|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
9-465 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 745.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 9 ISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGGATSAETYLSIEKILSVARRSGADAVHPG 88
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 89 YGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAAY 168
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 169 GGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVEE 248
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 249 APAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTL 328
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 329 DYA--DPEPVGHSIEFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEALE 406
Cdd:COG4770 322 PFTqeDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 655048759 407 RSRRALDEFEVAGMPTVLPFHRKVVRDRAFTGEDgtfgVFTRWIETEFDNDIPAWDGEA 465
Cdd:COG4770 402 RMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGD----VDTGFIERELAELLAAAAPEE 456
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
9-457 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 588.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 9 ISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGGATSAETYLSIEKILSVARRSGADAVHPG 88
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 89 YGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAAY 168
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 169 GGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVEE 248
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 249 APAPFLTAEQ-NEILYSASKAIlKEVGYVGAGTCEFLIGADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGT 327
Cdd:PRK08591 242 APSPAITEELrRKIGEAAVKAA-KAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 328 LDY--ADPEPVGHSIEFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEAL 405
Cdd:PRK08591 321 LSIkqEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 655048759 406 ERSRRALDEFEVAGMPTVLPFHRKVVRDRAF-TGedgtfGVFTRWIETEFDND 457
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFqAG-----DYNIHYLEKKLALQ 448
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
9-452 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 560.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 9 ISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALG-GATSAETYLSIEKILSVARRSGADAVHP 87
Cdd:PRK12999 5 IKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGeGKHPVRAYLDIDEIIRVAKQAGVDAIHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 88 GYGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAA 167
Cdd:PRK12999 85 GYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 168 YGGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVE 247
Cdd:PRK12999 165 AGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 248 EAPAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGT 327
Cdd:PRK12999 245 IAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGAT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 328 LDY--------ADPEPVGHSIEFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVT-AGDSVSGAFDSLLGKLIVTG 398
Cdd:PRK12999 325 LHDleigipsqEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAfAGAEITPYYDSLLVKLTAWG 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 655048759 399 RTREEALERSRRALDEFEVAGMPTVLPFHRKVVRDRAFTGEDGTfgvfTRWIET 452
Cdd:PRK12999 405 RTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYT----TSFIDE 454
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
9-452 |
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: 551.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 9 ISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHaRL-ADEAYALGGATSA-ETYLSIEKILSVARRSGADAVH 86
Cdd:COG1038 4 IKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLH-RFkADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 87 PGYGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKA 166
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 167 AYGGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLV 246
Cdd:COG1038 163 AAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 247 EEAPAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGG 326
Cdd:COG1038 243 EIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 327 TLDyaDPE----------PVGHSIEFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSG-VTAGDSVSGAFDSLLGKLI 395
Cdd:COG1038 323 SLD--DPEigipsqedirLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGnAYTGAVITPYYDSLLVKVT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 655048759 396 VTGRTREEALERSRRALDEFEVAGMPTVLPFHRKVVRDRAFTGEDGTfgvfTRWIET 452
Cdd:COG1038 401 AWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECT----TSFIDE 453
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
10-436 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 544.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 10 SKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGGATSAETYLSIEKILSVARRSGADAVHPGY 89
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 90 GFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAAYG 169
Cdd:PRK08654 83 GFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 170 GGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVEEA 249
Cdd:PRK08654 163 GGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 250 PAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIgADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTLD 329
Cdd:PRK08654 243 PSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 330 YA--DPEPVGHSIEFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEALER 407
Cdd:PRK08654 322 FKqeDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIAR 401
|
410 420
....*....|....*....|....*....
gi 655048759 408 SRRALDEFEVAGMPTVLPFHRKVVRDRAF 436
Cdd:PRK08654 402 MRRALYEYVIVGVKTNIPFHKAVMENENF 430
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
9-454 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 529.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 9 ISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGGATSAETYLSIEKILSVARRSGADAVHPG 88
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 89 YGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAAY 168
Cdd:PRK06111 82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 169 GGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVEE 248
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 249 APAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTL 328
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 329 DYA--DPEPVGHSIEFRINGEDPgRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEALE 406
Cdd:PRK06111 322 SFTqdDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAIS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 655048759 407 RSRRALDEFEVAGMPTVLPFHRKVVRDRAFTGEDGTFGVFTRWIETEF 454
Cdd:PRK06111 401 RLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQLVKKS 448
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
8-436 |
1.13e-171 |
|
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: 494.66 E-value: 1.13e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 8 GISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGGATSAETYLSIEKILSVARRSGADAVHP 87
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 88 GYGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAA 167
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 168 YGGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVE 247
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 248 EAPAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGT 327
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 328 LDYADPEPV--GHSIEFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEAL 405
Cdd:TIGR00514 321 LSLKQEDVVvrGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430
....*....|....*....|....*....|.
