|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
2-1142 |
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: 2194.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 2 LKKFNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGKGPIDAYLDMDGIIDLAKRKKVDA 81
Cdd:COG1038 1 MKKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 82 IHPGYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMI 161
Cdd:COG1038 81 IHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 162 KASNGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQK 241
Cdd:COG1038 161 KAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 242 IIEYAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQ 321
Cdd:COG1038 241 VVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 322 GYSLDSEEINIKSQDDVEIRGYSIQCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDGGNGFTGANISPHYDSLLVKTI 401
Cdd:COG1038 321 GYSLDDPEIGIPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 402 SWDRTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFIDENPDLFEITESKDRGTKLLQFIGDVIVN 481
Cdd:COG1038 401 AWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 482 DNAC---KEKPLFDALHDPRMDKDGSKSEGSKILFDKLGKSAYIEKIKNDKKLLLTDTTMRDAHQSLLATRIRTYDLLKA 558
Cdd:COG1038 481 GPPGvkgRPKPDFPKPKLPKVDLGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKI 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 559 AKPTEKYQKDLFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMFQMLLRASNGVGYKNYPDNVIEEFTKESARQG 638
Cdd:COG1038 561 APATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEAG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 639 IDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTGDILDKTKTKYNLEYYIKMAQELESLGADIIAIKDMSGLLKPY 718
Cdd:COG1038 641 IDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKPY 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 719 SAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALESMAGLTSQPSLNAIVEALKNTERDTGIDLFGY 798
Cdd:COG1038 721 AAYKLVKALKEEVDLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLDAL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 799 DELGKYYKDLRKVYNKFESDLTNSCAEIYNFEIPGGQYTNLKPQADSLGLVNRFDEVKEKYKEANEVVGDIIKVTPSSKV 878
Cdd:COG1038 801 QELSNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPSSKV 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 879 VGDLAIFMTKNKLDKDNIIEEGKNLSFPDSVVDYCKGMIGQPEGGIPKDLQEVVLKGEEAITVRPGSLLPAEDFDEIAKY 958
Cdd:COG1038 881 VGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDALRAE 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 959 LNEKYDINANIRNVISYALYPKVYEDYIKHLQHYNDISKLESDVFFYGLNKNEECEVEIEEGKVLTIRLVEIGEVKENGF 1038
Cdd:COG1038 961 LEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDEDGM 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 1039 RTIGFELNGMVREVEIKDKNFSGKINNVEKADMNDPLQIGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKT 1118
Cdd:COG1038 1041 RTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPR 1120
|
1130 1140
....*....|....*....|....
gi 489520803 1119 DGVIKSIKVKEDDMVEDKQLLMIM 1142
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: 2047.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 1 MLKKFNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGKGPIDAYLDMDGIIDLAKRKKVD 80
Cdd:PRK12999 1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 81 AIHPGYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVM 160
Cdd:PRK12999 81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 161 IKASNGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQ 240
Cdd:PRK12999 161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 241 KIIEYAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIA 320
Cdd:PRK12999 241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 321 QGYSLDSEEINIKSQDDVEIRGYSIQCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDGGNGFTGANISPHYDSLLVKT 400
Cdd:PRK12999 321 EGATLHDLEIGIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 401 ISWDRTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFIDENPDLFEITESKDRGTKLLQFIGDVIV 480
Cdd:PRK12999 401 TAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 481 NDNAC--KEKPLFDALHDPRMDKDGSKSEGSKILFDKLGKSAYIEKIKNDKKLLLTDTTMRDAHQSLLATRIRTYDLLKA 558
Cdd:PRK12999 481 NGFPGvkKKPPVFPDPRLPKVDLSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLLRI 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 559 AKPTEKYQKDLFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMFQMLLRASNGVGYKNYPDNVIEEFTKESARQG 638
Cdd:PRK12999 561 APATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAAAG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 639 IDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTGDILDKTKTKYNLEYYIKMAQELESLGADIIAIKDMSGLLKPY 718
Cdd:PRK12999 641 IDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLKPA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 719 SAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALESMAGLTSQPSLNAIVEALKNTERDTGIDLFGY 798
Cdd:PRK12999 721 AAYELVSALKEEVDLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDLDAI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 799 DELGKYYKDLRKVYNKFESDLTNSCAEIYNFEIPGGQYTNLKPQADSLGLVNRFDEVKEKYKEANEVVGDIIKVTPSSKV 878
Cdd:PRK12999 801 RKLSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVTPSSKV 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 879 VGDLAIFMTKNKLDKDNIIEEGKNLSFPDSVVDYCKGMIGQPEGGIPKDLQEVVLKGEEAITVRPGSLLPAEDFDEIAKY 958
Cdd:PRK12999 881 VGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFEAERAE 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 959 LNEKYDINANIRNVISYALYPKVYEDYIKHLQHYNDISKLESDVFFYGLNKNEECEVEIEEGKVLTIRLVEIGEVKENGF 1038
Cdd:PRK12999 961 LEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEPDEDGM 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 1039 RTIGFELNGMVREVEIKDKNFSGKINNVEKADMNDPLQIGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKT 1118
Cdd:PRK12999 1041 RTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPV 1120
|
1130 1140
....*....|....*....|....*
gi 489520803 1119 DGVIKSIKVKEDDMVEDKQLLMIMK 1143
Cdd:PRK12999 1121 DGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
7-1142 |
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: 1550.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 7 KILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEG--KGPIDAYLDMDGIIDLAKRKKVDAIHP 84
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 85 GYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMIKAS 164
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 165 NGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQKIIE 244
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 245 YAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQGYS 324
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 325 LDSEEINIKSQDDVEIRGYSIQCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDGGNGFTGANISPHYDSLLVKTISWD 404
Cdd:TIGR01235 321 LPTPQLGVPNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 405 RTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFIDENPDLFEITESKDRGTKLLQFIGDVIVNDN- 483
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNGHp 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 484 --ACKEKPLFDALHDPRMDKDGS-KSEGSKILFDKLGKSAYIEKIKNDKKLLLTDTTMRDAHQSLLATRIRTYDLLKAAK 560
Cdd:TIGR01235 481 eaKDKLKPLENAPRVVVLYADQNpVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIAP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 561 PTEKYQKDLFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMFQMLLRASNGVGYKNYPDNVIEEFTKESARQGID 640
Cdd:TIGR01235 561 TTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGID 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 641 VFRIFDSLNWVENMKPSINTALETGKIVEATMCYTGDILDKTKTKYNLEYYIKMAQELESLGADIIAIKDMSGLLKPYSA 720
Cdd:TIGR01235 641 IFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAAA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 721 YTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALESMAGLTSQPSLNAIVEALKNTERDTGIDLFGYDE 800
Cdd:TIGR01235 721 KLLIKALREKTDLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWIRE 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 801 LGKYYKDLRKVYNKFESDLTNSCAEIYNFEIPGGQYTNLKPQADSLGLVNRFDEVKEKYKEANEVVGDIIKVTPSSKVVG 880
Cdd:TIGR01235 801 LSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSSKVVG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 881 DLAIFMTKNKLDKDNIIEEGKNLSFPDSVVDYCKGMIGQPEGGIPKDLQEVVLKGEEAITVRPGSLLPAEDFDEIAKYLN 960
Cdd:TIGR01235 881 DMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIRKDLQ 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 961 EKYDINANIRNVISYALYPKVYEDYIKHLQHYNDISKLESDVFFYGLNKNEECEVEIEEGKVLTIRLVEIGEVKENGFRT 1040
Cdd:TIGR01235 961 EKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQGERE 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 1041 IGFELNGMVREVEIKDKNFSGKINNVEKADMNDPLQIGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDG 1120
Cdd:TIGR01235 1041 VFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDG 1120
|
1130 1140
....*....|....*....|..
