|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
58-468 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 668.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 58 FDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDASS------------------------------------------ 95
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDAlhvrladeavcigpapaaesylnidaiiaaakatgadaihpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 96 --------------AAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASA 161
Cdd:COG4770 82 ygflsenadfaeacEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 162 GGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 241
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 242 APSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPL 321
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 322 RHKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPIHlPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEA 401
Cdd:COG4770 322 PFTQEDIKLRGHAIECRINAEDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958680995 402 LKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFLSDVYPDGFkghmLTPSERDQLLAIA 468
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL----AAAAPEELALAAA 462
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
57-443 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 558.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 57 TFDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDAS-----------------------------SAAE--------- 98
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDalhvqladeavcigpapskksylnipaiiSAAEitgadaihp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 99 ------------------DVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKAS 160
Cdd:PRK08591 81 gygflsenadfaeicedsGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 161 AGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 240
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 241 EAPSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYP 320
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 321 LRHKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYqepiHLP---GVRVDSGIQPGSDISIYYDPMISKLVTYGSD 397
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNF-MPSPGKITRY----HPPggpGVRVDSAVYTGYTIPPYYDSMIGKLIVHGET 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958680995 398 RAEALKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFL 443
Cdd:PRK08591 396 REEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
58-443 |
3.54e-161 |
|
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: 470.78 E-value: 3.54e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 58 FDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDAS-----------------------------SAAE---------- 98
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDalhvlladeavcigpapsaksylnipniiSAAEitgadaihpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 99 -----------------DVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASA 161
Cdd:TIGR00514 82 ygflsenanfaeqcersGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 162 GGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 241
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 242 APSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPL 321
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 322 RHKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPIHlPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEA 401
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTF-LPSPGRITRYLPPGG-PGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958680995 402 LKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFL 443
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYL 441
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-322 |
1.96e-99 |
|
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: 303.07 E-value: 1.96e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 115 DKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGD 194
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 195 DRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDPETRRAMGEQAVALAKAVKYSSAGTV 274
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958680995 275 EFLVDS-QKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPLR 322
Cdd:pfam02786 161 EFALDPfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-443 |
7.09e-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: 166.43 E-value: 7.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 336 ECRVYAEDPYKSFgLPSIGRLSQYQEPIHlPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEALKRMEDALDSYVIR 415
Cdd:smart00878 1 ECRINAEDPANGF-LPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIR 78
|
90 100
....*....|....*....|....*...
gi 1958680995 416 GVTHNIPLLREVIINTRFVKGDISTKFL 443
Cdd:smart00878 79 GVKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| PCC_BT |
pfam18140 |
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ... |
464-592 |
7.69e-37 |
|
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.
Pssm-ID: 465666 [Multi-domain] Cd Length: 126 Bit Score: 133.91 E-value: 7.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 464 LLAIASSLFVASQLRAQRFQEHSRvPVIRPDVAKWELSVKLHDEDHTVVASNNGPTFNVEVDGSKLNVTSTWNLASPLLS 543
Cdd:pfam18140 1 LAAIAAAIHAVRELRARRISGQLR-GHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958680995 544 VNVDGTQRTVQClSRDAGGnMSIQFLGTVYKVHILTKLAAELNKFMLEK 592
Cdd:pfam18140 80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
600-666 |
6.07e-27 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 103.65 E-value: 6.07e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958680995 600 TLCSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVEL 666
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
602-667 |
3.32e-20 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 95.59 E-value: 3.32e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680995 602 CSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:PRK12999 1080 GAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
591-666 |
1.74e-19 |
|
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: 93.61 E-value: 1.74e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680995 591 EKVPKDTSSTLCSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVEL 666
Cdd:COG1038 1069 EKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
493-667 |
2.35e-19 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 92.21 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 493 PDVA----KWELSVKLHDEDHTVVASNNG----PT-FNVEVDGSKLNV--TSTWNLASPLLSVNVDGTQRTVQclsrdag 561
Cdd:PRK09282 432 PQIAkkflEEREAGELKPEPEPKEAAAAGaegiPTeFKVEVDGEKYEVkiEGVKAEGKRPFYLRVDGMPEEVV------- 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 562 gnmsiqflgtvykvhiltklAAELNKFMLEKVPK-DTSSTLCSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTA 640
Cdd:PRK09282 505 --------------------VEPLKEIVVGGRPRaSAPGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQA 564
|
170 180
....*....|....*....|....*..
