|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
35-1177 |
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 31543464 35 KPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENGVDAV 114
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 115 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFK 194
Cdd:COG1038 82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 195 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 274
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 275 VEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEG 354
Cdd:COG1038 242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 355 RSL--PDLGL-RQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIA 431
Cdd:COG1038 322 YSLddPEIGIpSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVTA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 432 HGKDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNG 511
Cdd:COG1038 402 WGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVNG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 512 PTTPIPVKVSPSPVDPIVPVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIA 591
Cdd:COG1038 482 PPGVKGRPKPDFPKPKLPKVDLGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKIA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 592 PYVAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGM 671
Cdd:COG1038 562 PATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEAGI 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 672 DVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAA 751
Cdd:COG1038 642 DVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKPYA 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 752 CTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERV 831
Cdd:COG1038 722 AYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLDAL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 832 FDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSS 911
Cdd:COG1038 801 QELSNYWEAVRKYYAPFE--SGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPSS 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 912 KIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELE 991
Cdd:COG1038 879 KVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDALR 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 992 KDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRA 1071
Cdd:COG1038 959 AELEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDED 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 1072 GQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTS 1151
Cdd:COG1038 1039 GMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITA 1118
|
1130 1140
....*....|....*....|....*.
gi 31543464 1152 PMEGTIRKVHVTKDMTLEGDDLILEI 1177
Cdd:COG1038 1119 PRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
33-1178 |
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 31543464 33 EYKPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENGVD 112
Cdd:PRK12999 1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 113 AVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPII 192
Cdd:PRK12999 81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 193 FKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQ 272
Cdd:PRK12999 161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 273 KVVEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVS 352
Cdd:PRK12999 241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 353 EGRSLPDLG---LRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKV 429
Cdd:PRK12999 321 EGATLHDLEigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 430 IAHGKDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMV 509
Cdd:PRK12999 401 TAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 510 NGPttPIPVKVSPSPVDPIV-PVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLK 588
Cdd:PRK12999 481 NGF--PGVKKKPPVFPDPRLpKVDLSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 589 KIAPYVAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKE 668
Cdd:PRK12999 559 RIAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 669 NGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLK 748
Cdd:PRK12999 639 AGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLK 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 749 PAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPL 828
Cdd:PRK12999 719 PAAAYELVSALKEEV-DLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDL 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 829 ERVFDYSEYWEGARGLYAAFdcTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVT 908
Cdd:PRK12999 798 DAIRKLSPYWEAVRPYYAPF--ESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVT 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 909 PSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLK 988
Cdd:PRK12999 876 PSSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFE 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 989 ELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDL 1068
Cdd:PRK12999 956 AERAELEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEP 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 1069 NRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETV 1148
Cdd:PRK12999 1036 DEDGMRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETT 1115
|
1130 1140 1150
....*....|....*....|....*....|
gi 31543464 1149 VTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1178
Cdd:PRK12999 1116 ITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
39-1178 |
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 31543464 39 KVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRG--LAPVQAYLHIPDIIKVAKENGVDAVHP 116
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 196
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 277 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 356
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 357 LP--DLGL-RQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIAHG 433
Cdd:TIGR01235 321 LPtpQLGVpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 434 KDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGpT 513
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNG-H 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 514 TPIPVKVSP--SPVDPIVPVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIA 591
Cdd:TIGR01235 480 PEAKDKLKPleNAPRVVVLYADQNPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 592 PYVAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGM 671
Cdd:TIGR01235 560 PTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGI 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 672 DVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAA 751
Cdd:TIGR01235 640 DIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAA 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 752 CTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERV 831
Cdd:TIGR01235 720 AKLLIKALREKT-DLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWI 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 832 FDYSEYWEGARGLYAAFDCtaTMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSS 911
Cdd:TIGR01235 799 RELSAYWEAVRNLYAAFES--DLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSS 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 912 KIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELE 991
Cdd:TIGR01235 877 KVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIR 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 992 KDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRA 1071
Cdd:TIGR01235 957 KDLQEKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQ 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 1072 GQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTS 1151
Cdd:TIGR01235 1037 GEREVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQA 1116
|
1130 1140
....*....|....*....|....*..
gi 31543464 1152 PMEGTIRKVHVTKDMTLEGDDLILEIE 1178
Cdd:TIGR01235 1117 PKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
36-497 |
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 31543464 36 PIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENGVDAVH 115
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIG-PAPAAESYLNIDAIIAAAKATGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 116 PGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKA 195
Cdd:COG4770 80 PGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 196 AYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVV 275
Cdd:COG4770 160 SAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 276 EIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGR 355
Cdd:COG4770 240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 356 SLPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKD 435
Cdd:COG4770 320 PLP---FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSMIAKLIVWGPD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543464 436 HPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQLRPAQNRA 497
Cdd:COG4770 396 REEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
37-484 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 627.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 37 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPvQAYLHIPDIIKVAKENGVDAVHP 116
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSK-KSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 196
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 277 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 356
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 357 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 436