gi 489520803 1121 VIKSIKVKEDDMVEDKQLLMIM 1142
Cdd:TIGR01235 1121 TIKEVLVKAGEQIDAKDLLLVL 1142
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
4-457 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 714.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 4 KFNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGKgPIDAYLDMDGIIDLAKRKKVDAIH 83
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAP-AAESYLNIDAIIAAAKATGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 84 PGYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMIKA 163
Cdd:COG4770 80 PGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 164 SNGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQKII 243
Cdd:COG4770 160 SAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 244 EYAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQGy 323
Cdd:COG4770 240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAG- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 324 sldsEEINIKsQDDVEIRGYSIQCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDGGnGFTGANISPHYDSLLVKTISW 403
Cdd:COG4770 319 ----EPLPFT-QEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSMIAKLIVW 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 489520803 404 DRTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFIDENPD 457
Cdd:COG4770 393 GPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELA 446
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
5-471 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 623.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 5 FNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGKgPIDAYLDMDGIIDLAKRKKVDAIHP 84
Cdd:PRK08654 2 FKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAP-PSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 85 GYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMIKAS 164
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 165 NGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQKIIE 244
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 245 YAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDaNGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQGYS 324
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 325 LDSEeiniksQDDVEIRGYSIQCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDGGNgFTGANISPHYDSLLVKTISWD 404
Cdd:PRK08654 320 LSFK------QEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGV-HMGYEIPPYYDSMISKLIVWG 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489520803 405 RTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFIDENPDLFE-----ITESKDRGTKL 471
Cdd:PRK08654 393 RTREEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILEemkryALEEEEREKTL 464
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
5-455 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 615.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 5 FNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGKGPiDAYLDMDGIIDLAKRKKVDAIHP 84
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSK-KSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 85 GYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMIKAS 164
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 165 NGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQKIIE 244
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 245 YAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQGys 324
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAG-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 325 ldsEEINIKsQDDVEIRGYSIQCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDGGnGFTGANISPHYDSLLVKTISWD 404
Cdd:PRK08591 319 ---EPLSIK-QEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489520803 405 RTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFIDEN 455
Cdd:PRK08591 394 ETREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
5-468 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 569.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 5 FNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGkgPIDAYLDMDGIIDLAKRKKVDAIHP 84
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD--PLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 85 GYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMIKAS 164
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 165 NGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQKIIE 244
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 245 YAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQGYS 324
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 325 LDSEeiniksQDDVEIRGYSIQCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDGGNgFTGANISPHYDSLLVKTISWD 404
Cdd:PRK07178 320 LSYK------QEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAI-YTGYTIPPYYDSMCAKLIVWA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489520803 405 RTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFIDENPDLFEITESKDRG 468
Cdd:PRK07178 393 LTWEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIKRKPE 456
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
5-452 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 558.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 5 FNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGKgPIDAYLDMDGIIDLAKRKKVDAIHP 84
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPR-VQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 85 GYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMIKAS 164
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 165 NGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQKIIE 244
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 245 YAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQGYS 324
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 325 LDSeeinikSQDDVEIRGYSIQCRITTEDPKNkFMPDTGKIQVYRTGSGFGIRLDGGNGfTGANISPHYDSLLVKTISWD 404
Cdd:PRK06111 321 LSF------TQDDIKRSGHAIEVRIYAEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMIAKLIAHG 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 489520803 405 RTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFI 452
Cdd:PRK06111 393 ETREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
5-455 |
4.45e-178 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 529.28 E-value: 4.45e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 5 FNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGKgPIDAYLDMDGIIDLAKRKKVDAIHP 84
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPAS-SKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 85 GYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMIKAS 164
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 165 NGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQKIIE 244
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 245 YAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQGYS 324
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 325 LDseeiniKSQDDVEIRGYSIQCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDgGNGFTGANISPHYDSLLVKTISWD 404
Cdd:PRK05586 321 LS------IKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVD-SAVYSGYTIPPYYDSMIGKLIVYG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489520803 405 RTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFIDEN 455
Cdd:PRK05586 394 KDREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKK 444
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
4-454 |
9.47e-175 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 520.86 E-value: 9.47e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 4 KFNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEgKGPIDAYLDMDGIIDLAKRKKVDAIH 83
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGP-APSAKSYLNIPNIISAAEITGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 84 PGYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMIKA 163
Cdd:TIGR00514 80 PGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 164 SNGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQKII 243
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 244 EYAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQGy 323
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAG- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 324 sldsEEINIKsQDDVEIRGYSIQCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDgGNGFTGANISPHYDSLLVKTISW 403
Cdd:TIGR00514 319 ----EPLSLK-QEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWD-SHVYSGYTVPPYYDSMIGKLITY 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489520803 404 DRTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFIDE 454
Cdd:TIGR00514 393 GKTREVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
529-1143 |
5.91e-173 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 521.71 E-value: 5.91e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 529 KKLLLTDTTMRDAHQSLLATRIRTYDLLKAAkptEKYQK-DLFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMF 607
Cdd:PRK09282 2 KKVKITDTTLRDAHQSLLATRMRTEDMLPIA---EKLDKvGFWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 608 QMLLRASNGVGYKNYPDNVIEEFTKESARQGIDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTgdildkTKTKYN 687
Cdd:PRK09282 79 QMLLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT------TSPVHT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 688 LEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALES 767
Cdd:PRK09282 153 IEKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEVDLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 768 MAGLTSQPSLNAIVEALKNTERDTGIDLFGYDELGKYYKDLRKVYNKFESDLTNSCAEIYNFEIPGGQYTNLKPQADSLG 847
Cdd:PRK09282 233 LAFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTIVDTRVLIHQVPGGMISNLVSQLKEQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 848 LVNRFDEVKEKYKEANEVVGDIIKVTPSSKVVGDLAIFmtknkldkdNIIEEGKNLSFPDSVVDYCKGMIGQPEGGIPKD 927
Cdd:PRK09282 313 ALDKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVL---------NVLTGERYKVITKEVKDYVKGLYGRPPAPINEE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 928 LQEVVLKGEEAITVRPGSLLPAEdFDEI-----AKYLNEKYDinanirnVISYALYPKVYEDYIKHLQHYNDISKLESDV 1002
Cdd:PRK09282 384 LRKKIIGDEEPITCRPADLLEPE-LEKArkeaeELGKSEKED-------VLTYALFPQIAKKFLEEREAGELKPEPEPKE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 1003 F-FYGLNKNEECEVEIEEGKVLTIRlveIGEVKENGFRTIGFELNGMVREVEIKDKNfsgKINNVEKADMNDPLQIGASI 1081
Cdd:PRK09282 456 AaAAGAEGIPTEFKVEVDGEKYEVK---IEGVKAEGKRPFYLRVDGMPEEVVVEPLK---EIVVGGRPRASAPGAVTSPM 529
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489520803 1082 PGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIMK 1143
Cdd:PRK09282 530 PGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-455 |
4.37e-165 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 495.80 E-value: 4.37e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 2 LKKFNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGKGPiDAYLDMDGIIDLAKRKKVDA 81
Cdd:PRK08462 1 KKEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSS-ESYLNIPAIISAAEIFEADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 82 IHPGYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMI 161
Cdd:PRK08462 80 IFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 162 KASNGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQK 241
Cdd:PRK08462 160 KAAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 242 IIEYAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQ 321
Cdd:PRK08462 240 LIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 322 GYSLdseeiniKSQDDVEIRGYSIQCRITTEDPKnKFMPDTGKIQVYRTGSGFGIRLDgGNGFTGANISPHYDSLLVKTI 401
Cdd:PRK08462 320 GEEL-------PSQESIKLKGHAIECRITAEDPK-KFYPSPGKITKWIAPGGRNVRMD-SHAYAGYVVPPYYDSMIGKLI 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 489520803 402 SWDRTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFIDEN 455
Cdd:PRK08462 391 VWGEDRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
533-815 |
2.04e-160 |
|
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: 476.54 E-value: 2.04e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 533 LTDTTMRDAHQSLLATRIRTYDLLKAAKPTEKYQkdLFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMFQMLLR 612
