|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-455 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 715.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPG 80
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 81 YGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAF 160
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 161 GGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEE 240
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 241 APAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPL 320
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 321 RLT-ADPAPRGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALR 399
Cdd:COG4770 322 PFTqEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2273475591 400 RARRALAEMEITGVATVLPFHRAVVQAPDFMSETalgIHTRWIETDFADSIAADPE 455
Cdd:COG4770 402 RMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGD---VDTGFIERELAELLAAAAP 454
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-447 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 575.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPG 80
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 81 YGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAF 160
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 161 GGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEE 240
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 241 APAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPL 320
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 321 RLT-ADPAPRGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALR 399
Cdd:PRK08591 322 SIKqEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2273475591 400 RARRALAEMEITGVATVLPFHRAVVQAPDFMSEtalGIHTRWIETDFA 447
Cdd:PRK08591 402 RMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAG---DYNIHYLEKKLA 446
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-431 |
5.19e-168 |
|
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: 485.42 E-value: 5.19e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPG 80
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 81 YGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAF 160
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 161 GGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEE 240
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 241 APAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPL 320
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 321 RLTADPAP-RGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALR 399
Cdd:TIGR00514 322 SLKQEDVVvRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIA 401
|
410 420 430
....*....|....*....|....*....|..
gi 2273475591 400 RARRALAEMEITGVATVLPFHRAVVQAPDFMS 431
Cdd:TIGR00514 402 RMKRALSEFIIDGIKTTIPFHQRILEDENFQH 433
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-321 |
7.13e-88 |
|
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: 271.10 E-value: 7.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 115 KITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVVREMDQIEESFDSAVREAVVAFGRG 194
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 195 ECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEEAPAPFLTDQQTQLIYDAAKAVCREASYSGAGTVE 274
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2273475591 275 FLV-AADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPLR 321
Cdd:pfam02786 162 FALdPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
334-443 |
4.34e-35 |
|
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: 127.91 E-value: 4.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 334 EFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALRRARRALAEMEITGV 413
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100 110
....*....|....*....|....*....|
gi 2273475591 414 ATVLPFHRAVVQAPDFMSETalgIHTRWIE 443
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGD---VDTGFLE 107
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
524-590 |
1.69e-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: 94.02 E-value: 1.69e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273475591 524 ELRADMAGTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
458-587 |
7.46e-15 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 77.66 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 458 TSVPDGERRTITVDVDGRRLAVGL-PADLLDGWARSGAAVPAGLSLDGAGLDGAADggaaagaadpgELRADMAGTVVKW 536
Cdd:PRK14040 470 AKAEPAGSETYTVEVEGKAYVVKVsEGGDISQITPAAPAAAPAAAAAAAPAAAAGE-----------PVTAPLAGNIFKV 538
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2273475591 537 LVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVL 587
Cdd:PRK14040 539 IVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
522-590 |
1.11e-14 |
|
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: 77.81 E-value: 1.11e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2273475591 522 PGELRADMAGTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:COG1038 1076 PGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
522-591 |
4.38e-14 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 75.56 E-value: 4.38e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 522 PGELRADMAGTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:PRK12999 1076 PGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
524-590 |
8.11e-14 |
|
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: 66.47 E-value: 8.11e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2273475591 524 ELRADMAGT-----VVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:pfam00364 2 EIKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
531-591 |
1.02e-04 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 45.11 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273475591 531 GTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:TIGR01347 15 GTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-455 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 715.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPG 80
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 81 YGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAF 160
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 161 GGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEE 240
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 241 APAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPL 320
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 321 RLT-ADPAPRGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALR 399
Cdd:COG4770 322 PFTqEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2273475591 400 RARRALAEMEITGVATVLPFHRAVVQAPDFMSETalgIHTRWIETDFADSIAADPE 455
Cdd:COG4770 402 RMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGD---VDTGFIERELAELLAAAAP 454
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-447 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 575.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPG 80
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 81 YGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAF 160
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 161 GGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEE 240
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 241 APAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPL 320
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 321 RLT-ADPAPRGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALR 399
Cdd:PRK08591 322 SIKqEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2273475591 400 RARRALAEMEITGVATVLPFHRAVVQAPDFMSEtalGIHTRWIETDFA 447
Cdd:PRK08591 402 RMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAG---DYNIHYLEKKLA 446