gi 655048759 406 ERSRRALDEFEVAGMPTVLPFHRKVVRDRAF 436
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENF 431
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
9-456 |
2.07e-167 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 483.83 E-value: 2.07e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 9 ISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGGATSAETYLSIEKILSVARRSGADAVHPG 88
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 89 YGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAAY 168
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 169 GGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVEE 248
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 249 APAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTL 328
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 329 DYA--DPEPVGHSIEFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEALE 406
Cdd:PRK05586 322 SIKqeDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQ 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 655048759 407 RSRRALDEFEVAGMPTVLPFHRKVVRDRAFTgeDGTFGvfTRWIETEFDN 456
Cdd:PRK05586 402 KMKRALGEFIIEGVNTNIDFQFIILEDEEFI--KGTYD--TSFIEKKLVD 447
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
9-469 |
1.29e-159 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 464.61 E-value: 1.29e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 9 ISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGGATSAETYLSIEKILSVARRSGADAVHPG 88
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 89 YGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAAY 168
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 169 GGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEgNVVVVSTRDCSLQRRHQKLVEE 248
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 249 APAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLI-GADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGT 327
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFdDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 328 LDYADPEPV--GHSIEFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEAL 405
Cdd:PRK12833 324 LRFAQGDIAlrGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAAL 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655048759 406 ERSRRALDEFEVAGMPTVLPFHRKVVRDRAFTGEDGTFGVFTRWIETEFDNDIPAWDGEAGPSA 469
Cdd:PRK12833 404 ARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAALDAAASAAVGEAA 467
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
9-436 |
1.75e-159 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 464.58 E-value: 1.75e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 9 ISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGgATSAETYLSIEKILSVARRSGADAVHPG 88
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIG-ADPLAGYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 89 YGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAAY 168
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 169 GGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVEE 248
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 249 APAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTL 328
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 329 DY--ADPEPVGHSIEFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEALE 406
Cdd:PRK07178 321 SYkqEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALD 400
|
410 420 430
....*....|....*....|....*....|
gi 655048759 407 RSRRALDEFEVAGMPTVLPFHRKVVRDRAF 436
Cdd:PRK07178 401 RGRRALDDMRVQGVKTTIPYYQEILRNPEF 430
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
11-452 |
1.82e-159 |
|
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: 485.87 E-value: 1.82e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 11 KVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALG---GATSAETYLSIEKILSVARRSGADAVHP 87
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGegpDLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 88 GYGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAA 167
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 168 YGGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVE 247
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 248 EAPAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGT 327
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 328 L--------DYADPEPVGHSIEFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVT-AGDSVSGAFDSLLGKLIVTG 398
Cdd:TIGR01235 321 LptpqlgvpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSyAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 655048759 399 RTREEALERSRRALDEFEVAGMPTVLPFHRKVVRDRAFTgeDGTFgvFTRWIET 452
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFL--DGSY--DTRFIDT 450
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
9-436 |
2.74e-149 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 437.64 E-value: 2.74e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 9 ISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGGATSAETYLSIEKILSVARRSGADAVHPG 88
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 89 YGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAAY 168
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 169 GGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVEE 248
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 249 APAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTL 328
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 329 dyADPEPV---GHSIEFRINGEDPgRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEAL 405
Cdd:PRK08462 324 --PSQESIklkGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAI 400
|
410 420 430
....*....|....*....|....*....|.
gi 655048759 406 ERSRRALDEFEVAGMPTVLPFHRKVVRDRAF 436
Cdd:PRK08462 401 AKMKRALKEFKVEGIKTTIPFHLEMMENADF 431
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
9-436 |
1.33e-145 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 429.23 E-value: 1.33e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 9 ISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGgATSAETYLSIEKILSVARRSGADAVHPG 88
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIG-TDPIKGYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 89 YGFLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGT-PGPVSGADEVVAFAREFGMPIAIKAA 167
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTeKLNSESMEEIKIFARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 168 YGGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVE 247
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 248 EAPAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGT 327
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 328 LDY--ADPEPVGHSIEFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEAL 405
Cdd:PRK08463 321 LDLeqSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLAV 400
|
410 420 430
....*....|....*....|....*....|.
