|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-1143 |
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: 2348.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1 MNRIKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGAGKKPIDAYLDIENIIEIAKESGADA 80
Cdd:COG1038 1 MKKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 81 IHPGYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMI 160
Cdd:COG1038 81 IHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 161 KASLGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQK 240
Cdd:COG1038 161 KAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 241 VVEVAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLV-EGDDFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIAD 319
Cdd:COG1038 241 VVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 320 GYALHDQLVAIPKQEDIHIHGSAIQSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAGNGFQGTVVTPFYDSLLVKLC 399
Cdd:COG1038 321 GYSLDDPEIGIPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 400 TWGMTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFIDTTPELFKFPHIRDRGTKTLRYIGNVTVN 479
Cdd:COG1038 401 AWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 480 GFPGIKHRDKPVYAEPRLPKIPYGSQISPGTKQILDAKGPEGVVDWVKKQEEVLLTDTTLRDAHQSLLATRVRSKDIFQI 559
Cdd:COG1038 481 GPPGVKGRPKPDFPKPKLPKVDLGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKI 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 560 ADAMAHLLPNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQMLLRGANAVGYKNYPDNVIREFVKQSAQSG 639
Cdd:COG1038 561 APATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEAG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 640 VDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTGDIDDDTRTKYTIDYYKDMAKELVAQGTHILGIKDMAGLLKPQ 719
Cdd:COG1038 641 IDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKPY 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 720 AAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMSGATSQPSMTGLYYGLVNGNRQTNLDAQNS 799
Cdd:COG1038 721 AAYKLVKALKEEVDLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLDAL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 800 QIINHYWEDVRHYYKDFDNALNSPQTEVYIHEMPGGQYTNLQQQAIAVGLGDRWDEVKEMYTVVNQMFGDIVKVTPSSKV 879
Cdd:COG1038 801 QELSNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPSSKV 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 880 VGDLALFMVQNELSEEDVYEKGDTIDFPDSVIEFFMGEIGQPYGGFPEKLQKLVLKGRTPLTDRPGALMEPVNFVEVKAE 959
Cdd:COG1038 881 VGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDALRAE 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 960 LKEKMGYEPTEKDVISYILYPKVFLDYQEMINKYGDVTVLDTPTFYKGMRLGETIEVELEKGKILLIKLNSIGEPIADGT 1039
Cdd:COG1038 961 LEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDEDGM 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1040 RVIYFELNGQPREINIQDMNVQSTVIARRKIDTTNPEHVGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPF 1119
Cdd:COG1038 1041 RTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPR 1120
|
1130 1140
....*....|....*....|....
gi 489827788 1120 DGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:COG1038 1121 DGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-1143 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 2215.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1 MNRIKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGAGKKPIDAYLDIENIIEIAKESGADA 80
Cdd:PRK12999 2 MKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 81 IHPGYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMI 160
Cdd:PRK12999 82 IHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 161 KASLGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQK 240
Cdd:PRK12999 162 KASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 241 VVEVAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGD-DFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIAD 319
Cdd:PRK12999 242 VVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADgNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 320 GYALHDQLVAIPKQEDIHIHGSAIQSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAGNGFQGTVVTPFYDSLLVKLC 399
Cdd:PRK12999 322 GATLHDLEIGIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 400 TWGMTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFIDTTPELFKFPHIRDRGTKTLRYIGNVTVN 479
Cdd:PRK12999 402 AWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTVN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 480 GFPGIKHRDkPVYAEPRLPKIPYGSQISPGTKQILDAKGPEGVVDWVKKQEEVLLTDTTLRDAHQSLLATRVRSKDIFQI 559
Cdd:PRK12999 482 GFPGVKKKP-PVFPDPRLPKVDLSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLLRI 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 560 ADAMAHLLPNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQMLLRGANAVGYKNYPDNVIREFVKQSAQSG 639
Cdd:PRK12999 561 APATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAAAG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 640 VDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTGDIDDDTRTKYTIDYYKDMAKELVAQGTHILGIKDMAGLLKPQ 719
Cdd:PRK12999 641 IDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLKPA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 720 AAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMSGATSQPSMTGLYYGLVNGNRQTNLDAQNS 799
Cdd:PRK12999 721 AAYELVSALKEEVDLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDLDAI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 800 QIINHYWEDVRHYYKDFDNALNSPQTEVYIHEMPGGQYTNLQQQAIAVGLGDRWDEVKEMYTVVNQMFGDIVKVTPSSKV 879
Cdd:PRK12999 801 RKLSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVTPSSKV 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 880 VGDLALFMVQNELSEEDVYEKGDTIDFPDSVIEFFMGEIGQPYGGFPEKLQKLVLKGRTPLTDRPGALMEPVNFVEVKAE 959
Cdd:PRK12999 881 VGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFEAERAE 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 960 LKEKMGYEPTEKDVISYILYPKVFLDYQEMINKYGDVTVLDTPTFYKGMRLGETIEVELEKGKILLIKLNSIGEPIADGT 1039
Cdd:PRK12999 961 LEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEPDEDGM 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1040 RVIYFELNGQPREINIQDMNVQSTVIARRKIDTTNPEHVGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPF 1119
Cdd:PRK12999 1041 RTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPV 1120
|
1130 1140
....*....|....*....|....
gi 489827788 1120 DGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:PRK12999 1121 DGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
6-1143 |
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: 1767.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 6 KVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGAG--KKPIDAYLDIENIIEIAKESGADAIHP 83
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 84 GYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMIKAS 163
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 164 LGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQKVVE 243
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 244 VAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGD-DFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGYA 322
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDgKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 323 LHDQLVAIPKQEDIHIHGSAIQSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAGNGFQGTVVTPFYDSLLVKLCTWG 402
Cdd:TIGR01235 321 LPTPQLGVPNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 403 MTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFIDTTPELFKFPHIRDRGTKTLRYIGNVTVNGFP 482
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNGHP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 483 GIKHRDKPVYAEPRLPKIPYGSQISP-GTKQILDAKGPEGVVDWVKKQEEVLLTDTTLRDAHQSLLATRVRSKDIFQIAD 561
Cdd:TIGR01235 481 EAKDKLKPLENAPRVVVLYADQNPVPrGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIAP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 562 AMAHLLPNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQMLLRGANAVGYKNYPDNVIREFVKQSAQSGVD 641
Cdd:TIGR01235 561 TTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGID 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 642 VFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTGDIDDDTRTKYTIDYYKDMAKELVAQGTHILGIKDMAGLLKPQAA 721
Cdd:TIGR01235 641 IFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAAA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 722 YRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMSGATSQPSMTGLYYGLVNGNRQTNLDAQNSQI 801
Cdd:TIGR01235 721 KLLIKALREKTDLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWIRE 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 802 INHYWEDVRHYYKDFDNALNSPQTEVYIHEMPGGQYTNLQQQAIAVGLGDRWDEVKEMYTVVNQMFGDIVKVTPSSKVVG 881
Cdd:TIGR01235 801 LSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSSKVVG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 882 DLALFMVQNELSEEDVYEKGDTIDFPDSVIEFFMGEIGQPYGGFPEKLQKLVLKGRTPLTDRPGALMEPVNFVEVKAELK 961
Cdd:TIGR01235 881 DMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIRKDLQ 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 962 EKMGYEPTEKDVISYILYPKVFLDYQEMINKYGDVTVLDTPTFYKGMRLGETIEVELEKGKILLIKLNSIGEPIADGTRV 1041
Cdd:TIGR01235 961 EKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQGERE 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1042 IYFELNGQPREINIQDMNVQSTVIARRKIDTTNPEHVGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDG 1121
Cdd:TIGR01235 1041 VFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDG 1120
|
1130 1140
....*....|....*....|..
