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Conserved domains on  [gi|736049878|ref|WP_034195525|]
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MULTISPECIES: acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha [Burkholderia]

Protein Classification

acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha( domain architecture ID 11469140)

acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha is a biotin-dependent carboxylase

CATH:  3.40.50.20|3.30.1490.20|3.30.470.20|3.30.700.40
EC:  6.4.-.-
Gene Ontology:  GO:0016421|GO:0005524|GO:0046872|GO:0004075
PubMed:  12769720|18247344

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-460 0e+00

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


:

Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 780.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:COG4770    1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:COG4770   81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:COG4770  161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGD-AFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:COG4770  241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADgNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 320 LPLQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLRLPDgvefaiGAPVRVDSGVREGDAITPFYDPMIAKLIVHGA 399
Cdd:COG4770  321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPG------GPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGP 394

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736049878 400 DRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIERNHDALFAPRKPP 460
Cdd:COG4770  395 DREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 598-662 1.62e-26

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: 102.49  E-value: 1.62e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736049878 598 LTAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGaQLLM 662
Cdd:cd06850    2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAG-QLLV 65
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-460 0e+00

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 780.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:COG4770    1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:COG4770   81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:COG4770  161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGD-AFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:COG4770  241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADgNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 320 LPLQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLRLPDgvefaiGAPVRVDSGVREGDAITPFYDPMIAKLIVHGA 399
Cdd:COG4770  321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPG------GPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGP 394

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736049878 400 DRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIERNHDALFAPRKPP 460
Cdd:COG4770  395 DREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-449 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 599.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGD-AFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNgEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 320 LPLQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLRLPDGVefaiGapVRVDSGVREGDAITPFYDPMIAKLIVHGA 399
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGP----G--VRVDSAVYTGYTIPPYYDSMIGKLIVHGE 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 736049878 400 DRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIERN 449
Cdd:PRK08591 395 TREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-448 1.58e-180

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: 520.09  E-value: 1.58e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878    1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGDA-FYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGeFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  320 LPLQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLrLPDGvefaiGAPVRVDSGVREGDAITPFYDPMIAKLIVHGA 399
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRY-LPPG-----GPGVRWDSHVYSGYTVPPYYDSMIGKLITYGK 394

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 736049878  400 DRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIER 448
Cdd:TIGR00514 395 TREVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 128-321 1.60e-72

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: 232.97  E-value: 1.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  128 VPLVPGYHGDDQTPAHLHREADRIGYPVLLKASAGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPR 207
Cdd:pfam02786  14 VPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNPQVLVEKSLKGPK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  208 HVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLEEAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIM--TGDAFYF 285
Cdd:pfam02786  94 HIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALdpFSGEYYF 173

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 736049878  286 MEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEPLP 321
Cdd:pfam02786 174 IEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 335-447 9.30e-48

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: 163.35  E-value: 9.30e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   335 EARLYAENPARGFLPSTGTLRHLRLPDGvefaigAPVRVDSGVREGDAITPFYDPMIAKLIVHGADRAEALGRMLRALRA 414
Cdd:smart00878   1 ECRINAEDPANGFLPSPGRITRYRFPGG------PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDE 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 736049878   415 CEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIE 447
Cdd:smart00878  75 FRIRGVKTNIPFLRALLRHPDFRAGDVDTGFLE 107
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 598-662 1.62e-26

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: 102.49  E-value: 1.62e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736049878 598 LTAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGaQLLM 662
Cdd:cd06850    2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAG-QLLV 65
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 586-662 9.07e-20

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: 94.38  E-value: 9.07e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736049878  586 AHAGDAEHGGgrltAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGaQLLM 662
Cdd:COG1038  1071 ADPGNPGHIG----APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAG-DLLI 1142
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 586-662 4.87e-18

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 88.66  E-value: 4.87e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736049878  586 AHAGDAEHGGgrltAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGaQLLM 662
Cdd:PRK12999 1071 ADPGNPGHVG----APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAG-DLLV 1142
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 598-663 1.65e-15

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: 71.48  E-value: 1.65e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736049878  598 LTAPMPGKVIA-----VLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGAQLLMM 663
Cdd:pfam00364   3 IKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 586-665 7.36e-15

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: 78.72  E-value: 7.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   586 AHAGDAEHGGgrltAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVaDGAQLLMMAE 665
Cdd:TIGR01235 1069 ADPGNPAHVG----APMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQI-DAKDLLLVLE 1143
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-460 0e+00