Cdd:PRK08591 321 LS---IKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHGETR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 31543464 437 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDEN 484
Cdd:PRK08591 397 EEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
38-487 |
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 31543464 38 KKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHPG 117
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPA-PPSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 118 YGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAAY 197
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 198 GGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEI 277
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 278 APATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKhGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRSL 357
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN-GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 358 PdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHP 437
Cdd:PRK08654 321 S---FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVD-SGVHMGYEIPPYYDSMISKLIVWGRTRE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 31543464 438 TAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPEL 487
Cdd:PRK08654 397 EAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
37-481 |
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 31543464 37 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENGVDAVHP 116
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIG-GPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 196
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 277 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 356
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 357 LPdlgLRQENIRINGCAIQCRVTTEDPaRSFQPDTGRIEVFRSGEGMGIRLDNASAfQGAVISPHYDSLLVKVIAHGKDH 436
Cdd:PRK06111 321 LS---FTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMIAKLIAHGETR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 31543464 437 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFI 481
Cdd:PRK06111 396 EEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
37-489 |
1.49e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 537.76 E-value: 1.49e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 37 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlaPVQAYLHIPDIIKVAKENGVDAVHP 116
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD--PLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 196
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 277 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 356
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 357 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 436
Cdd:PRK07178 320 LS---YKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTA-IYTGYTIPPYYDSMCAKLIVWALTW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 31543464 437 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFQ 489
Cdd:PRK07178 396 EEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTN 448
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
37-484 |
7.09e-178 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 530.05 E-value: 7.09e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 37 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHP 116
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPA-SSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 196
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 277 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 356
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 357 lpdLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 436
Cdd:PRK05586 321 ---LSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSA-VYSGYTIPPYYDSMIGKLIVYGKDR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 31543464 437 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDEN 484
Cdd:PRK05586 397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKK 444
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
37-483 |
1.41e-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: 1.41e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 37 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHP 116
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPA-PSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAA 196
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 277 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 356
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 357 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 436
Cdd:TIGR00514 321 LS---LKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSH-VYSGYTVPPYYDSMIGKLITYGKTR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 31543464 437 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDE 483
Cdd:TIGR00514 397 EVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
35-482 |
6.64e-164 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 494.27 E-value: 6.64e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 35 KPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPvQAYLHIPDIIKVAKENGVDAV 114
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAA-KSYLNPAAILAAARQCGADAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 115 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFK 194
Cdd:PRK12833 82 HPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 195 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYgNILHLYERDCSIQRRHQKV 274
Cdd:PRK12833 162 AAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 275 VEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKH-GKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSE 353
Cdd:PRK12833 241 LEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDArGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 354 GRSlpdLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHG 433
Cdd:PRK12833 321 GEP---LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVD-SLLYPGYRVPPFYDSLLAKLIVHG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 31543464 434 KDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFID 482
Cdd:PRK12833 397 EDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
565-848 |
3.57e-162 |
|
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163675 Cd Length: 275 Bit Score: 482.32 E-value: 3.57e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 565 LMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFnnLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 644
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 645 GANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDvadpsrTKYSLEYYM 724
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 725 GLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPdLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGM 804
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 31543464 805 TSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAF 848
Cdd:cd07937 232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
37-499 |
3.07e-158 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 480.08 E-value: 3.07e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 37 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlaPVQAYLHIPDIIKVAKENGVDAVHP 116
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTD--PIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTnSPIN--SLHEAHEFSNTYGFPIIFK 194
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGT-EKLNseSMEEIKIFARKIGYPVILK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 195 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 274
Cdd:PRK08463 159 ASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 275 VEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEG 354
Cdd:PRK08463 239 IEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 355 RSLPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGK 434
Cdd:PRK08463 319 EILD---LEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVD-SHIYKDYTIPPYYDSMLAKLIVKAT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543464 435 DHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDENPELFqLRPAQNRAQK 499
Cdd:PRK08463 395 SYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQEL-LEKTEDRHQE 458
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
35-484 |
1.13e-157 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 477.31 E-value: 1.13e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 35 KPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENGVDAV 114
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIG-GAKSSESYLNIPAIISAAEIFEADAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 115 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFK 194
Cdd:PRK08462 81 FPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 195 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 274
Cdd:PRK08462 161 AAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 275 VEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEG 354
Cdd:PRK08462 241 IEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 355 RSLPDlglrQENIRINGCAIQCRVTTEDPaRSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGK 434
Cdd:PRK08462 321 EELPS----QESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMD-SHAYAGYVVPPYYDSMIGKLIVWGE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 31543464 435 DHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGIVDTQFIDEN 484
Cdd:PRK08462 395 DRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
567-1178 |
4.82e-154 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 473.56 E-value: 4.82e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 567 DTTFRDAHQSLLATRVRTHDLKKIAP------YvahnfnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQ 640