gi 489827788 1122 EVSSIYVSDGDTIESGDLLIEV 1143
Cdd:TIGR01235 1121 TIKEVLVKAGEQIDAKDLLLVL 1142
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
4-452 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 699.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 4 IKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGaGKKPIDAYLDIENIIEIAKESGADAIHP 83
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIG-PAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 84 GYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMIKAS 163
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 164 lggggrgMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQKVVE 243
Cdd:COG4770 161 aggggkgMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 244 VAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGDD-FYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGYA 322
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGnFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 323 LHdqlvaiPKQEDIHIHGSAIQSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAGnGFQGTVVTPFYDSLLVKLCTWG 402
Cdd:COG4770 321 LP------FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSMIAKLIVWG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 489827788 403 MTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFIDT 452
Cdd:COG4770 394 PDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIER 443
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
4-451 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 606.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 4 IKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGAgKKPIDAYLDIENIIEIAKESGADAIHP 83
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGP-APSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 84 GYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMIKAS 163
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 164 LGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQKVVE 243
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 244 VAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGD-DFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGYA 322
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNgEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 323 LhdqlvaIPKQEDIHIHGSAIQSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAGnGFQGTVVTPFYDSLLVKLCTWG 402
Cdd:PRK08591 321 L------SIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHG 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 489827788 403 MTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFID 451
Cdd:PRK08591 394 ETREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLE 442
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
5-451 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 601.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 5 KKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGAGKkPIDAYLDIENIIEIAKESGADAIHPG 84
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAP-PSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 85 YGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMIKASL 164
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 165 GGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQKVVEV 244
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 245 APCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGDDFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGYALH 324
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 325 dqlvaiPKQEDIHIHGSAIQSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAGNgFQGTVVTPFYDSLLVKLCTWGMT 404
Cdd:PRK08654 322 ------FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGV-HMGYEIPPYYDSMISKLIVWGRT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489827788 405 FEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFID 451
Cdd:PRK08654 395 REEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIE 441
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
4-466 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 572.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 4 IKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGAgkKPIDAYLDIENIIEIAKESGADAIHP 83
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGA--DPLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 84 GYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMIKAS 163
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 164 LGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQKVVE 243
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 244 VAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGDD-FYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGYA 322
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGeVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 323 LHdqlvaiPKQEDIHIHGSAIQSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAGNgFQGTVVTPFYDSLLVKLCTWG 402
Cdd:PRK07178 320 LS------YKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAI-YTGYTIPPYYDSMCAKLIVWA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489827788 403 MTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFIDTTPELFKFPHIRDRG 466
Cdd:PRK07178 393 LTWEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIKRKPE 456
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
4-450 |
1.02e-178 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 531.14 E-value: 1.02e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 4 IKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGaGKKPIDAYLDIENIIEIAKESGADAIHP 83
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIG-GPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 84 GYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMIKAS 163
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 164 LGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQKVVE 243
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 244 VAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGD-DFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGYA 322
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQkNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 323 LHdqlvaiPKQEDIHIHGSAIQSRITTEDPlNNFMPDTGRVDTYRSTGGFGVRLDAGNGfQGTVVTPFYDSLLVKLCTWG 402
Cdd:PRK06111 321 LS------FTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMIAKLIAHG 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 489827788 403 MTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFI 450
Cdd:PRK06111 393 ETREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
532-1143 |
4.71e-174 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 524.79 E-value: 4.71e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 532 VLLTDTTLRDAHQSLLATRVRSKDIFQIADAMAHLlpNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQML 611
Cdd:PRK09282 4 VKITDTTLRDAHQSLLATRMRTEDMLPIAEKLDKV--GFWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 612 LRGANAVGYKNYPDNVIREFVKQSAQSGVDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTgdidddTRTKYTIDY 691
Cdd:PRK09282 82 LRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT------TSPVHTIEK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 692 YKDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMSG 771
Cdd:PRK09282 156 YVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEVDLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISPLAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 772 ATSQPSMTGLYYGLVNGNRQTNLDAQNSQIINHYWEDVRHYYKDFDNALNSPQTEVYIHEMPGGQYTNLQQQAIAVGLGD 851
Cdd:PRK09282 236 GTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTIVDTRVLIHQVPGGMISNLVSQLKEQNALD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 852 RWDEVKEMYTVVNQMFGDIVKVTPSSKVVGDLALFmvqNELSEEDvYEkgdTIdfPDSVIEFFMGEIGQPYGGFPEKLQK 931
Cdd:PRK09282 316 KLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVL---NVLTGER-YK---VI--TKEVKDYVKGLYGRPPAPINEELRK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 932 LVLKGRTPLTDRPGALMEPVnFVEVKAELKEkMGYEPTEkDVISYILYPKVFLDYQEMINKYGDVTVLDTPTFYKGMRLG 1011
Cdd:PRK09282 387 KIIGDEEPITCRPADLLEPE-LEKARKEAEE-LGKSEKE-DVLTYALFPQIAKKFLEEREAGELKPEPEPKEAAAAGAEG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1012 ETIEVELE-KGKILLIKLNSIGEPiadGTRVIYFELNGQPREINIQdmnVQSTVIARRKIDTTNPEHVGATMTGSVIQVV 1090
Cdd:PRK09282 464 IPTEFKVEvDGEKYEVKIEGVKAE---GKRPFYLRVDGMPEEVVVE---PLKEIVVGGRPRASAPGAVTSPMPGTVVKVK 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 489827788 1091 VKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:PRK09282 538 VKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
4-450 |
3.54e-171 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 511.56 E-value: 3.54e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 4 IKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGAGKkPIDAYLDIENIIEIAKESGADAIHP 83
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPAS-SKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 84 GYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMIKAS 163
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 164 LGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQKVVE 243
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 244 VAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGD-DFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGYA 322
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDgNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 323 LHdqlvaiPKQEDIHIHGSAIQSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAgNGFQGTVVTPFYDSLLVKLCTWG 402
Cdd:PRK05586 321 LS------IKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDS-AVYSGYTIPPYYDSMIGKLIVYG 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 489827788 403 MTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFI 450
Cdd:PRK05586 394 KDREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFI 441
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
4-452 |
3.56e-169 |
|
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: 506.61 E-value: 3.56e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 4 IKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGAgKKPIDAYLDIENIIEIAKESGADAIHP 83