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-444 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 548.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLG-GNAPSETYLDIPKLLRVAAESGADAVHP 79
Cdd:PRK12999 5 IKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGeGKHPVRAYLDIDEIIRVAKQAGVDAIHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 80 GYGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAA 159
Cdd:PRK12999 85 GYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 160 FGGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVE 239
Cdd:PRK12999 165 AGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 240 EAPAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEP 319
Cdd:PRK12999 245 IAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGAT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 320 LRLT-------ADPAPRGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSG-VRSGSIVAPQFDSLLAKLIVTG 391
Cdd:PRK12999 325 LHDLeigipsqEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGnAFAGAEITPYYDSLLVKLTAWG 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2273475591 392 ADRQQALRRARRALAEMEITGVATVLPFHRAVVQAPDFMSEtalGIHTRWIET 444
Cdd:PRK12999 405 RTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAG---DYTTSFIDE 454
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
3-447 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 532.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 3 KVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPGYG 82
Cdd:PRK06111 4 KVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPGYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 83 FLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAFGG 162
Cdd:PRK06111 84 LLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 163 GGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEEAP 242
Cdd:PRK06111 164 GGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 243 APFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPLRL 322
Cdd:PRK06111 244 SPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 323 T-ADPAPRGHSFEFRLNAEDvGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALRRA 401
Cdd:PRK06111 324 TqDDIKRSGHAIEVRIYAED-PKTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRL 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2273475591 402 RRALAEMEITGVATVLPFHRAVVQAPDFMS-ETALGIHTRWIETDFA 447
Cdd:PRK06111 403 HDALEELKVEGIKTNIPLLLQVLEDPVFKAgGYTTGFLTKQLVKKST 449
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-444 |
3.10e-179 |
|
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: 537.36 E-value: 3.10e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLG-GNAPSETYLDIPKLLRVAAESGADAVHP 79
Cdd:COG1038 4 IKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGeGKGPVDAYLDIEEIIRVAKEKGVDAIHP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 80 GYGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAA 159
Cdd:COG1038 84 GYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 160 FGGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVE 239
Cdd:COG1038 164 AGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 240 EAPAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEP 319
Cdd:COG1038 244 IAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 320 LrltADPA----------PRGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSG-VRSGSIVAPQFDSLLAKLI 388
Cdd:COG1038 324 L---DDPEigipsqedirLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGnAYTGAVITPYYDSLLVKVT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2273475591 389 VTGADRQQALRRARRALAEMEITGVATVLPFHRAVVQAPDFMSETAlgiHTRWIET 444
Cdd:COG1038 401 AWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGEC---TTSFIDE 453
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-443 |
6.36e-179 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 514.92 E-value: 6.36e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 2 RKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPGY 81
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 82 GFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAFG 161
Cdd:PRK08654 83 GFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 162 GGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEEA 241
Cdd:PRK08654 163 GGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 242 PAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVaADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPLR 321
Cdd:PRK08654 243 PSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 322 LTA-DPAPRGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALRR 400
Cdd:PRK08654 322 FKQeDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIAR 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2273475591 401 ARRALAEMEITGVATVLPFHRAVVQAPDFMSETalgIHTRWIE 443
Cdd:PRK08654 402 MRRALYEYVIVGVKTNIPFHKAVMENENFVRGN---LHTHFIE 441
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-431 |
5.19e-168 |
|
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: 485.42 E-value: 5.19e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPG 80
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 81 YGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAF 160
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 161 GGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEE 240
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 241 APAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPL 320
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 321 RLTADPAP-RGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALR 399
Cdd:TIGR00514 322 SLKQEDVVvRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIA 401
|
410 420 430
....*....|....*....|....*....|..
gi 2273475591 400 RARRALAEMEITGVATVLPFHRAVVQAPDFMS 431
Cdd:TIGR00514 402 RMKRALSEFIIDGIKTTIPFHQRILEDENFQH 433
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-431 |
1.18e-164 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 477.67 E-value: 1.18e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNaPSETYLDIPKLLRVAAESGADAVHPG 80
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD-PLAGYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 81 YGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAF 160
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 161 GGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEE 240
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 241 APAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPL 320
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 321 RLT-ADPAPRGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALR 399
Cdd:PRK07178 321 SYKqEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALD 400
|
410 420 430
....*....|....*....|....*....|..
gi 2273475591 400 RARRALAEMEITGVATVLPFHRAVVQAPDFMS 431
Cdd:PRK07178 401 RGRRALDDMRVQGVKTTIPYYQEILRNPEFRS 432
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-433 |
5.31e-163 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 472.66 E-value: 5.31e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 2 RKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPGY 81
Cdd:PRK05586 3 KKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 82 GFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAFG 161
Cdd:PRK05586 83 GFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 162 GGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEEA 241
Cdd:PRK05586 163 GGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 242 PAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPLR 321
Cdd:PRK05586 243 PSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 322 LT-ADPAPRGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALRR 400
Cdd:PRK05586 323 IKqEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQK 402
|
410 420 430
....*....|....*....|....*....|...
