
1.42e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 46.24 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 123 AAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGtpGPITTADEAVEFAKQYGTPIILKAAYggggrgirrV 202
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSY---------V 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 203 ------------DKLEE-VEEAFRRSyseaqaafGDGSLFVEKFVERPRHIEVQLLGDHH-----GNIVHLyER------ 258
Cdd:PRK05294 715 lggrameivydeEELERyMREAVKVS--------PDHPVLIDKFLEGAIEVDVDAICDGEdvligGIMEHI-EEagvhsg 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 259 D--CSVqrrhqkvveiaPAPALPEGVREKILADALRLARH---VGYQNagtVEFLVdQKGNYYFIEVNARlqVEHTV--T 331
Cdd:PRK05294 786 DsaCSL-----------PPQTLSEEIIEEIREYTKKLALElnvVGLMN---VQFAV-KDDEVYVIEVNPR--ASRTVpfV 848
|
250 260 270
....*....|....*....|....*....|.
gi 1845978298 332 EEITGVDLVQAQIRIAEGKSLDDLKLSQETI 362
Cdd:PRK05294 849 SKATGVPLAKIAARVMLGKKLAELGYTKGLI 879
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
708-794 |
1.54e-04 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 45.55 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 708 DKSRDkyDLKYYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRdKFPDIPIHVHTHDTSGAGVAAMLECAKAGA 787
Cdd:PRK11858 138 DASRT--DLDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELV-EAVDIPIEVHCHNDFGMATANALAGIEAGA 214
|
....*..
gi 1845978298 788 DVVDAAV 794
Cdd:PRK11858 215 KQVHTTV 221
|
|
| NQRA |
pfam05896 |
Na(+)-translocating NADH-quinone reductase subunit A (NQRA); This family consists of several ... |
1108-1157 |
2.12e-04 |
|
Na(+)-translocating NADH-quinone reductase subunit A (NQRA); This family consists of several bacterial Na(+)-translocating NADH-quinone reductase subunit A (NQRA) proteins. The Na(+)-translocating NADH: ubiquinone oxidoreductase (Na(+)-NQR) generates an electrochemical Na(+) potential driven by aerobic respiration.
Pssm-ID: 461773 Cd Length: 257 Bit Score: 44.50 E-value: 2.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1108 IGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKmEMVIDSPIAGTVKAIH 1157
Cdd:pfam05896 32 LGEDYVGLKPKMKVKEGDKVKAGQVLFEDKKNP-GVKFTSPASGTVVAIN 80
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
708-831 |
2.34e-04 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 45.31 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 708 DKSRDkyDLKYYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKfPDIPIHVHTHDTSGAGVAAMLECAKAGA 787
Cdd:PRK09389 136 DASRA--DLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSEL-VKGPVSIHCHNDFGLAVANTLAALAAGA 212
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1845978298 788 DVVDAAVDSMSGMTSQPSMGAIVASL-QGTKHDTGLSLDDISKYS 831
Cdd:PRK09389 213 DQVHVTINGIGERAGNASLEEVVMALkHLYDVETGIKLEELYELS 257
|
|
| PRK05352 |
PRK05352 |
Na(+)-translocating NADH-quinone reductase subunit A; Provisional |
1108-1174 |
2.44e-04 |
|
Na(+)-translocating NADH-quinone reductase subunit A; Provisional
Pssm-ID: 235426 [Multi-domain] Cd Length: 448 Bit Score: 45.17 E-value: 2.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845978298 1108 IGAPMPGDVLELKIKEGDKVTKKQPLFVlSAMKMEMVIDSPIAGTVKAIHapQGTKCSAGDLVVEVE 1174
Cdd:PRK05352 33 LGEDYVGLRPKMKVKEGDKVKKGQPLFE-DKKNPGVKFTSPASGTVVAIN--RGERRVLQSVVIEVE 96
|
|
| DRE_TIM_HOA_like |
cd07944 |
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ... |
713-800 |
3.01e-04 |
|
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: 44.09 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 713 KYDLKYYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKF-PDIPIHVHTHDTSGAGVAAMLECAKAGADVVD 791
Cdd:cd07944 134 GYSDEELLELLELVNEIKPDVFYIVDSFGSMYPEDIKRIISLLRSNLdKDIKLGFHAHNNLQLALANTLEAIELGVEIID 213
|
....*....
