|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
36-1178 |
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: 1938.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 36 KPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENGVDAV 115
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 116 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFK 195
Cdd:COG1038 82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 196 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 275
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 276 VEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEG 355
Cdd:COG1038 242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 356 RSL--PDLGL-RQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIA 432
Cdd:COG1038 322 YSLddPEIGIpSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVTA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 433 HGKDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNG 512
Cdd:COG1038 402 WGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVNG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 513 PTTPIPVKVSPSPVDPIVPVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIA 592
Cdd:COG1038 482 PPGVKGRPKPDFPKPKLPKVDLGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKIA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 593 PYVAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGM 672
Cdd:COG1038 562 PATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEAGI 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 673 DVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAA 752
Cdd:COG1038 642 DVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKPYA 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 753 CTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERV 832
Cdd:COG1038 722 AYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLDAL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 833 FDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSS 912
Cdd:COG1038 801 QELSNYWEAVRKYYAPFE--SGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPSS 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 913 KIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELE 992
Cdd:COG1038 879 KVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDALR 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 993 KDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRA 1072
Cdd:COG1038 959 AELEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDED 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 1073 GQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTS 1152
Cdd:COG1038 1039 GMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITA 1118
|
1130 1140
....*....|....*....|....*.
gi 564332048 1153 PMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:COG1038 1119 PRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
34-1179 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 1835.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 34 EYKPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENGVD 113
Cdd:PRK12999 1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 114 AVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPII 193
Cdd:PRK12999 81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 194 FKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQ 273
Cdd:PRK12999 161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 274 KVVEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVS 353
Cdd:PRK12999 241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 354 EGRSLPDLG---LRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKV 430
Cdd:PRK12999 321 EGATLHDLEigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 431 IAHGKDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMV 510
Cdd:PRK12999 401 TAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 511 NGPttPIPVKVSPSPVDPIV-PVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLK 589
Cdd:PRK12999 481 NGF--PGVKKKPPVFPDPRLpKVDLSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 590 KIAPYVAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKE 669
Cdd:PRK12999 559 RIAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 670 NGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLK 749
Cdd:PRK12999 639 AGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLK 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 750 PAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPL 829
Cdd:PRK12999 719 PAAAYELVSALKEEV-DLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDL 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 830 ERVFDYSEYWEGARGLYAAFdcTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVT 909
Cdd:PRK12999 798 DAIRKLSPYWEAVRPYYAPF--ESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVT 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 910 PSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLK 989
Cdd:PRK12999 876 PSSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFE 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 990 ELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDL 1069
Cdd:PRK12999 956 AERAELEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEP 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 1070 NRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETV 1149
Cdd:PRK12999 1036 DEDGMRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETT 1115
|
1130 1140 1150
....*....|....*....|....*....|
gi 564332048 1150 VTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK12999 1116 ITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
40-1179 |
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: 1735.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 40 KVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRG--LAPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 197
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 358 LP--DLGL-RQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIAHG 434
Cdd:TIGR01235 321 LPtpQLGVpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 435 KDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGpT 514
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNG-H 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 515 TPIPVKVSP--SPVDPIVPVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIA 592
Cdd:TIGR01235 480 PEAKDKLKPleNAPRVVVLYADQNPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 593 PYVAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGM 672
Cdd:TIGR01235 560 PTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGI 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 673 DVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAA 752
Cdd:TIGR01235 640 DIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAA 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 753 CTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERV 832
Cdd:TIGR01235 720 AKLLIKALREKT-DLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWI 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 833 FDYSEYWEGARGLYAAFDCtaTMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSS 912
Cdd:TIGR01235 799 RELSAYWEAVRNLYAAFES--DLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSS 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 913 KIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELE 992
Cdd:TIGR01235 877 KVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIR 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 993 KDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRA 1072
Cdd:TIGR01235 957 KDLQEKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQ 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 1073 GQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTS 1152
Cdd:TIGR01235 1037 GEREVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQA 1116
|
1130 1140
....*....|....*....|....*..
gi 564332048 1153 PMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:TIGR01235 1117 PKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
37-498 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 713.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 37 PIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENGVDAVH 116
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIG-PAPAAESYLNIDAIIAAAKATGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 117 PGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKA 196
Cdd:COG4770 80 PGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 197 AYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVV 276
Cdd:COG4770 160 SAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 277 EIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGR 356
Cdd:COG4770 240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 357 SLPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKD 436
Cdd:COG4770 320 PLP---FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSMIAKLIVWGPD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332048 437 HPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQLRPAQNRA 498
Cdd:COG4770 396 REEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
38-485 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 627.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPvQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSK-KSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 197
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 358 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 437
Cdd:PRK08591 321 LS---IKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHGETR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 564332048 438 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDEN 485
Cdd:PRK08591 397 EEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
39-488 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 583.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 39 KKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHPG 118
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPA-PPSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 119 YGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAAY 198
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 199 GGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEI 278