gi 1958680995 641 GKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:PRK09282 565 PVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
603-666 |
4.91e-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: 78.80 E-value: 4.91e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958680995 603 SPMPGVVVA-----VSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVEL 666
Cdd:pfam00364 5 SPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
592-667 |
4.46e-13 |
|
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: 72.94 E-value: 4.46e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680995 592 KVPKDTSSTLCSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:TIGR01235 1068 KADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
58-468 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 668.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 58 FDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDASS------------------------------------------ 95
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDAlhvrladeavcigpapaaesylnidaiiaaakatgadaihpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 96 --------------AAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASA 161
Cdd:COG4770 82 ygflsenadfaeacEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 162 GGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 241
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 242 APSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPL 321
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 322 RHKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPIHlPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEA 401
Cdd:COG4770 322 PFTQEDIKLRGHAIECRINAEDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958680995 402 LKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFLSDVYPDGFkghmLTPSERDQLLAIA 468
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL----AAAAPEELALAAA 462
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
57-443 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 558.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 57 TFDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDAS-----------------------------SAAE--------- 98
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDalhvqladeavcigpapskksylnipaiiSAAEitgadaihp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 99 ------------------DVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKAS 160
Cdd:PRK08591 81 gygflsenadfaeicedsGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 161 AGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVE 240
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 241 EAPSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYP 320
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 321 LRHKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYqepiHLP---GVRVDSGIQPGSDISIYYDPMISKLVTYGSD 397
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNF-MPSPGKITRY----HPPggpGVRVDSAVYTGYTIPPYYDSMIGKLIVHGET 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958680995 398 RAEALKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFL 443
Cdd:PRK08591 396 REEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
58-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 533.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 58 FDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDASS------------------------------------------ 95
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDAlhvkmadeayliggprvqesylnlekiieiakktgaeaihpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 96 --------------AAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASA 161
Cdd:PRK06111 82 ygllsenasfaercKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 162 GGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 241
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 242 APSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPL 321
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 322 RHKQEDIPISGWAVECRVYAEDPyKSFgLPSIGRLSQYQEPIHlPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEA 401
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDP-KTF-FPSPGKITDLTLPGG-EGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958680995 402 LKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFLSD 445
Cdd:PRK06111 399 ISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
58-445 |
3.83e-178 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 516.07 E-value: 3.83e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 58 FDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDASS-----------------------------AAED--------- 99
Cdd:PRK08654 2 FKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNAlfvkyadeaypigpappsksylnieriidVAKKagadaihpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 100 ------------------VTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASA 161
Cdd:PRK08654 82 ygflaenpefakacekagIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 162 GGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 241
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 242 APSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSqKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPL 321
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN-GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 322 RHKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPiHLPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEA 401
Cdd:PRK08654 321 SFKQEDITIRGHAIECRINAEDPLNDF-APSPGKIKRYRSP-GGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958680995 402 LKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFLSD 445
Cdd:PRK08654 399 IARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEE 442
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
58-443 |
3.54e-161 |
|
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: 470.78 E-value: 3.54e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 58 FDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDAS-----------------------------SAAE---------- 98
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDalhvlladeavcigpapsaksylnipniiSAAEitgadaihpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 99 -----------------DVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASA 161
Cdd:TIGR00514 82 ygflsenanfaeqcersGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 162 GGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 241
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 242 APSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPL 321
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 322 RHKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPIHlPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEA 401
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTF-LPSPGRITRYLPPGG-PGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958680995 402 LKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFL 443
