|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
37-1196 |
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: 1956.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 37 KPIRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKGLPPVEAYLNIPELIRVCKENDVDAV 116
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 117 HPGYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFK 196
Cdd:COG1038 82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 197 AA-----------YggggrgmrvvrKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYER 265
Cdd:COG1038 162 AAaggggrgmrvvR-----------SEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFER 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 266 DCSVQRRHQKVVEIAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGID 345
Cdd:COG1038 231 DCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGID 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 346 LVQSQIRVAEGMTL--PELG-YTQDKIVPRGYAIQCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSASAYAGAIISP 422
Cdd:COG1038 311 IVQSQILIAEGYSLddPEIGiPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 423 YYDSLLVKVISHASDLQSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDEHPQLFKFKPSLNRAQKL 502
Cdd:COG1038 391 YYDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 503 LNYMGEVLVNGPQTPlATTLKPALVSPHVPEVPLDlspeaiereergeakvTEPPKGLREVLVCEGPEAFAKEVRNRKEL 582
Cdd:COG1038 471 LTYLGDVTVNGPPGV-KGRPKPDFPKPKLPKVDLG----------------APPPKGTKQILDELGPEGFAKWLREQKKV 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 583 LLMDTTFRDAHQSLLATRVRSHDLLKISPYVTHKFNNLYSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPFQMLL 662
Cdd:COG1038 534 LLTDTTFRDAHQSLLATRVRTRDMLKIAPATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLL 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 663 RGANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTGDVSDPKRTKYDLKYY 742
Cdd:COG1038 614 RGSNAVGYTNYPDNVVRAFVKEAAEAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYY 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 743 TNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHpDIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDSMSG 822
Cdd:COG1038 694 VDLAKELEKAGAHILAIKDMAGLLKPYAAYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSG 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 823 MTSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFEctTTMRSGNADVYLNEIPGGQYTNLQFQAFSLGL 902
Cdd:COG1038 773 LTSQPSLNSLVAALEGTERDTGLDLDALQELSNYWEAVRKYYAPFE--SGLKAPTAEVYKHEMPGGQYSNLRQQARALGL 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 903 GDFFEDVKKAYREANLLLGDIIKVTPSSKVVGDLAQFMVQNDLTADQVLERAEELSFPKSVVEYLQGSIGIPHGGFPEPL 982
Cdd:COG1038 851 GDRWEEVKEMYAAVNRLFGDIVKVTPSSKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEEL 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 983 RSRVLKDMPRIEGRPGAELKDLDFDKLKKELQESHTC-VTNRDVMSAALYPQVTNDFLNFREKYGPVDKLDTRIFLTGPK 1061
Cdd:COG1038 931 QKKVLKGRKPITVRPGELLPPVDFDALRAELEEKLGRePSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLR 1010
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1062 VGEEFDVPLERGKTLSVKALAVSaDLKPNGIREVFFELNGQLRAVHILDKEAVKEIHVHPKANKSNKSEVGAPMPGTVID 1141
Cdd:COG1038 1011 PGEEIEVEIEEGKTLIIKLLAIG-EPDEDGMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVK 1089
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*
gi 24652222 1142 IRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMII 1196
Cdd:COG1038 1090 VLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
41-1197 |
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: 1953.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 41 SVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKG--LPPVEAYLNIPELIRVCKENDVDAVHP 118
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 119 GYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFKAA 198
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 199 YGGGGRGMRVVRKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERDCSVQRRHQKVVE 278
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 279 IAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEGMT 358
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 359 LP--ELGY-TQDKIVPRGYAIQCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSASAYAGAIISPYYDSLLVKVISHA 435
Cdd:TIGR01235 321 LPtpQLGVpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 436 SDLQSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDEHPQLFKFKPSLNRAQKLLNYMGEVLVNGpQ 515
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNG-H 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 516 TPLATTLKPALVSPHVPEVPLDLSPEaiereergeakvtepPKGLREVLVCEGPEAFAKEVRNRKELLLMDTTFRDAHQS 595
Cdd:TIGR01235 480 PEAKDKLKPLENAPRVVVLYADQNPV---------------PRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 596 LLATRVRSHDLLKISPYVTHKFNNLYSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPFQMLLRGANAVGYTSYPD 675
Cdd:TIGR01235 545 LLATRVRTHDLAKIAPTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPD 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 676 NVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTGDVSDPKRTKYDLKYYTNLADELVKAGTH 755
Cdd:TIGR01235 625 NVVKYFVKQAAQGGIDIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAH 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 756 VLCIKDMAGLLKPESARLLITAIRDKHpDIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDSMSGMTSQPSMGAVVAS 835
Cdd:TIGR01235 705 ILGIKDMAGLLKPAAAKLLIKALREKT-DLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAA 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 836 LQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFECttTMRSGNADVYLNEIPGGQYTNLQFQAFSLGLGDFFEDVKKAYRE 915
Cdd:TIGR01235 784 LEGSERDPGLNVAWIRELSAYWEAVRNLYAAFES--DLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYRE 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 916 ANLLLGDIIKVTPSSKVVGDLAQFMVQNDLTADQVLERAEELSFPKSVVEYLQGSIGIPHGGFPEPLRSRVLKDMPRIEG 995
Cdd:TIGR01235 862 ANQMFGDIVKVTPSSKVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITV 941
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 996 RPGAELKDLDFDKLKKELQESHTC-VTNRDVMSAALYPQVTNDFLNFREKYGPVDKLDTRIFLTGPKVGEEFDVPLERGK 1074
Cdd:TIGR01235 942 RPGSLLEPADLDAIRKDLQEKHEReVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGK 1021
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1075 TLSVKALAVSaDLKPNGIREVFFELNGQLRAVHILDKEAVKEIHVHPKANKSNKSEVGAPMPGTVIDIRVKVGDKVEKGQ 1154
Cdd:TIGR01235 1022 TLIIKLQAVG-ATDSQGEREVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGD 1100
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|...
gi 24652222 1155 PLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE 1197
Cdd:TIGR01235 1101 PLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
35-1197 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 1840.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 35 EYKPIRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKGLPPVEAYLNIPELIRVCKENDVD 114
Cdd:PRK12999 1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 115 AVHPGYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVI 194
Cdd:PRK12999 81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 195 FKAA--------YGGGGRgmrvvrkmEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERD 266
Cdd:PRK12999 161 LKASaggggrgmRIVRSE--------EELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 267 CSVQRRHQKVVEIAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGIDL 346
Cdd:PRK12999 233 CSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 347 VQSQIRVAEGMTLPELGY---TQDKIVPRGYAIQCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSASAYAGAIISPY 423
Cdd:PRK12999 313 VQSQILIAEGATLHDLEIgipSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 424 YDSLLVKVISHASDLQSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDEHPQLFKFKPSLNRAQKLL 503
Cdd:PRK12999 393 YDSLLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 504 NYMGEVLVNGPqtPLATTLKPALVSPHVPEVPLDlspeaiereergeakvTEPPKGLREVLVCEGPEAFAKEVRNRKELL 583
Cdd:PRK12999 473 TYIADVTVNGF--PGVKKKPPVFPDPRLPKVDLS----------------APPPAGTKQILDELGPEGFADWLRDQKRVL 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 584 LMDTTFRDAHQSLLATRVRSHDLLKISPYVTHKFNNLYSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPFQMLLR 663
Cdd:PRK12999 535 LTDTTFRDAHQSLLATRVRTKDLLRIAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLR 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 664 GANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTGDVSDPKRTKYDLKYYT 743
Cdd:PRK12999 615 GSNAVGYTNYPDNVVRAFVREAAAAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYV 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 744 NLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHpDIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDSMSGM 823
Cdd:PRK12999 695 DLAKELEKAGAHILAIKDMAGLLKPAAAYELVSALKEEV-DLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGL 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 824 TSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFEctTTMRSGNADVYLNEIPGGQYTNLQFQAFSLGLG 903
Cdd:PRK12999 774 TSQPSLNSIVAALEGTERDTGLDLDAIRKLSPYWEAVRPYYAPFE--SGLKSPTTEVYLHEMPGGQYSNLKQQARALGLG 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 904 DFFEDVKKAYREANLLLGDIIKVTPSSKVVGDLAQFMVQNDLTADQVLERAEELSFPKSVVEYLQGSIGIPHGGFPEPLR 983
Cdd:PRK12999 852 DRFEEVKEMYAAVNRMFGDIVKVTPSSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQ 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 984 SRVLKDMPRIEGRPGAELKDLDFDKLKKELQESHT-CVTNRDVMSAALYPQVTNDFLNFREKYGPVDKLDTRIFLTGPKV 1062
Cdd:PRK12999 932 KKVLKGEEPITVRPGELLEPVDFEAERAELEEKLGrEVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRP 1011
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1063 GEEFDVPLERGKTLSVKALAVSaDLKPNGIREVFFELNGQLRAVHILDKEAVKEIHVHPKANKSNKSEVGAPMPGTVIDI 1142
Cdd:PRK12999 1012 GEEIEVEIEPGKTLIIKLEAIG-EPDEDGMRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTV 1090
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*
gi 24652222 1143 RVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE 1197
Cdd:PRK12999 1091 LVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
38-499 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 706.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 38 PIRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGkGLPPVEAYLNIPELIRVCKENDVDAVH 117
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIG-PAPAAESYLNIDAIIAAAKATGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 118 PGYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFKA 197
Cdd:COG4770 80 PGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 198 A-----------YggggrgmrvvrKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERD 266
Cdd:COG4770 160 SaggggkgmrvvR-----------SEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 267 CSVQRRHQKVVEIAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGIDL 346
Cdd:COG4770 229 CSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 347 VQSQIRVAEGMTLPelgYTQDKIVPRGYAIQCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSAsAYAGAIISPYYDS 426
Cdd:COG4770 309 VEEQIRIAAGEPLP---FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDS 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24652222 427 LLVKVISHASDLQSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDEHPQLFKFKPSLNRA 499