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGP-APSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 84 GYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMIKAS 163
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 164 LGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQKVVE 243
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 244 VAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGD-DFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGYA 322
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNgEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 323 LHdqlvaiPKQEDIHIHGSAIQSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDaGNGFQGTVVTPFYDSLLVKLCTWG 402
Cdd:TIGR00514 321 LS------LKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWD-SHVYSGYTVPPYYDSMIGKLITYG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 489827788 403 MTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFIDT 452
Cdd:TIGR00514 394 KTREVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
534-816 |
1.04e-161 |
|
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163675 Cd Length: 275 Bit Score: 480.00 E-value: 1.04e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 534 LTDTTLRDAHQSLLATRVRSKDIFQIADAMAHLLpnMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQMLLR 613
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 614 GANAVGYKNYPDNVIREFVKQSAQSGVDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTGDidddtrTKYTIDYYK 693
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 694 DMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMSGAT 773
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVGLPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGGT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489827788 774 SQPSMTGLYYGLVNGNRQTNLDAQNSQIINHYWEDVRHYYKDF 816
Cdd:cd07937 233 SQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
3-452 |
2.28e-155 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 471.55 E-value: 2.28e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 3 RIKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGAGKKPiDAYLDIENIIEIAKESGADAIH 82
Cdd:PRK12833 4 RIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAA-KSYLNPAAILAAARQCGADAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 83 PGYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMIKA 162
Cdd:PRK12833 83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 163 SLGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHgNIVHLFERDCSIQRRHQKVV 242
Cdd:PRK12833 163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 243 EVAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLV--EGDDFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADG 320
Cdd:PRK12833 242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 321 YALHdqlvaiPKQEDIHIHGSAIQSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAgNGFQGTVVTPFYDSLLVKLCT 400
Cdd:PRK12833 322 EPLR------FAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDS-LLYPGYRVPPFYDSLLAKLIV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489827788 401 WGMTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFIDT 452
Cdd:PRK12833 395 HGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEA 446
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
4-452 |
6.51e-154 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 468.14 E-value: 6.51e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 4 IKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGagKKPIDAYLDIENIIEIAKESGADAIHP 83
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIG--TDPIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 84 GYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNG-PVAGIKEVEEFGEKNGYPLMIKA 162
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 163 SLGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQKVV 242
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 243 EVAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLV-EGDDFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGY 321
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 322 ALHDQlvaipkQEDIHIHGSAIQSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAgNGFQGTVVTPFYDSLLVKLCTW 401
Cdd:PRK08463 320 ILDLE------QSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDS-HIYKDYTIPPYYDSMLAKLIVK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489827788 402 GMTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFIDT 452
Cdd:PRK08463 393 ATSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIET 443
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-452 |
3.76e-149 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 454.20 E-value: 3.76e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1 MNRIKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGaGKKPIDAYLDIENIIEIAKESGADA 80
Cdd:PRK08462 1 KKEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIG-GAKSSESYLNIPAIISAAEIFEADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 81 IHPGYGFLSENIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMI 160
Cdd:PRK08462 80 IFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 161 KASLGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQK 240
Cdd:PRK08462 160 KAAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 241 VVEVAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGD-DFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIAD 319
Cdd:PRK08462 240 LIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNlDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 320 GYALhdqlvaiPKQEDIHIHGSAIQSRITTEDPlNNFMPDTGRVDTYRSTGGFGVRLDAgNGFQGTVVTPFYDSLLVKLC 399
Cdd:PRK08462 320 GEEL-------PSQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMDS-HAYAGYVVPPYYDSMIGKLI 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489827788 400 TWGMTFEQATRKMRRNLIEFRIRGVKTNIPFLLNVVRHPDFASGNYNTSFIDT 452
Cdd:PRK08462 391 VWGEDRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
531-986 |
1.68e-145 |
|
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: 448.19 E-value: 1.68e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 531 EVLLTDTTLRDAHQSLLATRVRSKDIFQIADAMAHLlpNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQM 610
Cdd:COG5016 3 KVKITDTTLRDGHQSLFATRMRTEDMLPIAEKLDEA--GFWSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 611 LLRGANAVGYKNYPDNVIREFVKQSAQSGVDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTgdidddTRTKYTID 690
Cdd:COG5016 81 LLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYT------ISPVHTVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 691 YYKDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMS 770
Cdd:COG5016 155 YYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEALDIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 771 GATSQPSMTGLYYGLVNGNRQTNLDAQNSQIINHYWEDVRHYYKDFDNALNSPQTEVYIHEMPGGQYTNLQQQAIAVGLG 850
Cdd:COG5016 235 GGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGVDPRVLVHQVPGGMLSNLVSQLKEQGAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 851 DRWDEV-KEMyTVVNQMFGDIVKVTPSSKVVGDLALFmvqNELSEEDvYEKgdtidFPDSVIEFFMGEIGQPYGGFPEKL 929
Cdd:COG5016 315 DRLDEVlEEI-PRVREDLGYPPLVTPTSQIVGTQAVL---NVLTGER-YKM-----ITKEVKDYVLGYYGKTPAPIDPEV 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 489827788 930 QKLVLKGRTPLTDRPGALMEPvnfvevkaELKE--KMGYEPTEKDVISYILYPKVFLDY 986
Cdd:COG5016 385 RKKALGDEEPITCRPADLLEP--------ELEKlrKEGLAKSDEDVLTYALFPQVAIKF 435
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
534-1140 |
2.94e-145 |
|
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: 449.24 E-value: 2.94e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 534 LTDTTLRDAHQSLLATRVRSKDIFQIADAMAHLlpNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQMLLR 613
Cdd:TIGR01108 1 ITDVVLRDAHQSLFATRMRTEDMLPIAEKLDDV--GYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 614 GANAVGYKNYPDNVIREFVKQSAQSGVDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTgdidddTRTKYTIDYYK 693
Cdd:TIGR01108 79 GQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT------TSPVHTLETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 694 DMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMSGAT 773
Cdd:TIGR01108 153 DLAEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRFGLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 774 SQPSMTGLYYGLVNGNRQTNLDAQNSQIINHYWEDVRHYYKDFDNALNSPQTEVYIHEMPGGQYTNLQQQAIAVGLGDRW 853
Cdd:TIGR01108 233 SHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFEGQLKGPDSRILVAQVPGGMLSNLESQLKEQNALDKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 854 DEVKEMYTVVNQMFGDIVKVTPSSKVVGDLAlfmVQNELseedVYEKGDTIdfPDSVIEFFMGEIGQPYGGFPEKLQKLV 933
Cdd:TIGR01108 313 DEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLNVL----TGERYKTI--TKETKGYLKGEYGRTPAPINAELQRKI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 934 LKGRTP-LTDRPGALMEPvNFVEVKAELKEKMGYEPTEKDVISYILYPKVfldyqeminkygdvtvldTPTFYKGMRLGE 1012
Cdd:TIGR01108 384 LGDEKPiVDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQV------------------GLKFLENRHNPA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1013 TIEVELEKGKILLIKLNSIGEPIADGTRVIYF-ELNGQPREINIQDMNVQSTVIARRKIDTTNP---------EHVGATM 1082
Cdd:TIGR01108 445 AFEPKPEEKVIEQEHAQVVGKYEETHASGSYTvEVEGKAFVVKVSPGGDVSQITASAPANTSGGtvaakagagTPVTAPI 524
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 489827788 1083 TGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLL 1140
Cdd:TIGR01108 525 AGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAVSVGQVL 582
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
534-1141 |
4.83e-127 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 401.62 E-value: 4.83e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 534 LTDTTLRDAHQSLLATRVRSKDIFQIADAMAHLlpNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQMLLR 613
Cdd:PRK14040 7 ITDVVLRDAHQSLFATRLRLDDMLPIAAKLDKV--GYWSLESWGGATFDACIRFLGEDPWERLRELKKAMPNTPQQMLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 614 GANAVGYKNYPDNVIREFVKQSAQSGVDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTgdidddTRTKYTIDYYK 693
Cdd:PRK14040 85 GQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT------TSPVHTLQTWV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 694 DMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMSGAT 773