Cdd:PRK09282 8 DTTLRDAHQSLLATRMRTEDMLPIAEkldkvgF--------WSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 641 MLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysL 720
Cdd:PRK09282 80 MLLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT---TSPVHT---I 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 721 EYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDS 800
Cdd:PRK09282 154 EKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEV-DLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 801 MSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMksGNSDVYENEIPGGQYTNLHFQAHS 880
Cdd:PRK09282 233 LAFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTI--VDTRVLIHQVPGGMISNLVSQLKE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 881 MGLGSKFKEVKK--AYVEANqmLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGYIGIPHGG 958
Cdd:PRK09282 311 QNALDKLDEVLEeiPRVRED--LGYPPLVTPTSQIVGTQAVLNVLTG-ERYK--------VITKEVKDYVKGLYGRPPAP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 959 FPEPFRSKVLKDLPRIEGRPGASLPPlnlkELEKdlIDRHGEE---VTPEDVLSAAMYPDV----FAQFKDFTATFGPLD 1031
Cdd:PRK09282 380 INEELRKKIIGDEEPITCRPADLLEP----ELEK--ARKEAEElgkSEKEDVLTYALFPQIakkfLEEREAGELKPEPEP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 1032 SLNTRlfLQGPKIAEEFEVELErGKTLHIKALAVSdlnRAGQRQVFFELNGQLRSILVkdtQAMKEMHFHPKALKDVKGQ 1111
Cdd:PRK09282 454 KEAAA--AGAEGIPTEFKVEVD-GEKYEVKIEGVK---AEGKRPFYLRVDGMPEEVVV---EPLKEIVVGGRPRASAPGA 524
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543464 1112 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1178
Cdd:PRK09282 525 VTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
563-1020 |
1.99e-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: 1.99e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 563 LLLMDTTFRDAHQSLLATRVRTHDLKKIAPY-VAHNFnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQM 641
Cdd:COG5016 4 VKITDTTLRDGHQSLFATRMRTEDMLPIAEKlDEAGF---WSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 642 LLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVAdpsrtkYSLE 721
Cdd:COG5016 81 LLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYTISPV------HTVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 722 YYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSM 801
Cdd:COG5016 155 YYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEAL-DIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 802 SGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMKsgNSDVYENEIPGGQYTNLHFQAHSM 881
Cdd:COG5016 234 AGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGV--DPRVLVHQVPGGMLSNLVSQLKEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 882 GLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGYIGIPHGGFPE 961
Cdd:COG5016 312 GALDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG-ERYK--------MITKEVKDYVLGYYGKTPAPIDP 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 31543464 962 PFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIdrhgeEVTPEDVLSAAMYPDVFAQF 1020
Cdd:COG5016 383 EVRKKALGDEEPITCRPADLLEP-ELEKLRKEGL-----AKSDEDVLTYALFPQVAIKF 435
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
567-1168 |
4.41e-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: 4.41e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 567 DTTFRDAHQSLLATRVRTHDLKKIAPyvAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGA 646
Cdd:TIGR01108 3 DVVLRDAHQSLFATRMRTEDMLPIAE--KLDDVGYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLRGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 647 NAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEYYMGL 726
Cdd:TIGR01108 81 NLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT---TSPVHT---LETYLDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 727 AEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMTS 806
Cdd:TIGR01108 155 AEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRF-GLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 807 QPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSK 886
Cdd:TIGR01108 234 HPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFE--GQLKGPDSRILVAQVPGGMLSNLESQLKEQNALDK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 887 FKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEAEAqaeelsfpRSVVEFLQGYIGIPHGGFPEPFRSK 966
Cdd:TIGR01108 312 LDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG-ERYKTIT--------KETKGYLKGEYGRTPAPINAELQRK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 967 VLKDL-PRIEGRPGASLPPlNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLntrlfLQGPKIA 1045
Cdd:TIGR01108 383 ILGDEkPIVDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQVGLKFLENRHNPAAFEPK-----PEEKVIE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 1046 EEfevelergktlHIKAlAVSDLNRAGQRQVFFELNGQLRSILVKD-------TQAMKEMHFHPKALKDVK--GQIGAPM 1116
Cdd:TIGR01108 457 QE-----------HAQV-VGKYEETHASGSYTVEVEGKAFVVKVSPggdvsqiTASAPANTSGGTVAAKAGagTPVTAPI 524
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 31543464 1117 PGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKV------HVTKDMTL 1168
Cdd:TIGR01108 525 AGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREIlvkvgdAVSVGQVL 582
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
563-1171 |
1.12e-101 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 334.21 E-value: 1.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 563 LLLMDTTFRDAHQSLLATRVRTHDLKKIAP------YvahnfnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPN 636
Cdd:PRK14040 5 LAITDVVLRDAHQSLFATRLRLDDMLPIAAkldkvgY--------WSLESWGGATFDACIRFLGEDPWERLRELKKAMPN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 637 IPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRT 716
Cdd:PRK14040 77 TPQQMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT---TSPVHT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 717 kysLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDV 796
Cdd:PRK14040 154 ---LQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRV-DVPLHLHCHATTGLSTATLLKAIEAGIDGVDT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 797 AVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHF 876
Cdd:PRK14040 230 AISSMSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFE--GQLKGVDSRILVAQVPGGMLTNMES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 877 QAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGyigiPH 956
Cdd:PRK14040 308 QLKEQGAADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQAVLNVLTG-ERYK--------TITKETAGVLKG----EY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 957 GGFPEPF----RSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRHGE------EVTPEDVLSAAMYPDV---FAQFKDF 1023
Cdd:PRK14040 375 GATPAPVnaelQARVLEGAEPITCRPADLLAP-ELDKLEAELRRQAQEkgitlaENAIDDVLTYALFPQIglkFLENRHN 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 1024 TATFGPLDSL-NTRLFLQGPKIAEE-FEVELErGKTLHIKalaVSDlnragqrqvffelNGQLRSILVKDTQAMKEMHFH 1101
Cdd:PRK14040 454 PAAFEPVPQAeAAQPAAKAEPAGSEtYTVEVE-GKAYVVK---VSE-------------GGDISQITPAAPAAAPAAAAA 516
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 1102 PKALKDVKGQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTkdmtlEGD 1171
Cdd:PRK14040 517 AAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVK-----EGD 581
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
565-1020 |
1.49e-97 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 318.18 E-value: 1.49e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 565 LMDTTFRDAHQSLLATRVRTHDLKKIApyvaHNFNNL--FSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQML 642
Cdd:PRK12331 6 ITETVLRDGQQSLIATRMTTEEMLPIL----EKLDNAgyHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 643 LRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEY 722
Cdd:PRK12331 82 LRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT---TSPVHT---IDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 723 YMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTsgSGVAAM--LACAQAGADVVDVAVDS 800
Cdd:PRK12331 156 FVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAV-TVPLEVHTHAT--SGIAEMtyLKAIEAGADIIDTAISP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 801 MSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLY-AAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAH 879
Cdd:PRK12331 233 FAGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYrEEGILNPKVKDVEPKTLIYQVPGGMLSNLLSQLK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 880 SMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEAeaqaeelsFPRSVVEFLQGYIGIPHGGF 959
Cdd:PRK12331 313 EQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALMNVISG-ERYKM--------VPNEIKDYVRGLYGRPPAPI 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543464 960 PEPFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRHGEEvtpEDVLSAAMYPDVFAQF 1020
Cdd:PRK12331 384 AEEIKKKIIGDEEVITCRPADLIEP-QLEKLREEIAEYAESE---EDVLSYALFPQQAKDF 440
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
861-1061 |
3.43e-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: 3.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 861 VYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSF 940
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 941 PRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQF 1020
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 31543464 1021 KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIK 1061
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
564-1178 |
7.16e-91 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 305.11 E-value: 7.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 564 LLMDTTFRDAHQSLLATRVRTHDLKKIAPYVahNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLL 643