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 279 APATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKhGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRSL 358
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN-GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 359 PdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHP 438
Cdd:PRK08654 321 S---FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVD-SGVHMGYEIPPYYDSMISKLIVWGRTRE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 564332048 439 TAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPEL 488
Cdd:PRK08654 397 EAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
38-482 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 567.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIG-GPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 197
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 358 LPdlgLRQENIRINGCAIQCRVTTEDPaRSFQPDTGRIEVFRSGEGMGIRLDNASAfQGAVISPHYDSLLVKVIAHGKDH 437
Cdd:PRK06111 321 LS---FTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMIAKLIAHGETR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 564332048 438 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFI 482
Cdd:PRK06111 396 EEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
38-490 |
1.52e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 537.76 E-value: 1.52e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlaPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD--PLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 197
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 358 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 437
Cdd:PRK07178 320 LS---YKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTA-IYTGYTIPPYYDSMCAKLIVWALTW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 564332048 438 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQ 490
Cdd:PRK07178 396 EEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTN 448
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
38-485 |
8.01e-178 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 529.67 E-value: 8.01e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPA-SSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 197
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 358 lpdLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 437
Cdd:PRK05586 321 ---LSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSA-VYSGYTIPPYYDSMIGKLIVYGKDR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 564332048 438 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDEN 485
Cdd:PRK05586 397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKK 444
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
38-484 |
1.46e-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: 523.94 E-value: 1.46e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPA-PSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 197
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 358 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 437
Cdd:TIGR00514 321 LS---LKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSH-VYSGYTVPPYYDSMIGKLITYGKTR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 564332048 438 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDE 484
Cdd:TIGR00514 397 EVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
36-483 |
6.25e-164 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 494.66 E-value: 6.25e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 36 KPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPvQAYLHIPDIIKVAKENGVDAV 115
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAA-KSYLNPAAILAAARQCGADAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 116 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFK 195
Cdd:PRK12833 82 HPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 196 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYgNILHLYERDCSIQRRHQKV 275
Cdd:PRK12833 162 AAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 276 VEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKH-GKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSE 354
Cdd:PRK12833 241 LEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDArGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 355 GRSlpdLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHG 434
Cdd:PRK12833 321 GEP---LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVD-SLLYPGYRVPPFYDSLLAKLIVHG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 564332048 435 KDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFID 483
Cdd:PRK12833 397 EDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
566-849 |
4.11e-162 |
|
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163675 Cd Length: 275 Bit Score: 481.93 E-value: 4.11e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 566 LMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFnnLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 645
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 646 GANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDvadpsrTKYSLEYYM 725
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 726 GLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPdLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGM 805
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 564332048 806 TSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAF 849
Cdd:cd07937 232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
38-500 |
3.05e-158 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 480.08 E-value: 3.05e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlaPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTD--PIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTnSPIN--SLHEAHEFSNTYGFPIIFK 195
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGT-EKLNseSMEEIKIFARKIGYPVILK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 196 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 275
Cdd:PRK08463 159 ASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 276 VEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEG 355
Cdd:PRK08463 239 IEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 356 RSLPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGK 435
Cdd:PRK08463 319 EILD---LEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVD-SHIYKDYTIPPYYDSMLAKLIVKAT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564332048 436 DHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFqLRPAQNRAQK 500
Cdd:PRK08463 395 SYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQEL-LEKTEDRHQE 458
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
36-485 |
1.21e-157 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 477.31 E-value: 1.21e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 36 KPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENGVDAV 115
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIG-GAKSSESYLNIPAIISAAEIFEADAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 116 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFK 195
Cdd:PRK08462 81 FPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 196 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 275
Cdd:PRK08462 161 AAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 276 VEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEG 355
Cdd:PRK08462 241 IEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 356 RSLPDlglrQENIRINGCAIQCRVTTEDPaRSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGK 435
Cdd:PRK08462 321 EELPS----QESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMD-SHAYAGYVVPPYYDSMIGKLIVWGE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 564332048 436 DHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDEN 485
Cdd:PRK08462 395 DRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
568-1179 |
4.98e-154 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 473.18 E-value: 4.98e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 568 DTTFRDAHQSLLATRVRTHDLKKIAP------YvahnfnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQ 641
Cdd:PRK09282 8 DTTLRDAHQSLLATRMRTEDMLPIAEkldkvgF--------WSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 642 MLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysL 721
Cdd:PRK09282 80 MLLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT---TSPVHT---I 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 722 EYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDS 801
Cdd:PRK09282 154 EKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEV-DLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 802 MSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMksGNSDVYENEIPGGQYTNLHFQAHS 881
Cdd:PRK09282 233 LAFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTI--VDTRVLIHQVPGGMISNLVSQLKE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 882 MGLGSKFKEVKK--AYVEANqmLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGYIGIPHGG 959
Cdd:PRK09282 311 QNALDKLDEVLEeiPRVRED--LGYPPLVTPTSQIVGTQAVLNVLTG-ERYK--------VITKEVKDYVKGLYGRPPAP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 960 FPEPFRSKVLKDLPRIEGRPGASLPPlnlkELEKdlIDRHGEE---VTPEDVLSAAMYPDV----FAQFKDFTATFGPLD 1032
Cdd:PRK09282 380 INEELRKKIIGDEEPITCRPADLLEP----ELEK--ARKEAEElgkSEKEDVLTYALFPQIakkfLEEREAGELKPEPEP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 1033 SLNTRlfLQGPKIAEEFEVELErGKTLHIKALAVSdlnRAGQRQVFFELNGQLRSILVkdtQAMKEMHFHPKALKDVKGQ 1112
Cdd:PRK09282 454 KEAAA--AGAEGIPTEFKVEVD-GEKYEVKIEGVK---AEGKRPFYLRVDGMPEEVVV---EPLKEIVVGGRPRASAPGA 524
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332048 1113 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK09282 525 VTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
564-1021 |
2.18e-130 |
|
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: 409.28 E-value: 2.18e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 564 LLLMDTTFRDAHQSLLATRVRTHDLKKIAPY-VAHNFnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQM 642
Cdd:COG5016 4 VKITDTTLRDGHQSLFATRMRTEDMLPIAEKlDEAGF---WSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 643 LLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVAdpsrtkYSLE 722
Cdd:COG5016 81 LLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYTISPV------HTVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 723 YYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSM 802