gi 2273475591 401 ARRALAEMEITGVATVLPFHRAVVQAPDFMSET 433
Cdd:PRK05586 403 MKRALGEFIIEGVNTNIDFQFIILEDEEFIKGT 435
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
3-444 |
3.93e-155 |
|
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: 474.70 E-value: 3.93e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 3 KVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLG---GNAPSETYLDIPKLLRVAAESGADAVHP 79
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGegpDLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 80 GYGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAA 159
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 160 FGGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVE 239
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 240 EAPAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEP 319
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 320 LRLTADPAP-------RGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVR-SGSIVAPQFDSLLAKLIVTG 391
Cdd:TIGR01235 321 LPTPQLGVPnqedirtNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSyAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2273475591 392 ADRQQALRRARRALAEMEITGVATVLPFHRAVVQAPDFMSETalgIHTRWIET 444
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGS---YDTRFIDT 450
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-444 |
4.67e-152 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 445.35 E-value: 4.67e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPG 80
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 81 YGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAF 160
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 161 GGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHgNVVVVGTRDCSLQRRHQKLVEE 240
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 241 APAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLV-AADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEP 319
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFdDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 320 LRLT-ADPAPRGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQAL 398
Cdd:PRK12833 324 LRFAqGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAAL 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2273475591 399 RRARRALAEMEITGVATVLPFHRAVVQAPDFMsetALGIHTRWIET 444
Cdd:PRK12833 404 ARAARALRELRIDGMKTTAPLHRALLADADVR---AGRFHTNFLEA 446
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-429 |
3.88e-150 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 440.79 E-value: 3.88e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNaPSETYLDIPKLLRVAAESGADAVHPG 80
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTD-PIKGYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 81 YGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDgPV--ASAAEVRTFAEEHGLPIAIKA 158
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTE-KLnsESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 159 AFGGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLV 238
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 239 EEAPAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGE 318
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 319 PLRLT-ADPAPRGHSFEFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQA 397
Cdd:PRK08463 320 ILDLEqSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430
....*....|....*....|....*....|..
gi 2273475591 398 LRRARRALAEMEITGVATVLPFHRAVVQAPDF 429
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREF 431
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-446 |
3.19e-142 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 419.53 E-value: 3.19e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPG 80
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 81 YGFLSENAGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAF 160
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 161 GGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEE 240
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 241 APAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPL 320
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 321 RLTADPAPRGHSFEFRLNAEDvGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALRR 400
Cdd:PRK08462 324 PSQESIKLKGHAIECRITAED-PKKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAK 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2273475591 401 ARRALAEMEITGVATVLPFHRAVVQAPDFMSETalgIHTRWIETDF 446
Cdd:PRK08462 403 MKRALKEFKVEGIKTTIPFHLEMMENADFINNK---YDTKYLEEHF 445
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
115-321 |
7.13e-88 |
|
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: 271.10 E-value: 7.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 115 KITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVVREMDQIEESFDSAVREAVVAFGRG 194
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 195 ECFVERYLDRPRHVEAQVLADQHGNVVVVGTRDCSLQRRHQKLVEEAPAPFLTDQQTQLIYDAAKAVCREASYSGAGTVE 274
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2273475591 275 FLV-AADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEPLR 321
Cdd:pfam02786 162 FALdPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-108 |
1.56e-54 |
|
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: 180.37 E-value: 1.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 2 RKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGGNAPSETYLDIPKLLRVAAESGADAVHPGY 81
Cdd:pfam00289 2 KKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPGY 81
|
90 100
....*....|....*....|....*..
gi 2273475591 82 GFLSENAGFAQAVLDAGLTWIGPNPEA 108
Cdd:pfam00289 82 GFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
61-319 |
1.03e-51 |
|
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: 178.14 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 61 DIPKLLRVAAE----SGADAVhpgygfLSENAG----FAQAVLDAGLTwiGPNPEAIRQLGNKITAREIAVRAGAPlVAG 132
Cdd:COG0439 1 DIDAIIAAAAElareTGIDAV------LSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 133 TDgPVASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLDRpRHVEAQV 212
Cdd:COG0439 72 FA-LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 213 LAdQHGNVVVvgtrdCSLQRRHQK---LVE---EAPAPfLTDQQTQLIYDAAKAVCREASYS-GAGTVEFLVAADGTVAF 285
Cdd:COG0439 150 LV-RDGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYL 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 2273475591 286 LEVNTRLQVEH--PITEETTGVDLVQEQFRIAAGEP 319
Cdd:COG0439 223 IEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
334-443 |
4.34e-35 |
|
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: 127.91 E-value: 4.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 334 EFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALRRARRALAEMEITGV 413
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100 110
....*....|....*....|....*....|
gi 2273475591 414 ATVLPFHRAVVQAPDFMSETalgIHTRWIE 443
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGD---VDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
334-444 |
7.83e-34 |
|
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: 124.14 E-value: 7.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 334 EFRLNAEDVGRGFLPSPGTVATFSGPTGPGIRLDSGVRSGSIVAPQFDSLLAKLIVTGADRQQALRRARRALAEMEITGV 413
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100 110
....*....|....*....|....*....|.