Cdd:COG4770 385 MIAKLIVWGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
39-486 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 631.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 39 IRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKGlPPVEAYLNIPELIRVCKENDVDAVHP 118
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPA-PSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 119 GYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFKAA 198
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 199 YGGGGRGMRVVRKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERDCSVQRRHQKVVE 278
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 279 IAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEGMt 358
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 359 lpELGYTQDKIVPRGYAIQCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSAsAYAGAIISPYYDSLLVKVISHASDL 438
Cdd:PRK08591 320 --PLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHGETR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 24652222 439 QSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDEH 486
Cdd:PRK08591 397 EEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
42-508 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 582.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 42 VLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKGlPPVEAYLNIPELIRVCKENDVDAVHPGYG 121
Cdd:PRK08654 5 ILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPA-PPSKSYLNIERIIDVAKKAGADAIHPGYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 122 FLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFKAAYGG 201
Cdd:PRK08654 84 FLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 202 GGRGMRVVRKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERDCSVQRRHQKVVEIAP 281
Cdd:PRK08654 164 GGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 282 APRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDeSGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEGMTLPe 361
Cdd:PRK08654 244 SPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELS- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 362 lgYTQDKIVPRGYAIQCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSaSAYAGAIISPYYDSLLVKVISHASDLQSS 441
Cdd:PRK08654 322 --FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDS-GVHMGYEIPPYYDSMISKLIVWGRTREEA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24652222 442 ASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDEHPQLfkfkpslnrAQKLLNYMGE 508
Cdd:PRK08654 399 IARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI---------LEEMKRYALE 456
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
39-488 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 552.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 39 IRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKGlPPVEAYLNIPELIRVCKENDVDAVHP 118
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGP-RVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 119 GYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFKAA 198
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 199 YGGGGRGMRVVRKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERDCSVQRRHQKVVE 278
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 279 IAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEGMT 358
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 359 LPelgYTQDKIVPRGYAIQCRVTTEDPaNDFQPNTGRLEVFRSGEGMGIRLDSASAyAGAIISPYYDSLLVKVISHASDL 438
Cdd:PRK06111 321 LS---FTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMIAKLIAHGETR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24652222 439 QSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDEHPQ 488
Cdd:PRK06111 396 EEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQLV 445
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
39-492 |
1.43e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 538.53 E-value: 1.43e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 39 IRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKGlpPVEAYLNIPELIRVCKENDVDAVHP 118
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD--PLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 119 GYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFKAA 198
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 199 YGGGGRGMRVVRKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERDCSVQRRHQKVVE 278
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 279 IAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEGMT 358
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 359 LPelgYTQDKIVPRGYAIQCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSAsAYAGAIISPYYDSLLVKVISHASDL 438
Cdd:PRK07178 320 LS---YKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTA-IYTGYTIPPYYDSMCAKLIVWALTW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 24652222 439 QSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDEHPQLFKF 492
Cdd:PRK07178 396 EEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNY 449
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
39-486 |
5.12e-178 |
|
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: 530.87 E-value: 5.12e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 39 IRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKGlPPVEAYLNIPELIRVCKENDVDAVHP 118
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPA-PSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 119 GYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFKAA 198
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 199 YGGGGRGMRVVRKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERDCSVQRRHQKVVE 278
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 279 IAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEGMT 358
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 359 LPelgYTQDKIVPRGYAIQCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSAsAYAGAIISPYYDSLLVKVISHASDL 438
Cdd:TIGR00514 321 LS---LKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSH-VYSGYTVPPYYDSMIGKLITYGKTR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 24652222 439 QSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDEH 486
Cdd:TIGR00514 397 EVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKK 444
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
39-485 |
2.14e-177 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 529.28 E-value: 2.14e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 39 IRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKGLPPvEAYLNIPELIRVCKENDVDAVHP 118
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSK-DSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 119 GYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFKAA 198
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 199 YGGGGRGMRVVRKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERDCSVQRRHQKVVE 278
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 279 IAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEGMt 358
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 359 lpELGYTQDKIVPRGYAIQCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSAsAYAGAIISPYYDSLLVKVISHASDL 438
Cdd:PRK05586 320 --KLSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSA-VYSGYTIPPYYDSMIGKLIVYGKDR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 24652222 439 QSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDE 485
Cdd:PRK05586 397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
584-867 |
2.97e-164 |
|
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163675 Cd Length: 275 Bit Score: 488.09 E-value: 2.97e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 584 LMDTTFRDAHQSLLATRVRSHDLLKISPYVTHkfNNLYSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPFQMLLR 663
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDE--AGFFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 664 GANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTGDvsdpkrTKYDLKYYT 743
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 744 NLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHPdIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDSMSGM 823
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 24652222 824 TSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPF 867
Cdd:cd07937 232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
579-1197 |
1.20e-161 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 493.59 E-value: 1.20e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 579 RKELLLMDTTFRDAHQSLLATRVRSHDLLKISPyvthKFNNL--YSLENWGGATFDVALRFLHECPWERLEEMRKRIPNI 656
Cdd:PRK09282 1 MKKVKITDTTLRDAHQSLLATRMRTEDMLPIAE----KLDKVgfWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 657 PFQMLLRGANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTgdVSdPKRTk 736
Cdd:PRK09282 77 PLQMLLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT--TS-PVHT- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 737 ydLKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHpDIPIHIHTHDTSGAGVASMLACANAGADVVDVA 816
Cdd:PRK09282 153 --IEKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEV-DLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 817 VDSMSGMTSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFECTTTMrsGNADVYLNEIPGGQYTNLQFQ 896
Cdd:PRK09282 230 ISPLAFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTI--VDTRVLIHQVPGGMISNLVSQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 897 AFSLGLGDFFEDVKKA---YREAnllLGDIIKVTPSSKVVGDLAqfmVQNDLTAdqvlERAEelSFPKSVVEYLQGSIGI 973
Cdd:PRK09282 308 LKEQNALDKLDEVLEEiprVRED---LGYPPLVTPTSQIVGTQA---VLNVLTG----ERYK--VITKEVKDYVKGLYGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 974 PHGGFPEPLRSRVLKDMPRIEGRPgAELKDLDFDKLKKELQESHTcVTNRDVMSAALYPQVTNDFLNFREKY--GPVDKL 1051
Cdd:PRK09282 376 PPAPINEELRKKIIGDEEPITCRP-ADLLEPELEKARKEAEELGK-SEKEDVLTYALFPQIAKKFLEEREAGelKPEPEP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1052 DTRIFLTGPKVGEEFDVPLErGKTLSVKALAVSADlkpnGIREVFFELNGQLRAVHIldkEAVKEIHVHPKANKSNKSEV 1131
Cdd:PRK09282 454 KEAAAAGAEGIPTEFKVEVD-GEKYEVKIEGVKAE----GKRPFYLRVDGMPEEVVV---EPLKEIVVGGRPRASAPGAV 525
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24652222 1132 GAPMPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE 1197
Cdd:PRK09282 526 TSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
37-484 |
8.98e-159 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 481.56 E-value: 8.98e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 37 KPIRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGkglpPVEA---YLNIPELIRVCKENDV 113
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIG----PSHAaksYLNPAAILAAARQCGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 114 DAVHPGYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPV 193
Cdd:PRK12833 79 DAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 194 IFKAAYGGGGRGMRVVRKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDkAGNVVHLYERDCSVQRRH 273
Cdd:PRK12833 159 MIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGD-GERVVHLFERECSLQRRR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 274 QKVVEIAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCD-ESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIR 352