gi 1845978298 792 AavdSMSGM 800
Cdd:cd07944 214 A---TVYGM 219
|
|
| PRK05692 |
PRK05692 |
hydroxymethylglutaryl-CoA lyase; Provisional |
722-839 |
3.10e-04 |
|
hydroxymethylglutaryl-CoA lyase; Provisional
Pssm-ID: 180206 Cd Length: 287 Bit Score: 44.11 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 722 LADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFPDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGMT 801
Cdd:PRK05692 160 VAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAERLAGHFHDTYGQALANIYASLEEGITVFDASVGGLGGCP 239
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1845978298 802 SQPsmGA--------IVASLQGTKHDTGLSLDDISKYSAYWESTRQ 839
Cdd:PRK05692 240 YAP--GAsgnvatedVLYMLHGLGIETGIDLDKLVRAGQFIQSKLG 283
|
|
| PRK06524 |
PRK06524 |
biotin carboxylase-like protein; Validated |
78-336 |
7.25e-04 |
|
biotin carboxylase-like protein; Validated
Pssm-ID: 180605 [Multi-domain] Cd Length: 493 Bit Score: 43.58 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 78 AYLVGKGLPPVAAYLTIDQIIEtalkhnidaihpgygflsersdfaAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEA 157
Cdd:PRK06524 98 EFIKRRGPGGKACFVMFDEETE------------------------ALARQAGLEVMHPPAELRHRLDSKIVTTRLANEA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 158 GVQVVPGTPGPITTADEAVEFAKQY--GTPIILKAAYGGGGRGIRRVdkleeveeAFRRSYSE-AQAAFGDGSLfveKFV 234
Cdd:PRK06524 154 GVPSVPHVLGRVDSYDELSALAHGAglGDDLVVQTPYGDSGSTTFFV--------RGQRDWDKyAGGIVGQPEI---KVM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 235 ERPRHIEVQLLG--DHHGNIVHLYERDCSvqrRHQKVV---------EIAPApALPEGVREKI------LADalRLARHv 297
Cdd:PRK06524 223 KRIRNVEVCIEAcvTRHGTVIGPAMTSLV---GYPELTpyrggwcgnDIWPG-ALPPAQTRKAremvrkLGD--VLSRE- 295
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1845978298 298 GYQNAGTVEFLVDQKGN-YYFIEVNARLQVEHTVTEEITG 336
Cdd:PRK06524 296 GYRGYFEVDLLHDLDADeLYLGEVNPRLSGASPMTNLTTE 335
|
|
| NqrA |
COG1726 |
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrA [Energy production and ... |
1089-1175 |
1.54e-03 |
|
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrA [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrA is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase
Pssm-ID: 441332 [Multi-domain] Cd Length: 445 Bit Score: 42.43 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1089 EASKEIVTRPR----ALpgvrghIGAPMPGDVLELKIKEGDKVTKKQPLFVlSAMKMEMVIDSPIAGTVKAIHapQGTKC 1164
Cdd:COG1726 14 APEQVIEDGPAsktvAL------LGEDYVGMKPKMLVKEGDRVKAGQPLFE-DKKNPGVKFTSPVSGTVVEIN--RGEKR 84
|
90
....*....|.