gi 655048759 406 ERSRRALDEFEVAGMPTVLPFHRKVVRDRAF 436
Cdd:PRK08463 401 NKLERALKEFVIDGIRTTIPFLIAITKTREF 431
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
122-329 |
3.17e-86 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 266.86 E-value: 3.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 122 DKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGMPIAIKAAYGGGGRGLKVAREFDEVEELFESATREAITAFGR 201
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 202 GECFVEKYLDKPRHVETQCLADAEGNVVVVSTRDCSLQRRHQKLVEEAPAPFLTAEQNEILYSASKAILKEVGYVGAGTC 281
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 655048759 282 EFLIGAD-GTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTLD 329
Cdd:pfam02786 161 EFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
9-116 |
2.41e-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: 190.39 E-value: 2.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 9 ISKVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGGATSAETYLSIEKILSVARRSGADAVHPG 88
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 655048759 89 YGFLAENAEFARAVIGAGLIWIGPSPEA 116
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
70-325 |
2.01e-48 |
|
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: 169.67 E-value: 2.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 70 IEKILSVARRSGADAVHPGYGFLAENAEFARAVIGagliWIGPSPEAIEALGDKVTARHVAEKVGAPlapgTPG--PVSG 147
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVETAAELAEELG----LPGPSPEAIRAMRDKVLMREALAAAGVP----VPGfaLVDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 148 ADEVVAFAREFGMPIAIKAAYGGGGRGLKVAREFDEVEELFESATREAITAFGRGECFVEKYLDKpRHVETQCLADaEGN 227
Cdd:COG0439 78 PEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVR-DGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 228 VVVvstrdCSLQRRHQK---LVE---EAPAPfLTAEQNEILYSASKAILKEVGYV-GAGTCEFLIGADGTISFLEVNTRL 300
Cdd:COG0439 156 VVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARL 229
|
250 260
....*....|....*....|....*..
gi 655048759 301 QVEH--PVSEEVTGIDLVREQFRIAEG 325
Cdd:COG0439 230 GGEHipPLTELATGVDLVREQIRLALG 256
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
341-451 |
1.42e-44 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 153.72 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 341 EFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEALERSRRALDEFEVAGM 420
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100 110
....*....|....*....|....*....|.
gi 655048759 421 PTVLPFHRKVVRDRAFtgEDGTFGvfTRWIE 451
Cdd:smart00878 81 KTNIPFLRALLRHPDF--RAGDVD--TGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
341-452 |
5.09e-42 |
|
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: 146.87 E-value: 5.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 341 EFRINGEDPGRGFLPAPGDIHVFKTFGGPGVRLDSGVTAGDSVSGAFDSLLGKLIVTGRTREEALERSRRALDEFEVAGM 420
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100 110
....*....|....*....|....*....|..
gi 655048759 421 PTVLPFHRKVVRDRAFTGEDgtfgVFTRWIET 452
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGE----VDTGFLEE 108
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
526-592 |
2.64e-23 |
|
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: 93.25 E-value: 2.64e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655048759 526 AVASPMQATVVKIAVEEGQQVVKGDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
469-592 |
2.48e-22 |
|
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: 102.08 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 469 AEPEGRHTVVVEVSGKRLEVSLPDRlSHAPAAVGRPVAvPPSRRSHassavsgasgdaVASPMQATVVKIAVEEGQQVVK 548
Cdd:COG1038 1035 PDEDGMRTVFFELNGQPREVRVRDR-SVKVTVASREKA-DPGNPGH------------IGAPMPGTVVKVLVKEGDEVKK 1100
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 655048759 549 GDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:COG1038 1101 GDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
467-593 |
3.74e-22 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 100.39 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 467 PSAEPEGRHTVVVEVSGKR--LEVSLPDRLSHAPAAVGRPVAVPPsrrshASSAVSGASGDAVASPMQATVVKIAVEEGQ 544
Cdd:PRK14040 470 AKAEPAGSETYTVEVEGKAyvVKVSEGGDISQITPAAPAAAPAAA-----AAAAPAAAAGEPVTAPLAGNIFKVIVTEGQ 544
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 655048759 545 QVVKGDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTIS 593
Cdd:PRK14040 545 TVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
463-592 |
9.83e-22 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 99.15 E-value: 9.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 463 GEAGPSAEPEGRHTVVVEVSGKRLEV-----SLPDRLSHAPAAVGRP--VAVPPSRRSHASSAVSGASGDAVASPMQATV 535
Cdd:PRK09282 454 KEAAAAGAEGIPTEFKVEVDGEKYEVkiegvKAEGKRPFYLRVDGMPeeVVVEPLKEIVVGGRPRASAPGAVTSPMPGTV 533
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 655048759 536 VKIAVEEGQQVVKGDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:PRK09282 534 VKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
469-593 |
1.51e-19 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 93.28 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 469 AEPEGRHTVVVEVSGKRLEVSLPDRlSHAPAAVGRPVAvPPSRRSHassavsgasgdaVASPMQATVVKIAVEEGQQVVK 548
Cdd:PRK12999 1035 PDEDGMRTVYFELNGQPREVQVRDR-SVKSTVAAREKA-DPGNPGH------------VGAPMPGSVVTVLVKEGDEVKA 1100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 655048759 549 GDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTIS 593
Cdd:PRK12999 1101 GDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
479-592 |
1.34e-18 |
|
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: 82.25 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 479 VEVSGKRLEVSLPDRLSHAPAAVGRPVAVPPSRRSHASS--AVSGASGDAVASPMQATV-------VKIAVEEGQQVVKG 549
Cdd:COG0511 13 LEVEEGEYKVRIKRGGAAAAAPVAAPAAAAPAAAAPAAAaaAAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAG 92
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 655048759 550 DLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:COG0511 93 DTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
487-593 |
2.88e-18 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 81.40 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 487 EVSLPDRLSHAPAAVGRPVAVP----PSRRSHASSAVSGASGDAVASPMQATVVKIAVEEGQQVVKGDLVVVLEAMKMEQ 562
Cdd:PRK06549 20 EIGAPAQAAAPAQPASTPVPVPteasPQVEAQAPQPAAAAGADAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMEN 99
|
90 100 110
....*....|....*....|....*....|.