Cdd:COG5016 155 YYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEAL-DIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 803 SGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMKsgNSDVYENEIPGGQYTNLHFQAHSM 882
Cdd:COG5016 234 AGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGV--DPRVLVHQVPGGMLSNLVSQLKEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 883 GLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGYIGIPHGGFPE 962
Cdd:COG5016 312 GALDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG-ERYK--------MITKEVKDYVLGYYGKTPAPIDP 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 564332048 963 PFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIdrhgeEVTPEDVLSAAMYPDVFAQF 1021
Cdd:COG5016 383 EVRKKALGDEEPITCRPADLLEP-ELEKLRKEGL-----AKSDEDVLTYALFPQVAIKF 435
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
568-1169 |
4.54e-125 |
|
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: 396.85 E-value: 4.54e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 568 DTTFRDAHQSLLATRVRTHDLKKIAPyvAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGA 647
Cdd:TIGR01108 3 DVVLRDAHQSLFATRMRTEDMLPIAE--KLDDVGYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLRGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 648 NAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEYYMGL 727
Cdd:TIGR01108 81 NLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT---TSPVHT---LETYLDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 728 AEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMTS 807
Cdd:TIGR01108 155 AEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRF-GLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 808 QPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSK 887
Cdd:TIGR01108 234 HPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFE--GQLKGPDSRILVAQVPGGMLSNLESQLKEQNALDK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 888 FKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEAEAqaeelsfpRSVVEFLQGYIGIPHGGFPEPFRSK 967
Cdd:TIGR01108 312 LDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG-ERYKTIT--------KETKGYLKGEYGRTPAPINAELQRK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 968 VLKDL-PRIEGRPGASLPPlNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLntrlfLQGPKIA 1046
Cdd:TIGR01108 383 ILGDEkPIVDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQVGLKFLENRHNPAAFEPK-----PEEKVIE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 1047 EEfevelergktlHIKAlAVSDLNRAGQRQVFFELNGQLRSILVKD-------TQAMKEMHFHPKALKDVK--GQIGAPM 1117
Cdd:TIGR01108 457 QE-----------HAQV-VGKYEETHASGSYTVEVEGKAFVVKVSPggdvsqiTASAPANTSGGTVAAKAGagTPVTAPI 524
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 564332048 1118 PGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKV------HVTKDMTL 1169
Cdd:TIGR01108 525 AGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREIlvkvgdAVSVGQVL 582
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
564-1172 |
1.16e-101 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 334.21 E-value: 1.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 564 LLLMDTTFRDAHQSLLATRVRTHDLKKIAP------YvahnfnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPN 637
Cdd:PRK14040 5 LAITDVVLRDAHQSLFATRLRLDDMLPIAAkldkvgY--------WSLESWGGATFDACIRFLGEDPWERLRELKKAMPN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 638 IPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRT 717
Cdd:PRK14040 77 TPQQMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT---TSPVHT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 718 kysLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDV 797
Cdd:PRK14040 154 ---LQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRV-DVPLHLHCHATTGLSTATLLKAIEAGIDGVDT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 798 AVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHF 877
Cdd:PRK14040 230 AISSMSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFE--GQLKGVDSRILVAQVPGGMLTNMES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 878 QAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGyigiPH 957
Cdd:PRK14040 308 QLKEQGAADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQAVLNVLTG-ERYK--------TITKETAGVLKG----EY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 958 GGFPEPF----RSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRHGE------EVTPEDVLSAAMYPDV---FAQFKDF 1024
Cdd:PRK14040 375 GATPAPVnaelQARVLEGAEPITCRPADLLAP-ELDKLEAELRRQAQEkgitlaENAIDDVLTYALFPQIglkFLENRHN 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 1025 TATFGPLDSL-NTRLFLQGPKIAEE-FEVELErGKTLHIKalaVSDlnragqrqvffelNGQLRSILVKDTQAMKEMHFH 1102
Cdd:PRK14040 454 PAAFEPVPQAeAAQPAAKAEPAGSEtYTVEVE-GKAYVVK---VSE-------------GGDISQITPAAPAAAPAAAAA 516
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 1103 PKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTkdmtlEGD 1172
Cdd:PRK14040 517 AAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVK-----EGD 581
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
566-1021 |
1.51e-97 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 318.18 E-value: 1.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 566 LMDTTFRDAHQSLLATRVRTHDLKKIApyvaHNFNNL--FSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQML 643
Cdd:PRK12331 6 ITETVLRDGQQSLIATRMTTEEMLPIL----EKLDNAgyHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 644 LRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEY 723
Cdd:PRK12331 82 LRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT---TSPVHT---IDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 724 YMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTsgSGVAAM--LACAQAGADVVDVAVDS 801
Cdd:PRK12331 156 FVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAV-TVPLEVHTHAT--SGIAEMtyLKAIEAGADIIDTAISP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 802 MSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLY-AAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAH 880
Cdd:PRK12331 233 FAGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYrEEGILNPKVKDVEPKTLIYQVPGGMLSNLLSQLK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 881 SMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEAeaqaeelsFPRSVVEFLQGYIGIPHGGF 960
Cdd:PRK12331 313 EQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALMNVISG-ERYKM--------VPNEIKDYVRGLYGRPPAPI 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332048 961 PEPFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRHGEEvtpEDVLSAAMYPDVFAQF 1021
Cdd:PRK12331 384 AEEIKKKIIGDEEVITCRPADLIEP-QLEKLREEIAEYAESE---EDVLSYALFPQQAKDF 440
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
862-1062 |
3.50e-95 |
|
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: 302.07 E-value: 3.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 862 VYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSF 941
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 942 PRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQF 1021
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564332048 1022 KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIK 1062
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
565-1179 |
7.24e-91 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 305.11 E-value: 7.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 565 LLMDTTFRDAHQSLLATRVRTHDLKKIAPYVahNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLL 644
Cdd:PRK14042 5 FITDVTLRDAHQCLIATRMRTEDMLPICNKM--DDVGFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSMLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 645 RGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvadpSRTKYSLEYY 724
Cdd:PRK14042 83 RGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT------TSPVHTLDNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 725 MGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRdRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSG 804
Cdd:PRK14042 157 LELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLK-QATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 805 MTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMKSGNSDVYenEIPGGQYTNLHFQAHSMGL 884
Cdd:PRK14042 236 GASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLY--QVPGGMISNLYNQLKEQNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 885 GSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlsraeaeaqAEELSFPRSVVEFLQGYIGIPHGGFPEPF 964
Cdd:PRK14042 314 LDKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQAVINVLTG---------ERYKTITNEVKLYCQGKYGTPPGKISSAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 965 RSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRhgeEVTPEDVLSAAMYPDVFAQFKDFTATFGPL-DSLNTRLFLQGP 1043
Cdd:PRK14042 385 RKKAIGRTEVIEVRPGDLLPN-ELDQLQNEISDL---ALSDEDVLLYAMFPEIGRQFLEQRKNNQLIpEPLLTQSSAPDN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 1044 KIAEEFEVELErGKTLHIKaLAVSDLNRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVID 1123
Cdd:PRK14042 461 SVMSEFDIILH-GESYHVK-VAGYGMIEHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPGSIIA 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 564332048 1124 VKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK14042 539 IHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
565-1054 |
5.63e-90 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 298.24 E-value: 5.63e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 565 LLMDTTFRDAHQSLLATRVRTHDLKKIAPyvAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLL 644
Cdd:PRK14041 4 MFVDTTLRDGHQSLIATRMRTEDMLPALE--AFDRMGFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQMLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 645 RGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEYY 724
Cdd:PRK14041 82 RGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT---VSPVHT---LEYY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 725 MGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSG 804
Cdd:PRK14041 156 LEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 805 MTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGL 884
Cdd:PRK14041 235 GTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYD--VGMKSPDSRILVSQIPGGMYSNLVKQLKEQKM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 885 GSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEaqaeelsfpRSVVEFLQGYIGIPHGGFPEPF 964