gi 2273475591 414 ATVLPFHRAVVQAPDFmseTALGIHTRWIET 444
Cdd:pfam02785 81 KTNIPFLRAILEHPDF---RAGEVDTGFLEE 108
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
524-590 |
1.69e-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: 94.02 E-value: 1.69e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273475591 524 ELRADMAGTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
454-590 |
9.24e-18 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 86.82 E-value: 9.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 454 PEFGTSVPDGERRTITVDVDGRRLAVGLPADLLDGWARSGAAVPAGLSLDGAGLDGAADGGAAAGAADPGELRADMAGTV 533
Cdd:PRK09282 454 KEAAAAGAEGIPTEFKVEVDGEKYEVKIEGVKAEGKRPFYLRVDGMPEEVVVEPLKEIVVGGRPRASAPGAVTSPMPGTV 533
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2273475591 534 VKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:PRK09282 534 VKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
458-587 |
7.46e-15 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 77.66 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 458 TSVPDGERRTITVDVDGRRLAVGL-PADLLDGWARSGAAVPAGLSLDGAGLDGAADggaaagaadpgELRADMAGTVVKW 536
Cdd:PRK14040 470 AKAEPAGSETYTVEVEGKAYVVKVsEGGDISQITPAAPAAAPAAAAAAAPAAAAGE-----------PVTAPLAGNIFKV 538
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2273475591 537 LVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVL 587
Cdd:PRK14040 539 IVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
522-590 |
1.11e-14 |
|
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: 77.81 E-value: 1.11e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2273475591 522 PGELRADMAGTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:COG1038 1076 PGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
522-591 |
4.38e-14 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 75.56 E-value: 4.38e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 522 PGELRADMAGTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:PRK12999 1076 PGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
524-591 |
5.65e-14 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 67.12 E-value: 5.65e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2273475591 524 ELRADMAGTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:PRK08225 3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
524-590 |
8.11e-14 |
|
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: 66.47 E-value: 8.11e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2273475591 524 ELRADMAGT-----VVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:pfam00364 2 EIKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
102-291 |
3.05e-13 |
|
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: 72.22 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 102 IGPNPEAIRQLGNKITAREIAVRAGAPLVAGtdGPVASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVVREMDQIEEsfd 181
Cdd:COG0458 102 LGTSPDAIDLAEDRELFKELLDKLGIPQPKS--GTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEE--- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 182 sAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVgtrdCSLQrrHqklVEEA-----------PAPFLTDQQ 250
Cdd:COG0458 177 -YLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKE 246
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2273475591 251 TQLIYDAAKAVCREASYSGAGTVEFLVaADGTVAFLEVNTR 291
Cdd:COG0458 247 YQRLRDATLKIARALGVVGLCNIQFAV-DDGRVYVIEVNPR 286
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
522-591 |
8.81e-13 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 65.69 E-value: 8.81e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273475591 522 PGELRADMAGTV-------VKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:COG0511 60 GGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
91-321 |
2.09e-12 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 70.41 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 91 AQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGtdGPVASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVV 170
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 171 REMDQIEESFdsavREAVVAFGRGECFVERYLDRPRHVEAQVLADqHGNVVVVGTRDcslqrrHqklVEEA--------- 241
Cdd:TIGR01369 724 YNEEELRRYL----EEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVLIPGIME------H---IEEAgvhsgdstc 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 242 --PAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAaDGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAGEP 319
Cdd:TIGR01369 790 vlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKK 868
|
..
gi 2273475591 320 LR 321
Cdd:TIGR01369 869 LE 870
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
91-335 |
3.14e-12 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 69.61 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 91 AQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAGtdGPVASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVV 170
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVV 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 171 REMDQIEESFDSAVR--EAVVafgrgecfVERYLDrPRHVEAQVLADqhGNVVVVGTrdcslQRRHqklVEEA------- 241
Cdd:PRK12815 725 YDEPALEAYLAENASqlYPIL--------IDQFID-GKEYEVDAISD--GEDVTIPG-----IIEH---IEQAgvhsgds 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 242 ----PAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVaADGTVAFLEVNTRLQVEHPITEETTGVDLVQEQFRIAAG 317
Cdd:PRK12815 786 iavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLG 864
|
250
....*....|....*...