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYL 441
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
58-445 |
4.88e-160 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 467.65 E-value: 4.88e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 58 FDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDAS-----------------------------SAAE---------- 98
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDalhvqladeavcigpasskdsylniqniiSATVltgaqaihpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 99 -----------------DVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASA 161
Cdd:PRK05586 82 fgflsenskfakmckecNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 162 GGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 241
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 242 APSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPL 321
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 322 RHKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQyqepIHLPG---VRVDSGIQPGSDISIYYDPMISKLVTYGSDR 398
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGF-MPCPGKIEE----LYIPGglgVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958680995 399 AEALKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFLSD 445
Cdd:PRK05586 397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
54-445 |
5.55e-156 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 479.63 E-value: 5.55e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 54 KEKTFDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDASS-------------------------------------- 95
Cdd:PRK12999 1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSlhrfkadeayligegkhpvrayldideiirvakqagvd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 96 -------------------AAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVM 156
Cdd:PRK12999 81 aihpgygflsenpefaracAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 157 IKASAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQ 236
Cdd:PRK12999 161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 237 KVVEEAPSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVA 316
Cdd:PRK12999 241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 317 KGYPLR------HKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPIHlPGVRVDSGIQ-PGSDISIYYDPMIS 389
Cdd:PRK12999 321 EGATLHdleigiPSQEDIRLRGYAIQCRITTEDPANNF-MPDTGRITAYRSPGG-FGVRLDGGNAfAGAEITPYYDSLLV 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680995 390 KLVTYGSDRAEALKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFLSD 445
Cdd:PRK12999 399 KLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE 454
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
56-442 |
2.36e-152 |
|
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: 469.95 E-value: 2.36e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 56 KTFDKILIANRGEIACRVIKTCRKMGIRTVAIHS-----------------------------------------DVDA- 93
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSeedryslhrfkadeayligegkgpvdayldieeiirvakekGVDAi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 94 ---------------SSAAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIK 158
Cdd:COG1038 82 hpgygflsenpefarACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 159 ASAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKV 238
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 239 VEEAPSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKG 318
Cdd:COG1038 242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 319 YPLRHK------QEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPIHlPGVRVDSG-IQPGSDISIYYDPMISKL 391
Cdd:COG1038 322 YSLDDPeigipsQEDIRLNGYAIQCRITTEDPANNF-MPDTGRITAYRSAGG-FGIRLDGGnAYTGAVITPYYDSLLVKV 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958680995 392 VTYGSDRAEALKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKF 442
Cdd:COG1038 400 TAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSF 450
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
58-443 |
2.92e-138 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 412.96 E-value: 2.92e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 58 FDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVD--------ASSA--------------------------------- 96
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADrhalhvkrADEAysigadplagylnprrlvnlavetgcdalhpgy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 97 ---------AED-----VTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASAG 162
Cdd:PRK07178 82 gflsenaelAEIcaergIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 163 GGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEA 242
Cdd:PRK07178 162 GGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 243 PSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPLR 322
Cdd:PRK07178 242 PSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 323 HKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPiHLPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEAL 402
Cdd:PRK07178 322 YKQEDIQHRGFALQFRINAEDPKNDF-LPSFGKITRYYAP-GGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEAL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958680995 403 KRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFL 443
Cdd:PRK07178 400 DRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFV 440
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
56-443 |
7.64e-137 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 409.14 E-value: 7.64e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 56 KTFDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDASSA--------------------------------------- 96
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLaarmadeavhigpshaaksylnpaailaaarqcgadaih 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 97 ------------AEDVT-----FIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKA 159
Cdd:PRK12833 83 pgygflsenaafAEAVEaagliFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 160 SAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHgNALWLNERECSIQRRNQKVV 239
Cdd:PRK12833 163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 240 EEAPSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKN-FYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKG 318
Cdd:PRK12833 242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGeFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 319 YPLRHKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPiHLPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDR 398
Cdd:PRK12833 322 EPLRFAQGDIALRGAALECRINAEDPLRDF-FPNPGRIDALVWP-QGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958680995 399 AEALKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFL 443
Cdd:PRK12833 400 AAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
58-448 |
2.06e-136 |
|