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 613 ASNGVGYKNYPDNVIEEFTKESARQGIDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTGDildktkTKYNLEYYI 692
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 693 KMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALESMAGLT 772
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVGLPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGGT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489520803 773 SQPSLNAIVEALKNTERDTGIDLFGYDELGKYYKDLRKVYNKF 815
Cdd:cd07937 233 SQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
5-463 |
1.10e-157 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 477.77 E-value: 1.10e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 5 FNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGkgPIDAYLDMDGIIDLAKRKKVDAIHP 84
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTD--PIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 85 GYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIR-STEEAKEVANKIGYPVMIKA 163
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSeSMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 164 SNGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQKII 243
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 244 EYAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQGY 323
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 324 SLDSEeiniksQDDVEIRGYSIQCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDgGNGFTGANISPHYDSLLVKTISW 403
Cdd:PRK08463 320 ILDLE------QSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVD-SHIYKDYTIPPYYDSMLAKLIVK 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489520803 404 DRTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFIDEN-PDLFEITE 463
Cdd:PRK08463 393 ATSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHmQELLEKTE 453
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
529-987 |
4.28e-156 |
|
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: 475.92 E-value: 4.28e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 529 KKLLLTDTTMRDAHQSLLATRIRTYDLLKAAkptEKYQK-DLFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMF 607
Cdd:COG5016 2 KKVKITDTTLRDGHQSLFATRMRTEDMLPIA---EKLDEaGFWSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 608 QMLLRASNGVGYKNYPDNVIEEFTKESARQGIDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTgdildkTKTKYN 687
Cdd:COG5016 79 QMLLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYT------ISPVHT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 688 LEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALES 767
Cdd:COG5016 153 VEYYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEALDIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 768 MAGLTSQPSLNAIVEALKNTERDTGIDLFGYDELGKYYKDLRKVYNKFESDLTNSCAEIYNFEIPGGQYTNLKPQADSLG 847
Cdd:COG5016 233 LAGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGVDPRVLVHQVPGGMLSNLVSQLKEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 848 LVNRFDEVKEKYKEANEVVGDIIKVTPSSKVVGDLAIFmtknkldkdNIIEEGKNLSFPDSVVDYCKGMIGQPEGGIPKD 927
Cdd:COG5016 313 ALDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVL---------NVLTGERYKMITKEVKDYVLGYYGKTPAPIDPE 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 928 LQEVVLKGEEAITVRPGSLLPaedfDEIAKYLNEkyDINANIRNVISYALYPKVYEDYIK 987
Cdd:COG5016 384 VRKKALGDEEPITCRPADLLE----PELEKLRKE--GLAKSDEDVLTYALFPQVAIKFLK 437
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-453 |
6.52e-154 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 467.31 E-value: 6.52e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 1 MLKKFNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGKGPiDAYLDMDGIIDLAKRKKVD 80
Cdd:PRK12833 1 MPSRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAA-KSYLNPAAILAAARQCGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 81 AIHPGYGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVM 160
Cdd:PRK12833 80 AIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 161 IKASNGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYgNIVHLYERDCSVQRRHQ 240
Cdd:PRK12833 160 IKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 241 KIIEYAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVD-ANGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILI 319
Cdd:PRK12833 239 KILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 320 AQGYSLDSEeiniksQDDVEIRGYSIQCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDgGNGFTGANISPHYDSLLVK 399
Cdd:PRK12833 319 ADGEPLRFA------QGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVD-SLLYPGYRVPPFYDSLLAK 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 489520803 400 TISWDRTFQGAINKTIRSIKELRVRGVKTNVGFLVNVLNNPIFSNGKCSTKFID 453
Cdd:PRK12833 392 LIVHGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
533-1139 |
2.86e-148 |
|
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: 456.94 E-value: 2.86e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 533 LTDTTMRDAHQSLLATRIRTYDLLKAAKPTEKYqkDLFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMFQMLLR 612
Cdd:TIGR01108 1 ITDVVLRDAHQSLFATRMRTEDMLPIAEKLDDV--GYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 613 ASNGVGYKNYPDNVIEEFTKESARQGIDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTgdildkTKTKYNLEYYI 692
Cdd:TIGR01108 79 GQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT------TSPVHTLETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 693 KMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALESMAGLT 772
Cdd:TIGR01108 153 DLAEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRFGLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 773 SQPSLNAIVEALKNTERDTGIDLFGYDELGKYYKDLRKVYNKFESDLTNSCAEIYNFEIPGGQYTNLKPQADSLGLVNRF 852
Cdd:TIGR01108 233 SHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFEGQLKGPDSRILVAQVPGGMLSNLESQLKEQNALDKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 853 DEVKEKYKEANEVVGDIIKVTPSSKVVGDLAIFmtknkldkdNIIEEGKNLSFPDSVVDYCKGMIGQPEGGIPKDLQEVV 932
Cdd:TIGR01108 313 DEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVL---------NVLTGERYKTITKETKGYLKGEYGRTPAPINAELQRKI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 933 LKGEEAI-TVRPGSLLPAEdFDEIAKYLNEKYDINANIRNVISYALYPKVYEDYIKHlqhyndisklesdvffyglNKNE 1011
Cdd:TIGR01108 384 LGDEKPIvDCRPADLLEPE-LDKLRAEVREAGAEKNSIEDVLTYALFPQVGLKFLEN-------------------RHNP 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 1012 ECEVEIEEGKVLTIRLVEI--GEVKENGFRTIGFELNGMVREVEIKDKNF---------SGKINNVEKADMNDPLQIGAS 1080
Cdd:TIGR01108 444 AAFEPKPEEKVIEQEHAQVvgKYEETHASGSYTVEVEGKAFVVKVSPGGDvsqitasapANTSGGTVAAKAGAGTPVTAP 523
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 489520803 1081 IPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLL 1139
Cdd:TIGR01108 524 IAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAVSVGQVL 582
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
529-1140 |
3.94e-132 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 415.10 E-value: 3.94e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 529 KKLLLTDTTMRDAHQSLLATRIRTYDLLKAAkptEKYQKDLF-SLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMF 607
Cdd:PRK14040 3 KPLAITDVVLRDAHQSLFATRLRLDDMLPIA---AKLDKVGYwSLESWGGATFDACIRFLGEDPWERLRELKKAMPNTPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 608 QMLLRASNGVGYKNYPDNVIEEFTKESARQGIDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTgdildkTKTKYN 687
Cdd:PRK14040 80 QMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT------TSPVHT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 688 LEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALES 767
Cdd:PRK14040 154 LQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRVDVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAISS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 768 MAGLTSQPSLNAIVEALKNTERDTGIDLFGYDELGKYYKDLRKVYNKFESDLTNSCAEIYNFEIPGGQYTNLKPQADSLG 847
Cdd:PRK14040 234 MSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNMESQLKEQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 848 LVNRFDEVKEKYKEANEVVGDIIKVTPSSKVVGDLAIFmtknkldkdNII--EEGKNLSFPDSVVdyCKGMIGQPEGGIP 925
Cdd:PRK14040 314 AADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQAVL---------NVLtgERYKTITKETAGV--LKGEYGATPAPVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 926 KDLQEVVLKGEEAITVRPGSLLPAE------DFDEIAKYLNEKYDINAnIRNVISYALYPKVyedYIKHLQHYNDISKLE 999
Cdd:PRK14040 383 AELQARVLEGAEPITCRPADLLAPEldkleaELRRQAQEKGITLAENA-IDDVLTYALFPQI---GLKFLENRHNPAAFE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 1000 SdvffyglnkneeceveieegkVLTIRLVE-IGEVKENGFRTIGFELNGMVREVEIKDknfSGKINNVEKADMNDPLQ-- 1076
Cdd:PRK14040 459 P---------------------VPQAEAAQpAAKAEPAGSETYTVEVEGKAYVVKVSE---GGDISQITPAAPAAAPAaa 514
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489520803 1077 ------------IGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLM 1140
Cdd:PRK14040 515 aaaapaaaagepVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
529-987 |
3.02e-125 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 391.76 E-value: 3.02e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 529 KKLLLTDTTMRDAHQSLLATRIRTYDLLKAAKPTEK--YqkdlFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIM 606
Cdd:PRK12331 2 TKIKITETVLRDGQQSLIATRMTTEEMLPILEKLDNagY----HSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 607 FQMLLRASNGVGYKNYPDNVIEEFTKESARQGIDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTgdildkTKTKY 686
Cdd:PRK12331 78 LQMLLRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT------TSPVH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 687 NLEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALE 766
Cdd:PRK12331 152 TIDYFVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAVTVPLEVHTHATSGIAEMTYLKAIEAGADIIDTAIS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 767 SMAGLTSQPSLNAIVEALKNTERDTGIDLFGYDELGKYYKDLRKVYNKfESDL------TNSCAEIYnfEIPGGQYTNLK 840
Cdd:PRK12331 232 PFAGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYRE-EGILnpkvkdVEPKTLIY--QVPGGMLSNLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 841 PQADSLGLVNRFDEVKEKYKEANEVVGDIIKVTPSSKVVGDLAIFmtknkldkdNIIEEGKNLSFPDSVVDYCKGMIGQP 920
Cdd:PRK12331 309 SQLKEQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALM---------NVISGERYKMVPNEIKDYVRGLYGRP 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 921 EGGIPKDLQEVVLKGEEAITVRPGSLLPAE--DF-DEIAKYLNEKYDinanirnVISYALYPKVYEDYIK 987
Cdd:PRK12331 380 PAPIAEEIKKKIIGDEEVITCRPADLIEPQleKLrEEIAEYAESEED-------VLSYALFPQQAKDFLG 442
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
530-1140 |
9.58e-108 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 350.18 E-value: 9.58e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 530 KLLLTDTTMRDAHQSLLATRIRTYDLLKAAKPTEKYqkDLFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMFQM 609
Cdd:PRK14042 3 KTFITDVTLRDAHQCLIATRMRTEDMLPICNKMDDV--GFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 610 LLRASNGVGYKNYPDNVIEEFTKESARQGIDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTgdildkTKTKYNLE 689
Cdd:PRK14042 81 LLRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT------TSPVHTLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 690 YYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALESMA 769
Cdd:PRK14042 155 NFLELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 770 GLTSQPSLNAIVEALKNTERDTGIDLFGYDELGKYYKDLRKVYNKFESDLTNSCAEIYNFEIPGGQYTNLKPQADSLGLV 849
Cdd:PRK14042 235 GGASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 850 NRFDEVKEKYKEANEVVGDIIKVTPSSKVVGDLAIFmtknkldkdNIIEEGKNLSFPDSVVDYCKGMIGQPEGGIPKDLQ 929
Cdd:PRK14042 315 DKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQAVI---------NVLTGERYKTITNEVKLYCQGKYGTPPGKISSALR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 930 EVVLKGEEAITVRPGSLLPaedfDEIAKYLNEKYDINANIRNVISYALYPKVYEDYIKHLQHYNDISKLESDVFFYGLNK 1009
Cdd:PRK14042 386 KKAIGRTEVIEVRPGDLLP----NELDQLQNEISDLALSDEDVLLYAMFPEIGRQFLEQRKNNQLIPEPLLTQSSAPDNS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 1010 NEECEVEIEEGKVLTIRLVEIGEVkENGFRTIGFELNGMVREVEIKDKNFSGKInnvEKADMND---PLQIGASIPGKVI 1086