gi 2273475591 318 EPLRLTADPAPRGHSFEF 335
Cdd:PRK12815 865 KSLAELGYPNGLWPGSPF 882
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
527-591 |
4.17e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 60.60 E-value: 4.17e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273475591 527 ADMAGTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:PRK06549 66 SPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
59-290 |
1.01e-10 |
|
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: 63.20 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 59 YLDIPKLLRVAAESGADAVHPG-YGFLSENaGFAQAVLD-AGLTWIGPNPEAIRqLG-NKITAREIAVRAGAPLVAGTDG 135
Cdd:COG1181 39 GIDVEDLPAALKELKPDVVFPAlHGRGGED-GTIQGLLElLGIPYTGSGVLASA-LAmDKALTKRVLAAAGLPTPPYVVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 136 PVASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVVREmdqiEESFDSAVREAVvAFGRgECFVERYLDrPRHVEAQVLAD 215
Cdd:COG1181 117 RRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKN----AEELAAALEEAF-KYDD-KVLVEEFID-GREVTVGVLGN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 216 QHGNVVVVG---------------TRDcslqrrhqKLVEEAPAPfLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAAD 280
Cdd:COG1181 190 GGPRALPPIeivpengfydyeakyTDG--------GTEYICPAR-LPEELEERIQELALKAFRALGCRGYARVDFRLDED 260
|
250
....*....|
gi 2273475591 281 GTVAFLEVNT 290
Cdd:COG1181 261 GEPYLLEVNT 270
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
1-330 |
1.79e-10 |
|
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: 63.01 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANrgeIAVR-IARACEDAGLESVAV--YADVDADAmhvgAAREAYSLGGNAPSETYLDIP-KLLRVAAESGADA 76
Cdd:COG2232 4 PPDLLIAG---FSARaLAQSARRAGYRVYAVdlFADLDTRA----LAERWVRLDAESCGFDLEDLPaALLELAAADDPDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 77 VHPGYGFLSENAGFAQavLDAGLTWIGPNPEAIRQLGNKitareiavRAGAPLVAGTDGPVAsaaEVRTFAEEHGLPIAI 156
Cdd:COG2232 77 LVYGSGFENFPELLER--LARRLPLLGNPPEVVRRVKDP--------LRFFALLDELGIPHP---ETRFEPPPDPGPWLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 157 KAAFGGGGRGLKVVREMdqieesfdsavreavvAFGRGECFVERYLDrPRHVEAQVLADQHgNVVVVGtrdCSLQrrhqk 236
Cdd:COG2232 144 KPIGGAGGWHIRPADSE----------------APPAPGRYFQRYVE-GTPASVLFLADGS-DARVLG---FNRQ----- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 237 LVEEAPA-PF----------LTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAfLEVNTRLQVEHPITEETTGV 305
Cdd:COG2232 198 LIGPAGErPFryggnigplaLPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYV-LEVNPRPQASLDLYEDATGG 276
|
330 340
....*....|....*....|....*
gi 2273475591 306 DLVQEQFRIAAGEpLRLTADPAPRG 330
Cdd:COG2232 277 NLFDAHLRACRGE-LPEVPRPKPRR 300
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
531-590 |
1.06e-09 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 55.07 E-value: 1.06e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 531 GTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
1-358 |
2.00e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 59.56 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIANRGEIAVRIARACEDAGLESVAVYADVDADAMHVGAAREAYSLGG-NAPSETYLDipKLLRVAAESGADAVHP 79
Cdd:COG3919 5 RFRVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDpGDDPEAFVD--ALLELAERHGPDVLIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 80 GY----GFLSENAgfaqAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPlVAGTDgPVASAAEVRTFAEEHGLPIA 155
Cdd:COG3919 83 TGdeyvELLSRHR----DELEEHYRLPYPDADLLDRLLDKERFYELAEELGVP-VPKTV-VLDSADDLDALAEDLGFPVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 156 IKAA--------FGGGGRGLKVVREMDQIEESFDSAVREAvvafgrGECFVERYLDRPRHVEAQV--LADQHGNVVVVGT 225
Cdd:COG3919 157 VKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAG------YELIVQEYIPGDDGEMRGLtaYVDRDGEVVATFT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 226 RdcslQRRHQK--------LVEEAPAPFLtdqqtqliYDAAKAVCREASYSGAGTVEFLV-AADGTVAFLEVNTRLQVEH 296