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 274264 [Multi-domain] Cd Length: 1201 Bit Score: 429.45 E-value: 2.06e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 58 FDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDASS------------------------------------------ 95
Cdd:TIGR02712 1 FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASqhvldadeavclggapaaesyldidkilaaakktgaqaihpg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 96 --------------AAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGfDGVVKDADEAVRIAREIGYPVMIKASA 161
Cdd:TIGR02712 81 ygflsenaafaeacEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 162 GGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 241
Cdd:TIGR02712 160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 242 APSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKN-FYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYP 320
Cdd:TIGR02712 240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 321 LRHKQ--EDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPihlPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDR 398
Cdd:TIGR02712 320 PDFASlnISLTPRGAAIEARVYAENPAKNF-QPSPGLLTDVQFP---DDVRVDTWVETGTEVSPEYDPMLAKIIVHGSDR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958680995 399 AEALKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFLSD-VYP 448
Cdd:TIGR02712 396 EDAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNSfVYT 446
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
60-444 |
1.77e-134 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 402.20 E-value: 1.77e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 60 KILIANRGEIACRVIKTCRKMGIRTVAIHS--DVDAS---------------------------SAAE------------ 98
Cdd:PRK08462 6 RILIANRGEIALRAIRTIQEMGKEAIAIYStaDKDALylkyadakiciggakssesylnipaiiSAAEifeadaifpgyg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 99 ---------------DVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASAGG 163
Cdd:PRK08462 86 flsenqnfveicshhNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 164 GGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAP 243
Cdd:PRK08462 166 GGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 244 SIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPLrH 323
Cdd:PRK08462 246 AVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL-P 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 324 KQEDIPISGWAVECRVYAEDPyKSFgLPSIGRLSQYqepiHLPG---VRVDSGIQPGSDISIYYDPMISKLVTYGSDRAE 400
Cdd:PRK08462 325 SQESIKLKGHAIECRITAEDP-KKF-YPSPGKITKW----IAPGgrnVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958680995 401 ALKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFLS 444
Cdd:PRK08462 399 AIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
58-443 |
2.53e-110 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 341.02 E-value: 2.53e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 58 FDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDA-------------------------------------------- 93
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDReclhvkiadeayrigtdpikgyldvkriveiakacgadaihpgy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 94 ---------SSAAED--VTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRI-AREIGYPVMIKASA 161
Cdd:PRK08463 82 gflsenyefAKAVEDagIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIfARKIGYPVILKASG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 162 GGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEE 241
Cdd:PRK08463 162 GGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 242 APSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPL 321
Cdd:PRK08463 242 APCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEIL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 322 RHKQEDIPISGWAVECRVYAEDPYKSFgLPSIGRLSQYQePIHLPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEA 401
Cdd:PRK08463 322 DLEQSDIKPRGFAIEARITAENVWKNF-IPSPGKITEYY-PALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958680995 402 LKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFL 443
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYI 441
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-322 |
1.96e-99 |
|
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: 303.07 E-value: 1.96e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 115 DKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGD 194
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 195 DRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDPETRRAMGEQAVALAKAVKYSSAGTV 274
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958680995 275 EFLVDS-QKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPLR 322
Cdd:pfam02786 161 EFALDPfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
65-316 |
8.37e-56 |
|
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: 190.85 E-value: 8.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 65 NRGEIACRVIKTCRKMGIRTVAIHSDVDASSAA---EDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTiPGFDgVVKDA 141
Cdd:COG0439 1 DIDAIIAAAAELARETGIDAVLSESEFAVETAAelaEELGLPGPSPEAIRAMRDKVLMREALAAAGVPV-PGFA-LVDSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 142 DEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNpRHIEIQVLGDkHGNA 221
Cdd:COG0439 79 EEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVR-DGEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 222 LWlnereCSIQRRNQK---VVE---EAPSIfLDPETRRAMGEQAVALAKAVKYS-SAGTVEFLVDSQKNFYFLEMNTRLQ 294
Cdd:COG0439 157 VV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLG 230
|
250 260
....*....|....*....|....
gi 1958680995 295 VEH--PVTECITGLDLVQEMILVA 316
Cdd:COG0439 231 GEHipPLTELATGVDLVREQIRLA 254
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-445 |
5.53e-49 |
|
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: 166.51 E-value: 5.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 336 ECRVYAEDPYKSFgLPSIGRLSQYQEPiHLPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEALKRMEDALDSYVIR 415
Cdd:pfam02785 1 EARIYAEDPDNNF-LPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIE 78
|
90 100 110
....*....|....*....|....*....|
gi 1958680995 416 GVTHNIPLLREVIINTRFVKGDISTKFLSD 445
Cdd:pfam02785 79 GVKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-443 |
7.09e-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: 166.43 E-value: 7.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 336 ECRVYAEDPYKSFgLPSIGRLSQYQEPIHlPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEALKRMEDALDSYVIR 415
Cdd:smart00878 1 ECRINAEDPANGF-LPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIR 78
|
90 100
....*....|....*....|....*...
gi 1958680995 416 GVTHNIPLLREVIINTRFVKGDISTKFL 443
Cdd:smart00878 79 GVKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| PCC_BT |
pfam18140 |
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ... |
464-592 |
7.69e-37 |
|
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.