gi 655048759 563 PIQAHKDGVVGAINAQAGATVSAGHQLLTIS 593
Cdd:PRK06549 100 EIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
62-299 |
3.98e-16 |
|
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: 81.46 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 62 TSAETY---LSIEKILSVARRSGADAVHPGYG-----FLAEnaEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKV 133
Cdd:COG0458 48 TADRLYfepLTVEDVLDIIEKEKPDGVIVQFGgqtalNLAV--ELEEAGILEGVKILGTSPDAIDLAEDRELFKELLDKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 134 GAPLAPGtpGPVSGADEVVAFAREFGMPIAIKAAYGGGGRGLKVAREFDEveelFESATREAITAFGRGECFVEKYLDKP 213
Cdd:COG0458 126 GIPQPKS--GTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEE----LEEYLERALKVSPDHPVLIDESLLGA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 214 RHVETQCLADAEGNVVVVstrdCSLQrrHqklVEEA-----------PAPFLTAEQNEILYSASKAILKEVGYVGAGTCE 282
Cdd:COG0458 200 KEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQ 270
|
250
....*....|....*..
gi 655048759 283 FLIgADGTISFLEVNTR 299
Cdd:COG0458 271 FAV-DDGRVYVIEVNPR 286
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
68-328 |
1.01e-15 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 80.81 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 68 LSIEKILSVARRSGAD--AVHPGyGFLAENAefARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGtpGPV 145
Cdd:TIGR01369 616 LTFEDVMNIIELEKPEgvIVQFG-GQTPLNL--AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTA 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 146 SGADEVVAFAREFGMPIAIKAAYGGGGRGLKVAREFDEVEELFEsatrEAITAFGRGECFVEKYLDKPRHVETQCLADae 225
Cdd:TIGR01369 691 TSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-- 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 226 GNVVVVSTrdcslQRRHqklVEEA-----------PAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIgADGTISFL 294
Cdd:TIGR01369 765 GEEVLIPG-----IMEH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV-KDGEVYVI 835
|
250 260 270
....*....|....*....|....*....|....
gi 655048759 295 EVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTL 328
Cdd:TIGR01369 836 EVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
479-592 |
2.54e-15 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 73.36 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 479 VEVSGKRLEVSLPDRLShAPAAVGRPVAVPPSRRSHASSAvsgASGDAVASPMQATVVKIAVEEGQQVVKGDLVVVLEAM 558
Cdd:PRK05641 43 IDLSAVQEQVPTPAPAP-APAVPSAPTPVAPAAPAPAPAS---AGENVVTAPMPGKILRILVREGQQVKVGQGLLILEAM 118
|
90 100 110
....*....|....*....|....*....|....
gi 655048759 559 KMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:PRK05641 119 KMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
11-360 |
8.82e-15 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 76.12 E-value: 8.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 11 KVLIANRGEIAVRIIRAARDSGKASVAVYADQDRDAMHARLADEAYALGG-ATSAETYlsIEKILSVARRSGADAVHPGY 89
Cdd:COG3919 7 RVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDpGDDPEAF--VDALLELAERHGPDVLIPTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 90 ----GFLAENaefaRAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPlAPGTpGPVSGADEVVAFAREFGMPIAIK 165
Cdd:COG3919 85 deyvELLSRH----RDELEEHYRLPYPDADLLDRLLDKERFYELAEELGVP-VPKT-VVLDSADDLDALAEDLGFPVVVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 166 AAYG--------GGGRGLKVAREFDEVEELFEsatreAITAFGrGECFVEKYLDKPRHVE--TQCLADAEGNVVVVSTrd 235
Cdd:COG3919 159 PADSvgydelsfPGKKKVFYVDDREELLALLR-----RIAAAG-YELIVQEYIPGDDGEMrgLTAYVDRDGEVVATFT-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 236 cslqrrHQKLVEeAPAPF-----LTAEQNEILYSASKAILKEVGYVGAGTCEFLIGA-DGTISFLEVNTRLQVEHPVSeE 309
Cdd:COG3919 231 ------GRKLRH-YPPAGgnsaaRESVDDPELEEAARRLLEALGYHGFANVEFKRDPrDGEYKLIEINPRFWRSLYLA-T 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 655048759 310 VTGIDLVREQFRIAEGGtldyaDPEPVghsiefriNGEDPGRGFLPAPGDI 360
Cdd:COG3919 303 AAGVNFPYLLYDDAVGR-----PLEPV--------PAYREGVLWRVLPGDL 340
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
68-342 |
4.21e-13 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 72.69 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 68 LSIEKILSVARRSGADAVHPGYGFLAENAeFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGtpGPVSG 147
Cdd:PRK12815 617 LTLEDVLNVAEAENIKGVIVQFGGQTAIN-LAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATD 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 148 ADEVVAFAREFGMPIAIKAAYGGGGRGLKVAREFDEVEELFESATR--EAITafgrgecfVEKYLDKpRHVETQCLADae 225
Cdd:PRK12815 694 EEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENASqlYPIL--------IDQFIDG-KEYEVDAISD-- 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 226 GNVVVVSTrdcslQRRHqklVEEA-----------PAPFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIgADGTISFL 294