Cdd:PRK14042 462 VMSEFDIILHGESYHVKVAGYGMI-EHGQQSCFLWVDGVPEEVVVQHSELHDKI---ERSSVNNkigPGDITVAIPGSII 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 489520803 1087 KIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLM 1140
Cdd:PRK14042 538 AIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLI 591
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
529-987 |
1.15e-102 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 332.13 E-value: 1.15e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 529 KKLLLTDTTMRDAHQSLLATRIRTYDLLKAAKPTEkyQKDLFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMFQ 608
Cdd:PRK14041 1 MKVMFVDTTLRDGHQSLIATRMRTEDMLPALEAFD--RMGFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 609 MLLRASNGVGYKNYPDNVIEEFTKESARQGIDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTgdildkTKTKYNL 688
Cdd:PRK14041 79 MLLRGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT------VSPVHTL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 689 EYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALESM 768
Cdd:PRK14041 153 EYYLEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKFGVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 769 AGLTSQPSLNAIVEALKNTERDTGIDLFGYDELGKYYKDLRKVYNKFESDLTNSCAEIYNFEIPGGQYTNLKPQADSLGL 848
Cdd:PRK14041 233 SMGTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYDVGMKSPDSRILVSQIPGGMYSNLVKQLKEQKM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 849 VNRFDEVKEKYKEANEVVGDIIKVTPSSKVVGDLAIFmtknkldkdNIIEEGKNLSFPDSVVDYCKGMIGQPEGGIPKDL 928
Cdd:PRK14041 313 LHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQAVL---------NVLTGERYKRVTNETKNYVKGLYGRPPAPIDEEL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 489520803 929 QEVVLKGEEAITVRPGSLLPAedfdEIAKYLNEKYDINANIRNVISYALYPKVYEDYIK 987
Cdd:PRK14041 384 MKKILGDEKPIDCRPADLLEP----ELEKARKELGILAETDEDLLIYVILGEVGKKFLK 438
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
528-988 |
9.14e-91 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 300.91 E-value: 9.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 528 DKKLLLTDTTMRDAHQSLLATRIRTYDLLKAAKPTEkyQKDLFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMF 607
Cdd:PRK12330 2 PRKIGVTELALRDAHQSLMATRMAMEDMVGACEDID--NAGYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 608 QMLLRASNGVGYKNYPDNVIEEFTKESARQGIDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTGDILdktktkYN 687
Cdd:PRK12330 80 QMLLRGQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYTVSPI------HT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 688 LEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNV--KAPIHLHTHDTSGNGVATCLMASEAGVDIIDAAL 765
Cdd:PRK12330 154 VEGFVEQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgeDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 766 ESMA-GLTSQPSlNAIVEALKNTERDTGIDLFGYDELGKYYKDLRKVYNKFESDLTNSCAEIYNFEIPGGQYTNLKPQAD 844
Cdd:PRK12330 234 SSMSlGPGHNPT-ESLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTTGVETEIFKSQIPGGMLSNMESQLK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 845 SLGLVNRFDEVKEKYKEANEVVGDIIKVTPSSKVVGDLAIFmtknkldkDNIIEEGKNLS--FPDSVVDYCKGMIGqpeg 922
Cdd:PRK12330 313 QQGAGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVF--------NVLMGRYKVLTgeFADLMLGYYGETPG---- 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489520803 923 giPKDlQEVVLK-----GEEAITVRPGSLLPAEdFDEIAKYLNEKYDINANIRNVISYALYPKVYEDYIKH 988
Cdd:PRK12330 381 --ERN-PEVVEQakkqaKKEPITCRPADLLEPE-WDKLRAEALALEGCDGSDEDVLTYALFPQVAPKFFAT 447
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
826-1026 |
1.67e-89 |
|
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: 286.27 E-value: 1.67e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 826 IYNFEIPGGQYTNLKPQADSLGLVNRFDEVKEKYKEANEVVGDIIKVTPSSKVVGDLAIFMTKNKLDKDNIIEEGKNLSF 905
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 906 PDSVVDYCKGMIGQPEGGIPKDLQEVVLKGEEAITVRPGSLLPAEDFDEIAKYLNEKYDINANIRNVISYALYPKVYEDY 985
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489520803 986 IKHLQHYNDISKLESDVFFYGLNKNEECEVEIEEGKVLTIR 1026
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
119-326 |
5.31e-85 |
|
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: 274.18 E-value: 5.31e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 119 DKINSKKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMIKASNGGGGRGMRIVHREEDLELEYETACSESRKAFGE 198
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 199 DIIFIEKYIADPKHIEVQILGDNYGNIVHLYERDCSVQRRHQKIIEYAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTL 278
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489520803 279 EFLVDA-NGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQGYSLD 326
Cdd:pfam02786 161 EFALDPfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
529-1000 |
8.23e-74 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 253.12 E-value: 8.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 529 KKLLLTDTTMRDAHQSLLATRIRTYDLLKAAKPTEKYqkDLFSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMFQ 608
Cdd:PRK12581 11 QQVAITETVLRDGHQSLMATRLSIEDMLPVLTILDKI--GYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRLQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 609 MLLRASNGVGYKNYPDNVIEEFTKESARQGIDVFRIFDSLNWVENMKPSINTALETGKIVEATMCYTgdildkTKTKYNL 688
Cdd:PRK12581 89 MLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT------TSPVHTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 689 EYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDAALESM 768
Cdd:PRK12581 163 NYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIKAMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALSPF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 769 AGLTSQPSLNAIVEALKNTERDTGIDLFGYDELGKYYKDLRKVY---NKFESDLTNSCAEIYNFEIPGGQYTNLKPQADS 845
Cdd:PRK12581 243 SEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYladGILDPSLLFPDPRTLQYQVPGGMLSNMLSQLKQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 846 LGLVNRFDEVKEKYKEANEVVGDIIKVTPSSKVVGDLAIFmtknkldkdNIIEEGKNLSFPDSVVDYCKGMIGQPEGGIP 925
Cdd:PRK12581 323 ANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAM---------NVILGKPYQMVSKEIKQYLAGDYGKTPAPVN 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489520803 926 KDLQEVVLKGEEAITVRPGSLLPAEdfDEIAKylNEKYDINANIRNVISYALYPKVYEDYIKHLQHYNDISKLES 1000
Cdd:PRK12581 394 EDLKRSQIGSAPVTTNRPADQLSPE--FEVLK--AEVADLAQTDEDVLTYALFPSVAKPFLTTKYQTDDVIKVTA 464
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
534-804 |
1.08e-69 |
|
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: 233.89 E-value: 1.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 534 TDTTMRDAHQSLLATRiRTYDLLKAAKPTEKYqkDLFSLEMWGGATYDVAyrFLKESPWRRLQKLREEIPSIMFQMLLRA 613
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEA--GVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 614 SngvgyknypdnviEEFTKESARQGIDVFRIFDSLN--------------WVENMKPSINTALETGKIVEATMCYTGDIl 679
Cdd:cd03174 76 R-------------EKGIERALEAGVDEVRIFDSASethsrknlnksreeDLENAEEAIEAAKEAGLEVEGSLEDAFGC- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 680 dktktKYNLEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKA-PIHLHTHDTSGNGVATCLMASEAGV 758
Cdd:cd03174 142 -----KTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDvPLGLHTHNTLGLAVANSLAALEAGA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489520803 759 DIIDAALESMAGLTSQPSLNAIVEALKNTERDTGIDLFGYDELGKY 804
Cdd:cd03174 217 DRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRY 262
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
66-322 |
9.58e-62 |
|
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: 211.65 E-value: 9.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 66 DMDGIID----LAKRKKVDAIhpgygfLAENAE----FARKCEENGITfiGPSSKVMNMMGDKINSKKIAKEVNVQTIPG 137
Cdd:COG0439 1 DIDAIIAaaaeLARETGIDAV------LSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 138 VekAIRSTEEAKEVANKIGYPVMIKASNGGGGRGMRIVHREEDLELEYETACSESRKAFGEDIIFIEKYIADPkHIEVQI 217
Cdd:COG0439 73 A--LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGR-EYSVEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 218 LGDNyGNIVHlyerdCSVQRRHQK---IIEY---APAfSLDDKVRKEICEDAVKLSKHVGYSN-AGTLEFLVDANGGHYF 290
Cdd:COG0439 150 LVRD-GEVVV-----CSITRKHQKppyFVELgheAPS-PLPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYL 222
|
250 260 270
....*....|....*....|....*....|....
gi 489520803 291 IEMNTRVQVEH--TVTEMVTGIDIVQSQILIAQG 322
Cdd:COG0439 223 IEINARLGGEHipPLTELATGVDLVREQIRLALG 256
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
5-113 |
1.25e-57 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 193.47 E-value: 1.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 5 FNKILVANRGEIAIRIFRACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGKgPIDAYLDMDGIIDLAKRKKVDAIHP 84
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGP-ASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*....
gi 489520803 85 GYGFLAENAEFARKCEENGITFIGPSSKV 113
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
346-453 |
1.61e-44 |
|
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: 156.03 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 346 QCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDGGNgFTGANISPHYDSLLVKTISWDRTFQGAINKTIRSIKELRVRG 425
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGV-YEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 489520803 426 VKTNVGFLVNVLNNPIFSNGKCSTKFID 453
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
346-454 |
6.49e-39 |
|
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: 140.32 E-value: 6.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 346 QCRITTEDPKNKFMPDTGKIQVYRTGSGFGIRLDGGnGFTGANISPHYDSLLVKTISWDRTFQGAINKTIRSIKELRVRG 425
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 489520803 426 VKTNVGFLVNVLNNPIFSNGKCSTKFIDE 454
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
530-795 |
3.06e-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: 115.13 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 530 KLLLTDTTMRDAHQSLlATRIRTYDLLKAAKptekyqkdlfSLEMWGGATYDVAYRFLKESPWRRLQKLREEIPSIMFQM 609
Cdd:pfam00682 1 AVAICDTTLRDGEQAL-GVAFSIDEKLAIAR----------ALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 610 LLRASngvgyknypDNVIEEFTKESARQGIDVFRIFDS---LNWVENMKPSINTALE-TGKIVEA----TMCYTGDILDK 681
Cdd:pfam00682 70 LCRAR---------EHDIKAAVEALKGAGAVRVHVFIAtsdLHRKYKLGKDREEVAKrAVAAVKAarsrGIDVEFSPEDA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 682 TKTkyNLEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNV--KAPIHLHTHDTSGNGVATCLMASEAGVD 759
Cdd:pfam00682 141 SRT--DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVpnKAIISVHCHNDLGMAVANSLAAVEAGAD 218
|
250 260 270
....*....|....*....|....*....|....*.
gi 489520803 760 IIDAALESMAGLTSQPSLNAIVEALKNTERDTGIDL 795
Cdd:pfam00682 219 RVDGTVNGIGERAGNAALEEVAAALEGLGVDTGLDL 254
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1076-1142 |
6.52e-25 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 98.64 E-value: 6.52e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489520803 1076 QIGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIM 1142
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
96-326 |
3.48e-19 |
|
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: 92.63 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 96 ARKCEEN----GITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGveKAIRSTEEAKEVANKIGYPVMIKASNGGGGRG 171
Cdd:COG0458 87 AVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKS--GTATSVEEALAIAEEIGYPVIVRPSYVLGGRG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 172 MRIVHREEDLElEYetaCSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYGNIVHLyerdCsvqrrhqkIIEY------ 245
Cdd:COG0458 165 MGIVYNEEELE-EY---LERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----G--------IMEHiepagv 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 246 --------APAFSLDDKVRKEICEDAVKLSKH---VGYSNagtLEFLVDaNGGHYFIEMNTRvqVEHTVTEM--VTGIDI 312
Cdd:COG0458 229 hsgdsicvAPPQTLSDKEYQRLRDATLKIARAlgvVGLCN---IQFAVD-DGRVYVIEVNPR--ASRSSPFAskATGYPI 302
|
250
....*....|....