Pssm-ID: 465666 [Multi-domain] Cd Length: 126 Bit Score: 133.91 E-value: 7.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 464 LLAIASSLFVASQLRAQRFQEHSRvPVIRPDVAKWELSVKLHDEDHTVVASNNGPTFNVEVDGSKLNVTSTWNLASPLLS 543
Cdd:pfam18140 1 LAAIAAAIHAVRELRARRISGQLR-GHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958680995 544 VNVDGTQRTVQClSRDAGGnMSIQFLGTVYKVHILTKLAAELNKFMLEK 592
Cdd:pfam18140 80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
600-666 |
6.07e-27 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 103.65 E-value: 6.07e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958680995 600 TLCSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVEL 666
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
602-667 |
3.32e-20 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 95.59 E-value: 3.32e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680995 602 CSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:PRK12999 1080 GAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
58-134 |
6.22e-20 |
|
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: 85.23 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 58 FDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDASS----AAEDVTFIGPDThAIQAM--GDKIESklLAKRAKVNTI 131
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSlhvrLADEAVCLGPGP-ASESYlnIDAIID--AAKETGADAI 77
|
....
gi 1958680995 132 -PGF 134
Cdd:pfam00289 78 hPGY 81
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
591-666 |
1.74e-19 |
|
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: 93.61 E-value: 1.74e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680995 591 EKVPKDTSSTLCSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVEL 666
Cdd:COG1038 1069 EKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
493-667 |
2.35e-19 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 92.21 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 493 PDVA----KWELSVKLHDEDHTVVASNNG----PT-FNVEVDGSKLNV--TSTWNLASPLLSVNVDGTQRTVQclsrdag 561
Cdd:PRK09282 432 PQIAkkflEEREAGELKPEPEPKEAAAAGaegiPTeFKVEVDGEKYEVkiEGVKAEGKRPFYLRVDGMPEEVV------- 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 562 gnmsiqflgtvykvhiltklAAELNKFMLEKVPK-DTSSTLCSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTA 640
Cdd:PRK09282 505 --------------------VEPLKEIVVGGRPRaSAPGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQA 564
|
170 180
....*....|....*....|....*..
gi 1958680995 641 GKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:PRK09282 565 PVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
591-667 |
3.02e-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: 81.48 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 591 EKVPKDTSSTLCSPMPGVV-------VAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLL 663
Cdd:COG0511 53 AAAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
|
....
gi 1958680995 664 VELE 667
Cdd:COG0511 133 FVIE 136
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
603-666 |
4.91e-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: 78.80 E-value: 4.91e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958680995 603 SPMPGVVVA-----VSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVEL 666
Cdd:pfam00364 5 SPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
98-292 |
1.71e-15 |
|
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: 79.92 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 98 EDVTFIGPDTHAIqamgDKIE-----SKLLaKRAKVNTIPGfdGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAW 172
Cdd:COG0458 97 EGVKILGTSPDAI----DLAEdrelfKELL-DKLGIPQPKS--GTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 173 DDEE----TRDGFRFSsqeaassfGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLnereCSIQrrNqkvVEEA------ 242
Cdd:COG0458 170 NEEEleeyLERALKVS--------PDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsgd 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958680995 243 -----PSIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKnFYFLEMNTR 292
Cdd:COG0458 233 sicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGR-VYVIEVNPR 286
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
605-667 |
2.82e-15 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 70.97 E-value: 2.82e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958680995 605 MPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:PRK08225 8 MAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
603-664 |
3.82e-15 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 72.54 E-value: 3.82e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958680995 603 SPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLV 664
Cdd:PRK06549 66 SPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
600-666 |
2.46e-14 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 70.66 E-value: 2.46e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958680995 600 TLCSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVEL 666
Cdd:PRK05641 86 VVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
104-291 |
2.64e-13 |
|
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: 70.91 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 104 GPDTHAIqAMgDKIESKLLAKRAKVNTIPGFdgVVKDADEAV--RIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGF 181
Cdd:COG1181 86 GVLASAL-AM-DKALTKRVLAAAGLPTPPYV--VLRRGELADleAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAAL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 182 rfssqEAASSFgDDRLLIEKFIDnPRHIEIQVLGDKHGNALWLNErecsIQRRN-----------QKVVEEAPSIfLDPE 250
Cdd:COG1181 162 -----EEAFKY-DDKVLVEEFID-GREVTVGVLGNGGPRALPPIE----IVPENgfydyeakytdGGTEYICPAR-LPEE 229