Cdd:PRK12815 763 GEDVTIPG-----IIEH---IEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVL 833
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 655048759 295 EVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTL-DYADPEPVGHSIEF 342
Cdd:PRK12815 834 EVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLaELGYPNGLWPGSPF 882
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
527-593 |
6.70e-12 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 60.96 E-value: 6.70e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655048759 527 VASPMQATVVKIAVEEGQQVVKGDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTIS 593
Cdd:PRK08225 4 VYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
527-592 |
1.41e-11 |
|
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: 60.31 E-value: 1.41e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655048759 527 VASPMQAT-----VVKIAVEEGQQVVKGDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:pfam00364 3 IKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
110-329 |
1.75e-10 |
|
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: 64.25 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 110 IGPSPEAIEALGDKVTARHVAEKVGAPLAPGtpGPVSGADEVVAFAREFGMPIAIKAAYGGGGRGLKVAREFDEVEELFE 189
Cdd:TIGR01369 115 LGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 190 SATREAITafgrGECFVEKYLDKPRHVETQCLADAEGNVVVVstrdCSLQRRHQKLVEE------APAPFLTAEQNEILY 263
Cdd:TIGR01369 193 RALSASPI----NQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNMENFDPMGVHTgdsivvAPSQTLTDKEYQMLR 264
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655048759 264 SASKAILKEVGYVGAGTCEFLIGAD-GTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTLD 329
Cdd:TIGR01369 265 DASIKIIRELGIEGGCNVQFALNPDsGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTLD 331
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
36-324 |
2.07e-09 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 58.80 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 36 VAVYADQDRDAMHARLADEAYALGG----ATSAETYLSIEKILSVARR---SGADAV-----HPGYGFlaenaEFARAVI 103
Cdd:COG0189 4 IAILTDPPDKDSTKALIEAAQRRGHevevIDPDDLTLDLGRAPELYRGedlSEFDAVlpridPPFYGL-----ALLRQLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 104 GAGLIWIgPSPEAIEALGDKVTARHVAEKVGAPlapgTP--GPVSGADEVVAFAREFGMPIAIKAAYGGGGRGLKVAREF 181
Cdd:COG0189 79 AAGVPVV-NDPEAIRRARDKLFTLQLLARAGIP----VPptLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 182 DEVEELFesatrEAITAFGRGECFVEKYLDKPRHVETQCLAdAEGNVVvvstrdCSLQR-------RHQKLVEEAPAPF- 253
Cdd:COG0189 154 DALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVLV-VGGEPV------AAIRRipaegefRTNLARGGRAEPVe 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655048759 254 LTAEQNEILYSASKAIlkEVGYVGagtCEFLIGADGTIsFLEVNTRLQVEHPvsEEVTGIDLVReqfRIAE 324
Cdd:COG0189 222 LTDEERELALRAAPAL--GLDFAG---VDLIEDDDGPL-VLEVNVTPGFRGL--ERATGVDIAE---AIAD 281
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
110-336 |
2.26e-09 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 60.37 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 110 IGPSPEAIEALGDKVTARHVAEKVGAPLAPGtpGPVSGADEVVAFAREFGMPIAIKAAYGGGGRGLKVAREFDEVEELFE 189
Cdd:PRK12815 116 LGTNIEAIQKGEDRERFRALMKELGEPVPES--EIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 190 SATRE-AITafgrgECFVEKYLDKPRHVETQCLADAEGNVVVVstrdCSLQRrhqklVEE-----------APAPFLTAE 257
Cdd:PRK12815 194 QGLQAsPIH-----QCLLEESIAGWKEIEYEVMRDRNGNCITV----CNMEN-----IDPvgihtgdsivvAPSQTLTDD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 258 QNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFL-EVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTLD------- 329
Cdd:PRK12815 260 EYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLiEVNPRVSRSSALASKATGYPIAKIAAKLAVGYTLNelknpvt 339
|
250
....*....|
gi 655048759 330 ---YADPEPV 336
Cdd:PRK12815 340 gltYASFEPA 349
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
70-329 |
2.63e-09 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 60.18 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 70 IEKILSVARrsgADAVHPGYG---------FLAENAEFARAvigaGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPG 140
Cdd:PLN02735 90 VEQVIAKER---PDALLPTMGgqtalnlavALAESGILEKY----GVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 141 tpGPVSGADEVVAFAREFG-MPIAIKAAYGGGGRGLKVAREFDEVEELFESATREAITAfgrgECFVEKYLDKPRHVETQ 219
Cdd:PLN02735 163 --GIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITS----QVLVEKSLLGWKEYELE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 220 CLADAEGNVVVVstrdCSLQRRHQKLVEE------APAPFLTAEQNEILYSASKAILKEVGY-VGAGTCEFLIG-ADGTI 291
Cdd:PLN02735 237 VMRDLADNVVII----CSIENIDPMGVHTgdsitvAPAQTLTDKEYQRLRDYSVAIIREIGVeCGGSNVQFAVNpVDGEV 312
|
250 260 270
....*....|....*....|....*....|....*...