Cdd:COG3919 231 G----RKLRHYppaggnsaARESVDDPEL--------EEAARRLLEALGYHGFANVEFKRdPRDGEYKLIEINPRFWRSL 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2273475591 297 PITEEtTGVDLVQEQFRIAAGEPLRLTADPAPRGHsfeFRLNAEDVGRGFLPSPGTVATFSG 358
Cdd:COG3919 299 YLATA-AGVNFPYLLYDDAVGRPLEPVPAYREGVL---WRVLPGDLLLRYLRDGELRKRLRE 356
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
1-203 |
4.35e-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: 58.03 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 1 MRKVLIA---NRGEIAVRIARACEDAGLEsvAVYADVDADAMHVGAAREayslggnapsetyldipkLLRVAAESGADAV 77
Cdd:COG0189 1 MMKIAILtdpPDKDSTKALIEAAQRRGHE--VEVIDPDDLTLDLGRAPE------------------LYRGEDLSEFDAV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 78 HPGYGFLSENAGFAQAVLDAGLTWIgPNPEAIRQLGNKITAREIAVRAGAP----LVAgtdgpvASAAEVRTFAEEHGLP 153
Cdd:COG0189 61 LPRIDPPFYGLALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPvpptLVT------RDPDDLRAFLEELGGP 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2273475591 154 IAIKAAFGGGGRGLKVVREMDQIEesfdsAVREAVVAFGRGECFVERYLD 203
Cdd:COG0189 134 VVLKPLDGSGGRGVFLVEDEDALE-----SILEALTELGSEPVLVQEFIP 178
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
530-590 |
6.75e-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: 52.83 E-value: 6.75e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273475591 530 AGTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:cd06663 13 DGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
104-283 |
7.83e-09 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 57.86 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 104 PNPEAIRQLGNKITAREIAVRAGAPLVAGTdgPVASAAEVRTFAEEHGLPIAIKAAFGG-GGRGLKVVREMDQIEESFDs 182
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFA--VVDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAWA- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 183 avreavvAFGRGECFVERYLDRPRhvEAQVLA--DQHGNVV---VVGTrdcsLQRRHQKLVEEAPAPFLTDQQTQlIYDA 257
Cdd:PRK06019 167 -------LLGSVPCILEEFVPFER--EVSVIVarGRDGEVVfypLVEN----VHRNGILRTSIAPARISAELQAQ-AEEI 232
|
170 180
....*....|....*....|....*.
gi 2273475591 258 AKAVCREASYSGAGTVEFLVAADGTV 283
Cdd:PRK06019 233 ASRIAEELDYVGVLAVEFFVTGDGEL 258
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
103-350 |
8.09e-09 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 58.71 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 103 GPNPEAIRQLGNKITAREIAVRAGAPlVAGTDGpVASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVVREMDQIEESFDS 182
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGID-VPRTHA-LALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 183 AVREavvafGRGECFVERYLDRPRH-VEAQVLADQHGNVVVVGTRdcslQRRHQKLVEEA---PAPFLTDQQTQLIYDAA 258
Cdd:PRK02186 174 LRRA-----GTRAALVQAYVEGDEYsVETLTVARGHQVLGITRKH----LGPPPHFVEIGhdfPAPLSAPQRERIVRTVL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 259 KAVCREASYSGAGTVEFLVAADgTVAFLEVNTRLQ--VEHPITEETTGVDLVQEQFRIAAGEPlrLTADPAPRGHS-FEF 335
Cdd:PRK02186 245 RALDAVGYAFGPAHTELRVRGD-TVVIIEINPRLAggMIPVLLEEAFGVDLLDHVIDLHLGVA--AFADPTAKRYGaIRF 321
|
250
....*....|....*...
gi 2273475591 336 RLNA---EDVGRGFLPSP 350
Cdd:PRK02186 322 VLPArsgVLRGLLFLPDD 339
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
136-291 |
1.30e-08 |
|
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: 54.57 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 136 PVASAAEVRTFAEEHGLPIAIKAAFGG-GGRGLKVVREMDQIEesfdsavrEAVVAFGRGECFVERYLDRPRHVEAQVLA 214
Cdd:pfam02222 12 AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP--------QAWEELGDGPVIVEEFVPFDRELSVLVVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 215 DQHGNVV---VVGTRdcslqRRHQKLVEE-APAPFLTDQQtQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNT 290
Cdd:pfam02222 84 SVDGETAfypVVETI-----QEDGICRLSvAPARVPQAIQ-AEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAP 157
|
.