Cdd:PRK14040 159 DLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRVDVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAISSMSMTY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 774 SQPSMTGLYYGLVNGNRQTNLDAQNSQIINHYWEDVRHYYKDFDNALNSPQTEVYIHEMPGGQYTNLQQQAIAVGLGDRW 853
Cdd:PRK14040 239 GHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNMESQLKEQGAADKL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 854 DEVKEMYTVVNQMFGDIVKVTPSSKVVGDLAlfmVQNELSEEDvYEkgdTIDFPDSVIefFMGEIGQPYGGFPEKLQKLV 933
Cdd:PRK14040 319 DEVLAEIPRVREDLGFIPLVTPTSQIVGTQA---VLNVLTGER-YK---TITKETAGV--LKGEYGATPAPVNAELQARV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 934 LKGRTPLTDRPGALMEPvNFVEVKAELKEK-------MGYEPTEkDVISYILYPKVFLDYQEmiNK----------YGDV 996
Cdd:PRK14040 390 LEGAEPITCRPADLLAP-ELDKLEAELRRQaqekgitLAENAID-DVLTYALFPQIGLKFLE--NRhnpaafepvpQAEA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 997 TVLDTPTFYKGmrlGETIEVELEkGKILLIKlnsigepIADGtrviyfelnGQPREINIQDMNVQSTVIARRKIDTTNPE 1076
Cdd:PRK14040 466 AQPAAKAEPAG---SETYTVEVE-GKAYVVK-------VSEG---------GDISQITPAAPAAAPAAAAAAAPAAAAGE 525
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489827788 1077 HVGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLI 1141
Cdd:PRK14040 526 PVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
532-988 |
7.22e-117 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 369.42 E-value: 7.22e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 532 VLLTDTTLRDAHQSLLATRVRSKDIFQIADAMAHLlpNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQML 611
Cdd:PRK12331 4 IKITETVLRDGQQSLIATRMTTEEMLPILEKLDNA--GYHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 612 LRGANAVGYKNYPDNVIREFVKQSAQSGVDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTgdidddTRTKYTIDY 691
Cdd:PRK12331 82 LRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT------TSPVHTIDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 692 YKDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMSG 771
Cdd:PRK12331 156 FVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAVTVPLEVHTHATSGIAEMTYLKAIEAGADIIDTAISPFAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 772 ATSQPSMTGLYYGLVNGNRQTNLDAQNSQIINHYWEDVR-HYYK--DFDNALNSPQTEVYIHEMPGGQYTNLQQQAIAVG 848
Cdd:PRK12331 236 GTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRdHYREegILNPKVKDVEPKTLIYQVPGGMLSNLLSQLKEQG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 849 LGDRWDEVKEMYTVVNQMFGDIVKVTPSSKVVGDLALFmvqNELSEEDvYEKgdtidFPDSVIEFFMGEIGQPYGGFPEK 928
Cdd:PRK12331 316 AEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALM---NVISGER-YKM-----VPNEIKDYVRGLYGRPPAPIAEE 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489827788 929 LQKLVLKGRTPLTDRPGALMEPvNFVEVKAELKEkmgYEPTEKDVISYILYPKV---FLDYQE 988
Cdd:PRK12331 387 IKKKIIGDEEVITCRPADLIEP-QLEKLREEIAE---YAESEEDVLSYALFPQQakdFLGRRE 445
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
827-1027 |
3.19e-112 |
|
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: 347.52 E-value: 3.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 827 VYIHEMPGGQYTNLQQQAIAVGLGDRWDEVKEMYTVVNQMFGDIVKVTPSSKVVGDLALFMVQNELSEEDVYEKGDTIDF 906
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 907 PDSVIEFFMGEIGQPYGGFPEKLQKLVLKGRTPLTDRPGALMEPVNFVEVKAELKEKMGYEPTEKDVISYILYPKVFLDY 986
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489827788 987 QEMINKYGDVTVLDTPTFYKGMRLGETIEVELEKGKILLIK 1027
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
532-991 |
2.64e-107 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 344.46 E-value: 2.64e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 532 VLLTDTTLRDAHQSLLATRVRSKDIFQIADAMAHLlpNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQML 611
Cdd:PRK14041 3 VMFVDTTLRDGHQSLIATRMRTEDMLPALEAFDRM--GFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 612 LRGANAVGYKNYPDNVIREFVKQSAQSGVDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTgdidddTRTKYTIDY 691
Cdd:PRK14041 81 LRGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT------VSPVHTLEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 692 YKDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMSG 771
Cdd:PRK14041 155 YLEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKFGVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 772 ATSQPSMTGLYYGLVNGNRQTNLDAQNSQIINHYWEDVRHYYKDFDNALNSPQTEVYIHEMPGGQYTNLQQQAIAVGLGD 851
Cdd:PRK14041 235 GTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYDVGMKSPDSRILVSQIPGGMYSNLVKQLKEQKMLH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 852 RWDEVKEMYTVVNQMFGDIVKVTPSSKVVGDLAlfmVQNELSEEDvYEKgdtidFPDSVIEFFMGEIGQPYGGFPEKLQK 931
Cdd:PRK14041 315 KLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQA---VLNVLTGER-YKR-----VTNETKNYVKGLYGRPPAPIDEELMK 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489827788 932 LVLKGRTPLTDRPGALMEPvnfvEVKAELKEKMGYEPTEKDVISYILYPKV---FL--DYQEMIN 991
Cdd:PRK14041 386 KILGDEKPIDCRPADLLEP----ELEKARKELGILAETDEDLLIYVILGEVgkkFLkkKYEEKIG 446
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
531-1143 |
6.87e-104 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 339.77 E-value: 6.87e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 531 EVLLTDTTLRDAHQSLLATRVRSKDIFQIADAMAHLlpNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQM 610
Cdd:PRK14042 3 KTFITDVTLRDAHQCLIATRMRTEDMLPICNKMDDV--GFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 611 LLRGANAVGYKNYPDNVIREFVKQSAQSGVDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTgdidddTRTKYTID 690
Cdd:PRK14042 81 LLRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT------TSPVHTLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 691 YYKDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMS 770
Cdd:PRK14042 155 NFLELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 771 GATSQPSMTGLYYGLVNGNRQTNLDAQNSQIINHYWEDVRHYYKDFDNALNSPQTEVYIHEMPGGQYTNLQQQAIAVGLG 850
Cdd:PRK14042 235 GGASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 851 DRWDEVKEMYTVVNQMFGDIVKVTPSSKVVGDLALFMVQNElseedvyEKGDTIdfPDSVIEFFMGEIGQPYGGFPEKLQ 930
Cdd:PRK14042 315 DKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQAVINVLTG-------ERYKTI--TNEVKLYCQGKYGTPPGKISSALR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 931 KLVLkGRTPLTD-RPGALMePVNFVEVKAELKEkmgYEPTEKDVISYILYPKVfldYQEMINKYGDVTVLDTPTFYKGMR 1009
Cdd:PRK14042 386 KKAI-GRTEVIEvRPGDLL-PNELDQLQNEISD---LALSDEDVLLYAMFPEI---GRQFLEQRKNNQLIPEPLLTQSSA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1010 LGETIEVELE---KGKILLIKLNSIGEpIADGTRVIYFELNGQPREINIQDMNVQSTVIARRKIDTTNPEHVGATMTGSV 1086
Cdd:PRK14042 458 PDNSVMSEFDiilHGESYHVKVAGYGM-IEHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPGSI 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 489827788 1087 IQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:PRK14042 537 IAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
531-982 |
8.91e-98 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 320.17 E-value: 8.91e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 531 EVLLTDTTLRDAHQSLLATRVRSKDIfqiADAMAHL-LPNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQ 609
Cdd:PRK12330 4 KIGVTELALRDAHQSLMATRMAMEDM---VGACEDIdNAGYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 610 MLLRGANAVGYKNYPDNVIREFVKQSAQSGVDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTgdidddTRTKYTI 689
Cdd:PRK12330 81 MLLRGQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT------VSPIHTV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 690 DYYKDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTV--DVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASS 767
Cdd:PRK12330 155 EGFVEQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgeDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAIS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 768 AMSGATSQPSMTGLYYGLVNGNRQTNLDAQNSQIINHYWEDVRHYYKDFDNALNSPQTEVYIHEMPGGQYTNLQQQAIAV 847
Cdd:PRK12330 235 SMSLGPGHNPTESLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTTGVETEIFKSQIPGGMLSNMESQLKQQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 848 GLGDRWDEVKEMYTVVNQMFGDIVKVTPSSKVVGDLALFMVQneLSEEDVYekgdTIDFPDsvieFFMGEIGQPYGgfpE 927
Cdd:PRK12330 315 GAGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVFNVL--MGRYKVL----TGEFAD----LMLGYYGETPG---E 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 928 KLQKLVLK-----GRTPLTDRPGALMEPvNFVEVKAELKEKMGYEPTEKDVISYILYPKV 982
Cdd:PRK12330 382 RNPEVVEQakkqaKKEPITCRPADLLEP-EWDKLRAEALALEGCDGSDEDVLTYALFPQV 440
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
529-1007 |
1.17e-85 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 285.86 E-value: 1.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 529 QEEVLLTDTTLRDAHQSLLATRVRSKDIFQIADAMAHLlpNMFSFEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMF 608
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDMLPVLTILDKI--GYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 609 QMLLRGANAVGYKNYPDNVIREFVKQSAQSGVDVFRVFDSLNWIKGMEVSIDAVREAGKIVEAAICYTgdidddTRTKYT 688
Cdd:PRK12581 88 QMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT------TSPVHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 689 IDYYKDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSA 768
Cdd:PRK12581 162 LNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIKAMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALSP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 769 MSGATSQPSMTGLYYGLVNGNRQTNLDAQ-NSQIINHYWEDVRHYYKD--FDNALNSPQTEVYIHEMPGGQYTNLQQQAI 845
Cdd:PRK12581 242 FSEGTSQPATESMYLALKEAGYDITLDETlLEQAANHLRQARQKYLADgiLDPSLLFPDPRTLQYQVPGGMLSNMLSQLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 846 AVGLGDRWDEVKEMYTVVNQMFGDIVKVTPSSKVVGDLALFMVQNELSEEDVYEKgdtidfpdsVIEFFMGEIGQPYGGF 925
Cdd:PRK12581 322 QANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVILGKPYQMVSKE---------IKQYLAGDYGKTPAPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 926 PEKLQKLVLKGRTPLTDRPGALMEPvNFVEVKAELKEkmgYEPTEKDVISYILYPKVFLDYqeMINKYGDVTVLDTPTFY 1005
Cdd:PRK12581 393 NEDLKRSQIGSAPVTTNRPADQLSP-EFEVLKAEVAD---LAQTDEDVLTYALFPSVAKPF--LTTKYQTDDVIKVTAFI 466
|
..