gi 655048759 292 SFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTLD 329
Cdd:PLN02735 313 MIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTLD 350
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
112-291 |
3.98e-09 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 58.63 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 112 PSPEAIEALGDKVTARHVAEKVGAPLAPGTPgpVSGADEVVAFAREFGMPIAIKAAYGG-GGRGLKVAREFDEVEELFEs 190
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFAV--VDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAWA- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 191 atreaitAFGRGECFVEKYLDkprhvetqclADAEGNVVVVSTRDCS-----LQRRHQK---LVE-EAPAPFLTAEQNEI 261
Cdd:PRK06019 167 -------LLGSVPCILEEFVP----------FEREVSVIVARGRDGEvvfypLVENVHRngiLRTsIAPARISAELQAQA 229
|
170 180 190
....*....|....*....|....*....|
gi 655048759 262 lYSASKAILKEVGYVGAGTCEFLIGADGTI 291
Cdd:PRK06019 230 -EEIASRIAEELDYVGVLAVEFFVTGDGEL 258
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
533-592 |
6.90e-09 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 52.44 E-value: 6.90e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 533 ATVVKIAVEEGQQVVKGDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
108-299 |
7.29e-09 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 59.02 E-value: 7.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 108 IWiGPSPEAIEALGDKVTARHVAEKVGAPLAPGtpGPVSGADEVVAFAREFGMPIAIKAAYGGGGRGLKVAREFDEVEEL 187
Cdd:PLN02735 689 IW-GTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTY 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 188 FESAtreaITAFGRGECFVEKYLDKPRHVETQCLADAEGNVVV-----------VSTRD--CSLqrrhqklveeaPAPFL 254
Cdd:PLN02735 766 LETA----VEVDPERPVLVDKYLSDATEIDVDALADSEGNVVIggimehieqagVHSGDsaCSL-----------PTQTI 830
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 655048759 255 TAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGTISFLEVNTR 299
Cdd:PLN02735 831 PSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR 875
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
11-414 |
1.14e-08 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 57.24 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 11 KVLIANrgeIAVRII-RAARDSGKASVAV--YADQDRDAmharLADEAYALGGATSAETYLSIE-KILSVARRSGADAVH 86
Cdd:COG2232 6 DLLIAG---FSARALaQSARRAGYRVYAVdlFADLDTRA----LAERWVRLDAESCGFDLEDLPaALLELAAADDPDGLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 87 PGYGFLAENAEFARavIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPlAPgtpgPVSGADEVVAFarefgmPIAIKA 166
Cdd:COG2232 79 YGSGFENFPELLER--LARRLPLLGNPPEVVRRVKDPLRFFALLDELGIP-HP----ETRFEPPPDPG------PWLVKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 167 AYGGGGRGLKVAREfdeveelfesatreaiTAFGRGECFVEKYLDKpRHVETQCLADAEGNVVVVSTRdcslqrrhQKLV 246
Cdd:COG2232 146 IGGAGGWHIRPADS----------------EAPPAPGRYFQRYVEG-TPASVLFLADGSDARVLGFNR--------QLIG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 247 EEAPAPF----------LTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGtISFLEVNTRLQVEHPVSEEVTGIDLV 316
Cdd:COG2232 201 PAGERPFryggnigplaLPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDG-PYVLEVNPRPQASLDLYEDATGGNLF 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 317 REQFRiAEGGTLDYADPEPVGHSIefringedpGRGFLPAPGDIHVFKTFGGP---------GVRLDSG---VTagdsvs 384
Cdd:COG2232 280 DAHLR-ACRGELPEVPRPKPRRVA---------AKAILYAPRDLTIPDDLSWPpwvadipapGTRIEKGepvCT------ 343
|
410 420 430
....*....|....*....|....*....|
gi 655048759 385 gafdsllgkLIVTGRTREEALERSRRALDE 414
Cdd:COG2232 344 ---------VLAEGPTAEAARALLERRAEE 364
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
527-593 |
1.39e-08 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 51.73 E-value: 1.39e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655048759 527 VASPMQATVVKIAVEEGQQVVKGDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTIS 593
Cdd:PRK05889 5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVIS 71
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
110-281 |
2.94e-07 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 53.56 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 110 IGPSPEAIEALGDKVTARHVAEKVGAPLAPGtpGPVSGADEVVAFAREFGMPIAIKAAYGGGGRGLKVAREFDEVEELFE 189
Cdd:PRK05294 116 IGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 190 SATREAITafgrGECFVEKYLDKPRHVETQCLADAEGNVVVVstrdCSLqrrhqklveE---------------APAPFL 254
Cdd:PRK05294 194 RGLDLSPV----TEVLIEESLLGWKEYEYEVMRDKNDNCIIV----CSI---------EnidpmgvhtgdsitvAPAQTL 256
|
170 180
....*....|....*....|....*..