Cdd:PRK14042 5 FITDVTLRDAHQCLIATRMRTEDMLPICNKM--DDVGFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSMLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 644 RGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvadpSRTKYSLEYY 723
Cdd:PRK14042 83 RGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT------TSPVHTLDNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 724 MGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRdRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSG 803
Cdd:PRK14042 157 LELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLK-QATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 804 MTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMKSGNSDVYenEIPGGQYTNLHFQAHSMGL 883
Cdd:PRK14042 236 GASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLY--QVPGGMISNLYNQLKEQNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 884 GSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlsraeaeaqAEELSFPRSVVEFLQGYIGIPHGGFPEPF 963
Cdd:PRK14042 314 LDKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQAVINVLTG---------ERYKTITNEVKLYCQGKYGTPPGKISSAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 964 RSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRhgeEVTPEDVLSAAMYPDVFAQFKDFTATFGPL-DSLNTRLFLQGP 1042
Cdd:PRK14042 385 RKKAIGRTEVIEVRPGDLLPN-ELDQLQNEISDL---ALSDEDVLLYAMFPEIGRQFLEQRKNNQLIpEPLLTQSSAPDN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 1043 KIAEEFEVELErGKTLHIKaLAVSDLNRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVID 1122
Cdd:PRK14042 461 SVMSEFDIILH-GESYHVK-VAGYGMIEHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPGSIIA 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 31543464 1123 VKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1178
Cdd:PRK14042 539 IHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
564-1053 |
5.25e-90 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 298.24 E-value: 5.25e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 564 LLMDTTFRDAHQSLLATRVRTHDLKKIAPyvAHNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLL 643
Cdd:PRK14041 4 MFVDTTLRDGHQSLIATRMRTEDMLPALE--AFDRMGFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQMLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 644 RGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEYY 723
Cdd:PRK14041 82 RGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT---VSPVHT---LEYY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 724 MGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSG 803
Cdd:PRK14041 156 LEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 804 MTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGL 883
Cdd:PRK14041 235 GTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYD--VGMKSPDSRILVSQIPGGMYSNLVKQLKEQKM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 884 GSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEaqaeelsfpRSVVEFLQGYIGIPHGGFPEPF 963
Cdd:PRK14041 313 LHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQAVLNVLTGERYKRVT---------NETKNYVKGLYGRPPAPIDEEL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 964 RSKVLKDLPRIEGRPGASLPPlnlkELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFkdftatfgpldsLNTRlFLQGPK 1043
Cdd:PRK14041 384 MKKILGDEKPIDCRPADLLEP----ELEKARKELGILAETDEDLLIYVILGEVGKKF------------LKKK-YEEKIG 446
|
490
....*....|
gi 31543464 1044 IAEEFEVELE 1053
Cdd:PRK14041 447 VDFNLLEELS 456
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
571-1020 |
8.01e-82 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 276.64 E-value: 8.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 571 RDAHQSLLATRVRTHDLKKI------APYvahnfnnlFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 644
Cdd:PRK12330 13 RDAHQSLMATRMAMEDMVGAcedidnAGY--------WSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQMLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 645 GANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEYYM 724
Cdd:PRK12330 85 GQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT---VSPIHT---VEGFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 725 GLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRF-PDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMS- 802
Cdd:PRK12330 159 EQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSMSl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 803 GMTSQPSMgALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATmkSGNSDVYENEIPGGQYTNLHFQAHSMG 882
Cdd:PRK12330 239 GPGHNPTE-SLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTT--GVETEIFKSQIPGGMLSNMESQLKQQG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 883 LGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlsraeaeaqaeelSFPRSVVEF---LQGYIGIPhggf 959
Cdd:PRK12330 316 AGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVFNVLMG-------------RYKVLTGEFadlMLGYYGET---- 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543464 960 PEPFRSKVLKDLPR------IEGRPGASLPPlNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQF 1020
Cdd:PRK12330 379 PGERNPEVVEQAKKqakkepITCRPADLLEP-EWDKLRAEALALEGCDGSDEDVLTYALFPQVAPKF 444
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
151-358 |
1.47e-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: 1.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 151 DKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGN 230
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 231 GALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTV 310
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 31543464 311 EFLVD-KHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRSLP 358
Cdd:pfam02786 161 EFALDpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
566-839 |
1.16e-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: 1.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 566 MDTTFRDAHQSLLATRvRTHDLKKIAPYVAHNfnNLFSIENWGGATFDVAmrFLYECPWRRLQELRELIPNIPFQMLLRG 645
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEA--GVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 646 anavgytnypdnvVFKFCEVAKENGMDVFRIFDSLNY--------------LPNMLLGMEAAGSAGGVVEAAISYTgdva 711
Cdd:cd03174 76 -------------REKGIERALEAGVDEVRIFDSASEthsrknlnksreedLENAEEAIEAAKEAGLEVEGSLEDA---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 712 dpSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGA 791
Cdd:cd03174 139 --FGCKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 31543464 792 DVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWE 839
Cdd:cd03174 217 DRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
560-1041 |
7.72e-66 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 230.78 E-value: 7.72e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 560 HQGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVahNFNNLFSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPF 639
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDMLPVLTIL--DKIGYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 640 QMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRIFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvadpSRTKYS 719
Cdd:PRK12581 88 QMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT------TSPVHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 720 LEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRdRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVD 799
Cdd:PRK12581 162 LNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIK-AMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 800 SMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAfDCT--ATMKSGNSDVYENEIPGGQYTNLHFQ 877
Cdd:PRK12581 241 PFSEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYLA-DGIldPSLLFPDPRTLQYQVPGGMLSNMLSQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 878 AHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEaqaeelsfpRSVVEFLQGYIGIPHG 957
Cdd:PRK12581 320 LKQANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVILGKPYQMVS---------KEIKQYLAGDYGKTPA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 958 GFPEPFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRhgeEVTPEDVLSAAMYPDVFAQFkdFTATFGPLDSLNTRL 1037
Cdd:PRK12581 391 PVNEDLKRSQIGSAPVTTNRPADQLSP-EFEVLKAEVADL---AQTDEDVLTYALFPSVAKPF--LTTKYQTDDVIKVTA 464
|
....
gi 31543464 1038 FLQG 1041
Cdd:PRK12581 465 FIKA 468
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
37-145 |
2.80e-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: 195.40 E-value: 2.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 37 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHP 116
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPG-PASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*....
gi 31543464 117 GYGFLSERADFAQACQDAGVRFIGPSPEV 145
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
98-355 |
1.16e-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: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 98 HIPDIIKVAKE----NGVDAVHPGYGFLSERAdfAQACQDAGVRfiGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTnsP 173
Cdd:COG0439 1 DIDAIIAAAAElareTGIDAVLSESEFAVETA--AELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFA--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 174 INSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKpRHIEVQILGDQ 253
Cdd:COG0439 75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVRD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 254 yGNILHlyerdCSIQRRHQK---VVE---IAPAThLDPQLRSRLTSDSVKLAKQVGYEN-AGTVEFLVDKHGKHYFIEVN 326
Cdd:COG0439 154 -GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYLIEIN 226
|
250 260 270
....*....|....*....|....*....|.