gi 489520803 313 VQSQILIAQGYSLD 326
Cdd:COG0458 303 AKIAAKLALGYTLD 316
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
96-325 |
6.14e-18 |
|
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: 89.67 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 96 ARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGveKAIRSTEEAKEVANKIGYPVMIKASNGGGGRGMRIV 175
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 176 HREEDLELEYETACSESrkafGEDIIFIEKYIADPKHIEVQILGDN-----YGNIVHlyerdcsvqrrhqkiIEYA---- 246
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVS----PEHPVLIDKYLEDAVEVDVDAVSDGeevliPGIMEH---------------IEEAgvhs 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 247 -------PAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDaNGGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILI 319
Cdd:TIGR01369 785 gdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRV 863
|
....*.
gi 489520803 320 AQGYSL 325
Cdd:TIGR01369 864 MLGKKL 869
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
48-296 |
9.12e-17 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 83.01 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 48 ADESYLIGEGKGPidAYLDMdgIIDLAKRKKVDAIHPGY----GFLAENAEfarKCEENGITFIGPSSKVMNMMGDKINS 123
Cdd:PRK12767 43 ADKFYVVPKVTDP--NYIDR--LLDICKKEKIDLLIPLIdpelPLLAQNRD---RFEEIGVKVLVSSKEVIEICNDKWLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 124 KKIAKEVNVQTIPGVEKAIRSTEEAKEVANKIGYPVMIKASNGGGGRGMRIVHREEDLELEYEtacsesrkaFGEDIIfI 203
Cdd:PRK12767 116 YEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLE---------YVPNLI-I 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 204 EKYIADPKhIEVQILGDNYGNIVHlyerdcSVQRRHQKII--EYAPAFSLDDKVRKEICEDAVKLSKHVGYSNagtLEFL 281
Cdd:PRK12767 186 QEFIEGQE-YTVDVLCDLNGEVIS------IVPRKRIEVRagETSKGVTVKDPELFKLAERLAEALGARGPLN---IQCF 255
|
250
....*....|....*
gi 489520803 282 VDaNGGHYFIEMNTR 296
Cdd:PRK12767 256 VT-DGEPYLFEINPR 269
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1077-1140 |
1.37e-16 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 77.98 E-value: 1.37e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489520803 1077 IGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLM 1140
Cdd:PRK05641 87 VTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
100-325 |
2.72e-16 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 84.64 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 100 EENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGvEKAiRSTEEAKEVANKIGYPVMIKASNGGGGRGMRIVHREE 179
Cdd:PRK12815 651 EEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG-LTA-TDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEP 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 180 DLELEYETACSesrkafGEDIIFIEKYIaDPKHIEVQILGDnyGNIVHLyerdcsvqrrhQKIIE------------YA- 246
Cdd:PRK12815 729 ALEAYLAENAS------QLYPILIDQFI-DGKEYEVDAISD--GEDVTI-----------PGIIEhieqagvhsgdsIAv 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 247 -PAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVdANGGHYFIEMNTRVQveHTV--TEMVTGIDIVQSQILIAQGY 323
Cdd:PRK12815 789 lPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVLEVNPRAS--RTVpfVSKATGVPLAKLATKVLLGK 865
|
..
gi 489520803 324 SL 325
Cdd:PRK12815 866 SL 867
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
22-297 |
6.75e-16 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 81.13 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 22 RACSELGIKSVGIYSKEDKYGLFRTKADESYLIGEGKGPIDAYLDmdGIIDLAKRKKVDAIHPGY----GFLAENAEFAR 97
Cdd:COG3919 22 RSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGDDPEAFVD--ALLELAERHGPDVLIPTGdeyvELLSRHRDELE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 98 KceenGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVekAIRSTEEAKEVANKIGYPVMIKASNG--------GGG 169
Cdd:COG3919 100 E----HYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTV--VLDSADDLDALAEDLGFPVVVKPADSvgydelsfPGK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 170 RGMRIVHREEDLELEYETAcsesrKAFGEDIIfIEKYIADPKHIEVQILG--DNYGNIVHLYErdcsvqrrHQKIIEYAP 247
Cdd:COG3919 174 KKVFYVDDREELLALLRRI-----AAAGYELI-VQEYIPGDDGEMRGLTAyvDRDGEVVATFT--------GRKLRHYPP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489520803 248 AF-------SLDDKvrkEICEDAVKLSKHVGYSNAGTLEFLVDA-NGGHYFIEMNTRV 297
Cdd:COG3919 240 AGgnsaareSVDDP---ELEEAARRLLEALGYHGFANVEFKRDPrDGEYKLIEINPRF 294
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1076-1142 |
7.34e-16 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 73.40 E-value: 7.34e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489520803 1076 QIGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIM 1142
Cdd:pfam00364 7 MIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
64-295 |
1.49e-15 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 78.61 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 64 YLDMDGIIDLAKRKKVD----AIHPGYGflaENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVe 139
Cdd:COG1181 39 GIDVEDLPAALKELKPDvvfpALHGRGG---EDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYV- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 140 kAIRSTE--EAKEVANKIGYPVMIKASNGGGGRGMRIVHREEDLeleyETACSESRKaFGEDIIfIEKYIaDPKHIEVQI 217
Cdd:COG1181 115 -VLRRGElaDLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEEL----AAALEEAFK-YDDKVL-VEEFI-DGREVTVGV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 218 LGDnyGNIVHL-----------------YERDcsvqrrhqKIIEYAPAfSLDDKVRKEICEDAVKLSKHVGYSNAGTLEF 280
Cdd:COG1181 187 LGN--GGPRALppieivpengfydyeakYTDG--------GTEYICPA-RLPEELEERIQELALKAFRALGCRGYARVDF 255
|
250
....*....|....*
gi 489520803 281 LVDANGGHYFIEMNT 295
Cdd:COG1181 256 RLDEDGEPYLLEVNT 270
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
48-326 |
2.10e-15 |
|
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: 81.58 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 48 ADESYLIgegkgPIDAYLdMDGIIdlaKRKKVDAIHPGYG-----FLAENAEFARKCEENGITFIGPSSKVMNMMGDKIN 122
Cdd:TIGR01369 60 ADKVYIE-----PLTPEA-VEKII---EKERPDAILPTFGgqtalNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDREL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 123 SKKIAKEVNVQTIPGveKAIRSTEEAKEVANKIGYPVMIKASNGGGGRGMRIVHREEDLELEYETACSESRKafgeDIIF 202
Cdd:TIGR01369 131 FREAMKEIGEPVPES--EIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 203 IEKYIADPKHIEVQILGDNYGNI-------------VHLYERdcsvqrrhqkiIEYAPAFSLDDKVRKEICEDAVKLSKH 269
Cdd:TIGR01369 205 VEKSLAGWKEIEYEVMRDSNDNCitvcnmenfdpmgVHTGDS-----------IVVAPSQTLTDKEYQMLRDASIKIIRE 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489520803 270 VGYSNAGTLEFLVDANGGHYF-IEMNTRVQVEHTVTEMVTGIDIVQSQILIAQGYSLD 326
Cdd:TIGR01369 274 LGIEGGCNVQFALNPDSGRYYvIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTLD 331
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1077-1143 |
1.13e-13 |
|
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: 69.15 E-value: 1.13e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489520803 1077 IGASIPGKV-------IKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIMK 1143
Cdd:COG0511 63 VKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
96-296 |
3.84e-13 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 74.36 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 96 ARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGveKAIRSTEEAKEVANKIGYPVMIKASNGGGGRGMRIV 175
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 176 HREEDLElEYETacsESRKAFGEDIIFIEKYIADPKHIEVQILGDnyGNIVHL---YErdcsvqrrHqkiIEYA------ 246
Cdd:PRK05294 724 YDEEELE-RYMR---EAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GEDVLIggiME--------H---IEEAgvhsgd 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489520803 247 -----PAFSLDDKVRKEICEDAVKLSKH---VGYSNagtLEFLVdANGGHYFIEMNTR 296
Cdd:PRK05294 787 sacslPPQTLSEEIIEEIREYTKKLALElnvVGLMN---VQFAV-KDDEVYVIEVNPR 840
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
119-295 |
5.23e-13 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 71.30 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 119 DKINSKKIAKEVNVQTIPGVekAIRSTEEAKEVANKIGYPVMIKASNGGGGRGMRIVHREEDLELEYETAcsesrKAFGE 198
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWI--VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELA-----FKYDD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 199 DIIfIEKYIADPKhIEVQILGD-------------NYGnivhlYErdcsvqrrhQKiieYAPAFS-------LDDKVRKE 258
Cdd:PRK01372 171 EVL-VEKYIKGRE-LTVAVLGGkalpvieivpageFYD-----YE---------AK---YLAGGTqyicpagLPAEIEAE 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 489520803 259 ICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNT 295
Cdd:PRK01372 232 LQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1076-1142 |
2.08e-12 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 63.27 E-value: 2.08e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489520803 1076 QIGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIM 1142
Cdd:PRK08225 3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEI 69
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
126-296 |
2.17e-12 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 71.73 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 126 IAKEVNVQTIPGveKAIRSTEEAKEVANKIGYPVMIKASNGGGGRGMRIVHREEDLELEYETACsesrKAFGEDIIFIEK 205
Cdd:PLN02735 709 ILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAV----EVDPERPVLVDK 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 206 YIADPKHIEVQILGDNYGNIV-------------HLYERDCSVqrrhqkiieyaPAFSLDDKVRKEICEDAVKLSKHVGY 272
Cdd:PLN02735 783 YLSDATEIDVDALADSEGNVViggimehieqagvHSGDSACSL-----------PTQTIPSSCLATIRDWTTKLAKRLNV 851
|
170 180
....*....|....*....|....