gi 2273475591 291 R 291
Cdd:pfam02222 158 R 158
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
524-590 |
1.70e-08 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 51.35 E-value: 1.70e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273475591 524 ELRADMAGTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:PRK05889 4 DVRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
469-591 |
8.34e-08 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 51.79 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 469 TVDVDGRRLAVGLPAdlLDGWARSGAAVPAGLSLDGAGLDGAADGGAAAGAADPGELRADMAGTVVKWLVEPGAEVAAGD 548
Cdd:PRK05641 33 TYEVEAKGLGIDLSA--VQEQVPTPAPAPAPAVPSAPTPVAPAAPAPAPASAGENVVTAPMPGKILRILVREGQQVKVGQ 110
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2273475591 549 AVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:PRK05641 111 GLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIELG 153
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
137-320 |
1.12e-07 |
|
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: 55.01 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 137 VASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVVREMDQIEESFDSAVREAVVafgrGECFVERYLDRPRHVEAQVLADQ 216
Cdd:TIGR01369 148 AHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVLVEKSLAGWKEIEYEVMRDS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 217 HGNVVVVgtrdCSLQRRHQKLVEE------APAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAAD-GTVAFLEVN 289
Cdd:TIGR01369 224 NDNCITV----CNMENFDPMGVHTgdsivvAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsGRYYVIEVN 299
|
170 180 190
....*....|....*....|....*....|.
gi 2273475591 290 TRLQVEHPITEETTGVDLVQEQFRIAAGEPL 320
Cdd:TIGR01369 300 PRVSRSSALASKATGYPIAKVAAKLAVGYTL 330
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
522-587 |
8.04e-07 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 52.03 E-value: 8.04e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2273475591 522 PGELRADMAGTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVL 587
Cdd:PRK14042 525 PGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVL 590
|
|
| PRK06524 |
PRK06524 |
biotin carboxylase-like protein; Validated |
96-304 |
1.61e-06 |
|
biotin carboxylase-like protein; Validated
Pssm-ID: 180605 [Multi-domain] Cd Length: 493 Bit Score: 50.89 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 96 DAGLTWIGPnPEAIRQ-LGNKITAREIAVRAGAPLVAGTDGPVASAAEVRTFAEEHGL--PIAIKAAFGGGGRGLKVVRE 172
Cdd:PRK06524 124 QAGLEVMHP-PAELRHrLDSKIVTTRLANEAGVPSVPHVLGRVDSYDELSALAHGAGLgdDLVVQTPYGDSGSTTFFVRG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 173 mdqiEESFDSAVREAVvafGRGECFVeryLDRPRHVEAQV--LADQHGNVV------VVGTRDCSLQRRH---QKLVEEA 241
Cdd:PRK06524 203 ----QRDWDKYAGGIV---GQPEIKV---MKRIRNVEVCIeaCVTRHGTVIgpamtsLVGYPELTPYRGGwcgNDIWPGA 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2273475591 242 PAPFLTDQQTQLIYDAAKAVCREAsYSGAGTVEFLVAADGTVAFL-EVNTRLQVEHPITEETTG 304
Cdd:PRK06524 273 LPPAQTRKAREMVRKLGDVLSREG-YRGYFEVDLLHDLDADELYLgEVNPRLSGASPMTNLTTE 335
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
142-320 |
1.76e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 51.32 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 142 EVRTFAEEHG-LPIAIKAAFGGGGRGLKVVREMdqieESFDSAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNV 220
Cdd:PLN02735 170 ECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNK----EEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 221 VVVgtrdCSLQRRHQKLVEE------APAPFLTDQQTQLIYDAAKAVCREASYS-GAGTVEFLV-AADGTVAFLEVNTRL 292
Cdd:PLN02735 246 VII----CSIENIDPMGVHTgdsitvAPAQTLTDKEYQRLRDYSVAIIREIGVEcGGSNVQFAVnPVDGEVMIIEMNPRV 321
|
170 180
....*....|....*....|....*...