gi 489827788 1006 KG 1007
Cdd:PRK12581 467 KA 468
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
118-323 |
3.12e-75 |
|
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: 247.22 E-value: 3.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 118 DKIKAKEQALLADIPVIPGSNGPVAGIKEVEEFGEKNGYPLMIKASLGGGGRGMRVVESKEHVKESFERASSEAKAAFGN 197
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 198 DEVYVEKCVMNPKHIEVQILGDTHGNIVHLFERDCSIQRRHQKVVEVAPCNAITSELRNRICDAAVKLMKNVDYINAGTV 277
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489827788 278 EFLVE--GDDFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGYAL 323
Cdd:pfam02786 161 EFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
535-808 |
1.13e-67 |
|
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163674 [Multi-domain] Cd Length: 265 Bit Score: 228.49 E-value: 1.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 535 TDTTLRDAHQSLLATRvRSKDIFQIADAMAHLlpNMFSFEMWGGATFDVAyrFLNEDPWVRLETLRKQIPNVMFQMLLRG 614
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEA--GVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 615 AnavgyknypdnviREFVKQSAQSGVDVFRVFDSLN--------------WIKGMEVSIDAVREAGKIVEAAICYTgdid 680
Cdd:cd03174 76 R-------------EKGIERALEAGVDEVRIFDSASethsrknlnksreeDLENAEEAIEAAKEAGLEVEGSLEDA---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 681 ddTRTKYTIDYYKDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTV-DVPIHLHTHDTSGNGIYTYAAAVSAGV 759
Cdd:cd03174 139 --FGCKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALpDVPLGLHTHNTLGLAVANSLAALEAGA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489827788 760 DIVDVASSAMSGATSQPSMTGLYYGLVNGNRQTNLDAQNSQIINHYWED 808
Cdd:cd03174 217 DRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVEE 265
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
4-112 |
3.26e-59 |
|
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: 198.09 E-value: 3.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 4 IKKVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFHRYKSDEAYLVGAGKkPIDAYLDIENIIEIAKESGADAIHP 83
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGP-ASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*....
gi 489827788 84 GYGFLSENIEFARRCEQEGIIFVGPKSKH 112
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
344-451 |
8.71e-53 |
|
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: 179.92 E-value: 8.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 344 QSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAGNgFQGTVVTPFYDSLLVKLCTWGMTFEQATRKMRRNLIEFRIRG 423
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGV-YEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 489827788 424 VKTNIPFLLNVVRHPDFASGNYNTSFID 451
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
65-320 |
1.08e-50 |
|
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: 180.07 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 65 DIENII----EIAKESGADAIhpgygfLSEN----IEFARRCEQEGIIfvGPKSKHLDMFGDKIKAKEQALLADIPViPG 136
Cdd:COG0439 1 DIDAIIaaaaELARETGIDAV------LSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 137 SnGPVAGIKEVEEFGEKNGYPLMIKASLGGGGRGMRVVESKEHVKESFERASSEAKAAFGNDEVYVEKCVMNPkHIEVQI 216
Cdd:COG0439 72 F-ALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGR-EYSVEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 217 LGDtHGNIVHlferdCSIQRRHQK---VVE---VAPCnAITSELRNRICDAAVKLMKNVDYIN-AGTVEFLVEGDD-FYF 288
Cdd:COG0439 150 LVR-DGEVVV-----CSITRKHQKppyFVElghEAPS-PLPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGePYL 222
|
250 260 270
....*....|....*....|....*....|....
gi 489827788 289 IEVNPRVQVEH--TITEMITGIDIVQSQLFIADG 320
Cdd:COG0439 223 IEINARLGGEHipPLTELATGVDLVREQIRLALG 256
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
344-452 |
1.31e-45 |
|
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: 159.20 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 344 QSRITTEDPLNNFMPDTGRVDTYRSTGGFGVRLDAGnGFQGTVVTPFYDSLLVKLCTWGMTFEQATRKMRRNLIEFRIRG 423
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 489827788 424 VKTNIPFLLNVVRHPDFASGNYNTSFIDT 452
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
532-797 |
1.08e-28 |
|
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: 116.29 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 532 VLLTDTTLRDAHQSLlatrvrsKDIFQIAD--AMAHLLpnmfsfEMWGGATFDVAYRFLNEDPWVRLETLRKQIPNVMFQ 609
Cdd:pfam00682 2 VAICDTTLRDGEQAL-------GVAFSIDEklAIARAL------DAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARIL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 610 MLLRGAnavgyknypDNVIREFVKQSAQSGVDVFRVFDSLNwIKGMEVSI-----DAVREAGKIVEAAICYTGDI----D 680
Cdd:pfam00682 69 VLCRAR---------EHDIKAAVEALKGAGAVRVHVFIATS-DLHRKYKLgkdreEVAKRAVAAVKAARSRGIDVefspE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 681 DDTRTkyTIDYYKDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVD--VPIHLHTHDTSGNGIYTYAAAVSAG 758
Cdd:pfam00682 139 DASRT--DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPnkAIISVHCHNDLGMAVANSLAAVEAG 216
|
250 260 270
....*....|....*....|....*....|....*....
gi 489827788 759 VDIVDVASSAMSGATSQPSMTGLYYGLVNGNRQTNLDAQ 797
Cdd:pfam00682 217 ADRVDGTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQ 255
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1077-1143 |
7.67e-27 |
|
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: 104.42 E-value: 7.67e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489827788 1077 HVGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1071-1143 |
1.46e-19 |
|
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: 86.10 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1071 DTTNPEHVGATMTGSV-------IQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:COG0511 56 AASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1078-1143 |
4.04e-18 |
|
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: 79.57 E-value: 4.04e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489827788 1078 VGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:pfam00364 8 IGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1078-1143 |
5.91e-18 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 81.83 E-value: 5.91e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489827788 1078 VGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:PRK05641 87 VTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1076-1144 |
7.24e-15 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 72.54 E-value: 7.24e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489827788 1076 EHVGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEVN 1144
Cdd:PRK06549 62 DAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1077-1143 |
1.11e-14 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 69.82 E-value: 1.11e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489827788 1077 HVGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:PRK08225 3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEI 69
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
65-295 |
7.89e-13 |
|
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: 72.60 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 65 DIENIIEiaKESgADAIHPGYGflseN---IEFARRCEQEGIIfvgpksKHLDMFG---DKIKAKE-----QALLAD--I 131
Cdd:COG0458 61 DVLDIIE--KEK-PDGVIVQFG----GqtaLNLAVELEEAGIL------EGVKILGtspDAIDLAEdrelfKELLDKlgI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 132 PVIPgsNGPVAGIKEVEEFGEKNGYPLMIKASLGGGGRGMRVVESKEHvkesFERASSEAKAAFGNDEVYVEKCVMNPKH 211
Cdd:COG0458 128 PQPK--SGTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEE----LEEYLERALKVSPDHPVLIDESLLGAKE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 212 IEVQILGDTHGNIV------HlFER------DcSIQrrhqkvveVAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEF 279
Cdd:COG0458 202 IEVDVVRDGEDNVIivgimeH-IEPagvhsgD-SIC--------VAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQF 271
|
250
....*....|....*.