gi 489520803 273 SNAGTLEFLVDANGGHYFIEMNTR 296
Cdd:PLN02735 852 CGLMNCQYAITPSGEVYIIEANPR 875
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1077-1127 |
1.04e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 63.29 E-value: 1.04e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489520803 1077 IGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKV 1127
Cdd:PRK06549 64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHV 114
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
647-766 |
2.73e-11 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 66.74 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 647 SLNWV-ENMKPSINTALETGKIVeatmCYTGDilDKTKTkyNLEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVK 725
Cdd:PRK11858 110 TREEVlERMVEAVEYAKDHGLYV----SFSAE--DASRT--DLDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVK 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489520803 726 ELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIID------------AALE 766
Cdd:PRK11858 182 ELVEAVDIPIEVHCHNDFGMATANALAGIEAGAKQVHttvnglgeragnAALE 234
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
146-295 |
1.62e-10 |
|
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: 61.95 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 146 EEAKEVANKIGYPVMIKASNGGGGRGMRIVHREEDLELEYETACSESRKafgediIFIEKYIaDPKHIEVQILGDNYGNI 225
Cdd:pfam07478 26 EWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEK------VLVEEGI-EGREIECAVLGNEDPEV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489520803 226 VHLYER--DCSVQRRHQKIIEYA-----PAfSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNT 295
Cdd:pfam07478 99 SPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
684-769 |
3.07e-10 |
|
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439889 [Multi-domain] Cd Length: 452 Bit Score: 64.03 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 684 TKYNLEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNV-KAPIHLHTHDTSGNGVATCLMASEAGVDIID 762
Cdd:COG0119 143 TRTDPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVpDVILSVHCHNDLGLAVANSLAAVEAGADQVE 222
|
90
....*....|....*....
gi 489520803 763 ------------AALESMA 769
Cdd:COG0119 223 gtingigeragnAALEEVV 241
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
19-314 |
3.09e-10 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 62.65 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 19 RIFRACSELGIKsvgiyskedkygLFRTKADESYLIGEGKGPIDAYL---DMDGIIDlakRKkvDAIHPGYGFLaenaef 95
Cdd:COG0189 18 ALIEAAQRRGHE------------VEVIDPDDLTLDLGRAPELYRGEdlsEFDAVLP---RI--DPPFYGLALL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 96 aRKCEENGITFIGPSSKVMNMmGDKINSKKIAKEVNVQTIPGVekAIRSTEEAKEVANKIGYPVMIKASNGGGGRGMRIV 175
Cdd:COG0189 75 -RQLEAAGVPVVNDPEAIRRA-RDKLFTLQLLARAGIPVPPTL--VTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 176 HREEDLELEYETacsesRKAFGEDIIFIEKYIADPKHIEVQI--LGdnyGNIVHLYER-----DCSVQRRHQKIIEyapA 248
Cdd:COG0189 151 EDEDALESILEA-----LTELGSEPVLVQEFIPEEDGRDIRVlvVG---GEPVAAIRRipaegEFRTNLARGGRAE---P 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489520803 249 FSLDDKVRkeicEDAVKLSKHVGYSNAGtLEFLVDaNGGHYFIEMNTRVQVEHtvTEMVTGIDIVQ 314
Cdd:COG0189 220 VELTDEER----ELALRAAPALGLDFAG-VDLIED-DDGPLVLEVNVTPGFRG--LERATGVDIAE 277
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
75-326 |
1.01e-09 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 63.06 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 75 KRKKVDAIHPGYGflAENA-EFARKCEENGI------TFIGPSSKVMNMMGDKINSKKIAKEVNVQTiPGVEKAiRSTEE 147
Cdd:PRK12815 79 AREKPDALLATLG--GQTAlNLAVKLHEDGIleqygvELLGTNIEAIQKGEDRERFRALMKELGEPV-PESEIV-TSVEE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 148 AKEVANKIGYPVMIKASNGGGGRGMRIVHREEDLELEYETACSESrkAFGEdiIFIEKYIADPKHIEVQILGDNYGNIVH 227
Cdd:PRK12815 155 ALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQAS--PIHQ--CLLEESIAGWKEIEYEVMRDRNGNCIT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 228 LyerdCSVqrrhQKI----------IEYAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYF-IEMNTR 296
Cdd:PRK12815 231 V----CNM----ENIdpvgihtgdsIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYlIEVNPR 302
|
250 260 270
....*....|....*....|....*....|
gi 489520803 297 VQVEHTVTEMVTGIDIVQSQILIAQGYSLD 326
Cdd:PRK12815 303 VSRSSALASKATGYPIAKIAAKLAVGYTLN 332
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
75-326 |
2.49e-09 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 61.72 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 75 KRKKVDAIHPGYG---------FLAENAEFARKceenGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPgveKAIRST 145
Cdd:PLN02735 95 AKERPDALLPTMGgqtalnlavALAESGILEKY----GVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP---SGIATT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 146 -EEAKEVANKIG-YPVMIKASNGGGGRGMRIVHREEdlelEYETACSESRKAFGEDIIFIEKYIADPKHIEVQILGDNYG 223
Cdd:PLN02735 168 lDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKE----EFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLAD 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 224 NIVHLyerdCSVQR------RHQKIIEYAPAFSLDDKVRKEICEDAVKLSKHVGYSNAGT-LEFLVD-ANGGHYFIEMNT 295
Cdd:PLN02735 244 NVVII----CSIENidpmgvHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSnVQFAVNpVDGEVMIIEMNP 319
|
250 260 270
....*....|....*....|....*....|.
gi 489520803 296 RVQVEHTVTEMVTGIDIVQSQILIAQGYSLD 326
Cdd:PLN02735 320 RVSRSSALASKATGFPIAKMAAKLSVGYTLD 350
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
695-797 |
3.83e-09 |
|
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF ) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163681 Cd Length: 263 Bit Score: 59.05 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 695 AQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVK-APIHLHTHDTSGNGVATCLMASEAGVDIIDAALESM---AG 770
Cdd:cd07943 147 AKLMESYGADCVYVTDSAGAMLPDDVRERVRALREALDpTPVGFHGHNNLGLAVANSLAAVEAGATRIDGSLAGLgagAG 226
|
90 100
....*....|....*....|....*..
gi 489520803 771 LTsqpSLNAIVEALKNTERDTGIDLFG 797
Cdd:cd07943 227 NT---PLEVLVAVLERMGIETGIDLYK 250
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1076-1142 |
4.99e-09 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 53.95 E-value: 4.99e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489520803 1076 QIGASIP-GKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIM 1142
Cdd:cd06849 7 DLGESMTeGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1076-1142 |
5.92e-09 |
|
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: 53.53 E-value: 5.92e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 1076 QIGASI-PGKVIKIMVKEEDEVKANQPLIVIEAMK--MEtiIVAKTDGVIKSIKVKEDDMVEDKQLLMIM 1142
Cdd:COG0508 9 DLGESMtEGTIVEWLVKEGDTVKEGDPLAEVETDKatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1077-1143 |
6.87e-09 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 59.84 E-value: 6.87e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489520803 1077 IGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIMK 1143
Cdd:PRK11855 127 IGEITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
32-295 |
7.35e-09 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 58.98 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 32 VGIyskeDKYGLFRTKADESYLIgegKGPIDAYLDMDGIIDLAKRK-KVDA----IHpgyGFLAEN------AEFArkce 100
Cdd:PRK01966 41 IGI----TKDGRWYLIDADNMEL---ADDDNDKEDLSLLILPSGGSeEVDVvfpvLH---GPPGEDgtiqglLELL---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 101 enGITFIGP---SSkVMNMmgDKINSKKIAKEVNVQTIPGVekAIRSTEEAK----EVANKIGYPVMIKASNGGGGRGMR 173
Cdd:PRK01966 107 --GIPYVGCgvlAS-ALSM--DKILTKRLLAAAGIPVAPYV--VLTRGDWEEaslaEIEAKLGLPVFVKPANLGSSVGIS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 174 IVHREEDLELEYETACSESRKafgediIFIEKYIaDPKHIEVQILGDNY-----GNIVHL---------YERDCSvqrrh 239
Cdd:PRK01966 180 KVKNEEELAAALDLAFEYDRK------VLVEQGI-KGREIECAVLGNDPkasvpGEIVKPddfydyeakYLDGSA----- 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489520803 240 QKIIeyaPAfSLDDKVRKEICEDAVKLSKHVGysnAGTL---EFLVDANGGHYFIEMNT 295
Cdd:PRK01966 248 ELII---PA-DLSEELTEKIRELAIKAFKALG---CSGLarvDFFLTEDGEIYLNEINT 299
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
119-207 |
1.59e-08 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 59.01 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 119 DKINSKKIAKEVNVQTIPGveKAIRSTEEAKEVANKIGYPVMIKASNGGGGRGMRI-VHREEDLELEYETACSESRkafg 197
Cdd:PRK14016 214 DKELTKRLLAAAGVPVPEG--RVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESS---- 287
|
90
....*....|
gi 489520803 198 eDIIfIEKYI 207
Cdd:PRK14016 288 -DVI-VERYI 295
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
688-795 |
2.28e-08 |
|
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163678 Cd Length: 268 Bit Score: 56.69 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 688 LEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVK---APIHLHTHDTSGNGVATCLMASEAGVDIIDAA 764
Cdd:cd07940 142 LDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPnikVPISVHCHNDLGLAVANSLAAVEAGARQVECT 221
|
90 100 110
....*....|....*....|....*....|....*...