Cdd:PRK12833 238 QKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 353 VAEGmtlPELGYTQDKIVPRGYAIQCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSaSAYAGAIISPYYDSLLVKVI 432
Cdd:PRK12833 318 IADG---EPLRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDS-LLYPGYRVPPFYDSLLAKLI 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 24652222 433 SHASDLQSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFID 484
Cdd:PRK12833 394 VHGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
39-488 |
5.80e-158 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 480.08 E-value: 5.80e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 39 IRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKGlpPVEAYLNIPELIRVCKENDVDAVHP 118
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTD--PIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 119 GYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDgPVT--TKEEALEFCKKHGLPVIFK 196
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTE-KLNseSMEEIKIFARKIGYPVILK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 197 AAYGGGGRGMRVVRKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERDCSVQRRHQKV 276
Cdd:PRK08463 159 ASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 277 VEIAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEG 356
Cdd:PRK08463 239 IEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 357 MTLpELgyTQDKIVPRGYAIQCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSaSAYAGAIISPYYDSLLVKVISHAS 436
Cdd:PRK08463 319 EIL-DL--EQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDS-HIYKDYTIPPYYDSMLAKLIVKAT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 24652222 437 DLQSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDEHPQ 488
Cdd:PRK08463 395 SYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQ 446
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
37-486 |
7.59e-153 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 465.37 E-value: 7.59e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 37 KPIRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGkGLPPVEAYLNIPELIRVCKENDVDAV 116
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIG-GAKSSESYLNIPAIISAAEIFEADAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 117 HPGYGFLSERSDFAQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFK 196
Cdd:PRK08462 81 FPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 197 AAYGGGGRGMRVVRKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERDCSVQRRHQKV 276
Cdd:PRK08462 161 AAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 277 VEIAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEG 356
Cdd:PRK08462 241 IEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 357 MTLPElgytQDKIVPRGYAIQCRVTTEDPaNDFQPNTGRLEVFRSGEGMGIRLDSaSAYAGAIISPYYDSLLVKVISHAS 436
Cdd:PRK08462 321 EELPS----QESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMDS-HAYAGYVVPPYYDSMIGKLIVWGE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24652222 437 DLQSSASKMNRALREFRIRGVKTNIPFLLNVLENQKFLHGVLDTYFIDEH 486
Cdd:PRK08462 395 DRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
580-1182 |
4.61e-136 |
|
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: 424.69 E-value: 4.61e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 580 KELLLMDTTFRDAHQSLLATRVRSHDLLKISPY---VthkfnNLYSLENWGGATFDVALRFLHECPWERLEEMRKRIPNI 656
Cdd:COG5016 2 KKVKITDTTLRDGHQSLFATRMRTEDMLPIAEKldeA-----GFWSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 657 PFQMLLRGANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTgdVSDPkrtk 736
Cdd:COG5016 77 PLQMLLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYT--ISPV---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 737 YDLKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHpDIPIHIHTHDTSGAGVASMLACANAGADVVDVA 816
Cdd:COG5016 151 HTVEYYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEAL-DIPIELHTHATSGLAPATYLKAIEAGVDIIDTA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 817 VDSMSGMTSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFEctTTMRSGNADVYLNEIPGGQYTNLQFQ 896
Cdd:COG5016 230 ISPLAGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFE--PEATGVDPRVLVHQVPGGMLSNLVSQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 897 AFSLGLGDFFEDVKKAYREANLLLGDIIKVTPSSKVVGDLAqfmVQNDLTAdqvlERAEelSFPKSVVEYLQGSIGIPHG 976
Cdd:COG5016 308 LKEQGALDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLNVLTG----ERYK--MITKEVKDYVLGYYGKTPA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 977 GFPEPLRSRVLKDMPRIEGRPgAELKDLDFDKLKKELQEshtcVTNRDVMSAALYPQVTNDFLNFREKYGPVDkldtrif 1056
Cdd:COG5016 379 PIDPEVRKKALGDEEPITCRP-ADLLEPELEKLRKEGLA----KSDEDVLTYALFPQVAIKFLKGRAAGEARP------- 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1057 ltgpkvgeefDVPLERGKTLSVKALAvsadlkpngirevffelngqlrAVHILDKEAVKEIHVHPKANKSNKSEVGAPMP 1136
Cdd:COG5016 447 ----------DAPLAELAAVEEVVVV----------------------AEGVVVVVVVGGGAEGVVVVVVGVPGAGAVAV 494
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 24652222 1137 GTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIA 1182
Cdd:COG5016 495 VAAAAAVAAAAAAAAAAAAAAAGAAVKKVVAVGGAVVVGVEVVVVV 540
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
586-1187 |
5.65e-128 |
|
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: 404.94 E-value: 5.65e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 586 DTTFRDAHQSLLATRVRSHDLLKISpyvtHKFN--NLYSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPFQMLLR 663
Cdd:TIGR01108 3 DVVLRDAHQSLFATRMRTEDMLPIA----EKLDdvGYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 664 GANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTgdvSDPKRTkydLKYYT 743
Cdd:TIGR01108 79 GQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT---TSPVHT---LETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 744 NLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRdKHPDIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDSMSGM 823
Cdd:TIGR01108 153 DLAEELLEMGVDSICIKDMAGILTPKAAYELVSALK-KRFGLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 824 TSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFEctTTMRSGNADVYLNEIPGGQYTNLQFQAFSLGLG 903
Cdd:TIGR01108 232 TSHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFE--GQLKGPDSRILVAQVPGGMLSNLESQLKEQNAL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 904 DFFEDVKKAYREANLLLGDIIKVTPSSKVVGDLAqfmVQNDLTAdqvlERAEELSfpKSVVEYLQGSIGIPHGGFPEPLR 983
Cdd:TIGR01108 310 DKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLNVLTG----ERYKTIT--KETKGYLKGEYGRTPAPINAELQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 984 SRVLKDM-PRIEGRPgAELKDLDFDKLKKELQESHTCV-TNRDVMSAALYPQVTNDFLNFREKYGPVDKLDTRIFLTGPK 1061
Cdd:TIGR01108 381 RKILGDEkPIVDCRP-ADLLEPELDKLRAEVREAGAEKnSIEDVLTYALFPQVGLKFLENRHNPAAFEPKPEEKVIEQEH 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1062 VGeefdvplergktlsvkalAVSADLKPNGIREVFFELNGQLRAVHILDKEAVKEIHVHPKANKSNKSE---------VG 1132
Cdd:TIGR01108 460 AQ------------------VVGKYEETHASGSYTVEVEGKAFVVKVSPGGDVSQITASAPANTSGGTVaakagagtpVT 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 24652222 1133 APMPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKL 1187
Cdd:TIGR01108 522 APIAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAV 576
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
580-1184 |
7.48e-115 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 370.03 E-value: 7.48e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 580 KELLLMDTTFRDAHQSLLATRVRSHDLLKISPyvthKFNNL--YSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIP 657
Cdd:PRK14040 3 KPLAITDVVLRDAHQSLFATRLRLDDMLPIAA----KLDKVgyWSLESWGGATFDACIRFLGEDPWERLRELKKAMPNTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 658 FQMLLRGANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTgdVSdPKRTky 737
Cdd:PRK14040 79 QQMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT--TS-PVHT-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 738 dLKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRdKHPDIPIHIHTHDTSGAGVASMLACANAGADVVDVAV 817
Cdd:PRK14040 154 -LQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIK-KRVDVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 818 DSMSGMTSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFEctTTMRSGNADVYLNEIPGGQYTNLQFQA 897
Cdd:PRK14040 232 SSMSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFE--GQLKGVDSRILVAQVPGGMLTNMESQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 898 FSLGLGDFFEDVKK---AYREAnllLGDIIKVTPSSKVVGDLAqfmVQNDLTAdqvlERAEELSfpKSVVEYLQGSIGIP 974
Cdd:PRK14040 310 KEQGAADKLDEVLAeipRVRED---LGFIPLVTPTSQIVGTQA---VLNVLTG----ERYKTIT--KETAGVLKGEYGAT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 975 HGGFPEPLRSRVLKDMPRIEGRPgAELKDLDFDKLKKELQESH-----TCVTNR--DVMSAALYPQVTNDFLNFR---EK 1044
Cdd:PRK14040 378 PAPVNAELQARVLEGAEPITCRP-ADLLAPELDKLEAELRRQAqekgiTLAENAidDVLTYALFPQIGLKFLENRhnpAA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1045 YGPVDKLDTRIFLTGPKVG--EEFDVPLErGKTLSVKalaVSADlkpngirevffelnGQLRAVHILDKEAVKEIHVHPK 1122
Cdd:PRK14040 457 FEPVPQAEAAQPAAKAEPAgsETYTVEVE-GKAYVVK---VSEG--------------GDISQITPAAPAAAPAAAAAAA 518
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652222 1123 ANKSNKSEVGAPMPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANG 1184
Cdd:PRK14040 519 PAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEG 580
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
584-1043 |
9.62e-110 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 351.31 E-value: 9.62e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 584 LMDTTFRDAHQSLLATRVRSHDLLKIspyvTHKFNNL--YSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPFQML 661
Cdd:PRK12331 6 ITETVLRDGQQSLIATRMTTEEMLPI----LEKLDNAgyHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 662 LRGANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTgdvSDPKRTkydLKY 741
Cdd:PRK12331 82 LRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT---TSPVHT---IDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 742 YTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKhPDIPIHIHTHDTSgaGVASM--LACANAGADVVDVAVDS 819
Cdd:PRK12331 156 FVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEA-VTVPLEVHTHATS--GIAEMtyLKAIEAGADIIDTAISP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 820 MSGMTSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFECTTTMRSG-NADVYLNEIPGGQYTNLQFQAF 898
Cdd:PRK12331 233 FAGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYREEGILNPKVKDvEPKTLIYQVPGGMLSNLLSQLK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 899 SLGLGDFFEDVKKAYREANLLLGDIIKVTPSSKVVGDLAqfmVQNDLTAdqvlERAEELsfPKSVVEYLQGSIGIPHGGF 978
Cdd:PRK12331 313 EQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQA---LMNVISG----ERYKMV--PNEIKDYVRGLYGRPPAPI 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24652222 979 PEPLRSRVLKDMPRIEGRPgAELKDLDFDKLKKELQESHTCvtNRDVMSAALYPQVTNDFLNFRE 1043
Cdd:PRK12331 384 AEEIKKKIIGDEEVITCRP-ADLIEPQLEKLREEIAEYAES--EEDVLSYALFPQQAKDFLGRRE 445
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
880-1079 |
1.30e-100 |
|
Conserved carboxylase domain; This domain represents a conserved region in pyruvate carboxylase (PYC), oxaloacetate decarboxylase alpha chain (OADA), and transcarboxylase 5s subunit. The domain is found adjacent to the HMGL-like domain (pfam00682) and often close to the biotin_lipoyl domain (pfam00364) of biotin requiring enzymes.