gi 489827788 280 LVEGDDFYFIEVNPRV 295
Cdd:COG0458 272 AVDDGRVYVIEVNPRA 287
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1076-1140 |
1.29e-12 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 64.06 E-value: 1.29e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489827788 1076 EHVGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLL 1140
Cdd:PRK05889 3 EDVRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1075-1143 |
2.88e-11 |
|
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: 60.15 E-value: 2.88e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489827788 1075 PEHVGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1078-1143 |
5.27e-11 |
|
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: 59.34 E-value: 5.27e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489827788 1078 VGATMT-GSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:cd06849 8 LGESMTeGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1078-1143 |
4.91e-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: 56.61 E-value: 4.91e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489827788 1078 VGATMT-GSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:COG0508 10 LGESMTeGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
4-325 |
6.40e-09 |
|
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: 60.40 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 4 IKKVLVANRGEIAI--------RVMRACTELK---IKTVAIYS-----QEDTGSfhrykSDEAYLVgagkkPIDAYLdIE 67
Cdd:TIGR01369 6 IKKILVIGSGPIVIgqaaefdySGSQACKALKeegYRVILVNSnpatiMTDPEM-----ADKVYIE-----PLTPEA-VE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 68 NIIEiaKESgADAIHPGYG---FLSENIEFARR--CEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGsnGPVA 142
Cdd:TIGR01369 75 KIIE--KER-PDAILPTFGgqtALNLAVELEESgvLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIAH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 143 GIKEVEEFGEKNGYPLMIKASLGGGGRGMRVVESKEHVKESFERASSEAKAafgnDEVYVEKCVMNPKHIEVQILGDTHG 222
Cdd:TIGR01369 150 SVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVLVEKSLAGWKEIEYEVMRDSND 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 223 NIVHLferdCSIQR-----RH--QKVVeVAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLV--EGDDFYFIEVNP 293
Cdd:TIGR01369 226 NCITV----CNMENfdpmgVHtgDSIV-VAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALnpDSGRYYVIEVNP 300
|
330 340 350
....*....|....*....|....*....|..
gi 489827788 294 RVQVEHTITEMITGIDIVQSQLFIADGYALHD 325
Cdd:TIGR01369 301 RVSRSSALASKATGYPIAKVAAKLAVGYTLDE 332
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
65-311 |
9.86e-09 |
|
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: 59.63 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 65 DIENIIEIAKESGAdAIHPGyGFLSENIefARRCEQEGIIFVGPKSKHLDMFGDKikAKEQALLADIPVIPGSNGPVAGI 144
Cdd:TIGR01369 620 DVMNIIELEKPEGV-IVQFG-GQTPLNL--AKALEEAGVPILGTSPESIDRAEDR--EKFSELLDELGIPQPKWKTATSV 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 145 KEVEEFGEKNGYPLMIKASLGGGGRGMRVVESKEHVKESFERASSEAKaafgNDEVYVEKCVMNPKHIEVQILGDtHGNI 224
Cdd:TIGR01369 694 EEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSP----EHPVLIDKYLEDAVEVDVDAVSD-GEEV 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 225 -------------VHLFERDCSIqrrhqkvvevaPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGDDFYFIEV 291
Cdd:TIGR01369 769 lipgimehieeagVHSGDSTCVL-----------PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEV 837
|
250 260
....*....|....*....|
gi 489827788 292 NPRVQVEHTITEMITGIDIV 311
Cdd:TIGR01369 838 NPRASRTVPFVSKATGVPLA 857
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
64-312 |
1.03e-08 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 59.60 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 64 LDIENIIEIAKESGADAIHPGYGFLSEnIEFARRCEQEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVIPGsnGPVAG 143
Cdd:PRK12815 617 LTLEDVLNVAEAENIKGVIVQFGGQTA-INLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATD 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 144 IKEVEEFGEKNGYPLMIKASLGGGGRGMRVVESKEHVKESFERASSeakaafGNDEVYVEKCVmNPKHIEVQILGD---- 219
Cdd:PRK12815 694 EEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENAS------QLYPILIDQFI-DGKEYEVDAISDgedv 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 220 THGNIVHLFER------DcSIQrrhqkvveVAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGDDFYFIEVNP 293
Cdd:PRK12815 767 TIPGIIEHIEQagvhsgD-SIA--------VLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNP 837
|
250 260
....*....|....*....|.
gi 489827788 294 RVQveHT--ITEMITGIDIVQ 312
Cdd:PRK12815 838 RAS--RTvpFVSKATGVPLAK 856
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
6-295 |
2.90e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 57.25 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 6 KVLVANRGEIAIRVMRACTELKIKTVAIYSQEDTGSFH-RYkSDEAYLVGAGKKPIDAYLDieNIIEIAKESGADAIHPG 84
Cdd:COG3919 7 RVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARsRY-VDEVVVVPDPGDDPEAFVD--ALLELAERHGPDVLIPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 85 Y----GFLSENIEFARrceqEGIIFVGPKSKHLDMFGDKIKAKEQALLADIPVipgsngP----VAGIKEVEEFGEKNGY 156
Cdd:COG3919 84 GdeyvELLSRHRDELE----EHYRLPYPDADLLDRLLDKERFYELAEELGVPV------PktvvLDSADDLDALAEDLGF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 157 PLMIKASLGGggrgmRVVESKEHVKESFERASSEAKAafgnDEVYVEKCVMNPKHIeVQ--ILG------------DTHG 222
Cdd:COG3919 154 PVVVKPADSV-----GYDELSFPGKKKVFYVDDREEL----LALLRRIAAAGYELI-VQeyIPGddgemrgltayvDRDG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489827788 223 NIVHLFerdcSIQRRHQKVVEVAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGDD--FYFIEVNPRV 295
Cdd:COG3919 224 EVVATF----TGRKLRHYPPAGGNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDgeYKLIEINPRF 294
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1084-1143 |
2.68e-07 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 54.83 E-value: 2.68e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1084 GSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVI 75
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1078-1143 |
3.64e-07 |
|
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: 54.11 E-value: 3.64e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489827788 1078 VGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATL 73
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1071-1143 |
5.29e-07 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 53.85 E-value: 5.29e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489827788 1071 DTTNPEhVGATmTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLL--IEV 1143
Cdd:PRK11854 208 DVNVPD-IGGD-EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLImrFEV 280
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1070-1141 |
6.63e-07 |
|
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: 53.34 E-value: 6.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489827788 1070 IDTTNPEhVGATMTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLI 1141
Cdd:TIGR01348 117 QEVTVPD-IGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLIL 187
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
659-771 |
7.46e-07 |
|
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: 52.01 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 659 IDAVREAGKIVEAAI-----C-YTGDIDDDTRTkytidyykDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTV 732
Cdd:cd07938 120 AELAKAAGLRVRGYVstafgCpYEGEVPPERVA--------EVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERF 191
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489827788 733 -DVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDvasSAMSG 771
Cdd:cd07938 192 pDEKLALHFHDTRGQALANILAALEAGVRRFD---SSVGG 228
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
45-294 |
1.34e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 51.81 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 45 YKSDEAYLVgagkKPIDA--YLDIenIIEIAKESGADAIHPGY----GFLSENiefARRCEQEGIIFVGPkSKHL-DMFG 117
Cdd:PRK12767 41 YFADKFYVV----PKVTDpnYIDR--LLDICKKEKIDLLIPLIdpelPLLAQN---RDRFEEIGVKVLVS-SKEViEICN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 118 DKIK----AKEQALLADIPVIPGSngpVAGIKEVEEFGEkNGYPLMIK-----ASLGgggrgMRVVESKEHVKESFERas 188
Cdd:PRK12767 111 DKWLtyefLKENGIPTPKSYLPES---LEDFKAALAKGE-LQFPLFVKprdgsASIG-----VFKVNDKEELEFLLEY-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 189 seakaafgNDEVYVEKCVmNPKHIEVQILGDTHGNIVHlferdcSIQRRHQKVVEVAPCNAITSElRNRICDAAVKLMKN 268
Cdd:PRK12767 180 --------VPNLIIQEFI-EGQEYTVDVLCDLNGEVIS------IVPRKRIEVRAGETSKGVTVK-DPELFKLAERLAEA 243
|
250 260
....*....|....*....|....*.