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958680995 251 TRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNT 291
Cdd:COG1181 230 LEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
592-667 |
4.46e-13 |
|
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: 72.94 E-value: 4.46e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958680995 592 KVPKDTSSTLCSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:TIGR01235 1068 KADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
100-325 |
9.22e-13 |
|
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: 71.57 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 100 VTFIGPDTHAIqamgDKIE-----SKLLaKRAKVNTIPGfdGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDD 174
Cdd:TIGR01369 654 VPILGTSPESI----DRAEdrekfSELL-DELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNE 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 175 EETRDGFRfssqEAASSFGDDRLLIEKFIDNPRHIEIQVLGDkHGNALwlnerECSIQRRnqkvVEEA-----------P 243
Cdd:TIGR01369 727 EELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVL-----IPGIMEH----IEEAgvhsgdstcvlP 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 244 SIFLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDsQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMI-------LVA 316
Cdd:TIGR01369 793 PQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVrvmlgkkLEE 871
|
....*....
gi 1958680995 317 KGYPLRHKQ 325
Cdd:TIGR01369 872 LGVGKEKEP 880
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
73-291 |
1.67e-12 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 68.60 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 73 VIKTCRKMGIRTVAIhsDVDASSAAE------DVTFI------GPD--------------TH------AIqAMgDKIESK 120
Cdd:PRK01372 28 VLAALREAGYDAHPI--DPGEDIAAQlkelgfDRVFNalhgrgGEDgtiqgllellgipyTGsgvlasAL-AM-DKLRTK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 121 LLAKRAKVNTIPGfdGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFrfssqEAASSFgDDRLLIE 200
Cdd:PRK01372 104 LVWQAAGLPTPPW--IVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAAL-----ELAFKY-DDEVLVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 201 KFIDNPrhiEIQ--VLGDKhgnALwlnerecsiqrrnqKVVE-EAPSIF-------------------LDPETRRAMGEQ 258
Cdd:PRK01372 176 KYIKGR---ELTvaVLGGK---AL--------------PVIEiVPAGEFydyeakylaggtqyicpagLPAEIEAELQEL 235
|
250 260 270
....*....|....*....|....*....|...
gi 1958680995 259 AVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNT 291
Cdd:PRK01372 236 ALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
603-666 |
1.75e-10 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 63.80 E-value: 1.75e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958680995 603 SPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVEL 666
Cdd:PRK14040 529 APLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
607-666 |
2.90e-09 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 53.95 E-value: 2.90e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 607 GVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVEL 666
Cdd:cd06849 15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
97-293 |
3.51e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 59.17 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 97 AEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFdgVVKDADEAVRIAREIGYPVMIKASaggggkgMRIAWDD-- 174
Cdd:COG3919 99 EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTV--VLDSADDLDALAEDLGFPVVVKPA-------DSVGYDEls 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 175 -EETRDGFRFSSQEA------ASSFGDDRLLIEKFIDNPRHIEIQVLG--DKHGNALWLnereCSIQRRNQKVVEEAPSI 245
Cdd:COG3919 170 fPGKKKVFYVDDREEllallrRIAAAGYELIVQEYIPGDDGEMRGLTAyvDRDGEVVAT----FTGRKLRHYPPAGGNSA 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958680995 246 FLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKN-FYFLEMNTRL 293
Cdd:COG3919 246 ARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGeYKLIEINPRF 294
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
100-310 |
1.96e-08 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 57.67 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 100 VTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGfdGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRD 179
Cdd:PRK12815 655 LTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 180 GFRfssqEAASSfgDDRLLIEKFIDNpRHIEIQVLGDkhGNALWLN---ERecsiqrrnqkvVEEA-----------PSI 245
Cdd:PRK12815 733 YLA----ENASQ--LYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiEH-----------IEQAgvhsgdsiavlPPQ 792
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958680995 246 FLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQkNFYFLEMNTRLQVEHPVTECITGLDLVQ 310
Cdd:PRK12815 793 SLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAND-EIYVLEVNPRASRTVPFVSKATGVPLAK 856
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
607-666 |
2.52e-08 |
|
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: 51.29 E-value: 2.52e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 607 GVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVEL 666
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
605-667 |
9.28e-08 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 55.11 E-value: 9.28e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958680995 605 MPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:PRK14042 532 IPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
136-213 |
1.05e-07 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 55.49 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 136 GVVKDADEAVRIAREIGYPVMIKAS------AggggkgMRIAWDDEETRDGFRfssqEAASSFGDDRLLIEKFIDNPrhI 209
Cdd:PRK05294 688 GTATSVEEALEVAEEIGYPVLVRPSyvlggrA------MEIVYDEEELERYMR----EAVKVSPDHPVLIDKFLEGA--I 755
|
....