gi 31543464 327 SRLQVEH--TVTEEITDVDLVHAQIHVSEGR 355
Cdd:COG0439 227 ARLGGEHipPLTELATGVDLVREQIRLALGE 257
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
375-482 |
2.72e-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: 2.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 375 QCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRG 454
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVD-SGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 31543464 455 VKTNIPFLQNVLNNQQFLAGIVDTQFID 482
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
375-483 |
2.83e-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: 2.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 375 QCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRG 454
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVD-SGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 31543464 455 VKTNIPFLQNVLNNQQFLAGIVDTQFIDE 483
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
565-837 |
3.17e-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: 118.21 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 565 LMDTTFRDAHQSLlATRVRTHDLKKIAPyvahnfnnlfSIENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 644
Cdd:pfam00682 4 ICDTTLRDGEQAL-GVAFSIDEKLAIAR----------ALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 645 GAnavgytnypDNVVFKFCEVAKENGMDVFRIFDSLNYLP-NMLLGM---EAAGSAGGVVEAAISYTGDVA----DPSRT 716
Cdd:pfam00682 73 AR---------EHDIKAAVEALKGAGAVRVHVFIATSDLHrKYKLGKdreEVAKRAVAAVKAARSRGIDVEfspeDASRT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 717 kySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPD-LPLHIHTHDTSGSGVAAMLACAQAGADVVD 795
Cdd:pfam00682 144 --DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVD 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 31543464 796 VAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEY 837
Cdd:pfam00682 222 GTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANL 263
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1111-1177 |
1.94e-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: 1.94e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543464 1111 QIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1177
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1111-1177 |
1.44e-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: 81.11 E-value: 1.44e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543464 1111 QIGAPMPGKVID-----VKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1177
Cdd:pfam00364 2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
35-329 |
4.04e-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: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 35 KPIKKVMVANRGEIAI-----------RVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIgrglaPVQAYlHIPDII 103
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIgqaaefdysgsQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIE-----PLTPE-AVEKII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 104 KvaKENgVDAVHPGYG---------FLSERAdfaqACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGtnSPI 174
Cdd:TIGR01369 78 E--KER-PDAILPTFGgqtalnlavELEESG----VLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 175 NSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRayseALAAFGNGALFVEKFIEKPRHIEVQILGDQY 254
Cdd:TIGR01369 149 HSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAER----ALSASPINQVLVEKSLAGWKEIEYEVMRDSN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 255 GNILHLyerdCSIQR-----RH--QKVVeIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVD-KHGKHYFIEVN 326
Cdd:TIGR01369 225 DNCITV----CNMENfdpmgVHtgDSIV-VAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNpDSGRYYVIEVN 299
|
...
gi 31543464 327 SRL 329
Cdd:TIGR01369 300 PRV 302
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1110-1178 |
8.13e-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: 8.13e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31543464 1110 GQIGAPMPGKV-------IDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1178
Cdd:COG0511 61 GAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
101-413 |
1.62e-13 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 75.39 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 101 DIIKVAKENGVDAVHPGYGflSERA-DFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSpiNSLHE 179
Cdd:PRK12815 621 DVLNVAEAENIKGVIVQFG--GQTAiNLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTA--TDEEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 180 AHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSealaafGNGALFVEKFIEKpRHIEVQILGDQY----- 254
Cdd:PRK12815 697 AFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENAS------QLYPILIDQFIDG-KEYEVDAISDGEdvtip 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 255 GNILHLYER-----DcSIQrrhqkvveIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVdKHGKHYFIEVNSRl 329
Cdd:PRK12815 770 GIIEHIEQAgvhsgD-SIA--------VLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVLEVNPR- 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 330 qVEHTV--TEEITDVDLVHAQIHVSEGRSLPDLGLRQENIRINGcaiqcRVTTEDPARSFQ--PDTGRI---EVFRSGEG 402
Cdd:PRK12815 839 -ASRTVpfVSKATGVPLAKLATKVLLGKSLAELGYPNGLWPGSP-----FIHVKMPVFSYLkyPGVDNTlgpEMKSTGEV 912
|
330
....*....|.
gi 31543464 403 MGIRLDNASAF 413
Cdd:PRK12815 913 MGIDKDLEEAL 923
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1112-1174 |
9.55e-13 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 66.37 E-value: 9.55e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31543464 1112 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLE-GDDLI 1174
Cdd:PRK06549 64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNpGDGLI 127
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
128-419 |
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 31543464 128 AQACQDAGVRFIGPSPEVVrkmgDKVEARAIAIAA----GVPVVPGtnSPINSLHEAHEFSNTYGFPIIFKAAYGGGGRG 203
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESI----DRAEDREKFSELldelGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 204 MRVVHSYEELeenyTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQ-----YGNILHLyER------DCSIqrrhq 272
Cdd:TIGR01369 720 MEIVYNEEEL----RRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGeevliPGIMEHI-EEagvhsgDSTC----- 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 273 kvveIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVdKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVS 352
Cdd:TIGR01369 790 ----VLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV-KDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVM 864
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543464 353 EGRSLPDLGLRQEniringcAIQCRVTTEDPARSFQPDTGR-----IEVFRSGEGMGIRLDNASAFQGAVIS 419
Cdd:TIGR01369 865 LGKKLEELGVGKE-------KEPKYVAVKEPVFSFSKLAGVdpvlgPEMKSTGEVMGIGRDLAEAFLKAQLS 929
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
128-328 |
1.15e-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: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 128 AQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTnsPINSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVV 207
Cdd:COG0458 91 EEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSG--TATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 208 HSYEELEEnytrAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNIL------HLyER------DcSIqrrhqkVV 275
Cdd:COG0458 169 YNEEELEE----YLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIivgimeHI-EPagvhsgD-SI------CV 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 31543464 276 eiAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKhGKHYFIEVNSR 328
Cdd:COG0458 237 --APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDD-GRVYVIEVNPR 286
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1110-1174 |
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 31543464 1110 GQIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLE-GDDLI 1174
Cdd:PRK05641 85 NVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDtGQPLI 150
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
100-347 |
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 31543464 100 PDIIKVAKENGVDAVHPGYGFLSERADFAQACQDAGVRFIgPSPEVVRKMGDKVEARAIAIAAGVPVvpgtnsP----IN 175
Cdd:COG0189 46 PELYRGEDLSEFDAVLPRIDPPFYGLALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPV------PptlvTR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 176 SLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEenytrAYSEALAAFGNGALFVEKFIEKPRHIEVQI--LGDQ 253
Cdd:COG0189 119 DPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALE-----SILEALTELGSEPVLVQEFIPEEDGRDIRVlvVGGE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 254 YgniLHLYER-----DCSIQRRHQKVVEiapATHLDPQLRSRLtsdsVKLAKQVGYENAGtVEFLVDKHGkHYFIEVNSR 328
Cdd:COG0189 194 P---VAAIRRipaegEFRTNLARGGRAE---PVELTDEERELA----LRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVT 261
|
250
....*....|....*....
gi 31543464 329 LQVEHtvTEEITDVDLVHA 347
Cdd:COG0189 262 PGFRG--LERATGVDIAEA 278
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1111-1178 |
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 31543464 1111 QIGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTK-DMTLEGDDLiLEIE 1178
Cdd:PRK08225 3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEgDFVNEGDVL-LEIE 70
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
690-798 |
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 31543464 690 MEAAGSAGGVVEAAIS------YTGDVaDPSRTkysleyyMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRF 763
Cdd:cd07938 120 AELAKAAGLRVRGYVStafgcpYEGEV-PPERV-------AEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERF 191
|
90 100 110
....*....|....*....|....*....|....*
gi 31543464 764 PDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAV 798
Cdd:cd07938 192 PDEKLALHFHDTRGQALANILAALEAGVRRFDSSV 226
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
151-326 |
2.33e-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: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 151 DKVEARAIAIAAGVPVVPGTNSPINSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEALaAFGN 230
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAA----ALEEAF-KYDD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 231 GALfVEKFIEkPRHIEVQILGDQYGNILHL---------------YERDcsiqrrhqKVVEIAPAtHLDPQLRSRLTSDS 295
Cdd:COG1181 170 KVL-VEEFID-GREVTVGVLGNGGPRALPPieivpengfydyeakYTDG--------GTEYICPA-RLPEELEERIQELA 238
|
170 180 190
....*....|....*....|....*....|.