Cdd:PRK14041 313 LHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQAVLNVLTGERYKRVT---------NETKNYVKGLYGRPPAPIDEEL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 965 RSKVLKDLPRIEGRPGASLPPlnlkELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFkdftatfgpldsLNTRlFLQGPK 1044
Cdd:PRK14041 384 MKKILGDEKPIDCRPADLLEP----ELEKARKELGILAETDEDLLIYVILGEVGKKF------------LKKK-YEEKIG 446
|
490
....*....|
gi 564332048 1045 IAEEFEVELE 1054
Cdd:PRK14041 447 VDFNLLEELS 456
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
572-1021 |
7.99e-82 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 276.64 E-value: 7.99e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 572 RDAHQSLLATRVRTHDLKKI------APYvahnfnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 645
Cdd:PRK12330 13 RDAHQSLMATRMAMEDMVGAcedidnAGY--------WSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQMLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 646 GANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEYYM 725
Cdd:PRK12330 85 GQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT---VSPIHT---VEGFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 726 GLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRF-PDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMS- 803
Cdd:PRK12330 159 EQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSMSl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 804 GMTSQPSMgALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATmkSGNSDVYENEIPGGQYTNLHFQAHSMG 883
Cdd:PRK12330 239 GPGHNPTE-SLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTT--GVETEIFKSQIPGGMLSNMESQLKQQG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 884 LGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlsraeaeaqaeelSFPRSVVEF---LQGYIGIPhggf 960
Cdd:PRK12330 316 AGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVFNVLMG-------------RYKVLTGEFadlMLGYYGET---- 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332048 961 PEPFRSKVLKDLPR------IEGRPGASLPPlNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQF 1021
Cdd:PRK12330 379 PGERNPEVVEQAKKqakkepITCRPADLLEP-EWDKLRAEALALEGCDGSDEDVLTYALFPQVAPKF 444
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
152-359 |
1.48e-76 |
|
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: 251.46 E-value: 1.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 152 DKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGN 231
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 232 GALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTV 311
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564332048 312 EFLVD-KHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRSLP 359
Cdd:pfam02786 161 EFALDpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
567-840 |
1.25e-71 |
|
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: 239.67 E-value: 1.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 567 MDTTFRDAHQSLLATRvRTHDLKKIAPYVAHNfnNLFSIENWGGATFDVAmrFLYECPWRRLQELRELIPNIPFQMLLRG 646
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEA--GVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 647 anavgytnypdnvVFKFCEVAKENGMDVFRIFDSLNY--------------LPNMLLGMEAAGSAGGVVEAAISYTgdva 712
Cdd:cd03174 76 -------------REKGIERALEAGVDEVRIFDSASEthsrknlnksreedLENAEEAIEAAKEAGLEVEGSLEDA---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 713 dpSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGA 792
Cdd:cd03174 139 --FGCKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 564332048 793 DVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWE 840
Cdd:cd03174 217 DRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
561-1042 |
7.68e-66 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 230.78 E-value: 7.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 561 HQGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVahNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPF 640
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDMLPVLTIL--DKIGYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 641 QMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvadpSRTKYS 720
Cdd:PRK12581 88 QMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT------TSPVHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 721 LEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRdRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVD 800
Cdd:PRK12581 162 LNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIK-AMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 801 SMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAfDCT--ATMKSGNSDVYENEIPGGQYTNLHFQ 878
Cdd:PRK12581 241 PFSEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYLA-DGIldPSLLFPDPRTLQYQVPGGMLSNMLSQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 879 AHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEaqaeelsfpRSVVEFLQGYIGIPHG 958
Cdd:PRK12581 320 LKQANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVILGKPYQMVS---------KEIKQYLAGDYGKTPA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 959 GFPEPFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRhgeEVTPEDVLSAAMYPDVFAQFkdFTATFGPLDSLNTRL 1038
Cdd:PRK12581 391 PVNEDLKRSQIGSAPVTTNRPADQLSP-EFEVLKAEVADL---AQTDEDVLTYALFPSVAKPF--LTTKYQTDDVIKVTA 464
|
....
gi 564332048 1039 FLQG 1042
Cdd:PRK12581 465 FIKA 468
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
38-146 |
2.62e-58 |
|
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: 195.78 E-value: 2.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPG-PASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*....
gi 564332048 118 GYGFLSERADFAQACQDAGVRFIGPSPEV 146
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
99-356 |
1.12e-54 |
|
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: 191.24 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 99 HIPDIIKVAKE----NGVDAVHPGYGFLSERAdfAQACQDAGVRfiGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTnsP 174
Cdd:COG0439 1 DIDAIIAAAAElareTGIDAVLSESEFAVETA--AELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFA--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 175 INSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKpRHIEVQILGDQ 254
Cdd:COG0439 75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVRD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 255 yGNILHlyerdCSIQRRHQK---VVE---IAPAThLDPQLRSRLTSDSVKLAKQVGYEN-AGTVEFLVDKHGKHYFIEVN 327
Cdd:COG0439 154 -GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYLIEIN 226
|
250 260 270
....*....|....*....|....*....|.
gi 564332048 328 SRLQVEH--TVTEEITDVDLVHAQIHVSEGR 356
Cdd:COG0439 227 ARLGGEHipPLTELATGVDLVREQIRLALGE 257
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
376-483 |
2.64e-49 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 169.90 E-value: 2.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 376 QCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRG 455
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVD-SGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 564332048 456 VKTNIPFLQNVLNNQQFLAGIVDTQFID 483
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
376-484 |
2.78e-43 |
|
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: 152.65 E-value: 2.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 376 QCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRG 455
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVD-SGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 564332048 456 VKTNIPFLQNVLNNQQFLAGIVDTQFIDE 484
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
566-838 |
3.24e-29 |
|
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: 117.83 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 566 LMDTTFRDAHQSLlATRVRTHDLKKIAPyvahnfnnlfSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 645
Cdd:pfam00682 4 ICDTTLRDGEQAL-GVAFSIDEKLAIAR----------ALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 646 GAnavgytnypDNVVFKFCEVAKENGMDVFRIFDSLNYLP-NMLLGM---EAAGSAGGVVEAAISYTGDVA----DPSRT 717
Cdd:pfam00682 73 AR---------EHDIKAAVEALKGAGAVRVHVFIATSDLHrKYKLGKdreEVAKRAVAAVKAARSRGIDVEfspeDASRT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 718 kySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPD-LPLHIHTHDTSGSGVAAMLACAQAGADVVD 796
Cdd:pfam00682 144 --DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVD 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 564332048 797 VAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEY 838
Cdd:pfam00682 222 GTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANL 263
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1112-1178 |
2.16e-24 |
|
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: 97.49 E-value: 2.16e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332048 1112 QIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1112-1178 |
1.52e-18 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 80.72 E-value: 1.52e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332048 1112 QIGAPMPGKVID-----VKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:pfam00364 2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
36-330 |
4.15e-14 |
|
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: 77.35 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 36 KPIKKVMVANRGEIAI-----------RVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIgrglaPVQAYlHIPDII 104
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIgqaaefdysgsQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIE-----PLTPE-AVEKII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 105 KvaKENgVDAVHPGYG---------FLSERAdfaqACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGtnSPI 175
Cdd:TIGR01369 78 E--KER-PDAILPTFGgqtalnlavELEESG----VLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 176 NSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRayseALAAFGNGALFVEKFIEKPRHIEVQILGDQY 255
Cdd:TIGR01369 149 HSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAER----ALSASPINQVLVEKSLAGWKEIEYEVMRDSN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 256 GNILHLyerdCSIQR-----RH--QKVVeIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVD-KHGKHYFIEVN 327
Cdd:TIGR01369 225 DNCITV----CNMENfdpmgVHtgDSIV-VAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNpDSGRYYVIEVN 299
|
...