gi 1958680995 210 EIQV 213
Cdd:PRK05294 756 EVDV 759
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
99-291 |
1.78e-07 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 53.59 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 99 DVTFIGPDTHAiQAMG-DKIESKLLAKRAKVNTIPGFdgVVKDADEAVRIAREI----GYPVMIKASaggggkgmriawd 173
Cdd:PRK01966 107 GIPYVGCGVLA-SALSmDKILTKRLLAAAGIPVAPYV--VLTRGDWEEASLAEIeaklGLPVFVKPA------------- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 174 deetRDGfrfssqeaaSSFG--------------------DDRLLIEKFIdNPRHIEIQVLGdkhgnalwlNERECSiqr 233
Cdd:PRK01966 171 ----NLG---------SSVGiskvkneeelaaaldlafeyDRKVLVEQGI-KGREIECAVLG---------NDPKAS--- 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958680995 234 rnqkVVEE--APSIFLD-------------------PETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNT 291
Cdd:PRK01966 225 ----VPGEivKPDDFYDyeakyldgsaeliipadlsEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
607-666 |
2.39e-07 |
|
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: 48.52 E-value: 2.39e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 607 GVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVEL 666
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
91-220 |
6.87e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 52.86 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 91 VDASSAAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGfdGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRI 170
Cdd:PLN02735 678 PPSASGNGNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEI 755
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958680995 171 AWDDEETRdgfrfSSQEAASSFGDDR-LLIEKFIDNPRHIEIQVLGDKHGN 220
Cdd:PLN02735 756 VYSDDKLK-----TYLETAVEVDPERpVLVDKYLSDATEIDVDALADSEGN 801
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
607-667 |
1.54e-06 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 51.41 E-value: 1.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958680995 607 GVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:TIGR01348 14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
100-293 |
4.42e-06 |
|
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: 50.00 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 100 VTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFdgVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEE--- 176
Cdd:TIGR01369 112 VEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESE--IAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREElke 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 177 -TRDGFRFSSQeaassfgdDRLLIEKFIDNPRHIEIQVLGDKHGNALWLnereCSIQrrN----------QKVVeeAPSI 245
Cdd:TIGR01369 190 iAERALSASPI--------NQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNME--NfdpmgvhtgdSIVV--APSQ 253
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958680995 246 FLDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQ-KNFYFLEMNTRL 293
Cdd:TIGR01369 254 TLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsGRYYVIEVNPRV 302
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
150-291 |
4.52e-06 |
|
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: 48.08 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 150 EIGYPVMIKASAGGGGKGMRIAWDDEETRDGFrfssqEAASSFgDDRLLIEKFIDNpRHIEIQVLGDKHGNALWLNER-- 227
Cdd:pfam07478 34 ALGYPVFVKPARLGSSVGVSKVESREELQAAI-----EEAFQY-DEKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvp 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958680995 228 ECSIQRRNQKVVEEAPSIF----LDPETRRAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNT 291
Cdd:pfam07478 107 SGGFYDYEAKYIDDSAQIVvpadLEEEQEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
609-667 |
8.54e-06 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 49.05 E-value: 8.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958680995 609 VVAVSVKPGDMVAEGQEICVIEAMK--MQnsMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:PRK11855 135 VIEWLVKVGDTVEEDQSLITVETDKatME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
600-667 |
1.14e-05 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 43.85 E-value: 1.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958680995 600 TLCSPMPGVV-------VAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:PRK07051 5 EIVSPLPGTFyrrpspdAPPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
592-646 |