gi 31543464 296 VKLAKQVGYENAGTVEFLVDKHGKHYFIEVN 326
Cdd:COG1181 239 LKAFRALGCRGYARVDFRLDEDGEPYLLEVN 269
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
699-798 |
7.31e-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: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 699 VVEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHD 774
Cdd:COG0119 124 AVKYAKEHGLEVEfsaeDATRT--DPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHN 201
|
90 100
....*....|....*....|....
gi 31543464 775 TSGSGVAAMLACAQAGADVVDVAV 798
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 ... |
161-326 |
2.33e-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: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 161 AAGVPVVP-----GTNSPINSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEALAAfgNGALFV 235
Cdd:pfam07478 4 AAGLPVVPfvtftRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQA----AIEEAFQY--DEKVLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 236 EKFIEKpRHIEVQILGDQYGNILHLYER--DCSIQRRHQKVVE-----IAPAtHLDPQLRSRLTSDSVKLAKQVGYENAG 308
Cdd:pfam07478 78 EEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDdsaqiVVPA-DLEEEQEEQIQELALKAYKALGCRGLA 155
|
170
....*....|....*...
gi 31543464 309 TVEFLVDKHGKHYFIEVN 326
Cdd:pfam07478 156 RVDFFLTEDGEIVLNEVN 173
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
78-328 |
8.00e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 52.58 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 78 QKADEAYLIGRGLAPvqAYlhIPDIIKVAKENGVDAVHPGY----GFLSE-RADFaqacQDAGVRFIGPSPEVVRKMGDK 152
Cdd:PRK12767 41 YFADKFYVVPKVTDP--NY--IDRLLDICKKEKIDLLIPLIdpelPLLAQnRDRF----EEIGVKVLVSSKEVIEICNDK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 153 VEARAIAIAAGVPVvPGTNSPINSLH-EAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEenytRAYSEalaafgNG 231
Cdd:PRK12767 113 WLTYEFLKENGIPT-PKSYLPESLEDfKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEY------VP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 232 ALFVEKFIEkprHIE--VQILGDQYGNILHlyerdcSIQRRHQKVV--EIAPA-THLDPQLRSRLtsdsVKLAKQVGYEN 306
Cdd:PRK12767 182 NLIIQEFIE---GQEytVDVLCDLNGEVIS------IVPRKRIEVRagETSKGvTVKDPELFKLA----ERLAEALGARG 248
|
250 260
....*....|....*....|..
gi 31543464 307 AGTVEFLVDKhGKHYFIEVNSR 328
Cdd:PRK12767 249 PLNIQCFVTD-GEPYLFEINPR 269
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
135-329 |
2.32e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 51.89 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 135 GVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVvpgTNSPI-NSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEEL 213
Cdd:PRK12815 112 GVELLGTNIEAIQKGEDRERFRALMKELGEPV---PESEIvTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 214 EENYTRAysEALAAFGNgaLFVEKFIEKPRHIEVQILGDQYGNILHLyerdCSIQRrhqkvVE-----------IAPATH 282
Cdd:PRK12815 189 EQLFKQG--LQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCITV----CNMEN-----IDpvgihtgdsivVAPSQT 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 31543464 283 LDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYF-IEVNSRL 329
Cdd:PRK12815 256 LTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYlIEVNPRV 303
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
712-798 |
2.78e-06 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 51.48 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 712 DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRfPDLPLHIHTHDTSGSGVAAMLACAQAGA 791
Cdd:PRK09389 136 DASRA--DLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSEL-VKGPVSIHCHNDFGLAVANTLAALAAGA 212
|
....*..
gi 31543464 792 DVVDVAV 798
Cdd:PRK09389 213 DQVHVTI 219
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
128-368 |
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 31543464 128 AQACQDAGVRFIGPSPEVVrkmgDKVEAR----AIAIAAGVPvvpgtnSPIN----SLHEAHEFSNTYGFPIIFKAAYGG 199
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAI----DLAEDRerfsKLLEKLGIP------QPPNgtatSVEEALEVAEEIGYPVLVRPSYVL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 200 GGRGMRVVHSYEELEEnYTRaysEALAAFGNGALFVEKFIEKPRHIEVQILGD----QYGNIL-HLyER------D--CS 266
Cdd:PRK05294 716 GGRAMEIVYDEEELER-YMR---EAVKVSPDHPVLIDKFLEGAIEVDVDAICDgedvLIGGIMeHI-EEagvhsgDsaCS 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 267 IqrrhqkvveiaPATHLDPQLRSRLTSDSVKLAKQ---VGYENagtVEFLVdKHGKHYFIEVN---SRlqvehTV--TEE 338
Cdd:PRK05294 791 L-----------PPQTLSEEIIEEIREYTKKLALElnvVGLMN---VQFAV-KDDEVYVIEVNpraSR-----TVpfVSK 850
|
250 260 270
....*....|....*....|....*....|
gi 31543464 339 ITDVDLVHAQIHVSEGRSLPDLGLRQENIR 368
Cdd:PRK05294 851 ATGVPLAKIAARVMLGKKLAELGYTKGLIP 880
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1111-1177 |
3.70e-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: 3.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543464 1111 QIGAPM-PGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1177
Cdd:COG0508 9 DLGESMtEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
700-798 |
5.07e-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: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 700 VEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFP--DLPLHIHTH 773
Cdd:cd07940 120 VEYAKSHGLDVEfsaeDATRT--DLDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPniKVPISVHCH 197
|
90 100
....*....|....*....|....*
gi 31543464 774 DTSGSGVAAMLACAQAGADVVDVAV 798
Cdd:cd07940 198 NDLGLAVANSLAAVEAGARQVECTI 222
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
141-324 |
1.73e-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: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 141 PSPEVVRKMGDKVEARAIAIAAGVPVVPgtNSPINSLHEAHEFSNTYGFPIIFKAAyggggrgmR---------VVHSYE 211
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAP--FAAVDSLEDLEAAIAELGLPAVLKTR--------RggydgkgqvVIKSAA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 212 ELEenytraysEALAAFGNGALFVEKFI--EKprhiEVQILG--DQYGNILHlY---ErdcSIQRRHQKVVEIAPAtHLD 284
Cdd:COG0026 149 DLE--------AAWAALGGGPCILEEFVpfER----ELSVIVarSPDGEVAT-YpvvE---NVHRNGILDESIAPA-RIS 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 31543464 285 PQLRSRLTSDSVKLAKQVGYenAGT--VEFLVDKHGK--------------HYFIE 324
Cdd:COG0026 212 EALAAEAEEIAKRIAEALDY--VGVlaVEFFVTKDGEllvneiaprphnsgHWTIE 265
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
723-804 |
2.09e-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: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 723 YMGLAEELVR-------AGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVD 795
Cdd:cd07943 136 HMASPEELAEqaklmesYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRID 215
|
....*....