gi 564332048 328 SRL 330
Cdd:TIGR01369 300 PRV 302
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1111-1179 |
8.46e-14 |
|
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: 69.54 E-value: 8.46e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332048 1111 GQIGAPMPGKV-------IDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:COG0511 61 GAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
102-414 |
1.59e-13 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 75.39 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 102 DIIKVAKENGVDAVHPGYGflSERA-DFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSpiNSLHE 180
Cdd:PRK12815 621 DVLNVAEAENIKGVIVQFG--GQTAiNLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTA--TDEEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 181 AHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSealaafGNGALFVEKFIEKpRHIEVQILGDQY----- 255
Cdd:PRK12815 697 AFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENAS------QLYPILIDQFIDG-KEYEVDAISDGEdvtip 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 256 GNILHLYER-----DcSIQrrhqkvveIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVdKHGKHYFIEVNSRl 330
Cdd:PRK12815 770 GIIEHIEQAgvhsgD-SIA--------VLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVLEVNPR- 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 331 qVEHTV--TEEITDVDLVHAQIHVSEGRSLPDLGLRQENIRINGcaiqcRVTTEDPARSFQ--PDTGRI---EVFRSGEG 403
Cdd:PRK12815 839 -ASRTVpfVSKATGVPLAKLATKVLLGKSLAELGYPNGLWPGSP-----FIHVKMPVFSYLkyPGVDNTlgpEMKSTGEV 912
|
330
....*....|.
gi 564332048 404 MGIRLDNASAF 414
Cdd:PRK12815 913 MGIDKDLEEAL 923
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1113-1175 |
9.75e-13 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 66.37 E-value: 9.75e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332048 1113 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLE-GDDLI 1175
Cdd:PRK06549 64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNpGDGLI 127
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
129-420 |
1.36e-12 |
|
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: 72.34 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 129 AQACQDAGVRFIGPSPEVVrkmgDKVEARAIAIAA----GVPVVPGtnSPINSLHEAHEFSNTYGFPIIFKAAYGGGGRG 204
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESI----DRAEDREKFSELldelGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 205 MRVVHSYEELeenyTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQ-----YGNILHLyER------DCSIqrrhq 273
Cdd:TIGR01369 720 MEIVYNEEEL----RRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGeevliPGIMEHI-EEagvhsgDSTC----- 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 274 kvveIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVdKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVS 353
Cdd:TIGR01369 790 ----VLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV-KDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVM 864
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332048 354 EGRSLPDLGLRQEniringcAIQCRVTTEDPARSFQPDTGR-----IEVFRSGEGMGIRLDNASAFQGAVIS 420
Cdd:TIGR01369 865 LGKKLEELGVGKE-------KEPKYVAVKEPVFSFSKLAGVdpvlgPEMKSTGEVMGIGRDLAEAFLKAQLS 929
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
129-329 |
1.16e-11 |
|
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: 68.75 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 129 AQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTnsPINSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVV 208
Cdd:COG0458 91 EEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSG--TATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 209 HSYEELEEnytrAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNIL------HLyER------DcSIqrrhqkVV 276
Cdd:COG0458 169 YNEEELEE----YLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIivgimeHI-EPagvhsgD-SI------CV 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564332048 277 eiAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKhGKHYFIEVNSR 329
Cdd:COG0458 237 --APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDD-GRVYVIEVNPR 286
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1111-1175 |
2.74e-11 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 62.96 E-value: 2.74e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564332048 1111 GQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLE-GDDLI 1175
Cdd:PRK05641 85 NVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDtGQPLI 150
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
101-348 |
4.97e-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: 61.88 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 101 PDIIKVAKENGVDAVHPGYGFLSERADFAQACQDAGVRFIgPSPEVVRKMGDKVEARAIAIAAGVPVvpgtnsP----IN 176
Cdd:COG0189 46 PELYRGEDLSEFDAVLPRIDPPFYGLALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPV------PptlvTR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 177 SLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEenytrAYSEALAAFGNGALFVEKFIEKPRHIEVQI--LGDQ 254
Cdd:COG0189 119 DPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALE-----SILEALTELGSEPVLVQEFIPEEDGRDIRVlvVGGE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 255 YgniLHLYER-----DCSIQRRHQKVVEiapATHLDPQLRSRLtsdsVKLAKQVGYENAGtVEFLVDKHGkHYFIEVNSR 329
Cdd:COG0189 194 P---VAAIRRipaegEFRTNLARGGRAE---PVELTDEERELA----LRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVT 261
|
250
....*....|....*....
gi 564332048 330 LQVEHtvTEEITDVDLVHA 348
Cdd:COG0189 262 PGFRG--LERATGVDIAEA 278
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1112-1179 |
5.40e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 56.72 E-value: 5.40e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564332048 1112 QIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTK-DMTLEGDDLiLEIE 1179
Cdd:PRK08225 3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEgDFVNEGDVL-LEIE 70
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
691-799 |
5.90e-10 |
|
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163676 Cd Length: 274 Bit Score: 61.64 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 691 MEAAGSAGGVVEAAIS------YTGDVaDPSRTkysleyyMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRF 764
Cdd:cd07938 120 AELAKAAGLRVRGYVStafgcpYEGEV-PPERV-------AEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERF 191
|
90 100 110
....*....|....*....|....*....|....*
gi 564332048 765 PDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAV 799
Cdd:cd07938 192 PDEKLALHFHDTRGQALANILAALEAGVRRFDSSV 226
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
152-327 |
2.29e-09 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 60.12 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 152 DKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEALaAFGN 231
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAA----ALEEAF-KYDD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 232 GALfVEKFIEkPRHIEVQILGDQYGNILHL---------------YERDcsiqrrhqKVVEIAPAtHLDPQLRSRLTSDS 296
Cdd:COG1181 170 KVL-VEEFID-GREVTVGVLGNGGPRALPPieivpengfydyeakYTDG--------GTEYICPA-RLPEELEERIQELA 238
|
170 180 190
....*....|....*....|....*....|.