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 780.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:COG4770    1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:COG4770   81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:COG4770  161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGD-AFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:COG4770  241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADgNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 320 LPLQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLRLPDgvefaiGAPVRVDSGVREGDAITPFYDPMIAKLIVHGA 399
Cdd:COG4770  321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPG------GPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGP 394

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736049878 400 DRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIERNHDALFAPRKPP 460
Cdd:COG4770  395 DREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-449 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 599.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGD-AFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNgEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 320 LPLQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLRLPDGVefaiGapVRVDSGVREGDAITPFYDPMIAKLIVHGA 399
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGP----G--VRVDSAVYTGYTIPPYYDSMIGKLIVHGE 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 736049878 400 DRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIERN 449
Cdd:PRK08591 395 TREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-448 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 595.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:PRK06111   1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:PRK06111  81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGDA-FYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 320 LPLQQHELRVQGHAIEARLYAENPARgFLPSTGTLRHLRLPDGVEfaigapVRVDSGVREGDAITPFYDPMIAKLIVHGA 399
Cdd:PRK06111 321 LSFTQDDIKRSGHAIEVRIYAEDPKT-FFPSPGKITDLTLPGGEG------VRHDHAVENGVTVTPFYDPMIAKLIAHGE 393

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 736049878 400 DRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIER 448
Cdd:PRK06111 394 TREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
1-451 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 566.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:PRK08654   1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:PRK08654  81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGDAFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEPL 320
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 321 PLQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLRLPDGvefaIGapVRVDSGVREGDAITPFYDPMIAKLIVHGAD 400
Cdd:PRK08654 321 SFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGG----PG--VRVDSGVHMGYEIPPYYDSMISKLIVWGRT 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 736049878 401 RAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIERNHD 451
Cdd:PRK08654 395 REEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETT 445
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
1-450 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 522.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:PRK05586   1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:PRK05586  81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGDA-FYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGnFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 320 LPLQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLRLPDGVEfaigapVRVDSGVREGDAITPFYDPMIAKLIVHGA 399
Cdd:PRK05586 321 LSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLG------VRVDSAVYSGYTIPPYYDSMIGKLIVYGK 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 736049878 400 DRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIERNH 450
Cdd:PRK05586 395 DREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKL 445
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-448 1.58e-180

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: 520.09  E-value: 1.58e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878    1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGDA-FYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGeFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  320 LPLQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLrLPDGvefaiGAPVRVDSGVREGDAITPFYDPMIAKLIVHGA 399
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRY-LPPG-----GPGVRWDSHVYSGYTVPPYYDSMIGKLITYGK 394

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 736049878  400 DRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIER 448
Cdd:TIGR00514 395 TREVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
urea_carbox TIGR02712
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ...
 2-451 1.47e-179

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: 542.70  E-value: 1.47e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878     2 FDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHPG 81
Cdd:TIGR02712    1 FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878    82 YGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGyhgddqTPAHLHRE-----ADRIGYPVL 156
Cdd:TIGR02712   81 YGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG------TGLLSSLDealeaAKEIGYPVM 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   157 LKASAGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQ 236
Cdd:TIGR02712  155 LKSTAGGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQ 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   237 KVLEEAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTG--DAFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRV 314
Cdd:TIGR02712  235 KVVEETPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEarDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRI 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   315 AAGEPLPLQQ--HELRVQGHAIEARLYAENPARGFLPSTGTLRHLRLPDGvefaigapVRVDSGVREGDAITPFYDPMIA 392
Cdd:TIGR02712  315 AAGELPDFASlnISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPDD--------VRVDTWVETGTEVSPEYDPMLA 386

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 736049878   393 KLIVHGADRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIERNHD 451
Cdd:TIGR02712  387 KIIVHGSDREDAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNSFVY 445
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 1-461 1.09e-169

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 515.46  E-value: 1.09e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878    1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIG-GSAAADSYLRIERIIEAARATGAQAIH 79
Cdd:PRK12999    4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGeGKHPVRAYLDIDEIIRVAKQAGVDAIH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   80 PGYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKA 159
Cdd:PRK12999   84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  160 SAGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVL 239
Cdd:PRK12999  164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  240 EEAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGD-AFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGE 318
Cdd:PRK12999  244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADgNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGA 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  319 PL------PLQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLRLPDgvefaiGAPVRVDSG-VREGDAITPFYDPMI 391
Cdd:PRK12999  324 TLhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPG------GFGVRLDGGnAFAGAEITPYYDSLL 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  392 AKLIVHGADRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIERNHDALFAPRKPPR 461
Cdd:PRK12999  398 VKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDR 467
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 1-459 6.82e-169