gi 489520803 765 LESM---AGLTsqpSLNAIVEALK----NTERDTGIDL 795
Cdd:cd07940 222 INGIgerAGNA---ALEEVVMALKtrydYYGVETGIDT 256
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
684-795 |
3.36e-08 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 57.64 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 684 TKYNLEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIIDA 763
Cdd:PRK09389 138 SRADLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSELVKGPVSIHCHNDFGLAVANTLAALAAGADQVHV 217
|
90 100 110
....*....|....*....|....*....|...
gi 489520803 764 ALESMAGLTSQPSLNAIVEALKNT-ERDTGIDL 795
Cdd:PRK09389 218 TINGIGERAGNASLEEVVMALKHLyDVETGIKL 250
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1077-1141 |
4.50e-08 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 57.32 E-value: 4.50e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489520803 1077 IGASiPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMI 1141
Cdd:PRK11854 10 IGAD-EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMI 73
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
70-297 |
8.33e-08 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 56.64 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 70 IIdlaKRKKVDAIHPGYG-----FLAenAEFARK--CEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGveKAI 142
Cdd:PRK05294 77 II---EKERPDAILPTMGgqtalNLA--VELAESgvLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 143 RSTEEAKEVANKIGYPVMIKASNGGGGRGMRIVHREEDLELEYETACSESRkaFGEdiIFIEKYIADPKHIEVQILGDNY 222
Cdd:PRK05294 150 HSMEEALEVAEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSP--VTE--VLIEESLLGWKEYEYEVMRDKN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 223 GN--IVhlyerdCSvqrrhqkiIE--------------YAPAFSLDDK-----------VRKEICEDAvklskhvGYSNa 275
Cdd:PRK05294 226 DNciIV------CS--------IEnidpmgvhtgdsitVAPAQTLTDKeyqmlrdasiaIIREIGVET-------GGCN- 283
|
250 260
....*....|....*....|...
gi 489520803 276 gtLEFLVDANGGHYF-IEMNTRV 297
Cdd:PRK05294 284 --VQFALNPKDGRYIvIEMNPRV 304
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
688-801 |
1.14e-07 |
|
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: 54.43 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 688 LEYYIKMAQELeslGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIID----- 762
Cdd:cd07939 141 LIEFAEVAQEA---GADRLRFADTVGILDPFTTYELIRRLRAATDLPLEFHAHNDLGLATANTLAAVRAGATHVSvtvng 217
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489520803 763 -------AALEsmagltsqpslnAIVEALKNTE-RDTGIDLFGYDEL 801
Cdd:cd07939 218 lgeragnAALE------------EVVMALKHLYgRDTGIDTTRLPEL 252
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1083-1141 |
2.15e-07 |
|
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: 49.36 E-value: 2.15e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489520803 1083 GKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMI 1141
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVK 72
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1077-1143 |
2.17e-07 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 54.83 E-value: 2.17e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489520803 1077 IGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIMK 1143
Cdd:PRK11855 10 IGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1070-1143 |
2.64e-07 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 55.01 E-value: 2.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489520803 1070 DMNDPlQIGASiPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIMK 1143
Cdd:PRK11854 208 DVNVP-DIGGD-EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE 279
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
692-771 |
4.77e-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: 52.78 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 692 IKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNV-KAPIHLHTHDTSGNGVATCLMASEAGVDIIDAaleSMAG 770
Cdd:cd07938 152 AEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFpDEKLALHFHDTRGQALANILAALEAGVRRFDS---SVGG 228
|
.
gi 489520803 771 L 771
Cdd:cd07938 229 L 229
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
141-297 |
5.37e-07 |
|
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: 50.72 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 141 AIRSTEEAKEVANKIGYPVMIKASNGG-GGRGMRIVHREEDLELEYETACSESrkafgediIFIEKYIadPKHIEVQILG 219
Cdd:pfam02222 12 AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEELGDGP--------VIVEEFV--PFDRELSVLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 220 DNYGN-IVHLYErdcSVQRRHQK---IIEYAPAfSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNT 295
Cdd:pfam02222 82 VRSVDgETAFYP---VVETIQEDgicRLSVAPA-RVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAP 157
|
..
gi 489520803 296 RV 297
Cdd:pfam02222 158 RP 159
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1083-1141 |
5.56e-07 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 53.85 E-value: 5.56e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489520803 1083 GKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMI 1141
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMV 176
|
|
| PRK08195 |
PRK08195 |
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated |
695-796 |
9.22e-07 |
|
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
Pssm-ID: 181282 [Multi-domain] Cd Length: 337 Bit Score: 52.14 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 695 AQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVK--APIHLHTHDTSGNGVATCLMASEAGVDIIDAALESM-AGL 771
Cdd:PRK08195 150 AKLMESYGAQCVYVVDSAGALLPEDVRDRVRALRAALKpdTQVGFHGHNNLGLGVANSLAAVEAGATRIDGSLAGLgAGA 229
|
90 100
....*....|....*....|....*
gi 489520803 772 TSQPsLNAIVEALKNTERDTGIDLF 796
Cdd:PRK08195 230 GNTP-LEVLVAVLDRMGWETGVDLY 253
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
63-292 |
1.87e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 51.31 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 63 AYLDMDGIIDLAKRkkVDAIhpGYGFlaEN--AEFARKCEENGITFigPSSKVMNMMGDKINSKKIAKEVNVQTIPgvEK 140
Cdd:PRK06019 50 DYDDVAALRELAEQ--CDVI--TYEF--ENvpAEALDALAARVPVP--PGPDALAIAQDRLTEKQFLDKLGIPVAP--FA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 141 AIRSTEEAKEVANKIGYPVMIKASNGG-GGRGMRIVHREEDLEleyetacsESRKAFGEDIIFIEKYIADPKhiEVQILG 219
Cdd:PRK06019 120 VVDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLE--------AAWALLGSVPCILEEFVPFER--EVSVIV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 220 --DNYGNIVH--LYErdcSVQRRHQKIIEYAPAfSLDDKVRKEICEDAVKLSKHVGYSnaGTL--EFLVDANG------- 286
Cdd:PRK06019 190 arGRDGEVVFypLVE---NVHRNGILRTSIAPA-RISAELQAQAEEIASRIAEELDYV--GVLavEFFVTGDGellvnei 263
|
250
....*....|...
gi 489520803 287 -------GHYFIE 292
Cdd:PRK06019 264 aprphnsGHWTIE 276
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1077-1142 |
2.63e-06 |
|
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: 51.41 E-value: 2.63e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489520803 1077 IGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIM 1142
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATL 73
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1077-1143 |
3.90e-06 |
|
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: 51.03 E-value: 3.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489520803 1077 IGASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIMK 1143
Cdd:TIGR01348 124 IGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
39-294 |
6.55e-06 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 50.59 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 39 DKYGLFRTKADESYLIGEGKGpiDAYLDMDGIIDLAKrkkVDAIHPG-YGFLAENAEFARKCEENGITFIGPSSKVMNMM 117
Cdd:PRK14573 492 NRQGLWETVSSLETAIEEDSG--KSVLSSEIAQALAK---VDVVLPIlHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIA 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 118 GDKINSKKIAKEVNVQTIPGVE---KAIRSTEEA--KEVANKIGYPVMIKASNGGGGRGMRIVHREEDLEleyeTACSEs 192
Cdd:PRK14573 567 MDKVLTKRFASDVGVPVVPYQPltlAGWKREPELclAHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELR----DKISE- 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 193 rkAFGEDI-IFIEKYIADPKHIEVQILGDNYGN--IVHLYERdcsvqRRHQKIIEYAPAFSLDDKVRKEICEDaVKLSKH 269
Cdd:PRK14573 642 --AFLYDTdVFVEESRLGSREIEVSCLGDGSSAyvIAGPHER-----RGSGGFIDYQEKYGLSGKSSAQIVFD-LDLSKE 713
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489520803 270 V----------------GYSNAgTLEFLVDANGGHYFIEMN 294
Cdd:PRK14573 714 SqeqvlelaeriyrllqGKGSC-RIDFFLDEEGNFWLSEMN 753
|
|
| DRE_TIM_HCS |
cd07948 |
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ... |
698-762 |
8.45e-06 |
|
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel domain; Homocitrate synthase (HCS) catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate, the first step in the lysine biosynthesis pathway. This family includes the Yarrowia lipolytica LYS1 protein as well as the Saccharomyces cerevisiae LYS20 and LYS21 proteins. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163685 Cd Length: 262 Bit Score: 48.87 E-value: 8.45e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489520803 698 LESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGVDIID 762
Cdd:cd07948 150 VDKLGVNRVGIADTVGIATPRQVYELVRTLRGVVSCDIEFHGHNDTGCAIANAYAALEAGATHID 214