gi 655048759 255 TAEQNEILYSASKAILKEVGyVGAGTC 281
Cdd:PRK05294 257 TDKEYQMLRDASIAIIREIG-VETGGC 282
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
131-299 |
2.97e-06 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 47.63 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 131 EKVGAPLAPGTPgpVSGADEVVAFAREFGMPIAIKAAYGG-GGRGLKVAREFDEVEelfesatrEAITAFGRGECFVEKY 209
Cdd:pfam02222 1 QKLGLPTPRFMA--AESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP--------QAWEELGDGPVIVEEF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 210 LDkprhvetqclADAEGNVVVVSTRDCS------LQRRHQK--LVEE-APAPFlTAEQNEILYSASKAILKEVGYVGAGT 280
Cdd:pfam02222 71 VP----------FDRELSVLVVRSVDGEtafypvVETIQEDgiCRLSvAPARV-PQAIQAEAQDIAKRLVDELGGVGVFG 139
|
170
....*....|....*....
gi 655048759 281 CEFLIGADGTISFLEVNTR 299
Cdd:pfam02222 140 VELFVTEDGDLLINELAPR 158
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
533-592 |
6.56e-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: 44.29 E-value: 6.56e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 533 ATVVKIAVEEGQQVVKGDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
524-592 |
3.47e-05 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 46.64 E-value: 3.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 524 GD-AVASPmqATVVKIAVEEGQQVVKGDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:PRK14042 526 GDiTVAIP--GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
497-592 |
6.67e-05 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 44.83 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 497 APAAVGRPVAVPPSRRSHASSAVSGASGDAVASPMQATV-----------VKIaveeGQQVVKGDLVVVLEAMKMEQPIQ 565
Cdd:PLN02983 170 QPAPSAPASSPPPTPASPPPAKAPKSSHPPLKSPMAGTFyrspapgeppfVKV----GDKVQKGQVVCIIEAMKLMNEIE 245
|
90 100
....*....|....*....|....*..
gi 655048759 566 AHKDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:PLN02983 246 ADQSGTIVEILAEDGKPVSVDTPLFVI 272
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
121-299 |
2.99e-04 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 42.27 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 121 GDKVTARHVAEKVGAPLAPGTPgpVSGADEVVAFAREFGMPIA-IKAAYGGGGRGLKVAREFDE----VEELFESAtrea 195
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYET--FTDPEEAKSYIQEAGFPAIvVKADGLAAGKGVIVASSNEEaikaVDEILEQK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 196 itAFGRGEC--FVEKYLDKPRhVETQCLADAEGNVVVVSTRDcslqrrHQKLVEE------------APAPFLTAE---- 257
Cdd:pfam01071 75 --KFGEAGEtvVIEEFLEGEE-VSVLAFVDGKTVKPLPPAQD------HKRAGEGdtgpntggmgaySPAPVITPEller 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 655048759 258 -QNEILYSASKAILKEVG-YVGAGTCEFLIGADGtISFLEVNTR 299
Cdd:pfam01071 146 iKETIVEPTVDGLRKEGIpFKGVLYAGLMLTKDG-PKVLEFNCR 188
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
105-329 |
4.90e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 43.16 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 105 AGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGtpGPVSGADEVVAFAREFGMPIAIKAAYGGGGRGLKVAREFDEV 184
Cdd:PRK05294 652 AGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEEL 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 185 EELFesatREAITAFGRGECFVEKYLDKPRHVETQCLADAEgNVVVVSTRDcslqrrHqklVEEA-----------PAPF 253
Cdd:PRK05294 730 ERYM----REAVKVSPDHPVLIDKFLEGAIEVDVDAICDGE-DVLIGGIME------H---IEEAgvhsgdsacslPPQT 795
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655048759 254 LTAEQNEILYSASKAILKEVGYVGAGTCEFLIgADGTISFLEVNTRLQVEHPVSEEVTGIDLVREQFRIAEGGTLD 329
Cdd:PRK05294 796 LSEEIIEEIREYTKKLALELNVVGLMNVQFAV-KDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLA 870
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
524-593 |