gi 1845978298 1165 SAGDLVVEVEP 1175
Cdd:COG1726 85 VLLSVVIEVDG 95
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
272-350 |
1.70e-03 |
|
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: 42.21 E-value: 1.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845978298 272 IAPAPaLPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGnYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGK 350
Cdd:COG2232 213 IGPLA-LPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDG-PYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRGE 289
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
129-321 |
1.93e-03 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 41.64 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 129 AGIVFIGPspDVMA-RMG-DKVAARQAAIEAGVQVVPG---TPGPITTADEAvEFAKQYGTPIILKAA--------Yggg 195
Cdd:PRK01966 106 LGIPYVGC--GVLAsALSmDKILTKRLLAAAGIPVAPYvvlTRGDWEEASLA-EIEAKLGLPVFVKPAnlgssvgiS--- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 196 grgirRVDKLEEVEEAFrrsyseaQAAFG-DGSLFVEKFVErPRHIEVQLLGdhhgnivhlYERDCSVqrrhqkVVEIAP 274
Cdd:PRK01966 180 -----KVKNEEELAAAL-------DLAFEyDRKVLVEQGIK-GREIECAVLG---------NDPKASV------PGEIVK 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845978298 275 A-------------------PA-LPEGVREKILADALR---------LARhvgyqnagtVEFLVDQKGNYYFIEVN 321
Cdd:PRK01966 232 PddfydyeakyldgsaeliiPAdLSEELTEKIRELAIKafkalgcsgLAR---------VDFFLTEDGEIYLNEIN 298
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
137-339 |
5.08e-03 |
|
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: 40.41 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 137 SPDVMARMGDKVAARQAAIEAGVqvvpgtPGPITTA----DEAVEFAKQYGTPIILKAA---YGGGGRGIRRVDKLEEVE 209
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGI------PLPRTGLagspEEALKLIEEIGFPVVLKPVfgsWGRGVSLARDRQAAESLL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 210 EAFRrsyseaQAAFGDGSLFVEKFVERP--RHIEVQLLGDhhgNIVHLYERDCSVQRRHQ--KVVEIAPAPALPEGvrEK 285
Cdd:TIGR00768 153 EHFE------QLNGPQNLFLVQEYIKKPggRDIRVFVVGD---EVVAAIYRITSGHWRSNlaRGGKAEPCSLTEEI--EE 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1845978298 286 IladALRLARHVGYQNAGtVEFLVDQKGnYYFIEVNArlQVEHTVTEEITGVDL 339
Cdd:TIGR00768 222 L---AIKAAKALGLDVAG-VDLLESEDG-LLVNEVNA--NPEFKNSVKTTGVNI 268
|
|
| RnfC_N |
pfam13375 |
RnfC Barrel sandwich hybrid domain; This domain is part of the barrel sandwich hybrid ... |
1088-1172 |
8.19e-03 |
|
RnfC Barrel sandwich hybrid domain; This domain is part of the barrel sandwich hybrid superfamily. It is found at the N-terminus of the RnfC Electron transport complex protein. It appears to be most related to the N-terminal NQRA domain (pfam05896).
Pssm-ID: 433157 [Multi-domain] Cd Length: 101 Bit Score: 37.15 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 1088 KEASKEIVTRPRALPG-----VRGHIGAPmpgdvLELKIKEGDKVTKKQPL-----FVLSAmkmemvIDSPIAGTVKAIH 1157
Cdd:pfam13375 13 KELSKDKPIEKLPLPKelvipLSQHIGAP-----AEPIVKVGDRVLKGQKIaeadgFVSAP------VHASVSGTVKAIE 81
|
90
....*....|....*...
gi 1845978298 1158 ---APQGTKCSAgdLVVE 1172
Cdd:pfam13375 82 prpVPHGSGVNC--IVIE 97
|
|
| PRK00915 |
PRK00915 |
2-isopropylmalate synthase; Validated |
687-790 |
9.85e-03 |
|
2-isopropylmalate synthase; Validated
Pssm-ID: 234864 [Multi-domain] Cd Length: 513 Bit Score: 40.09 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845978298 687 EAVGKAGGVVEAAIAYTGDV----TDKSRDkyDLKYYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFPDI 762
Cdd:PRK00915 117 EVLEMAVEAVKYARSYTDDVefsaEDATRT--DLDFLCRVVEAAIDAGATTINIPDTVGYTTPEEFGELIKTLRERVPNI 194
|
90 100 110
....*....|....*....|....*....|.
gi 1845978298 763 ---PIHVHTHDTSGAGVAAMLECAKAGADVV 790
Cdd:PRK00915 195 dkaIISVHCHNDLGLAVANSLAAVEAGARQV 225
|
|
| |