gi 31543464 796 VavdSMSGM 804
Cdd:cd07943 216 G---SLAGL 221
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
151-326 |
2.78e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 47.41 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 151 DKVEARAIAIAAGVPVVPGT--NSPINSLHEAHEFsntyGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEAlAAF 228
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIvlTREEDLLAAIDKL----GLPLVVKPAREGSSVGVSKVKEEDELQA----ALELA-FKY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 229 GNGALfVEKFIeKPRHIEVQILGDQygnILhlyerdcsiqrrhqKVVEIAPATH--------------------LDPQLR 288
Cdd:PRK01372 169 DDEVL-VEKYI-KGRELTVAVLGGK---AL--------------PVIEIVPAGEfydyeakylaggtqyicpagLPAEIE 229
|
170 180 190
....*....|....*....|....*....|....*...
gi 31543464 289 SRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVN 326
Cdd:PRK01372 230 AELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVN 267
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
138-326 |
3.98e-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: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 138 FIGPSPEVVRKMGDKVEARAIAIAAGVPVVPgtNSPINsLHE--------AHEFSNTYGFPIIFKAAYGGGGRGMRVVHS 209
Cdd:PRK14573 555 YTGPSLAFSAIAMDKVLTKRFASDVGVPVVP--YQPLT-LAGwkrepelcLAHIVEAFSFPMFVKTAHLGSSIGVFEVHN 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 210 YEELEEnytrAYSEALAAfgNGALFVEKFIEKPRHIEVQILGDQYGN--ILHLYERdC------SIQRRH----QKVVEI 277
Cdd:PRK14573 632 VEELRD----KISEAFLY--DTDVFVEESRLGSREIEVSCLGDGSSAyvIAGPHER-RgsggfiDYQEKYglsgKSSAQI 704
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 31543464 278 APATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVN 326
Cdd:PRK14573 705 VFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMN 753
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1114-1177 |
7.50e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 42.10 E-value: 7.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31543464 1114 APMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1177
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
717-839 |
9.26e-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: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 717 KYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDV 796
Cdd:cd07945 143 RDSPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVLAAVKAGIKGLHT 222
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 31543464 797 AVDSMSGMTSQPSMGALVACTKG-TPLDTEVPLERVFDYSEYWE 839
Cdd:cd07945 223 TVNGLGERAGNAPLASVIAVLKDkLKVKTNIDEKRLNRASRLVE 266
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1112-1178 |
1.59e-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: 1.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543464 1112 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1178
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
712-798 |
2.62e-04 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 44.78 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 712 DPSRTKYS-LEYYMGLAEElvrAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGSGVAAMLACAQAG 790
Cdd:PRK11858 138 DASRTDLDfLIEFAKAAEE---AGADRVRFCDTVGILDPFTMYELVKELVEAV-DIPIEVHCHNDFGMATANALAGIEAG 213
|
....*...
gi 31543464 791 ADVVDVAV 798
Cdd:PRK11858 214 AKQVHTTV 221
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
37-328 |
2.99e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 45.09 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 37 IKKVMVANRGEI--------------AIRVFRactELGIRTVAVYSEQDTGQMHRQKADEAYLIgrglaPVQaylhiPDI 102
Cdd:PRK05294 7 IKKILIIGSGPIvigqacefdysgtqACKALR---EEGYRVVLVNSNPATIMTDPEMADATYIE-----PIT-----PEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 103 I-KV-AKENgVDAVHPGYG---------------FLSERadfaqacqdaGVRFIGPSPEVVRKMGDKVEARAIAIAAGVP 165
Cdd:PRK05294 74 VeKIiEKER-PDAILPTMGgqtalnlavelaesgVLEKY----------GVELIGAKLEAIDKAEDRELFKEAMKKIGLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 166 VVPGTnsPINSLHEAHEFSNTYGFPIIFKAAYGgggrgM-----RVVHSYEELEENYTRayseALAAFGNGALFVEKFIE 240
Cdd:PRK05294 143 VPRSG--IAHSMEEALEVAEEIGYPVIIRPSFT-----LggtggGIAYNEEELEEIVER----GLDLSPVTEVLIEESLL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 241 KPRHIEVQILGDQYGN--ILhlyerdCSIqrrhqkvvE--------------IAPATHLDPQLRSRLTSDSVKLAKQVGY 304
Cdd:PRK05294 212 GWKEYEYEVMRDKNDNciIV------CSI--------EnidpmgvhtgdsitVAPAQTLTDKEYQMLRDASIAIIREIGV 277
|
330 340
....*....|....*....|....*.
gi 31543464 305 ENAGT-VEFLVD-KHGKHYFIEVNSR 328
Cdd:PRK05294 278 ETGGCnVQFALNpKDGRYIVIEMNPR 303
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
136-419 |
3.42e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 45.15 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 136 VRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTNSpiNSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEe 215
Cdd:PLN02735 687 VKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIA--RSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK- 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 216 nytRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNI-------------LHLYERDCSIqrrhqkvveiaPATH 282
Cdd:PLN02735 764 ---TYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVviggimehieqagVHSGDSACSL-----------PTQT 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 283 LDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRlqVEHT---VTEEITDVDLVHAQIhVSEGRSLPD 359
Cdd:PLN02735 830 IPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR--ASRTvpfVSKAIGHPLAKYASL-VMSGKSLKD 906
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543464 360 LGLRQENIrINGCAIQCRVTtedPARSFQ-PDTGRIEVFRS-GEGMGIRLDNASAFQGAVIS 419
Cdd:PLN02735 907 LGFTEEVI-PAHVSVKEAVL---PFDKFQgCDVLLGPEMRStGEVMGIDYEFSKAFAKAQIA 964
|
|
| DRE_TIM_LeuA3 |
cd07941 |
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ... |
756-794 |
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 31543464 756 VSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVV 794
Cdd:cd07941 186 VKEVRERLPGVPLGIHAHNDSGLAVANSLAAVEAGATQV 224
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
699-798 |
9.57e-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: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 699 VVEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHD 774
Cdd:cd07939 115 LVGRAKDRGLFVSvgaeDASRA--DPDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAAT-DLPLEFHAHN 191
|
90 100
....*....|....*....|....