gi 2273475591 293 QVEHPITEETTGVDLVQEQFRIAAGEPL 320
Cdd:PLN02735 322 SRSSALASKATGFPIAKMAAKLSVGYTL 349
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
98-292 |
4.28e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 49.97 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 98 GLTWIGPNPEAIrQLGNKITA-REIAVRAGAPLvaGTDGPVASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVVREMDQI 176
Cdd:PRK12815 112 GVELLGTNIEAI-QKGEDRERfRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 177 EESFDSAVREAVVAfgrgECFVERYLDRPRHVEAQVLADQHGNVVVVG-----------TRDcSLqrrhqkLVeeAPAPF 245
Cdd:PRK12815 189 EQLFKQGLQASPIH----QCLLEESIAGWKEIEYEVMRDRNGNCITVCnmenidpvgihTGD-SI------VV--APSQT 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2273475591 246 LTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGT-VAFLEVNTRL 292
Cdd:PRK12815 256 LTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKqYYLIEVNPRV 303
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
148-290 |
5.15e-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: 47.70 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 148 EEHGLPIAIKAAFGGGGRGLKVVREMDQIEESFDSAVREAvvafgrGECFVERYLDrPRHVEAQVLADQHGNVVVVGTR- 226
Cdd:pfam07478 33 EALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYD------EKVLVEEGIE-GREIECAVLGNEDPEVSPVGEIv 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 227 -DCSLQRRHQKLVEEA-----PAPfLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADGTVAFLEVNT 290
Cdd:pfam07478 106 pSGGFYDYEAKYIDDSaqivvPAD-LEEEQEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
538-590 |
2.29e-05 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 42.69 E-value: 2.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2273475591 538 VEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
102-291 |
3.92e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 46.63 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 102 IGPNPEAIRQLGNKITAREIAVRAGAPLVAGtdGPVASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVVREmdqiEESFD 181
Cdd:PRK05294 116 IGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVIIRPSFTLGGTGGGIAYN----EEELE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 182 SAVREAVVAFGRGECFVERYLDRPRHVEAQVLADQHGNVVVVgtrdCSLqrrhqklveE---------------APAPFL 246
Cdd:PRK05294 190 EIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIV----CSI---------EnidpmgvhtgdsitvAPAQTL 256
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2273475591 247 TDQQTQLIYDAAKAVCREAS-YSGAGTVEFLV-AADGTVAFLEVNTR 291
Cdd:PRK05294 257 TDKEYQMLRDASIAIIREIGvETGGCNVQFALnPKDGRYIVIEMNPR 303
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
531-591 |
1.02e-04 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 45.11 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273475591 531 GTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:TIGR01347 15 GTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE 75
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
531-591 |
1.21e-04 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 44.83 E-value: 1.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273475591 531 GTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:PRK05704 17 ATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRID 77
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
135-291 |
1.49e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 44.77 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 135 GPVASAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVVREMDQIEESFDSAVReavVAFGRgECFVERYLDRPRHVEAQVLA 214
Cdd:PLN02735 721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVE---VDPER-PVLVDKYLSDATEIDVDALA 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 215 DQHGNVVVVGTRD-------------CSLqrrhqklveeaPAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVAADG 281
Cdd:PLN02735 797 DSEGNVVIGGIMEhieqagvhsgdsaCSL-----------PTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSG 865
|
170
....*....|
gi 2273475591 282 TVAFLEVNTR 291
Cdd:PLN02735 866 EVYIIEANPR 875
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
88-203 |
2.41e-04 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 43.96 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 88 AGFAQAVLDAGLTWIGPNPEAIRQLGNKITAREIAVRAGAPLVAG---TDgpvasAAEVRTFAEEHGLPIAIKAAFGGGG 164
Cdd:PLN02257 76 AGLADDLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYetfTD-----PAAAKKYIKEQGAPIVVKADGLAAG 150
|
90 100 110
....*....|....*....|....*....|....*....
gi 2273475591 165 RGLKVVREMDQIEESFDSAVREAVVAFGRGECFVERYLD 203
Cdd:PLN02257 151 KGVVVAMTLEEAYEAVDSMLVKGAFGSAGSEVVVEEFLD 189
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
531-591 |
3.47e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 43.27 E-value: 3.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273475591 531 GTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
531-590 |
3.94e-04 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 43.13 E-value: 3.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 531 GTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:PTZ00144 59 GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEI 118
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
139-320 |
6.41e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 42.78 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 139 SAAEVRTFAEEHGLPIAIKAAFGGGGRGLKVVREMDQIEESfdsaVREAVVAFGRGECFVERYLDRPRHVEAQVLADqhG 218
Cdd:PRK05294 692 SVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERY----MREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--G 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 219 NVVVVGTrdcSLQrrHqklVEEA-----------PAPFLTDQQTQLIYDAAKAVCREASYSGAGTVEFLVaADGTVAFLE 287
Cdd:PRK05294 766 EDVLIGG---IME--H---IEEAgvhsgdsacslPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAV-KDDEVYVIE 836
|
170 180 190
....*....|....*....|....*....|...
gi 2273475591 288 VNTRLQVEHPITEETTGVDLVQEQFRIAAGEPL 320
Cdd:PRK05294 837 VNPRASRTVPFVSKATGVPLAKIAARVMLGKKL 869
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
531-591 |
6.47e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 42.50 E-value: 6.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273475591 531 GTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
531-590 |
2.27e-03 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 40.70 E-value: 2.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273475591 531 GTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALI 590
Cdd:PRK14875 17 GKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVV 76
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
531-591 |
3.44e-03 |
|
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: 40.24 E-value: 3.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273475591 531 GTVVKWLVEPGAEVAAGDAVVVLEAMKMETQVTAHRAGMLTGVRAEAGGVVNAGAVLALIG 591
Cdd:TIGR01348 14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| |