Pssm-ID: 460557 [Multi-domain] Cd Length: 201 Bit Score: 317.09 E-value: 1.30e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 880 VYLNEIPGGQYTNLQFQAFSLGLGDFFEDVKKAYREANLLLGDIIKVTPSSKVVGDLAQFMVQNDLTADQVLERAEELSF 959
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 960 PKSVVEYLQGSIGIPHGGFPEPLRSRVLKDMPRIEGRPGAELKDLDFDKLKKELQESHTC-VTNRDVMSAALYPQVTNDF 1038
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGReTTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24652222 1039 LNFREKYGPVDKLDTRIFLTGPKVGEEFDVPLERGKTLSVK 1079
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
583-1197 |
5.00e-94 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 313.97 E-value: 5.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 583 LLMDTTFRDAHQSLLATRVRSHDLLKISpyvtHKFNNL--YSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPFQM 660
Cdd:PRK14042 5 FITDVTLRDAHQCLIATRMRTEDMLPIC----NKMDDVgfWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 661 LLRGANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTgdvSDPKRTkydLK 740
Cdd:PRK14042 81 LLRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT---TSPVHT---LD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 741 YYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRdKHPDIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDSM 820
Cdd:PRK14042 155 NFLELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLK-QATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 821 SGMTSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFEctTTMRSGNADVYLNEIPGGQYTNLQFQAFSL 900
Cdd:PRK14042 234 SGGASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFE--SEAQNIDPRVQLYQVPGGMISNLYNQLKEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 901 GLGDFFEDVKKAYREANLLLGDIIKVTPSSKVVGDLAqfmVQNDLTADQVLERAEELSFpksvveYLQGSIGIPHGGFPE 980
Cdd:PRK14042 312 NALDKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQA---VINVLTGERYKTITNEVKL------YCQGKYGTPPGKISS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 981 PLRSRVLKDMPRIEGRPGAELKDlDFDKLKKELqeSHTCVTNRDVMSAALYPQVTNDFLNFREKYGPV-DKLDTRIFLTG 1059
Cdd:PRK14042 383 ALRKKAIGRTEVIEVRPGDLLPN-ELDQLQNEI--SDLALSDEDVLLYAMFPEIGRQFLEQRKNNQLIpEPLLTQSSAPD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1060 PKVGEEFDVPLErGKTLSVKALAVSadLKPNGIREVFFELNGQLRAVHILDKEAVKEIHVHPKANKSNKSEVGAPMPGTV 1139
Cdd:PRK14042 460 NSVMSEFDIILH-GESYHVKVAGYG--MIEHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPGSI 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 24652222 1140 IDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE 1197
Cdd:PRK14042 537 IAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
580-1045 |
1.47e-93 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 308.25 E-value: 1.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 580 KELLLMDTTFRDAHQSLLATRVRSHDLLKIspYVTHKFNNLYSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPFQ 659
Cdd:PRK14041 1 MKVMFVDTTLRDGHQSLIATRMRTEDMLPA--LEAFDRMGFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 660 MLLRGANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTgdVSdPKRTkydL 739
Cdd:PRK14041 79 MLLRGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT--VS-PVHT---L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 740 KYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHpDIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDS 819
Cdd:PRK14041 153 EYYLEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 820 MSGMTSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFEctTTMRSGNADVYLNEIPGGQYTNLQFQAFS 899
Cdd:PRK14041 232 FSMGTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYD--VGMKSPDSRILVSQIPGGMYSNLVKQLKE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 900 LGLGDFFEDVKKAYREANLLLGDIIKVTPSSKVVGDLAqfmVQNDLTAdqvlERAEELSfpKSVVEYLQGSIGIPHGGFP 979
Cdd:PRK14041 310 QKMLHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQA---VLNVLTG----ERYKRVT--NETKNYVKGLYGRPPAPID 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24652222 980 EPLRSRVLKDMPRIEGRPgAELKDLDFDKLKKELqeSHTCVTNRDVMSAALYPQVTNDFLnfREKY 1045
Cdd:PRK14041 381 EELMKKILGDEKPIDCRP-ADLLEPELEKARKEL--GILAETDEDLLIYVILGEVGKKFL--KKKY 441
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
579-1047 |
3.02e-83 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 280.88 E-value: 3.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 579 RKELLLMDTTFRDAHQSLLATRVRSHDLLKISPYVTHKfnNLYSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPF 658
Cdd:PRK12330 2 PRKIGVTELALRDAHQSLMATRMAMEDMVGACEDIDNA--GYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 659 QMLLRGANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTgdVSdPKRTKYD 738
Cdd:PRK12330 80 QMLLRGQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT--VS-PIHTVEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 739 lkyYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKH-PDIPIHIHTHDTSGAGVASMLACANAGADVVDVAV 817
Cdd:PRK12330 157 ---FVEQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 818 DSMS-GMTSQPSMgAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFECTTTmrSGNADVYLNEIPGGQYTNLQFQ 896
Cdd:PRK12330 234 SSMSlGPGHNPTE-SLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTT--GVETEIFKSQIPGGMLSNMESQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 897 AFSLGLGDFFEDVKKAYREANLLLGDIIKVTPSSKVVGDLAQFmvqNDLTADQVLERAEelsFPKSVVEYLQGSIGIPHG 976
Cdd:PRK12330 311 LKQQGAGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVF---NVLMGRYKVLTGE---FADLMLGYYGETPGERNP 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652222 977 GFPEPLRSRVLKDmpRIEGRPgAELKDLDFDKLKKELQESHTCV-TNRDVMSAALYPQVTNDFLNFREKyGP 1047
Cdd:PRK12330 385 EVVEQAKKQAKKE--PITCRP-ADLLEPEWDKLRAEALALEGCDgSDEDVLTYALFPQVAPKFFATRAE-GP 452
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
153-360 |
8.57e-82 |
|
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: 266.09 E-value: 8.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 153 DKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFKAAYGGGGRGMRVVRKMEDVEESFQRASSEAKAAFGN 232
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 233 GAMFIEKFIERPRHIEVQLLGDKAGNVVHLYERDCSVQRRHQKVVEIAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTV 312
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24652222 313 EFLCD-ESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEGMTLP 360
Cdd:pfam02786 161 EFALDpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
579-1057 |
4.84e-73 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 251.19 E-value: 4.84e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 579 RKELLLMDTTFRDAHQSLLATRVRSHDLLKISPYVTHKfnNLYSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPF 658
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDMLPVLTILDKI--GYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 659 QMLLRGANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTgdvSDPKRTkyd 738
Cdd:PRK12581 88 QMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT---TSPVHT--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 739 LKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRdKHPDIPIHIHTHDTSGAGVASMLACANAGADVVDVAVD 818
Cdd:PRK12581 162 LNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIK-AMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 819 SMSGMTSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLY-APFECTTTMRSGNADVYLNEIPGGQYTNLQFQA 897
Cdd:PRK12581 241 PFSEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYlADGILDPSLLFPDPRTLQYQVPGGMLSNMLSQL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 898 FSLGLGDFFEDVKKAYREANLLLGDIIKVTPSSKVVGDLAQFMVqndltadqVLERAEELsFPKSVVEYLQGSIGIPHGG 977
Cdd:PRK12581 321 KQANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNV--------ILGKPYQM-VSKEIKQYLAGDYGKTPAP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 978 FPEPLRSRVLKDMPRIEGRPGAELkDLDFDKLKKELQEshTCVTNRDVMSAALYPQVTNDFLNfrEKYGPVDKLDTRIFL 1057
Cdd:PRK12581 392 VNEDLKRSQIGSAPVTTNRPADQL-SPEFEVLKAEVAD--LAQTDEDVLTYALFPSVAKPFLT--TKYQTDDVIKVTAFI 466
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
585-859 |
4.30e-72 |
|
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: 241.21 E-value: 4.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 585 MDTTFRDAHQSLLATRvRSHDLLKISPYVTHkfNNLYSLENWGGATFDVAlrFLHECPWERLEEMRKRIPNIPFQMLLRG 664
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDE--AGVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 665 anavgytsypdnvVYKFCELAVQTGMDIFRVFDSLNY--------------LPNLILGMEAAGKAGGVVEAAISYTGDVs 730
Cdd:cd03174 76 -------------REKGIERALEAGVDEVRIFDSASEthsrknlnksreedLENAEEAIEAAKEAGLEVEGSLEDAFGC- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 731 dpkrtKYDLKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHPDIPIHIHTHDTSGAGVASMLACANAGA 810
Cdd:cd03174 142 -----KTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 24652222 811 DVVDVAVDSMSGMTSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQ 859
Cdd:cd03174 217 DRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVEE 265
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
39-147 |
5.28e-57 |
|
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: 191.93 E-value: 5.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 39 IRSVLVANRGEIAIRVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKGlPPVEAYLNIPELIRVCKENDVDAVHP 118
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPG-PASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*....
gi 24652222 119 GYGFLSERSDFAQAVIDAGLRFIGPSPEV 147
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
100-356 |
6.45e-56 |
|
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: 195.09 E-value: 6.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 100 NIPELIRVCKE----NDVDAVhpgygfLSErSDFAQ---AVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPiVPGT 172
Cdd:COG0439 1 DIDAIIAAAAElareTGIDAV------LSE-SEFAVetaAELAEELGLPGPSPEAIRAMRDKVLMREALAAAGVP-VPGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 173 DgPVTTKEEALEFCKKHGLPVIFKAAYGGGGRGMRVVRKMEDVEESFQRASSEAKAAFGNGAMFIEKFIERpRHIEVQLL 252
Cdd:COG0439 73 A-LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 253 GDKaGNVVHlyerdCSVQRRHQK---VVE---IAPAPrLPIEIRDKMTEAAVRLARHVGYEN-AGTVEFLCDESGNFYFI 325
Cdd:COG0439 151 VRD-GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYLI 223
|
250 260 270
....*....|....*....|....*....|...