gi 564332048 297 VKLAKQVGYENAGTVEFLVDKHGKHYFIEVN 327
Cdd:COG1181 239 LKAFRALGCRGYARVDFRLDEDGEPYLLEVN 269
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
700-799 |
7.32e-09 |
|
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: 59.41 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 700 VVEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHD 775
Cdd:COG0119 124 AVKYAKEHGLEVEfsaeDATRT--DPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHN 201
|
90 100
....*....|....*....|....
gi 564332048 776 TSGSGVAAMLACAQAGADVVDVAV 799
Cdd:COG0119 202 DLGLAVANSLAAVEAGADQVEGTI 225
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
162-327 |
2.34e-07 |
|
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: 52.70 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 162 AAGVPVVP-----GTNSPINSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEALAAfgNGALFV 236
Cdd:pfam07478 4 AAGLPVVPfvtftRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQA----AIEEAFQY--DEKVLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 237 EKFIEKpRHIEVQILGDQYGNILHLYER--DCSIQRRHQKVVE-----IAPAtHLDPQLRSRLTSDSVKLAKQVGYENAG 309
Cdd:pfam07478 78 EEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDdsaqiVVPA-DLEEEQEEQIQELALKAYKALGCRGLA 155
|
170
....*....|....*...
gi 564332048 310 TVEFLVDKHGKHYFIEVN 327
Cdd:pfam07478 156 RVDFFLTEDGEIVLNEVN 173
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
79-329 |
7.94e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 52.58 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 79 QKADEAYLIGRGLAPvqAYlhIPDIIKVAKENGVDAVHPGY----GFLSE-RADFaqacQDAGVRFIGPSPEVVRKMGDK 153
Cdd:PRK12767 41 YFADKFYVVPKVTDP--NY--IDRLLDICKKEKIDLLIPLIdpelPLLAQnRDRF----EEIGVKVLVSSKEVIEICNDK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 154 VEARAIAIAAGVPVvPGTNSPINSLH-EAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEenytRAYSEalaafgNG 232
Cdd:PRK12767 113 WLTYEFLKENGIPT-PKSYLPESLEDfKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEY------VP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 233 ALFVEKFIEkprHIE--VQILGDQYGNILHlyerdcSIQRRHQKVV--EIAPA-THLDPQLRSRLtsdsVKLAKQVGYEN 307
Cdd:PRK12767 182 NLIIQEFIE---GQEytVDVLCDLNGEVIS------IVPRKRIEVRagETSKGvTVKDPELFKLA----ERLAEALGARG 248
|
250 260
....*....|....*....|..
gi 564332048 308 AGTVEFLVDKhGKHYFIEVNSR 329
Cdd:PRK12767 249 PLNIQCFVTD-GEPYLFEINPR 269
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
136-330 |
2.30e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 52.28 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 136 GVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVvpgTNSPI-NSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEEL 214
Cdd:PRK12815 112 GVELLGTNIEAIQKGEDRERFRALMKELGEPV---PESEIvTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 215 EENYTRAysEALAAFGNgaLFVEKFIEKPRHIEVQILGDQYGNILHLyerdCSIQRrhqkvVE-----------IAPATH 283
Cdd:PRK12815 189 EQLFKQG--LQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCITV----CNMEN-----IDpvgihtgdsivVAPSQT 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564332048 284 LDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYF-IEVNSRL 330
Cdd:PRK12815 256 LTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYlIEVNPRV 303
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
713-799 |
2.79e-06 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 51.48 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 713 DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRfPDLPLHIHTHDTSGSGVAAMLACAQAGA 792
Cdd:PRK09389 136 DASRA--DLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSEL-VKGPVSIHCHNDFGLAVANTLAALAAGA 212
|
....*..
gi 564332048 793 DVVDVAV 799
Cdd:PRK09389 213 DQVHVTI 219
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
129-369 |
3.25e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 51.64 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 129 AQACQDAGVRFIGPSPEVVrkmgDKVEAR----AIAIAAGVPvvpgtnSPIN----SLHEAHEFSNTYGFPIIFKAAYGG 200
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAI----DLAEDRerfsKLLEKLGIP------QPPNgtatSVEEALEVAEEIGYPVLVRPSYVL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 201 GGRGMRVVHSYEELEEnYTRaysEALAAFGNGALFVEKFIEKPRHIEVQILGD----QYGNIL-HLyER------D--CS 267
Cdd:PRK05294 716 GGRAMEIVYDEEELER-YMR---EAVKVSPDHPVLIDKFLEGAIEVDVDAICDgedvLIGGIMeHI-EEagvhsgDsaCS 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 268 IqrrhqkvveiaPATHLDPQLRSRLTSDSVKLAKQ---VGYENagtVEFLVdKHGKHYFIEVN---SRlqvehTV--TEE 339
Cdd:PRK05294 791 L-----------PPQTLSEEIIEEIREYTKKLALElnvVGLMN---VQFAV-KDDEVYVIEVNpraSR-----TVpfVSK 850
|
250 260 270
....*....|....*....|....*....|
gi 564332048 340 ITDVDLVHAQIHVSEGRSLPDLGLRQENIR 369
Cdd:PRK05294 851 ATGVPLAKIAARVMLGKKLAELGYTKGLIP 880
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1112-1178 |
3.64e-06 |
|
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: 45.83 E-value: 3.64e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564332048 1112 QIGAPM-PGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:COG0508 9 DLGESMtEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
701-799 |
5.08e-06 |
|
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163678 Cd Length: 268 Bit Score: 49.37 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 701 VEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFP--DLPLHIHTH 774
Cdd:cd07940 120 VEYAKSHGLDVEfsaeDATRT--DLDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPniKVPISVHCH 197
|
90 100
....*....|....*....|....*
gi 564332048 775 DTSGSGVAAMLACAQAGADVVDVAV 799
Cdd:cd07940 198 NDLGLAVANSLAAVEAGARQVECTI 222
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
142-325 |
1.72e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 48.53 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 142 PSPEVVRKMGDKVEARAIAIAAGVPVVPgtNSPINSLHEAHEFSNTYGFPIIFKAAyggggrgmR---------VVHSYE 212
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAP--FAAVDSLEDLEAAIAELGLPAVLKTR--------RggydgkgqvVIKSAA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 213 ELEenytraysEALAAFGNGALFVEKFI--EKprhiEVQILG--DQYGNILHlY---ErdcSIQRRHQKVVEIAPAtHLD 285
Cdd:COG0026 149 DLE--------AAWAALGGGPCILEEFVpfER----ELSVIVarSPDGEVAT-YpvvE---NVHRNGILDESIAPA-RIS 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564332048 286 PQLRSRLTSDSVKLAKQVGYenAGT--VEFLVDKHGK--------------HYFIE 325
Cdd:COG0026 212 EALAAEAEEIAKRIAEALDY--VGVlaVEFFVTKDGEllvneiaprphnsgHWTIE 265
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
724-805 |
2.15e-05 |
|
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF ) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163681 Cd Length: 263 Bit Score: 47.49 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 724 YMGLAEELVR-------AGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVD 796
Cdd:cd07943 136 HMASPEELAEqaklmesYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRID 215
|
....*....