gi 31543464 775 TSGSGVAAMLACAQAGADVVDVAV 798
Cdd:cd07939 192 DLGLATANTLAAVRAGATHVSVTV 215
|
|
| PLN02746 |
PLN02746 |
hydroxymethylglutaryl-CoA lyase |
726-837 |
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 31543464 726 LAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGSGVAAMLACAQAGADVVDVAVDSMSGMT 805
Cdd:PLN02746 202 VAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTVDSSVAGLGGCP 281
|
90 100 110
....*....|....*....|....*....|....*...
gi 31543464 806 SQPSMGALVACT------KGTPLDTEVPLERVFDYSEY 837
Cdd:PLN02746 282 YAKGASGNVATEdvvymlNGLGVSTNVDLGKLMAAGDF 319
|
|
| YcjR |
COG1082 |
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism]; |
99-167 |
1.95e-03 |
|
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 440699 [Multi-domain] Cd Length: 254 Bit Score: 41.54 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 99 IPDIIKVAKENGVDAVHPGYGFLSE--RADFAQACQDAGVRFIG---------PSPEVVRKMGDKVEaRAIAIAA--GVP 165
Cdd:COG1082 15 LEEALRAAAELGYDGVELAGGDLDEadLAELRAALADHGLEISSlhapglnlaPDPEVREAALERLK-RAIDLAAelGAK 93
|
..
gi 31543464 166 VV 167
Cdd:COG1082 94 VV 95
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1112-1178 |
2.10e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 42.12 E-value: 2.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543464 1112 IGAPMPGKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1178
Cdd:PRK11855 10 IGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1118-1178 |
2.47e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 41.73 E-value: 2.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543464 1118 GKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1178
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
37-329 |
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 31543464 37 IKKVMVANRGEIAI-----------RVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLigrglAPVQaylhiPDIIK- 104
Cdd:PLN02735 23 LKKIMILGAGPIVIgqacefdysgtQACKALKEEGYEVVLINSNPATIMTDPETADRTYI-----APMT-----PELVEq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 105 -VAKENGvDAVHPGYG---------FLSERADFAQAcqdaGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVP-GTNsp 173
Cdd:PLN02735 93 vIAKERP-DALLPTMGgqtalnlavALAESGILEKY----GVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPsGIA-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 174 iNSLHEAHEFSNTYG-FPIIFKAAYGGGGRGMRVVHSYEELEENYTraysEALAAFGNGALFVEKFIEKPRHIEVQILGD 252
Cdd:PLN02735 166 -TTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICK----AGLAASITSQVLVEKSLLGWKEYELEVMRD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 253 QYGNILHLyerdCSIQRRHQKVVE------IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGT-VEFLVD-KHGKHYFIE 324
Cdd:PLN02735 241 LADNVVII----CSIENIDPMGVHtgdsitVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSnVQFAVNpVDGEVMIIE 316
|
....*
gi 31543464 325 VNSRL 329
Cdd:PLN02735 317 MNPRV 321
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1118-1178 |
4.60e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 41.14 E-value: 4.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543464 1118 GKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1178
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
|
|
| PLN03228 |
PLN03228 |
methylthioalkylmalate synthase; Provisional |
721-818 |
6.38e-03 |
|
methylthioalkylmalate synthase; Provisional
Pssm-ID: 178767 [Multi-domain] Cd Length: 503 Bit Score: 40.68 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 721 EYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFP---DLPLHIHTHDTSGSGVAAMLACAQAGADVVDVA 797
Cdd:PLN03228 239 EFLCKILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKANTPgidDIVFSVHCHNDLGLATANTIAGICAGARQVEVT 318
|
90 100
....*....|....*....|.
gi 31543464 798 VDSMSGMTSQPSMGALVACTK 818
Cdd:PLN03228 319 INGIGERSGNASLEEVVMALK 339
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1104-1178 |
6.81e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 40.37 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 1104 ALKDVKgqigapMP------GKVIDVKVAAGAKVVKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1177
Cdd:PRK11854 205 GVKDVN------VPdiggdeVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF 278
|
.
gi 31543464 1178 E 1178
Cdd:PRK11854 279 E 279
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
66-363 |
8.37e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 40.22 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 66 VYSEQDT---GQMHRQKA----DEAYLI--GRGLAPVQAYLHIPDIikVAKENGVDAVHpgyGFLSERADFA--QACQDA 134
Cdd:PRK02186 6 VFIESNTtgtGELLLRKAllrgFTPYFLtaNRGKYPFLDAIRVVTI--SADTSDPDRIH---RFVSSLDGVAgiMSSSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 135 gvrFIGPSPEVVRKMG-DKVEARAIAIA------------AGVPVvPGT---NSPINSLHEAHEFSntygFPIIFKAAYG 198
Cdd:PRK02186 81 ---FIEVASEVARRLGlPAANTEAIRTCrdkkrlartlrdHGIDV-PRThalALRAVALDALDGLT----YPVVVKPRMG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 199 GGGRGMRVVHSYEELEenytrAYSEALAAFGNGALFVEKFIEKPRHiEVQILGDQYGniLHLYerdcSIQRRHQ----KV 274
Cdd:PRK02186 153 SGSVGVRLCASVAEAA-----AHCAALRRAGTRAALVQAYVEGDEY-SVETLTVARG--HQVL----GITRKHLgpppHF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543464 275 VEIA---PATHLDPQlRSRLTSDSVKLAKQVGYE-NAGTVEFLVdKHGKHYFIEVNSRLQ--VEHTVTEEITDVDLVHAQ 348
Cdd:PRK02186 221 VEIGhdfPAPLSAPQ-RERIVRTVLRALDAVGYAfGPAHTELRV-RGDTVVIIEINPRLAggMIPVLLEEAFGVDLLDHV 298
|
330
....*....|....*
gi 31543464 349 IHVSEGRSlPDLGLR 363
Cdd:PRK02186 299 IDLHLGVA-AFADPT 312
|
|
| |