gi 24652222 326 EVNARLQVEH--TVTEEITGIDLVQSQIRVAEG 356
Cdd:COG0439 224 EINARLGGEHipPLTELATGVDLVREQIRLALG 256
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
377-484 |
2.88e-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: 164.12 E-value: 2.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 377 QCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSAsAYAGAIISPYYDSLLVKVISHASDLQSSASKMNRALREFRIRG 456
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSG-VYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 24652222 457 VKTNIPFLLNVLENQKFLHGVLDTYFID 484
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
377-485 |
1.89e-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: 147.64 E-value: 1.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 377 QCRVTTEDPANDFQPNTGRLEVFRSGEGMGIRLDSAsAYAGAIISPYYDSLLVKVISHASDLQSSASKMNRALREFRIRG 456
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 24652222 457 VKTNIPFLLNVLENQKFLHGVLDTYFIDE 485
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
584-847 |
1.72e-31 |
|
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: 124.76 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 584 LMDTTFRDAHQSLlATRVRSHDLLKISpyvthkfnnlYSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPFQMLLR 663
Cdd:pfam00682 4 ICDTTLRDGEQAL-GVAFSIDEKLAIA----------RALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 664 GAnavgytsypDNVVYKFCELAVQTGMDIFRVFDSLNYLP-NLILGM---EAAGKAGGVVEAAISYTGDV--SDPKRTKY 737
Cdd:pfam00682 73 AR---------EHDIKAAVEALKGAGAVRVHVFIATSDLHrKYKLGKdreEVAKRAVAAVKAARSRGIDVefSPEDASRT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 738 DLKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHPD-IPIHIHTHDTSGAGVASMLACANAGADVVDVA 816
Cdd:pfam00682 144 DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVDGT 223
|
250 260 270
....*....|....*....|....*....|.
gi 24652222 817 VDSMSGMTSQPSMGAVVASLQGTPLDTNLDL 847
Cdd:pfam00682 224 VNGIGERAGNAALEEVAAALEGLGVDTGLDL 254
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1130-1196 |
2.93e-25 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 99.80 E-value: 2.93e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24652222 1130 EVGAPMPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMII 1196
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1130-1196 |
4.88e-20 |
|
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: 85.34 E-value: 4.88e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652222 1130 EVGAPMPGTVID-----IRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMII 1196
Cdd:pfam00364 2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
130-421 |
3.58e-16 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 84.28 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 130 AQAVIDAGLRFIGPSPEVVQKMGDKvaARVAAI--EAGVPIVPGtdGPVTTKEEALEFCKKHGLPVIFKAAYGGGGRGMR 207
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDR--EKFSELldELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAME 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 208 VVRKMEDVEESFQRASSEAKaafgNGAMFIEKFIERPRHIEVQLLGD--------------KAGnvVHLYERDCSVqrrh 273
Cdd:TIGR01369 722 IVYNEEELRRYLEEAVAVSP----EHPVLIDKYLEDAVEVDVDAVSDgeevlipgimehieEAG--VHSGDSTCVL---- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 274 qkvveiaPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDEsGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRV 353
Cdd:TIGR01369 792 -------PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRV 863
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24652222 354 AEGMTLPELGYTQDKIvPRGYAIQCRVTTEDPANDFQPNTGrLEVFRSGEGMGIRLDSASAYAGAIIS 421
Cdd:TIGR01369 864 MLGKKLEELGVGKEKE-PKYVAVKEPVFSFSKLAGVDPVLG-PEMKSTGEVMGIGRDLAEAFLKAQLS 929
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1121-1197 |
6.73e-16 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 75.70 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1121 PKANKSNKSEVGAPMPGTV-------IDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLI 1193
Cdd:COG0511 53 AAAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
|
....
gi 24652222 1194 MIIE 1197
Cdd:COG0511 133 FVIE 136
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1131-1196 |
1.32e-12 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 65.99 E-value: 1.32e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24652222 1131 VGAPMPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLE-GEDLIMII 1196
Cdd:PRK06549 64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNpGDGLITIG 130
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
130-365 |
1.84e-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: 71.45 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 130 AQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGtdGPVTTKEEALEFCKKHGLPVIFKAAYGGGGRGmrvv 209
Cdd:COG0458 91 EEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKS--GTATSVEEALAIAEEIGYPVIVRPSYVLGGRG---- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 210 rkMEDV--EESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVV------HLyER------DCSVqrrhqk 275
Cdd:COG0458 165 --MGIVynEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIivgimeHI-EPagvhsgDSIC------ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 276 vveIAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDeSGNFYFIEVNARlqVEHTVT--EEITGIDLVQSQIRV 353
Cdd:COG0458 236 ---VAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD-DGRVYVIEVNPR--ASRSSPfaSKATGYPIAKIAAKL 309
|
250
....*....|..
gi 24652222 354 AEGMTLPELGYT 365
Cdd:COG0458 310 ALGYTLDELGND 321
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1137-1197 |
2.19e-12 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 71.19 E-value: 2.19e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24652222 1137 GTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE 1197
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1129-1195 |
2.26e-12 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 63.27 E-value: 2.26e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24652222 1129 SEVGAPMPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKL-EGEDLIMI 1195
Cdd:PRK08225 2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVnEGDVLLEI 69
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1131-1193 |
2.48e-12 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 66.04 E-value: 2.48e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24652222 1131 VGAPMPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLE-GEDLI 1193
Cdd:PRK05641 87 VTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDtGQPLI 150
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
37-362 |
1.70e-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: 68.87 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 37 KPIRSVLVANRGEIAI-----------RVFRACTELGIKSVAVYSEQDKMHMHRQKADESYIVgkglpPVEAYlNIPELI 105
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIgqaaefdysgsQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIE-----PLTPE-AVEKII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 106 RvcKENdVDAVHPGYGF---------LSERsdfaqAVIDA-GLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGtdGP 175
Cdd:TIGR01369 78 E--KER-PDAILPTFGGqtalnlaveLEES-----GVLEKyGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 176 VTTKEEALEFCKKHGLPVIFKAAYGGGGRGMRVVRKMEDVEESFQRASSEAKAafgnGAMFIEKFIERPRHIEVQLLGDK 255
Cdd:TIGR01369 148 AHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVLVEKSLAGWKEIEYEVMRDS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 256 AGNVVHLyerdCSVQR-----RH--QKVVeIAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCD-ESGNFYFIEV 327
Cdd:TIGR01369 224 NDNCITV----CNMENfdpmgVHtgDSIV-VAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNpDSGRYYVIEV 298
|
330 340 350
....*....|....*....|....*....|....*
gi 24652222 328 NARLQVEHTVTEEITGIDLVQSQIRVAEGMTLPEL 362
Cdd:TIGR01369 299 NPRVSRSSALASKATGYPIAKVAAKLAVGYTLDEL 333
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
56-331 |
1.93e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 67.26 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 56 RACTELGIKSVAVYSEQDKMHMHRQKADESYIVGKGLPPVEAYLNipELIRVCKENDVDAVHPGY----GFLSERsdfaQ 131
Cdd:COG3919 22 RSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGDDPEAFVD--ALLELAERHGPDVLIPTGdeyvELLSRH----R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 132 AVIDAGLRFIGPSPEVVQKMGDKVA-ARVAAiEAGVPI----VPGTDGPVTTKEEALEFckkhglPVIFKAAYGGGGRGM 206
Cdd:COG3919 96 DELEEHYRLPYPDADLLDRLLDKERfYELAE-ELGVPVpktvVLDSADDLDALAEDLGF------PVVVKPADSVGYDEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 207 RVVRK-----MEDVEEsFQRASSEAKAAFGNgaMFIEKFIERPRHIEVQLLG--DKAGNVVHLyerdCSVQRRHQKVVEI 279
Cdd:COG3919 169 SFPGKkkvfyVDDREE-LLALLRRIAAAGYE--LIVQEYIPGDDGEMRGLTAyvDRDGEVVAT----FTGRKLRHYPPAG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 24652222 280 -APAPRLPIEIRDkMTEAAVRLARHVGYENAGTVEFLCDE-SGNFYFIEVNARL 331
Cdd:COG3919 242 gNSAARESVDDPE-LEEAARRLLEALGYHGFANVEFKRDPrDGEYKLIEINPRF 294
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1113-1197 |
1.00e-10 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 66.18 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1113 AVKEIHVhpkanksnkSEVGAPmPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDL 1192
Cdd:PRK11854 104 AAKDVHV---------PDIGSD-EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSL 173
|
....*
gi 24652222 1193 IMIIE 1197
Cdd:PRK11854 174 IMVFE 178
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
130-416 |
1.55e-10 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 65.76 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 130 AQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGtdGPVTTKEEALEFCKKHGLPVIFKAAYGGGGRgmrvv 209
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQ----- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 210 rKMEDVEESFQRASSEAKAAFGNGAMFIEKFIErPRHIEVQLLGD--------------KAGnvVHLYERDCsvqrrhqk 275
Cdd:PRK12815 720 -GMAVVYDEPALEAYLAENASQLYPILIDQFID-GKEYEVDAISDgedvtipgiiehieQAG--VHSGDSIA-------- 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 276 vveIAPAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDEsGNFYFIEVNARlqVEHTV--TEEITGIDLVQSQIRV 353
Cdd:PRK12815 788 ---VLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAN-DEIYVLEVNPR--ASRTVpfVSKATGVPLAKLATKV 861
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24652222 354 AEGMTLPELGYtQDKIVPRGYAIqcrvTTEDPANDFQ--PNTGRL---EVFRSGEGMGIRLDSASAYA 416
Cdd:PRK12815 862 LLGKSLAELGY-PNGLWPGSPFI----HVKMPVFSYLkyPGVDNTlgpEMKSTGEVMGIDKDLEEALY 924
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1130-1197 |
1.92e-10 |
|
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: 64.90 E-value: 1.92e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24652222 1130 EVGAPMPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE 1197
Cdd:TIGR01348 7 DIGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1137-1197 |
2.34e-10 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 64.64 E-value: 2.34e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24652222 1137 GTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE 1197
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE 279
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1137-1196 |
5.11e-10 |
|
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: 56.64 E-value: 5.11e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1137 GTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMII 1196