2.02e-05 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 46.76 E-value: 2.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958680995 592 KVPKDTSSTLCSPMPGVVVAVS-------VKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKV 646
Cdd:PLN02983 191 KAPKSSHPPLKSPMAGTFYRSPapgeppfVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTI 252
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
99-293 |
4.27e-05 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 46.89 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 99 DVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTipGFDGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETR 178
Cdd:PRK12815 112 GVELLGTNIEAIQKGEDRERFRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 179 DGFRfsSQEAASSFGDdrLLIEKFIDNPRHIEIQVLGDKHGNALWLNERE----CSIQRRNQKVVeeAPSIFLDPETRRA 254
Cdd:PRK12815 190 QLFK--QGLQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCITVCNMEnidpVGIHTGDSIVV--APSQTLTDDEYQM 263
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958680995 255 MGEQAVALAKAVKYSSAGTVEFLVD-SQKNFYFLEMNTRL 293
Cdd:PRK12815 264 LRSASLKIISALGVVGGCNIQFALDpKSKQYYLIEVNPRV 303
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
607-667 |
6.92e-05 |
|
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: 46.02 E-value: 6.92e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958680995 607 GVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:TIGR01348 130 VTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
609-667 |
1.32e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 45.20 E-value: 1.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958680995 609 VVAVSVKPGDMVAEGQEICVIEAMK--MQnsMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:PRK11855 18 VIEWLVKEGDTVEEDQPLVTVETDKatME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
118-159 |
2.14e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 44.35 E-value: 2.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958680995 118 ESKLLAKRAKVNTIPGfdGVVKDADEAVRIAREIGYPVMIKA 159
Cdd:COG1042 492 EAKALLAAYGIPVVPT--RLARSAEEAVAAAEEIGYPVVLKI 531
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
609-663 |
2.75e-04 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 39.79 E-value: 2.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958680995 609 VVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLL 663
Cdd:PRK05889 13 VLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLI 67
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
99-221 |
7.49e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 42.78 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 99 DVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGfdGVVKDADEAVRIAREIGYPVMIkasaggggkgmR--------- 169
Cdd:PRK05294 112 GVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVII-----------Rpsftlggtg 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 170 --IAWDDEETRD----GFRFS--SQeaassfgddrLLIEKFIDNPRHIEIQVLGDKHGNA 221
Cdd:PRK05294 179 ggIAYNEEELEEiverGLDLSpvTE----------VLIEESLLGWKEYEYEVMRDKNDNC 228
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
90-289 |
1.02e-03 |
|
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: 41.98 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 90 DVDASSAAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTiPGFDgVVKDADEAVRIAREIGYPVMIKAsaggggkgmr 169
Cdd:COG0026 64 PAEALEALEAEVPVRPGPEALEIAQDRLLEKAFLAELGIPV-APFA-AVDSLEDLEAAIAELGLPAVLKT---------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958680995 170 iawddeeTRDG------FRFSSQE----AASSFGDDRLLIEKFIDNPRhiEIQVLG--DKHGN-ALW---LNerecsIQR 233
Cdd:COG0026 132 -------RRGGydgkgqVVIKSAAdleaAWAALGGGPCILEEFVPFER--ELSVIVarSPDGEvATYpvvEN-----VHR 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958680995 234 RNQKVVEEAPSiFLDPETRRAMGEQAVALAKAVKYssAGT--VEFLVDSQKNFYFLEM 289
Cdd:COG0026 198 NGILDESIAPA-RISEALAAEAEEIAKRIAEALDY--VGVlaVEFFVTKDGELLVNEI 252
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
137-158 |
2.31e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 40.15 E-value: 2.31e-03
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
136-158 |
3.94e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 40.52 E-value: 3.94e-03
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
607-667 |
8.74e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 39.22 E-value: 8.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958680995 607 GVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE 667
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
|
|
| |