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: 513.09  E-value: 6.82e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878    1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIG-GSAAADSYLRIERIIEAARATGAQAIH 79
Cdd:COG1038     3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGeGKGPVDAYLDIEEIIRVAKEKGVDAIH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   80 PGYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKA 159
Cdd:COG1038    83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  160 SAGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVL 239
Cdd:COG1038   163 AAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  240 EEAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMT-GDAFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGE 318
Cdd:COG1038   243 EIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDdDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGY 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  319 PL-------PlQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLRLPDgvefaiGAPVRVDSG-VREGDAITPFYDPM 390
Cdd:COG1038   323 SLddpeigiP-SQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAG------GFGIRLDGGnAYTGAVITPYYDSL 395

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736049878  391 IAKLIVHGADRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIErNHDALFAPRKP 459
Cdd:COG1038   396 LVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFID-ETPELFDFPKR 463
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
1-483 2.56e-154

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 454.18  E-value: 2.56e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAAdSYLRIERIIEAARATGAQAIHP 80
Cdd:PRK07178   1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPLA-GYLNPRRLVNLAVETGCDALHP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:PRK07178  80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIM-TGDAFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 320 LPLQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLrlpdgveFAIGAP-VRVDSGVREGDAITPFYDPMIAKLIVHG 398
Cdd:PRK07178 320 LSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRY-------YAPGGPgVRTDTAIYTGYTIPPYYDSMCAKLIVWA 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 399 ADRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIErNHDAL--FAPRKPPRAALALACAALfarer 476
Cdd:PRK07178 393 LTWEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVE-SHPELtnYSIKRKPEELAAAIAAAI----- 466


                 ....*..
gi 736049878 477 daAAHAG 483
Cdd:PRK07178 467 --AAHAG 471
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 4-447 8.04e-153

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 449.98  E-value: 8.04e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   4 KILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHPGYG 83
Cdd:PRK12833   7 KVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGYG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  84 FLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKASAGG 163
Cdd:PRK12833  87 FLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAGG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 164 GGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHgNTVYLFDRDCSVQRRHQKVLEEAP 243
Cdd:PRK12833 167 GGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 244 APGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIM--TGDAFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEPLP 321
Cdd:PRK12833 246 SPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLR 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 322 LQQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLRLPDgvefaiGAPVRVDSGVREGDAITPFYDPMIAKLIVHGADR 401
Cdd:PRK12833 326 FAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQ------GPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDR 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 736049878 402 AEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIE 447
Cdd:PRK12833 400 AAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
4-449 1.06e-152

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 448.81  E-value: 1.06e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   4 KILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHPGYG 83
Cdd:PRK08462   6 RILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGYG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  84 FLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKASAGG 163
Cdd:PRK08462  86 FLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 164 GGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLEEAP 243
Cdd:PRK08462 166 GGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 244 APGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIM-TGDAFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEPLPl 322
Cdd:PRK08462 246 AVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELP- 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 323 QQHELRVQGHAIEARLYAENPARgFLPSTGTLRHLRLPDGVEfaigapVRVDSGVREGDAITPFYDPMIAKLIVHGADRA 402
Cdd:PRK08462 325 SQESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPGGRN------VRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRN 397

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 736049878 403 EALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIERN 449
Cdd:PRK08462 398 RAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 1-449 5.33e-151

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 445.80  E-value: 5.33e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   1 MFDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGgSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:PRK08463   1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIG-TDPIKGYLDVKRIVEIAKACGADAIHP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHG-DDQTPAHLHREADRIGYPVLLKA 159
Cdd:PRK08463  80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 160 SAGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVL 239
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 240 EEAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTG-DAFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGE 318
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDyNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 319 PLPLQQHELRVQGHAIEARLYAENPARGFLPSTGTLrhlrlpDGVEFAIGAPVRVDSGVREGDAITPFYDPMIAKLIVHG 398
Cdd:PRK08463 320 ILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKI------TEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKA 393

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 736049878 399 ADRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIERN 449
Cdd:PRK08463 394 TSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETH 444
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 4-454 6.29e-136