Cdd:cd06849 15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
709-817 |
8.76e-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: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 709 MEAAGKAGGVVEAAIS------YTGDVsDPKRTkydlkyyTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKH 782
Cdd:cd07938 120 AELAKAAGLRVRGYVStafgcpYEGEV-PPERV-------AEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERF 191
|
90 100 110
....*....|....*....|....*....|....*
gi 24652222 783 PDIPIHIHTHDTSGAGVASMLACANAGADVVDVAV 817
Cdd:cd07938 192 PDEKLALHFHDTRGQALANILAALEAGVRRFDSSV 226
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1137-1196 |
9.69e-10 |
|
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: 55.84 E-value: 9.69e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1137 GTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMII 1196
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1130-1197 |
1.07e-09 |
|
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: 62.58 E-value: 1.07e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24652222 1130 EVGAPMPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE 1197
Cdd:TIGR01348 123 DIGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1137-1197 |
1.14e-09 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 62.53 E-value: 1.14e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24652222 1137 GTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE 1197
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1130-1196 |
3.53e-09 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 54.43 E-value: 3.53e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24652222 1130 EVGAPMPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMII 1196
Cdd:PRK05889 4 DVRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
98-348 |
5.02e-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: 58.80 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 98 YLNIPELIRVCKE---NDVDAVHPGYGFLSERSDFAQAVIDAGLRFIgPSPEVVQKMGDKVAARVAAIEAGVPIvpgtdg 174
Cdd:COG0189 39 TLDLGRAPELYRGedlSEFDAVLPRIDPPFYGLALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPV------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 175 PVT----TKEEALEFCKKHGLPVIFKAAYGGggrGMRVVRKMEDVEESFQRAssEAKAAFGNGAMFIEKFI--ERPRHIE 248
Cdd:COG0189 112 PPTlvtrDPDDLRAFLEELGGPVVLKPLDGS---GGRGVFLVEDEDALESIL--EALTELGSEPVLVQEFIpeEDGRDIR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 249 VQLLGDKagnVVHLYER-----DCSVQRRHQKVVEiapaprlPIEIRDKMTEAAVRLARHVGYENAGtVEFLCDESGnFY 323
Cdd:COG0189 187 VLVVGGE---PVAAIRRipaegEFRTNLARGGRAE-------PVELTDEERELALRAAPALGLDFAG-VDLIEDDDG-PL 254
|
250 260
....*....|....*....|....*
gi 24652222 324 FIEVNARLQVEHtvTEEITGIDLVQ 348
Cdd:COG0189 255 VLEVNVTPGFRG--LERATGVDIAE 277
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1137-1197 |
7.03e-09 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 59.84 E-value: 7.03e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24652222 1137 GTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE 1197
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1130-1196 |
1.08e-08 |
|
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: 52.83 E-value: 1.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24652222 1130 EVGAPMP------GTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMII 1196
Cdd:cd06663 1 TILIPDLaqhlgdGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
139-421 |
1.03e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 56.71 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 139 RFIGPSPEVVQKMGDKvaARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGLPVIFKAAYGGGGRGmrvvrkMEDV--E 216
Cdd:PLN02735 688 KIWGTSPDSIDAAEDR--ERFNAILNELKIEQPKGGIARSEADALAIAKRIGYPVVVRPSYVLGGRA------MEIVysD 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 217 ESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNVV-------------HLYERDCSVqrrhqkvveiaPAP 283
Cdd:PLN02735 760 DKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVViggimehieqagvHSGDSACSL-----------PTQ 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 284 RLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEGMTLPELG 363
Cdd:PLN02735 829 TIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSLKDLG 908
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 364 YTQDkIVPRGYAIQCRVTtedPANDFQPNTGRL--EVFRSGEGMGIRLDSASAYAGAIIS 421
Cdd:PLN02735 909 FTEE-VIPAHVSVKEAVL---PFDKFQGCDVLLgpEMRSTGEVMGIDYEFSKAFAKAQIA 964
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
710-848 |
1.32e-07 |
|
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: 54.38 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 710 EAAGKAGGVVEAAISYTGDV----SDPKRTkyDLKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRD--KHP 783
Cdd:cd07940 111 EVLERAVEAVEYAKSHGLDVefsaEDATRT--DLDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKEnvPNI 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652222 784 DIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDSM---SGMTsqpSMGAVVASL----QGTPLDTNLDLR 848
Cdd:cd07940 189 KVPISVHCHNDLGLAVANSLAAVEAGARQVECTINGIgerAGNA---ALEEVVMALktryDYYGVETGIDTE 257
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
735-854 |
1.77e-07 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 55.33 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 735 TKYDLKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKhPDIPIHIHTHDTSGAGVASMLACANAGADVVD 814
Cdd:PRK09389 138 SRADLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSEL-VKGPVSIHCHNDFGLAVANTLAALAAGADQVH 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 24652222 815 VAVDSMSGMTSQPSMGAVVASL-QGTPLDTNLDL-------RTVSEYS 854
Cdd:PRK09389 217 VTINGIGERAGNASLEEVVMALkHLYDVETGIKLeelyelsRLVSRLT 264
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
707-854 |
2.04e-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: 54.79 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 707 LGM---EAAGKAGGVVEAAISYTGDVS----DPKRTkyDLKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIR 779
Cdd:COG0119 110 LRKtreEVLEMAVEAVKYAKEHGLEVEfsaeDATRT--DPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 780 DKHPDIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDSM---SGMTsqpSMGAVVASLQG-TPLDTNLDL-------R 848
Cdd:COG0119 188 ERVPDVILSVHCHNDLGLAVANSLAAVEAGADQVEGTINGIgerAGNA---ALEEVVMNLKLkYGVDTGIDLskltelsR 264
|
....*.
gi 24652222 849 TVSEYS 854
Cdd:COG0119 265 LVSEIT 270
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
90-328 |
2.76e-07 |
|
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: 53.57 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 90 KGLPPVEAYLNIPELIRVCKENDVDAVHPG-YGFLSErsD-FAQAVID-AGLRFIGPSPevvqkMG-----DKVAARVAA 161
Cdd:COG1181 31 AGYDVVPIGIDVEDLPAALKELKPDVVFPAlHGRGGE--DgTIQGLLElLGIPYTGSGV-----LAsalamDKALTKRVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 162 IEAGVPIVPG---TDGPVTTKEEALEfckKHGLPVIFKAA--------YggggrgmrvvrKMEDVEEsFQRASSEAkAAF 230
Cdd:COG1181 104 AAAGLPTPPYvvlRRGELADLEAIEE---ELGLPLFVKPAregssvgvS-----------KVKNAEE-LAAALEEA-FKY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 231 GNGAMfIEKFIErPRHIEVQLLGDK---AGNVVHL------------YERDcsvqrrhqKVVEIAPApRLPIEIRDKMTE 295
Cdd:COG1181 168 DDKVL-VEEFID-GREVTVGVLGNGgprALPPIEIvpengfydyeakYTDG--------GTEYICPA-RLPEELEERIQE 236
|
250 260 270
....*....|....*....|....*....|...
gi 24652222 296 AAVRLARHVGYENAGTVEFLCDESGNFYFIEVN 328
Cdd:COG1181 237 LALKAFRALGCRGYARVDFRLDEDGEPYLLEVN 269
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
143-328 |
1.59e-06 |
|
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: 51.61 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 143 PSPEVVQKMGDKVAARVAAIEAGVPIVPGTdgPVTTKEEALEFCKKHGLPVIFKAAyggggrgmrvvrKM---------- 212
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAPFA--AVDSLEDLEAAIAELGLPAVLKTR------------RGgydgkgqvvi 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 213 ---EDVEesfqrassEAKAAFGNGAMFIEKFI--ERprhiEVQLLG--DKAGNVVHlY---ErdcSVQRRHQKVVEIAPA 282
Cdd:COG0026 145 ksaADLE--------AAWAALGGGPCILEEFVpfER----ELSVIVarSPDGEVAT-YpvvE---NVHRNGILDESIAPA 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24652222 283 pRLPIEIRDKMTEAAVRLARHVGYenAGT--VEFLCDESGNFYfieVN 328
Cdd:COG0026 209 -RISEALAAEAEEIAKRIAEALDY--VGVlaVEFFVTKDGELL---VN 250
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
749-823 |
2.12e-06 |
|
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF ) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163681 Cd Length: 263 Bit Score: 50.58 E-value: 2.12e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24652222 749 LVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHPDIPIHIHTHDTSGAGVASMLACANAGADVVDVavdSMSGM 823
Cdd:cd07943 150 MESYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRIDG---SLAGL 221
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
718-846 |
2.31e-06 |
|
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: 50.84 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 718 VVEAAIS-------YTGDVSDPKRTKYDlkYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHPDIPIHIH 790
Cdd:cd07945 120 VIEYAIKngievniYLEDWSNGMRDSPD--YVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFH 197
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24652222 791 THDTSGAGVASMLACANAGADVVDVAVDSMSGMTSQPSMGAVVASLQG-TPLDTNLD 846
Cdd:cd07945 198 AHNDYDLAVANVLAAVKAGIKGLHTTVNGLGERAGNAPLASVIAVLKDkLKVKTNID 254
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1137-1197 |
2.61e-06 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 51.33 E-value: 2.61e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24652222 1137 GTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE 1197
Cdd:PRK11856 17 GEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIE 77
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
80-330 |
3.19e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 50.65 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 80 QKADESYIVgkglPPVEAYLNIPELIRVCKENDVDAVHPGY----GFLSE-RSDFAqaviDAGLRFIGPSPEVVQKMGDK 154
Cdd:PRK12767 41 YFADKFYVV----PKVTDPNYIDRLLDICKKEKIDLLIPLIdpelPLLAQnRDRFE----EIGVKVLVSSKEVIEICNDK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 155 VAARVAAIEAGVPiVPGTDGPvTTKEEALE--FCKKHGLPVIFKAAYGGGGRGMRVVRKMEDVEESFQRasseakaafgN 232
Cdd:PRK12767 113 WLTYEFLKENGIP-TPKSYLP-ESLEDFKAalAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEY----------V 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 233 GAMFIEKFIErprHIE--VQLLGDKAGNVVHlyerdcSVQRRHQKVVeIAPAPRLPIEIRDKMTEAAVRLARHVGYENAG 310
Cdd:PRK12767 181 PNLIIQEFIE---GQEytVDVLCDLNGEVIS------IVPRKRIEVR-AGETSKGVTVKDPELFKLAERLAEALGARGPL 250
|
250 260
....*....|....*....|
gi 24652222 311 TVEFLCDEsGNFYFIEVNAR 330
Cdd:PRK12767 251 NIQCFVTD-GEPYLFEINPR 269
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
164-328 |
5.63e-06 |
|
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: 48.47 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 164 AGVPIVP-----GTDGPVTTKEEALEFCKKHGLPVIFKAAyggGGRGMRVVRKMEDVEEsFQRAsseAKAAFG-NGAMFI 237
Cdd:pfam07478 5 AGLPVVPfvtftRADWKLNPKEWCAQVEEALGYPVFVKPA---RLGSSVGVSKVESREE-LQAA---IEEAFQyDEKVLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 238 EKFIErPRHIEVQLLGDKAGNVVHLYER--DCSVQRRHQKVVE-----IAPAPrLPIEIRDKMTEAAVRLARHVGYENAG 310
Cdd:pfam07478 78 EEGIE-GREIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDdsaqiVVPAD-LEEEQEEQIQELALKAYKALGCRGLA 155
|
170
....*....|....*...