5.96e-04 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 42.36 E-value: 5.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 524 GDAVASpmqATVVKIAVEEGQQVVKGDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTIS 593
Cdd:PTZ00144 53 GDSISE---GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID 119
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
96-299 |
9.78e-04 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 42.03 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 96 AEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPgpVSGADEVVAFAREFGMPIAIKAAYGGGGRGL 175
Cdd:PLN02257 76 AGLADDLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYET--FTDPAAAKKYIKEQGAPIVVKADGLAAGKGV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 176 KVAREFDEVEELFESATREAitAFGR--GECFVEKYLDKpRHVETQCLADAEGNVVVVSTRDcslqrrHQKLVE------ 247
Cdd:PLN02257 154 VVAMTLEEAYEAVDSMLVKG--AFGSagSEVVVEEFLDG-EEASFFALVDGENAIPLESAQD------HKRVGDgdtgpn 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655048759 248 ------EAPAPFLTAE-----QNEILYSASKAILKE----VGYVGAGTceFLIGADGTISFLEVNTR 299
Cdd:PLN02257 225 tggmgaYSPAPVLTPEleskvMETIIYPTVKGMAAEgckfVGVLYAGL--MIEKKSGLPKLLEYNVR 289
|
|
| PRK06524 |
PRK06524 |
biotin carboxylase-like protein; Validated |
91-186 |
9.88e-04 |
|
biotin carboxylase-like protein; Validated
Pssm-ID: 180605 [Multi-domain] Cd Length: 493 Bit Score: 42.03 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 91 FLAENAEFARAVIGAGLIWIGPSPEAIEALGDKVTARHVAEKVGAPLAPGTPGPVSGADEVVAFAREFGM--PIAIKAAY 168
Cdd:PRK06524 111 FVMFDEETEALARQAGLEVMHPPAELRHRLDSKIVTTRLANEAGVPSVPHVLGRVDSYDELSALAHGAGLgdDLVVQTPY 190
|
90 100
....*....|....*....|.
gi 655048759 169 GGGGRG---LKVAREFDEVEE 186
Cdd:PRK06524 191 GDSGSTtffVRGQRDWDKYAG 211
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
540-592 |
2.17e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 37.30 E-value: 2.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 655048759 540 VEEGQQVVKGDLVVVLEAMKMEQPIQAHKDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
164-301 |
3.97e-03 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 38.52 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 164 IKAAYGGGGRGlkvAREFDEVEELFESATREAITAFGRGEcfvekyldkprHVETQCLADAEGNVVVVstrdCSLQRRHQ 243
Cdd:pfam02655 36 VKPRDGCGGEG---VRKVENGREDEAFIENVLVQEFIEGE-----------PLSVSLLSDGEKALPLS----VNRQYIDN 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655048759 244 KLVEEAPA----PFLTAEQNEILYSASKAILKEVGYVGAGTCEFLIGADGtISFLEVNTRLQ 301
Cdd:pfam02655 98 GGSGFVYAgnvtPSRTELKEEIIELAEEVVECLPGLRGYVGVDLVLKDNE-PYVIEVNPRIT 158
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
527-559 |
4.55e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 35.50 E-value: 4.55e-03
10 20 30
....*....|....*....|....*....|...
gi 655048759 527 VASPMQATVVKIAVEEGQQVVKGDLVVVLEAMK 559
Cdd:pfam13533 5 IASPVSGKVVAVNVKEGQQVKKGDVLATLDSPE 37
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
527-556 |
6.56e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 38.88 E-value: 6.56e-03
10 20 30
....*....|....*....|....*....|
gi 655048759 527 VASPMQATVVKIAVEEGQQVVKGDLVVVLE 556
Cdd:COG1566 48 VAAKVSGRVTEVLVKEGDRVKKGQVLARLD 77
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
497-592 |
8.33e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 39.04 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655048759 497 APAAVGRPVAVPPSRRSHASSAVSGASGDAVASPM-------QATVVKIAVEEGQQVVKGDLVVVLEAMK--MEQPiqAH 567
Cdd:PRK11855 90 AAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVpdigeitEVEVIEWLVKVGDTVEEDQSLITVETDKatMEIP--SP 167
|
90 100
....*....|....*....|....*
gi 655048759 568 KDGVVGAINAQAGATVSAGHQLLTI 592
Cdd:PRK11855 168 VAGVVKEIKVKVGDKVSVGSLLVVI 192
|
|
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