gi 489827788 269 VDYINAGTVEFLVEGDDFYFIEVNPR 294
Cdd:PRK12767 244 LGARGPLNIQCFVTDGEPYLFEINPR 269
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1084-1143 |
2.49e-06 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 51.54 E-value: 2.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489827788 1084 GSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLL--IEV 1143
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLImvFEV 179
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
146-324 |
4.64e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 51.12 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 146 EVEEFGEKNGYPLMIKASLGGGGRGMRVVESKEHVKESFERASSEAKAafgnDEVYVEKCVMNPKHIEVQILGDTHGNIV 225
Cdd:PRK12815 154 EALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPI----HQCLLEESIAGWKEIEYEVMRDRNGNCI 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 226 HLferdCSIQRrhqkvVE-----------VAPCNAITSELRNRICDAAVKLMKNVDYINAGTVEFLV--EGDDFYFIEVN 292
Cdd:PRK12815 230 TV----CNMEN-----IDpvgihtgdsivVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALdpKSKQYYLIEVN 300
|
170 180 190
....*....|....*....|....*....|..
gi 489827788 293 PRVQVEHTITEMITGIDIVQSQLFIADGYALH 324
Cdd:PRK12815 301 PRVSRSSALASKATGYPIAKIAAKLAVGYTLN 332
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1075-1143 |
4.68e-06 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 50.77 E-value: 4.68e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489827788 1075 PEhVGATmTGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:PRK11854 8 PD-IGAD-EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF 74
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1084-1143 |
7.94e-06 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 49.82 E-value: 7.94e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 1084 GSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVI 192
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
681-764 |
1.12e-05 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 49.02 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 681 DDTRTKytIDYYKDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSG----NGIytyaAAVS 756
Cdd:PRK11858 138 DASRTD--LDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELVEAVDIPIEVHCHNDFGmataNAL----AGIE 211
|
....*...
gi 489827788 757 AGVDIVDV 764
Cdd:PRK11858 212 AGAKQVHT 219
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1078-1140 |
3.46e-05 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 47.63 E-value: 3.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489827788 1078 VGATMT-GSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLL 1140
Cdd:PRK14875 10 WGLSMTeGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
129-293 |
1.01e-04 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 44.61 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 129 ADIPVIP--------GSNGPVAGIKEVEEfgeKNGYPLMIKASLGGGGRGMRVVESKEHVKESFErasseakAAFGNDE- 199
Cdd:pfam07478 5 AGLPVVPfvtftradWKLNPKEWCAQVEE---ALGYPVFVKPARLGSSVGVSKVESREELQAAIE-------EAFQYDEk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 200 VYVEKCVmNPKHIEVQILGDTHGNIVHLFER--DCSIQRRHQKVVE-----VAPCNaITSELRNRICDAAVKLMKNVDYI 272
Cdd:pfam07478 75 VLVEEGI-EGREIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDdsaqiVVPAD-LEEEQEEQIQELALKAYKALGCR 152
|
170 180
....*....|....*....|..
gi 489827788 273 NAGTVEFLVEGDD-FYFIEVNP 293
Cdd:pfam07478 153 GLARVDFFLTEDGeIVLNEVNT 174
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
1091-1143 |
1.22e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 41.54 E-value: 1.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 489827788 1091 VKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
181-327 |
1.43e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 46.31 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 181 KESFERASSEAKAAFGNDEVYVEKCVMNPKHIEVQILGDTHGNIVHLferdCSIQRRHQKVVE------VAPCNAITSEL 254
Cdd:PLN02735 202 KEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVII----CSIENIDPMGVHtgdsitVAPAQTLTDKE 277
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489827788 255 RNRICDAAVKLMKNVDYINAGT-VEFLVEGDD--FYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGYALhDQL 327
Cdd:PLN02735 278 YQRLRDYSVAIIREIGVECGGSnVQFAVNPVDgeVMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTL-DQI 352
|
|
| DRE_TIM_HCS |
cd07948 |
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ... |
703-764 |
1.43e-04 |
|
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel domain; Homocitrate synthase (HCS) catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate, the first step in the lysine biosynthesis pathway. This family includes the Yarrowia lipolytica LYS1 protein as well as the Saccharomyces cerevisiae LYS20 and LYS21 proteins. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163685 Cd Length: 262 Bit Score: 45.02 E-value: 1.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489827788 703 GTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSGNGIYTYAAAVSAGVDIVDV 764
Cdd:cd07948 154 GVNRVGIADTVGIATPRQVYELVRTLRGVVSCDIEFHGHNDTGCAIANAYAALEAGATHIDT 215
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
93-294 |
3.01e-04 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 45.05 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 93 EFARRC------------------EQEGIIfVGPKSKHLDMFGDKIKAKEQALLADIPVIPGSNgpVAGIKEVEEFGEKN 154
Cdd:PLN02948 79 EFAKRCdvltveiehvdvdtlealEKQGVD-VQPKSSTIRIIQDKYAQKVHFSKHGIPLPEFME--IDDLESAEKAGDLF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 155 GYPLMIKAS-LGGGGRGMRVVESKEHVkesferasSEAKAAFGNDE--VYVEKCVMNPKHIEVQILGDTHGNIV--HLFE 229
Cdd:PLN02948 156 GYPLMLKSRrLAYDGRGNAVAKTEEDL--------SSAVAALGGFErgLYAEKWAPFVKELAVMVARSRDGSTRcyPVVE 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489827788 230 rdcSIQRRHQKVVEVAPCNaITSELRNRICDAAVKLMKNVDyiNAGT--VE-FLVEGDDFYFIEVNPR 294
Cdd:PLN02948 228 ---TIHKDNICHVVEAPAN-VPWKVAKLATDVAEKAVGSLE--GAGVfgVElFLLKDGQILLNEVAPR 289
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
1084-1144 |
3.90e-04 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 44.34 E-value: 3.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489827788 1084 GSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEVN 1144
Cdd:TIGR01347 15 GTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE 75
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
1083-1143 |
6.22e-04 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 43.52 E-value: 6.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489827788 1083 TGSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLLIEV 1143
Cdd:PTZ00144 58 EGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEI 118
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
118-294 |
6.86e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 44.00 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 118 DKIKAKE-----QALLADIPVipgsNGPVAGIKEVEE----FGEKNGYPLMIKASLGGGGRGMRVVESKEHVKESFERAS 188
Cdd:PLN02735 695 DSIDAAEdrerfNAILNELKI----EQPKGGIARSEAdalaIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAV 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 189 SEAKaafgNDEVYVEKCVMNPKHIEVQILGDTHGNIV-------------HLFERDCSIqrrhqkvvevaPCNAITSELR 255
Cdd:PLN02735 771 EVDP----ERPVLVDKYLSDATEIDVDALADSEGNVViggimehieqagvHSGDSACSL-----------PTQTIPSSCL 835
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489827788 256 NRICDAAVKLMKNVDYINAGTVEFLV-EGDDFYFIEVNPR 294
Cdd:PLN02735 836 ATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPR 875
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
62-295 |
7.88e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.22 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 62 AYLDIENIIEIAKESgaDAIhpGYGFlsENI--EFARRCEQEGIIFVGPKS-KHLdmfGDKIKakEQALLAD--IPVIPG 136
Cdd:PRK06019 50 DYDDVAALRELAEQC--DVI--TYEF--ENVpaEALDALAARVPVPPGPDAlAIA---QDRLT--EKQFLDKlgIPVAPF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 137 SngPVAGIKEVEEFGEKNGYPLMIKASlggggrgmR---------VVESKEHVkesferasSEAKAAFGNDEVYVEKCVm 207
Cdd:PRK06019 119 A--VVDSAEDLEAALADLGLPAVLKTR--------RggydgkgqwVIRSAEDL--------EAAWALLGSVPCILEEFV- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 208 NPKHiEVQILG--DTHGNIVH--LFErdcSIQRRHQKVVEVAPCnAITSELRNRICDAAVKLMKNVDYInaGT--VEFLV 281
Cdd:PRK06019 180 PFER-EVSVIVarGRDGEVVFypLVE---NVHRNGILRTSIAPA-RISAELQAQAEEIASRIAEELDYV--GVlaVEFFV 252
|
250
....*....|....*
gi 489827788 282 EGDDFYFI-EVNPRV 295
Cdd:PRK06019 253 TGDGELLVnEIAPRP 267
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1084-1140 |
9.39e-04 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 42.90 E-value: 9.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489827788 1084 GSVIQVVVKKGDSVKKGDPLLITEAMKMETTIQAPFDGEVSSIYVSDGDTIESGDLL 1140
Cdd:PRK05704 17 ATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVL 73
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
681-764 |
1.20e-03 |
|
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: 42.11 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 681 DDTRTKytIDYYKDMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVPIHLHTHDTSG----NGIytyaAAVS 756
Cdd:cd07939 132 DASRAD--PDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAATDLPLEFHAHNDLGlataNTL----AAVR 205
|
....*...