gi 24652222 311 TVEFLCDESGNFYFIEVN 328
Cdd:pfam07478 156 RVDFFLTEDGEIVLNEVN 173
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
137-421 |
1.45e-05 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 49.58 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 137 GLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIvpGTDGPVTTKEEALEFCKKHGLPVIFKAAYGGGGRGMRVVRKMEDVE 216
Cdd:PRK12815 112 GVELLGTNIEAIQKGEDRERFRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 217 ESFQRASSEakAAFGNgaMFIEKFIERPRHIEVQLLGDKAGNVVHLyerdCS--------VQRRHQKVVeiAPAPRLPIE 288
Cdd:PRK12815 190 QLFKQGLQA--SPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCITV----CNmenidpvgIHTGDSIVV--APSQTLTDD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 289 IRDKMTEAAVRLARHVGYENAGTVEFLCD-ESGNFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEGMTLPEL----- 362
Cdd:PRK12815 260 EYQMLRSASLKIISALGVVGGCNIQFALDpKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAVGYTLNELknpvt 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24652222 363 GYTQDKIVPRGYAIQCRVT----TEDPANDFQPNTgrlEVFRSGEGMGIRLDSASAYAGAIIS 421
Cdd:PRK12815 340 GLTYASFEPALDYVVVKFPrwpfDKFGYADRTLGT---QMKATGEVMAIGRNFESAFQKALRS 399
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
101-376 |
2.27e-05 |
|
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: 47.99 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 101 IPELIRVCKENDVDAVHPGYGFLSERSDFAQavIDAGLRFIGPSPEVVQKMGDKvaARVAAI--EAGVPI------VPGT 172
Cdd:COG2232 62 PAALLELAAADDPDGLVYGSGFENFPELLER--LARRLPLLGNPPEVVRRVKDP--LRFFALldELGIPHpetrfePPPD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 173 DGPVTTKeealefckkhglPV-------IFKAAYGGGgrgmrvvrkmEDVEESFQRasseakaafgngamFIE------K 239
Cdd:COG2232 138 PGPWLVK------------PIggaggwhIRPADSEAP----------PAPGRYFQR--------------YVEgtpasvL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 240 FIERPRHIEV-----QLLGDK-------AGNVVHLyerdcsvqrrhqkvveiapapRLPIEIRDKMTEAAVRLARHVGYE 307
Cdd:COG2232 182 FLADGSDARVlgfnrQLIGPAgerpfryGGNIGPL---------------------ALPPALAEEMRAIAEALVAALGLV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24652222 308 NAGTVEFLCDESGnFYFIEVNARLQVEHTVTEEITGIDLVQSQIRVAEGmTLPELGYTQDKIVpRGYAI 376
Cdd:COG2232 241 GLNGVDFILDGDG-PYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRG-ELPEVPRPKPRRV-AAKAI 306
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
130-376 |
2.40e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 48.94 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 130 AQAVIDAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGtdGPVTTKEEALEFCKKHGLPVIFKAAYggggrgmrvv 209
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSYvlg------g 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 210 rkMEDV--EESFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDK-----AGNVVHLyER------D--CSVqrrhq 274
Cdd:PRK05294 718 raMEIVydEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGedvliGGIMEHI-EEagvhsgDsaCSL----- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 275 kvveiaPAPRLPIEIRDKMTEAAVRLARH---VGYENagtVEFLCDEsGNFYFIEVNARlqVEHTV--TEEITGIDLVQS 349
Cdd:PRK05294 792 ------PPQTLSEEIIEEIREYTKKLALElnvVGLMN---VQFAVKD-DEVYVIEVNPR--ASRTVpfVSKATGVPLAKI 859
|
250 260
....*....|....*....|....*..
gi 24652222 350 QIRVAEGMTLPELGYTqDKIVPRGYAI 376
Cdd:PRK05294 860 AARVMLGKKLAELGYT-KGLIPPYVAV 885
|
|
| PLN03228 |
PLN03228 |
methylthioalkylmalate synthase; Provisional |
748-864 |
3.01e-05 |
|
methylthioalkylmalate synthase; Provisional
Pssm-ID: 178767 [Multi-domain] Cd Length: 503 Bit Score: 47.99 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 748 ELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHP---DIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDSMSGMT 824
Cdd:PLN03228 247 EAIKAGATSVGIADTVGINMPHEFGELVTYVKANTPgidDIVFSVHCHNDLGLATANTIAGICAGARQVEVTINGIGERS 326
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24652222 825 SQPSMGAVVASLQ--GTPL----DTNLDLRTVSEYSAYWEQTRTLY 864
Cdd:PLN03228 327 GNASLEEVVMALKcrGAYLmngvYTGIDTRQIMATSKMVQEYTGMY 372
|
|
| PRK08195 |
PRK08195 |
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated |
752-817 |
5.39e-05 |
|
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
Pssm-ID: 181282 [Multi-domain] Cd Length: 337 Bit Score: 46.75 E-value: 5.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24652222 752 AGTHVLCIKDMAGLLKPESARLLITAIRDK-HPDIPIHIHTHDTSGAGVASMLACANAGADVVDVAV 817
Cdd:PRK08195 156 YGAQCVYVVDSAGALLPEDVRDRVRALRAAlKPDTQVGFHGHNNLGLGVANSLAAVEAGATRIDGSL 222
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
153-328 |
9.70e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 45.87 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 153 DKVAARVAAIEAGVPIVPGTdgpVTTKEEALEFCKKH-GLPVIFKAA--------YggggrgmrvvrKMEDVEEsFQRAS 223
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWI---VLTREEDLLAAIDKlGLPLVVKPAregssvgvS-----------KVKEEDE-LQAAL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 224 SEAkAAFGNGAMfIEKFIErPRHIEVQLLGDKAGNVVHL------------YERDCSvqrRHqkvveIAPAPrLPIEIRD 291
Cdd:PRK01372 163 ELA-FKYDDEVL-VEKYIK-GRELTVAVLGGKALPVIEIvpagefydyeakYLAGGT---QY-----ICPAG-LPAEIEA 230
|
170 180 190
....*....|....*....|....*....|....*..
gi 24652222 292 KMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVN 328
Cdd:PRK01372 231 ELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVN 267
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
718-817 |
1.07e-04 |
|
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163677 [Multi-domain] Cd Length: 259 Bit Score: 45.19 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 718 VVEAAISYTGDVS----DPKRTkyDLKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRdKHPDIPIHIHTHD 793
Cdd:cd07939 115 LVGRAKDRGLFVSvgaeDASRA--DPDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLR-AATDLPLEFHAHN 191
|
90 100
....*....|....*....|....