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
96-312 |
9.25e-06 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 48.88 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 96 ARKCEENGITFIGPSSKVMNMmGDKI-NSKKIAKEVNVQTIPGVekaIRSTEEAKEVANKIGYPVMIKASNGGGGRGMRI 174
Cdd:TIGR00768 66 LRYLESLGVPVINSSDAILNA-GDKFlSHQLLAKAGIPLPRTGL---AGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 175 VHREEDLEleyetACSESRKAFGED--IIFIEKYIADPKH--IEVQILGDNY-GNIVHLYERD----CSVQRRhqkiiey 245
Cdd:TIGR00768 142 ARDRQAAE-----SLLEHFEQLNGPqnLFLVQEYIKKPGGrdIRVFVVGDEVvAAIYRITSGHwrsnLARGGK------- 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489520803 246 APAFSLDDkvrkEICEDAVKLSKHVGYSNAGTleFLVDANGGHYFIEMNTRVQVEHTVteMVTGIDI 312
Cdd:TIGR00768 210 AEPCSLTE----EIEELAIKAAKALGLDVAGV--DLLESEDGLLVNEVNANPEFKNSV--KTTGVNI 268
|
|
| DRE_TIM_LeuA3 |
cd07941 |
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ... |
685-758 |
4.08e-05 |
|
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel domain; Desulfobacterium autotrophicum LeuA3 is sequence-similar to alpha-isopropylmalate synthase (LeuA) but its exact function is unknown. Members of this family have an N-terminal TIM barrel domain that belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163679 Cd Length: 273 Bit Score: 46.68 E-value: 4.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489520803 685 KYNLEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVK-APIHLHTHDTSGNGVATCLMASEAGV 758
Cdd:cd07941 147 KANPEYALATLKAAAEAGADWLVLCDTNGGTLPHEIAEIVKEVRERLPgVPLGIHAHNDSGLAVANSLAAVEAGA 221
|
|
| PRK12344 |
PRK12344 |
putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional |
685-758 |
7.54e-05 |
|
putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional
Pssm-ID: 237068 [Multi-domain] Cd Length: 524 Bit Score: 46.62 E-value: 7.54e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489520803 685 KYNLEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHLHTHDTSGNGVATCLMASEAGV 758
Cdd:PRK12344 154 KANPEYALATLKAAAEAGADWVVLCDTNGGTLPHEVAEIVAEVRAAPGVPLGIHAHNDSGCAVANSLAAVEAGA 227
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1083-1133 |
1.15e-04 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 45.94 E-value: 1.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 489520803 1083 GKVIKIMVKEEDEVKANQPLIVIEAMK--MEtiIVAKTDGVIKSIKVKEDDMV 1133
Cdd:PRK11856 17 GEIVEWLVKVGDTVKEGQPLAEVETDKatVE--IPSPVAGTVAKLLVEEGDVV 67
|
|
| PRK00915 |
PRK00915 |
2-isopropylmalate synthase; Validated |
688-795 |
1.20e-04 |
|
2-isopropylmalate synthase; Validated
Pssm-ID: 234864 [Multi-domain] Cd Length: 513 Bit Score: 46.26 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 688 LEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNV----KAPIHLHTHDTSGNGVATCLMASEAGVDIIDA 763
Cdd:PRK00915 148 LDFLCRVVEAAIDAGATTINIPDTVGYTTPEEFGELIKTLRERVpnidKAIISVHCHNDLGLAVANSLAAVEAGARQVEC 227
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489520803 764 ALESM---AGLTsqpSLNAIVEALKnTERD-----TGIDL 795
Cdd:PRK00915 228 TINGIgerAGNA---ALEEVVMALK-TRKDiygveTGINT 263
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
48-322 |
1.29e-04 |
|
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: 45.68 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 48 ADESYLIGEGKGPIDAYLDMDGIIDLAKRKKVDAIHPGYGFLAENAEFARKCEenGITFIGPSSKVMNMMGDKInskKIA 127
Cdd:COG2232 43 AERWVRLDAESCGFDLEDLPAALLELAAADDPDGLVYGSGFENFPELLERLAR--RLPLLGNPPEVVRRVKDPL---RFF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 128 KEVNVQTIPGVEkaIRSTEEAKEvankigYPVMIKASNGGGGRGMRIVHREEDLeleyetacsesrkafGEDIIFIEK-- 205
Cdd:COG2232 118 ALLDELGIPHPE--TRFEPPPDP------GPWLVKPIGGAGGWHIRPADSEAPP---------------APGRYFQRYve 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 206 -------YIADPKHIEV-----QILGDN------Y-GNIVHlyerdcsvqrrhqkiieyapaFSLDDKVRKEICEDAVKL 266
Cdd:COG2232 175 gtpasvlFLADGSDARVlgfnrQLIGPAgerpfrYgGNIGP---------------------LALPPALAEEMRAIAEAL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489520803 267 SKHVGYSNAGTLEFLVDANgGHYFIEMNTRVQVEHTVTEMVTGIDIVQSQILIAQG 322
Cdd:COG2232 234 VAALGLVGLNGVDFILDGD-GPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRG 288
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1079-1142 |
2.08e-04 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 40.56 E-value: 2.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489520803 1079 ASIPGKVIKIMVKEEDEVKANQPLIVIEAMKMETIIVAKTDGVIKSIKVKEDDMVEDKQLLMIM 1142
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| DRE_TIM_HOA_like |
cd07944 |
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ... |
684-768 |
5.27e-04 |
|
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of bacterial enzymes is sequence-similar to 4-hydroxy-2-oxovalerate aldolase (HOA) but its exact function is unknown. This family includes the Bacteroides vulgatus Bvu_2661 protein and belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163682 Cd Length: 266 Bit Score: 43.32 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 684 TKYNLEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKNVKAPIHL--HTHDTSGNGVATCLMASEAGVDII 761
Cdd:cd07944 133 SGYSDEELLELLELVNEIKPDVFYIVDSFGSMYPEDIKRIISLLRSNLDKDIKLgfHAHNNLQLALANTLEAIELGVEII 212
|
....*..
gi 489520803 762 DAALESM 768
Cdd:cd07944 213 DATVYGM 219
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
685-794 |
8.57e-04 |
|
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic TIM barrel domain; Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step of the citramalate pathway. Citramalate is only found in Leptospira interrogans and a few other microorganisms. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163683 [Multi-domain] Cd Length: 280 Bit Score: 42.75 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 685 KYNLEYYIKMAQELESLGADIIAIKDMSGLLKPYSAYTLVKELKKnvKAP-IHL--HTHDTSGNGVATCLMASEAGVDII 761
Cdd:cd07945 143 RDSPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVK--RYPnLHFdfHAHNDYDLAVANVLAAVKAGIKGL 220
|
90 100 110
....*....|....*....|....*....|....
gi 489520803 762 DAALESMAGLTSQPSLNAIVEALKN-TERDTGID 794
Cdd:cd07945 221 HTTVNGLGERAGNAPLASVIAVLKDkLKVKTNID 254
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1073-1106 |
1.49e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.96 E-value: 1.49e-03
10 20 30
....*....|....*....|....*....|....
gi 489520803 1073 DPLQIGASIPGKVIKIMVKEEDEVKANQPLIVIE 1106
Cdd:COG1566 44 RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLD 77
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
70-295 |
4.70e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 40.43 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 70 IIDLAKRKKVDAIHpgyGFLAENAEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIPGVEKAIRSTEEak 149
Cdd:PRK14569 52 LLELKPDKCFVALH---GEDGENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPTPMAKFLTDKLVAE-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 150 evaNKIGYPVMIKASNGGGGRGMRIVHREEDLELEYETAcsesrKAFGEdiIFIEKYIADpKHIEVQILGDNYGNIV--- 226
Cdd:PRK14569 127 ---DEISFPVAVKPSSGGSSIATFKVKSIQELKHAYEEA-----SKYGE--VMIEQWVTG-KEITVAIVNDEVYSSVwie 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489520803 227 ---HLYERDcsvQRRHQKIIEYAPAfSLDDKVRKEICEDAVKLSKHVGYSNAGTLEFLVDANGGHYFIEMNT 295
Cdd:PRK14569 196 pqnEFYDYE---SKYSGKSIYHSPS-GLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEINS 263
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1071-1106 |
4.81e-03 |
|
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: 38.72 E-value: 4.81e-03
10 20 30
....*....|....*....|....*....|....*.
gi 489520803 1071 MNdplQIGASIPGKVIKIMVKEEDEVKANQPLIVIE 1106
Cdd:COG0511 104 MN---EIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
60-198 |
5.13e-03 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 40.77 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 60 PIDAyLDMDGIIDLAKRKKVDAIHPGygflAEN---AEFARKCEENGITFIGPSSKVMNMMGDKINSKKIAKEVNVQTIP 136
Cdd:COG0151 45 DIDV-TDIEALVAFAKEENIDLVVVG----PEAplvAGIVDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAA 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489520803 137 GveKAIRSTEEAKEVANKIGYPVMIKASngG--GGRGMRIVhreEDLElEYETACSE--SRKAFGE 198
Cdd:COG0151 120 Y--RVFTDLEEALAYLEEQGAPIVVKAD--GlaAGKGVVVA---ETLE-EALAAVDDmlADGKFGD 177
|
|
| PRK06748 |
PRK06748 |
hypothetical protein; Validated |
1083-1143 |
5.46e-03 |
|
hypothetical protein; Validated
Pssm-ID: 180678 [Multi-domain] Cd Length: 83 Bit Score: 37.15 E-value: 5.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489520803 1083 GKVIKIMVKEEDEVKANQPLIVIEAM--KMETIIVAkTDGVIKSIKVKEDDMVEDKQLLMIMK 1143
Cdd:PRK06748 13 GKVEKLFVRESSYVYEWEKLALIETIdkQKVEIKVG-ISGYIESLEVVEGQAIADQKLLITVR 74
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
61-182 |
5.68e-03 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 40.81 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520803 61 IDAYLDMDGIIDLAKRKKVDAI---HPgygflaeNAEFARKCEENGITfIGPSSKVMNMMGDKINSKKIAKEVNVQTIPG 137
Cdd:PLN02948 68 VGSFDDRAAVREFAKRCDVLTVeieHV-------DVDTLEALEKQGVD-VQPKSSTIRIIQDKYAQKVHFSKHGIPLPEF 139
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489520803 138 VEkaIRSTEEAKEVANKIGYPVMIKASNGG-GGRGMRIVHREEDLE 182
Cdd:PLN02948 140 ME--IDDLESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTEEDLS 183
|
|
| |