gi 564332048 797 VavdSMSGM 805
Cdd:cd07943 216 G---SLAGL 221
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
152-327 |
2.76e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 47.41 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 152 DKVEARAIAIAAGVPVVPGT--NSPINSLHEAHEFsntyGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEAlAAF 229
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIvlTREEDLLAAIDKL----GLPLVVKPAREGSSVGVSKVKEEDELQA----ALELA-FKY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 230 GNGALfVEKFIeKPRHIEVQILGDQygnILhlyerdcsiqrrhqKVVEIAPATH--------------------LDPQLR 289
Cdd:PRK01372 169 DDEVL-VEKYI-KGRELTVAVLGGK---AL--------------PVIEIVPAGEfydyeakylaggtqyicpagLPAEIE 229
|
170 180 190
....*....|....*....|....*....|....*...
gi 564332048 290 SRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVN 327
Cdd:PRK01372 230 AELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVN 267
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
139-327 |
3.95e-05 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 47.89 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 139 FIGPSPEVVRKMGDKVEARAIAIAAGVPVVPgtNSPINsLHE--------AHEFSNTYGFPIIFKAAYGGGGRGMRVVHS 210
Cdd:PRK14573 555 YTGPSLAFSAIAMDKVLTKRFASDVGVPVVP--YQPLT-LAGwkrepelcLAHIVEAFSFPMFVKTAHLGSSIGVFEVHN 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 211 YEELEEnytrAYSEALAAfgNGALFVEKFIEKPRHIEVQILGDQYGN--ILHLYERdC------SIQRRH----QKVVEI 278
Cdd:PRK14573 632 VEELRD----KISEAFLY--DTDVFVEESRLGSREIEVSCLGDGSSAyvIAGPHER-RgsggfiDYQEKYglsgKSSAQI 704
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564332048 279 APATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVN 327
Cdd:PRK14573 705 VFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMN 753
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1115-1178 |
7.81e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 42.10 E-value: 7.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564332048 1115 APMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
718-840 |
9.27e-05 |
|
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic TIM barrel domain; Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step of the citramalate pathway. Citramalate is only found in Leptospira interrogans and a few other microorganisms. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163683 [Multi-domain] Cd Length: 280 Bit Score: 45.83 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 718 KYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDV 797
Cdd:cd07945 143 RDSPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVLAAVKAGIKGLHT 222
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 564332048 798 AVDSMSGMTSQPSMGALVACTKG-TPLDTEVPLERVFDYSEYWE 840
Cdd:cd07945 223 TVNGLGERAGNAPLASVIAVLKDkLKVKTNIDEKRLNRASRLVE 266
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1113-1179 |
1.57e-04 |
|
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: 45.64 E-value: 1.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332048 1113 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
713-799 |
2.63e-04 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 44.78 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 713 DPSRTKYS-LEYYMGLAEElvrAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAG 791
Cdd:PRK11858 138 DASRTDLDfLIEFAKAAEE---AGADRVRFCDTVGILDPFTMYELVKELVEAV-DIPIEVHCHNDFGMATANALAGIEAG 213
|
....*...
gi 564332048 792 ADVVDVAV 799
Cdd:PRK11858 214 AKQVHTTV 221
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
38-329 |
3.05e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 45.09 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 38 IKKVMVANRGEI--------------AIRVFRactELGIRTVAVYSEQDTGQMHRQKADEAYLIgrglaPVQaylhiPDI 103
Cdd:PRK05294 7 IKKILIIGSGPIvigqacefdysgtqACKALR---EEGYRVVLVNSNPATIMTDPEMADATYIE-----PIT-----PEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 104 I-KV-AKENgVDAVHPGYG---------------FLSERadfaqacqdaGVRFIGPSPEVVRKMGDKVEARAIAIAAGVP 166
Cdd:PRK05294 74 VeKIiEKER-PDAILPTMGgqtalnlavelaesgVLEKY----------GVELIGAKLEAIDKAEDRELFKEAMKKIGLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 167 VVPGTnsPINSLHEAHEFSNTYGFPIIFKAAYGgggrgM-----RVVHSYEELEENYTRayseALAAFGNGALFVEKFIE 241
Cdd:PRK05294 143 VPRSG--IAHSMEEALEVAEEIGYPVIIRPSFT-----LggtggGIAYNEEELEEIVER----GLDLSPVTEVLIEESLL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 242 KPRHIEVQILGDQYGN--ILhlyerdCSIqrrhqkvvE--------------IAPATHLDPQLRSRLTSDSVKLAKQVGY 305
Cdd:PRK05294 212 GWKEYEYEVMRDKNDNciIV------CSI--------EnidpmgvhtgdsitVAPAQTLTDKEYQMLRDASIAIIREIGV 277
|
330 340
....*....|....*....|....*.
gi 564332048 306 ENAGT-VEFLVD-KHGKHYFIEVNSR 329
Cdd:PRK05294 278 ETGGCnVQFALNpKDGRYIVIEMNPR 303
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
137-420 |
3.43e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 45.15 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 137 VRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSpiNSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEe 216
Cdd:PLN02735 687 VKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIA--RSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK- 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 217 nytRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNI-------------LHLYERDCSIqrrhqkvveiaPATH 283
Cdd:PLN02735 764 ---TYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVviggimehieqagVHSGDSACSL-----------PTQT 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 284 LDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRlqVEHT---VTEEITDVDLVHAQIhVSEGRSLPD 360
Cdd:PLN02735 830 IPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR--ASRTvpfVSKAIGHPLAKYASL-VMSGKSLKD 906
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564332048 361 LGLRQENIrINGCAIQCRVTtedPARSFQ-PDTGRIEVFRS-GEGMGIRLDNASAFQGAVIS 420
Cdd:PLN02735 907 LGFTEEVI-PAHVSVKEAVL---PFDKFQgCDVLLGPEMRStGEVMGIDYEFSKAFAKAQIA 964
|
|
| DRE_TIM_LeuA3 |
cd07941 |
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ... |
757-795 |
6.11e-04 |
|
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: 43.21 E-value: 6.11e-04
10 20 30
....*....|....*....|....*....|....*....