gi 489827788 757 AGVDIVDV 764
Cdd:cd07939 206 AGATHVSV 213
|
|
| PLN02746 |
PLN02746 |
hydroxymethylglutaryl-CoA lyase |
694-795 |
1.28e-03 |
|
hydroxymethylglutaryl-CoA lyase
Pssm-ID: 178347 Cd Length: 347 Bit Score: 42.47 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 694 DMAKELVAQGTHILGIKDMAGLLKPQAAYRLIGELKDTVDVP-IHLHTHDTSGNGIYTYAAAVSAGVDIVDVASSAMSGA 772
Cdd:PLN02746 201 YVAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDkLAVHFHDTYGQALANILVSLQMGISTVDSSVAGLGGC 280
|
90 100 110
....*....|....*....|....*....|.
gi 489827788 773 TSQPSMTG-------LYygLVNGNR-QTNLD 795
Cdd:PLN02746 281 PYAKGASGnvatedvVY--MLNGLGvSTNVD 309
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
244-343 |
1.68e-03 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 42.21 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 244 VAPCNaITSELRNRICDAAVKLMKNVDYINAGTVEFLVEGDDFYFIEVNPRVQVEHTITEMITGIDIVQSQLFIADGyal 323
Cdd:COG2232 213 IGPLA-LPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRG--- 288
|
90 100
....*....|....*....|
gi 489827788 324 hdQLVAIPKQEDIHIHGSAI 343
Cdd:COG2232 289 --ELPEVPRPKPRRVAAKAI 306
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
66-295 |
1.97e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 42.39 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 66 IENIIEiaKEsGADAIHPGYG---FLSENIEFARRceqeGIIfvgpkSKH-LDMFGDKIKAKEQA--------LLADI-- 131
Cdd:PRK05294 74 VEKIIE--KE-RPDAILPTMGgqtALNLAVELAES----GVL-----EKYgVELIGAKLEAIDKAedrelfkeAMKKIgl 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 132 PVIPGsnGPVAGIKEVEEFGEKNGYPLMIKASLGgggrgM-----RVVESKEhvkeSFERASSEAKAAFGNDEVYVEKCV 206
Cdd:PRK05294 142 PVPRS--GIAHSMEEALEVAEEIGYPVIIRPSFT-----LggtggGIAYNEE----ELEEIVERGLDLSPVTEVLIEESL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 207 MNPKHIEVQILGDTHGN--IVhlferdCSIqrrhqkvvE--------------VAPCNAITSELRNRICDAAVKLMKNVD 270
Cdd:PRK05294 211 LGWKEYEYEVMRDKNDNciIV------CSI--------EnidpmgvhtgdsitVAPAQTLTDKEYQMLRDASIAIIREIG 276
|
250 260
....*....|....*....|....*...
gi 489827788 271 YINAGT-VEFLVEGDDF--YFIEVNPRV 295
Cdd:PRK05294 277 VETGGCnVQFALNPKDGryIVIEMNPRV 304
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
1114-1144 |
2.10e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 37.04 E-value: 2.10e-03
10 20 30
....*....|....*....|....*....|.
gi 489827788 1114 TIQAPFDGEVSSIYVSDGDTIESGDLLIEVN 1144
Cdd:pfam13533 4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLD 34
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
696-772 |
4.08e-03 |
|
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: 40.56 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 696 AKELVAQ-------GTHILGIKDMAGLLKPQAAYRLIGELKDTVDV-PIHLHTHDTSGNGIYTYAAAVSAGVDIVDvASS 767
Cdd:cd07943 140 PEELAEQaklmesyGADCVYVTDSAGAMLPDDVRERVRALREALDPtPVGFHGHNNLGLAVANSLAAVEAGATRID-GSL 218
|
....*
gi 489827788 768 AMSGA 772
Cdd:cd07943 219 AGLGA 223
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
140-295 |
6.75e-03 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 38.77 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 140 PVAGIKEVEEFGEKNGYPLMIKAS-LGGGGRGMRVVESKEHVKESFErasseakaAFGNDEVYVEKCVMNPKHIEVQILG 218
Cdd:pfam02222 12 AAESLEELIEAGQELGYPCVVKARrGGYDGKGQYVVRSEADLPQAWE--------ELGDGPVIVEEFVPFDRELSVLVVR 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489827788 219 DTHGNiVHLFERDCSIQRRHQKVVEVAPCnAITSELRNRICDAAVKLMKNVDYINAGTVE-FLVEGDDFYFIEVNPRV 295
Cdd:pfam02222 84 SVDGE-TAFYPVVETIQEDGICRLSVAPA-RVPQAIQAEAQDIAKRLVDELGGVGVFGVElFVTEDGDLLINELAPRP 159
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
686-762 |
9.57e-03 |
|
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases, as well as cobalamine (B12) independent methionine synthases. Despite their sequence similarities, members of this family have clearly different functions. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane, and methionine synthases transfer a methyl group from a folate cofactor to L-homocysteine in a reaction requiring zinc.
Pssm-ID: 238261 [Multi-domain] Cd Length: 306 Bit Score: 39.40 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489827788 686 KYTIDYYKDMAKELVAQGTHILGIKDMAG-----LLKPQA-------AYRLIGELKDTVDVPIHLHTHDTSGNGiytYAA 753
Cdd:cd00465 140 EYLTEFILEYAKTLIEAGAKALQIHEPAFsqinsFLGPKMfkkfalpAYKKVAEYKAAGEVPIVHHSCYDAADL---LEE 216
|
....*....
gi 489827788 754 AVSAGVDIV 762
Cdd:cd00465 217 MIQLGVDVI 225
|
|
| |