gi 24652222 794 TSGAGVASMLACANAGADVVDVAV 817
Cdd:cd07939 192 DLGLATANTLAAVRAGATHVSVTV 215
|
|
| RnfC_N |
pfam13375 |
RnfC Barrel sandwich hybrid domain; This domain is part of the barrel sandwich hybrid ... |
1119-1197 |
1.70e-04 |
|
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: 41.77 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1119 VHPKANK--SNKSEVG-APMPGTVI-----------DIRVKVGDKVEKGQPLV----VLSAmkmemVVQSPLAGVVKKLE 1180
Cdd:pfam13375 7 IHPPENKelSKDKPIEkLPLPKELViplsqhigapaEPIVKVGDRVLKGQKIAeadgFVSA-----PVHASVSGTVKAIE 81
|
90 100
....*....|....*....|
gi 24652222 1181 ---IANGTKLEGedliMIIE 1197
Cdd:pfam13375 82 prpVPHGSGVNC----IVIE 97
|
|
| DRE_TIM_HOA_like |
cd07944 |
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ... |
735-823 |
1.73e-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: 44.86 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 735 TKYDLKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDK-HPDIPIHIHTHDTSGAGVASMLACANAGADVV 813
Cdd:cd07944 133 SGYSDEELLELLELVNEIKPDVFYIVDSFGSMYPEDIKRIISLLRSNlDKDIKLGFHAHNNLQLALANTLEAIELGVEII 212
|
90
....*....|
gi 24652222 814 DVavdSMSGM 823
Cdd:cd07944 213 DA---TVYGM 219
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
761-817 |
2.10e-04 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 45.17 E-value: 2.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24652222 761 DMAGLLKPESARLLITAIRdKHPDIPIHIHTHDTSGAGVASMLACANAGADVVDVAV 817
Cdd:PRK11858 166 DTVGILDPFTMYELVKELV-EAVDIPIEVHCHNDFGMATANALAGIEAGAKQVHTTV 221
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
1121-1164 |
2.45e-04 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 44.44 E-value: 2.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 24652222 1121 PKANKSNKSEVGAPMPGTVIdiR---------VKVGDKVEKGQPLVVLSAMKM 1164
Cdd:PLN02983 190 AKAPKSSHPPLKSPMAGTFY--RspapgeppfVKVGDKVQKGQVVCIIEAMKL 240
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1131-1160 |
3.30e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.27 E-value: 3.30e-04
10 20 30
....*....|....*....|....*....|
gi 24652222 1131 VGAPMPGTVIDIRVKVGDKVEKGQPLVVLS 1160
Cdd:COG1566 48 VAAKVSGRVTEVLVKEGDRVKKGQVLARLD 77
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
1127-1159 |
3.62e-04 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 44.16 E-value: 3.62e-04
10 20 30
....*....|....*....|....*....|...
gi 24652222 1127 NKSEVGAPMPGTVIDIRVKVGDKVEKGQPLVVL 1159
Cdd:COG0845 22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARL 54
|
|
| PRK05692 |
PRK05692 |
hydroxymethylglutaryl-CoA lyase; Provisional |
709-862 |
5.74e-04 |
|
hydroxymethylglutaryl-CoA lyase; Provisional
Pssm-ID: 180206 Cd Length: 287 Bit Score: 43.34 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 709 MEAAGKAGGVVEAAIS------YTGDVSdPKRTkydlkyyTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKH 782
Cdd:PRK05692 126 AEAAKQAGVRVRGYVScvlgcpYEGEVP-PEAV-------ADVAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 783 PDIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDSMSGMTSQPsmGA--------VVASLQGTPLDTNLDLRTVSEYS 854
Cdd:PRK05692 198 PAERLAGHFHDTYGQALANIYASLEEGITVFDASVGGLGGCPYAP--GAsgnvatedVLYMLHGLGIETGIDLDKLVRAG 275
|
....*...
gi 24652222 855 AYWEQTRT 862
Cdd:PRK05692 276 QFIQSKLG 283
|
|
| PLN02746 |
PLN02746 |
hydroxymethylglutaryl-CoA lyase |
745-856 |
5.84e-04 |
|
hydroxymethylglutaryl-CoA lyase
Pssm-ID: 178347 Cd Length: 347 Bit Score: 43.62 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 745 LADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHPDIPIHIHTHDTSGAGVASMLACANAGADVVDvavDSMSGMT 824
Cdd:PLN02746 202 VAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTVD---SSVAGLG 278
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24652222 825 SQP-SMGA--------VVASLQGTPLDTNLDLRTVSEYSAY 856
Cdd:PLN02746 279 GCPyAKGAsgnvatedVVYMLNGLGVSTNVDLGKLMAAGDF 319
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
77-346 |
7.24e-04 |
|
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: 43.10 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 77 MHRQKADESYIVGKGLPPVEAYLNIPELIRvcKENDVDAVHPGYGFLSERSDFAQAVIDAGLRFIGPsPEVVQKMGDKVA 156
Cdd:TIGR00768 15 MLKEAAEELGIDYKVVTPPAINLTFNEGPR--ALAELDVVIVRIVSMFRGLAVLRYLESLGVPVINS-SDAILNAGDKFL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 157 ARVAAIEAGVPiVPGTdGPVTTKEEALEFCKKHGLPVIFKAAYgggGRGMRVVRKMEDVEESfqRASSEAKAAFGN--GA 234
Cdd:TIGR00768 92 SHQLLAKAGIP-LPRT-GLAGSPEEALKLIEEIGFPVVLKPVF---GSWGRGVSLARDRQAA--ESLLEHFEQLNGpqNL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 235 MFIEKFIERP--RHIEVQLLGDKagnVVHLYERdcsVQRRHQKVVEIAPAPRLPIEIRDKMTEAAVRLARHVGYENAGtV 312
Cdd:TIGR00768 165 FLVQEYIKKPggRDIRVFVVGDE---VVAAIYR---ITSGHWRSNLARGGKAEPCSLTEEIEELAIKAAKALGLDVAG-V 237
|
250 260 270
....*....|....*....|....*....|....
gi 24652222 313 EFLCDESGnFYFIEVNArlQVEHTVTEEITGIDL 346
Cdd:TIGR00768 238 DLLESEDG-LLVNEVNA--NPEFKNSVKTTGVNI 268
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
140-328 |
7.99e-04 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 43.65 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 140 FIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTdgPVTTK--EEALEFCKKH-----GLPVIFKAAYGGGGRGMRvvrKM 212
Cdd:PRK14573 555 YTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQ--PLTLAgwKREPELCLAHiveafSFPMFVKTAHLGSSIGVF---EV 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 213 EDVEEsFQRASSEAkaAFGNGAMFIEKFIERPRHIEVQLLGDKAGN--VVHLYERdC------SVQRRH----QKVVEIA 280
Cdd:PRK14573 630 HNVEE-LRDKISEA--FLYDTDVFVEESRLGSREIEVSCLGDGSSAyvIAGPHER-RgsggfiDYQEKYglsgKSSAQIV 705
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24652222 281 PAPRLPIEIRDKMTEAAVRLARHVGYENAGTVEFLCDESGNFYFIEVN 328
Cdd:PRK14573 706 FDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMN 753
|
|
| DRE_TIM_LeuA3 |
cd07941 |
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ... |
756-813 |
1.92e-03 |
|
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel domain; Desulfobacterium autotrophicum LeuA3 is sequence-similar to alpha-isopropylmalate synthase (LeuA) but its exact function is unknown. Members of this family have an N-terminal TIM barrel domain that belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163679 Cd Length: 273 Bit Score: 41.67 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 24652222 756 VLCikDMAGLLKPESARLLITAIRDKHPDIPIHIHTHDTSGAGVASMLACANAGADVV 813
Cdd:cd07941 169 VLC--DTNGGTLPHEIAEIVKEVRERLPGVPLGIHAHNDSGLAVANSLAAVEAGATQV 224
|
|
| PRK06524 |
PRK06524 |
biotin carboxylase-like protein; Validated |
135-199 |
2.44e-03 |
|
biotin carboxylase-like protein; Validated
Pssm-ID: 180605 [Multi-domain] Cd Length: 493 Bit Score: 42.03 E-value: 2.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24652222 135 DAGLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGTDGPVTTKEEALEFCKKHGL--PVIFKAAY 199
Cdd:PRK06524 124 QAGLEVMHPPAELRHRLDSKIVTTRLANEAGVPSVPHVLGRVDSYDELSALAHGAGLgdDLVVQTPY 190
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1130-1159 |
3.07e-03 |
|
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: 37.74 E-value: 3.07e-03
10 20 30
....*....|....*....|....*....|
gi 24652222 1130 EVGAPMPGTVIDIRVKVGDKVEKGQPLVVL 1159
Cdd:COG0508 47 EVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
137-330 |
4.28e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 41.24 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 137 GLRFIGPSPEVVQKMGDKVAARVAAIEAGVPIVPGtdGPVTTKEEALEFCKKHGLPVIFKAAYGgggrgmrvvrkM---- 212
Cdd:PRK05294 112 GVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVIIRPSFT-----------Lggtg 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 213 ----EDVEEsFQRASSEAKAAFGNGAMFIEKFIERPRHIEVQLLGDKAGNV-------------VHLYErdcSVqrrhqk 275
Cdd:PRK05294 179 ggiaYNEEE-LEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCiivcsienidpmgVHTGD---SI------ 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24652222 276 VVeiAPAPRLPieirDK----MTEAAVRLARHVGYENAGT-VEF-LCDESGNFYFIEVNAR 330
Cdd:PRK05294 249 TV--APAQTLT----DKeyqmLRDASIAIIREIGVETGGCnVQFaLNPKDGRYIVIEMNPR 303
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1130-1159 |
7.32e-03 |
|
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: 36.61 E-value: 7.32e-03
10 20 30
....*....|....*....|....*....|
gi 24652222 1130 EVGAPMPGTVIDIRVKVGDKVEKGQPLVVL 1159
Cdd:cd06849 45 EVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| RnfC |
COG4656 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ... |
1119-1182 |
7.77e-03 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 443694 [Multi-domain] Cd Length: 451 Bit Score: 40.12 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652222 1119 VHPKANK--SNKSEVG-APMPGTVI-----------DIRVKVGDKVEKGQPL----VVLSAmkmemVVQSPLAGVVKKLE 1180
Cdd:COG4656 10 IHPPENKelSADKPIErLPLPEKLViplqqhigapaEPLVKVGDKVLKGQLIaeadGFVSA-----PVHAPVSGTVVAIE 84
|
..
gi 24652222 1181 IA 1182
Cdd:COG4656 85 PA 86
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1130-1159 |
8.41e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 40.19 E-value: 8.41e-03
10 20 30
....*....|....*....|....*....|
gi 24652222 1130 EVGAPMPGTVIDIRVKVGDKVEKGQPLVVL 1159
Cdd:PRK11855 163 EIPSPVAGVVKEIKVKVGDKVSVGSLLVVI 192
|
|
| |