gi 564332048 757 VSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVV 795
Cdd:cd07941 186 VKEVRERLPGVPLGIHAHNDSGLAVANSLAAVEAGATQV 224
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
700-799 |
9.58e-04 |
|
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163677 [Multi-domain] Cd Length: 259 Bit Score: 42.49 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 700 VVEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHD 775
Cdd:cd07939 115 LVGRAKDRGLFVSvgaeDASRA--DPDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAAT-DLPLEFHAHN 191
|
90 100
....*....|....*....|....
gi 564332048 776 TSGSGVAAMLACAQAGADVVDVAV 799
Cdd:cd07939 192 DLGLATANTLAAVRAGATHVSVTV 215
|
|
| PLN02746 |
PLN02746 |
hydroxymethylglutaryl-CoA lyase |
727-838 |
1.75e-03 |
|
hydroxymethylglutaryl-CoA lyase
Pssm-ID: 178347 Cd Length: 347 Bit Score: 42.08 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 727 LAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMT 806
Cdd:PLN02746 202 VAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTVDSSVAGLGGCP 281
|
90 100 110
....*....|....*....|....*....|....*...
gi 564332048 807 SQPSMGALVACT------KGTPLDTEVPLERVFDYSEY 838
Cdd:PLN02746 282 YAKGASGNVATEdvvymlNGLGVSTNVDLGKLMAAGDF 319
|
|
| YcjR |
COG1082 |
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism]; |
100-168 |
1.93e-03 |
|
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 440699 [Multi-domain] Cd Length: 254 Bit Score: 41.54 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 100 IPDIIKVAKENGVDAVHPGYGFLSE--RADFAQACQDAGVRFIG---------PSPEVVRKMGDKVEaRAIAIAA--GVP 166
Cdd:COG1082 15 LEEALRAAAELGYDGVELAGGDLDEadLAELRAALADHGLEISSlhapglnlaPDPEVREAALERLK-RAIDLAAelGAK 93
|
..
gi 564332048 167 VV 168
Cdd:COG1082 94 VV 95
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1113-1179 |
2.07e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 42.12 E-value: 2.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564332048 1113 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK11855 10 IGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1119-1179 |
2.46e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 41.73 E-value: 2.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332048 1119 GKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
38-330 |
2.50e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.07 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 38 IKKVMVANRGEIAI-----------RVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLigrglAPVQaylhiPDIIK- 105
Cdd:PLN02735 23 LKKIMILGAGPIVIgqacefdysgtQACKALKEEGYEVVLINSNPATIMTDPETADRTYI-----APMT-----PELVEq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 106 -VAKENGvDAVHPGYG---------FLSERADFAQAcqdaGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVP-GTNsp 174
Cdd:PLN02735 93 vIAKERP-DALLPTMGgqtalnlavALAESGILEKY----GVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPsGIA-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 175 iNSLHEAHEFSNTYG-FPIIFKAAYGGGGRGMRVVHSYEELEENYTraysEALAAFGNGALFVEKFIEKPRHIEVQILGD 253
Cdd:PLN02735 166 -TTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICK----AGLAASITSQVLVEKSLLGWKEYELEVMRD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 254 QYGNILHLyerdCSIQRRHQKVVE------IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGT-VEFLVD-KHGKHYFIE 325
Cdd:PLN02735 241 LADNVVII----CSIENIDPMGVHtgdsitVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSnVQFAVNpVDGEVMIIE 316
|
....*
gi 564332048 326 VNSRL 330
Cdd:PLN02735 317 MNPRV 321
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1119-1179 |
4.64e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 41.14 E-value: 4.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564332048 1119 GKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
|
|
| PLN03228 |
PLN03228 |
methylthioalkylmalate synthase; Provisional |
722-819 |
6.39e-03 |
|
methylthioalkylmalate synthase; Provisional
Pssm-ID: 178767 [Multi-domain] Cd Length: 503 Bit Score: 40.68 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 722 EYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFP---DLPLHIHTHDTSGSGVAAMLACAQAGADVVDVA 798
Cdd:PLN03228 239 EFLCKILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKANTPgidDIVFSVHCHNDLGLATANTIAGICAGARQVEVT 318
|
90 100
....*....|....*....|.
gi 564332048 799 VDSMSGMTSQPSMGALVACTK 819
Cdd:PLN03228 319 INGIGERSGNASLEEVVMALK 339
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1105-1179 |
6.76e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 40.76 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 1105 ALKDVKgqigapMP------GKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:PRK11854 205 GVKDVN------VPdiggdeVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF 278
|
.
gi 564332048 1179 E 1179
Cdd:PRK11854 279 E 279
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
67-364 |
7.77e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 40.60 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 67 VYSEQDT---GQMHRQKA----DEAYLI--GRGLAPVQAYLHIPDIikVAKENGVDAVHpgyGFLSERADFA--QACQDA 135
Cdd:PRK02186 6 VFIESNTtgtGELLLRKAllrgFTPYFLtaNRGKYPFLDAIRVVTI--SADTSDPDRIH---RFVSSLDGVAgiMSSSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 136 gvrFIGPSPEVVRKMG-DKVEARAIAIA------------AGVPVvPGT---NSPINSLHEAHEFSntygFPIIFKAAYG 199
Cdd:PRK02186 81 ---FIEVASEVARRLGlPAANTEAIRTCrdkkrlartlrdHGIDV-PRThalALRAVALDALDGLT----YPVVVKPRMG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 200 GGGRGMRVVHSYEELEenytrAYSEALAAFGNGALFVEKFIEKPRHiEVQILGDQYGniLHLYerdcSIQRRHQ----KV 275
Cdd:PRK02186 153 SGSVGVRLCASVAEAA-----AHCAALRRAGTRAALVQAYVEGDEY-SVETLTVARG--HQVL----GITRKHLgpppHF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564332048 276 VEIA---PATHLDPQlRSRLTSDSVKLAKQVGYE-NAGTVEFLVdKHGKHYFIEVNSRLQ--VEHTVTEEITDVDLVHAQ 349
Cdd:PRK02186 221 VEIGhdfPAPLSAPQ-RERIVRTVLRALDAVGYAfGPAHTELRV-RGDTVVIIEINPRLAggMIPVLLEEAFGVDLLDHV 298
|
330
....*....|....*
gi 564332048 350 IHVSEGRSlPDLGLR 364
Cdd:PRK02186 299 IDLHLGVA-AFADPT 312
|
|
| |