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: 426.94  E-value: 6.29e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878     4 KILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIG---GSAAADSYLRIERIIEAARATGAQAIHP 80
Cdd:TIGR01235    1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGegpDLGPIEAYLSIDEIIRVAKLNGVDAIHP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878    81 GYGFLSENEDFAQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDQTPAHLHREADRIGYPVLLKAS 160
Cdd:TIGR01235   81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   161 AGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLE 240
Cdd:TIGR01235  161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   241 EAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGDA-FYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:TIGR01235  241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGkFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   320 LPL------QQHELRVQGHAIEARLYAENPARGFLPSTGTLRHLRlpdgveFAIGAPVRVDSGVR-EGDAITPFYDPMIA 392
Cdd:TIGR01235  321 LPTpqlgvpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYR------SAGGFGIRLDGGNSyAGAIITPYYDSLLV 394

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736049878   393 KLIVHGADRAEALGRMLRALRACEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIErNHDALF 454
Cdd:TIGR01235  395 KVSAWASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFID-TTPELF 455
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 128-321 1.60e-72

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: 232.97  E-value: 1.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  128 VPLVPGYHGDDQTPAHLHREADRIGYPVLLKASAGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRPR 207
Cdd:pfam02786  14 VPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNPQVLVEKSLKGPK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  208 HVEVQVFGDTHGNTVYLFDRDCSVQRRHQKVLEEAPAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIM--TGDAFYF 285
Cdd:pfam02786  94 HIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALdpFSGEYYF 173

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 736049878  286 MEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEPLP 321
Cdd:pfam02786 174 IEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 2-109 5.83e-57

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: 188.08  E-value: 5.83e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878    2 FDKILIANRGEIACRVAATCKRLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLRIERIIEAARATGAQAIHPG 81
Cdd:pfam00289   1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80

                          90       100
                  ....*....|....*....|....*...
gi 736049878   82 YGFLSENEDFAQACHAAGIAFIGPPVDA 109
Cdd:pfam00289  81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 335-448 4.14e-48

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: 164.20  E-value: 4.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  335 EARLYAENPARGFLPSTGTLRHLRLPDGvefaigAPVRVDSGVREGDAITPFYDPMIAKLIVHGADRAEALGRMLRALRA 414
Cdd:pfam02785   1 EARIYAEDPDNNFLPSPGKVTRYRFPGG------PGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAE 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 736049878  415 CEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIER 448
Cdd:pfam02785  75 FRIEGVKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 335-447 9.30e-48

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: 163.35  E-value: 9.30e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   335 EARLYAENPARGFLPSTGTLRHLRLPDGvefaigAPVRVDSGVREGDAITPFYDPMIAKLIVHGADRAEALGRMLRALRA 414
Cdd:smart00878   1 ECRINAEDPANGFLPSPGRITRYRFPGG------PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDE 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 736049878   415 CEVVGLHTNTAFLQRIVACEPFTMPDLDTGLIE 447
Cdd:smart00878  75 FRIRGVKTNIPFLRALLRHPDFRAGDVDTGFLE 107
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 63-319 7.34e-45

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: 160.81  E-value: 7.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  63 IERIIEAA----RATGAQAIhpgygfLSENED----FAQACHAAGIAfiGPPVDAIAAMGSKAAAKALMHAAAVPlVPGY 134
Cdd:COG0439    2 IDAIIAAAaelaRETGIDAV------LSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPGF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 135 HGDDqTPAHLHREADRIGYPVLLKASAGGGGKGMRVVERSEDFPAALASCQREAASSFGNDRVLIEKYLTRpRHVEVQVF 214
Cdd:COG0439   73 ALVD-SPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 215 GDtHGNTVYlfdrdCSVQRRHQK------VLEEAPAPgLHDDVRQAMGEAAVAAARAVGYV-GAGTVEFIMTGD-AFYFM 286
Cdd:COG0439  151 VR-DGEVVV-----CSITRKHQKppyfveLGHEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDgEPYLI 223

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 736049878 287 EMNTRLQVEH--PVTEMVTGLDLVEWQLRVAAGEP 319
Cdd:COG0439  224 EINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 598-662 1.62e-26

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: 102.49  E-value: 1.62e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736049878 598 LTAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGaQLLM 662
Cdd:cd06850    2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAG-QLLV 65
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 586-662 9.07e-20

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: 94.38  E-value: 9.07e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736049878  586 AHAGDAEHGGgrltAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGaQLLM 662
Cdd:COG1038  1071 ADPGNPGHIG----APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAG-DLLI 1142
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 586-662 4.87e-18

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 88.66  E-value: 4.87e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736049878  586 AHAGDAEHGGgrltAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGaQLLM 662
Cdd:PRK12999 1071 ADPGNPGHVG----APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAG-DLLV 1142
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 542-666 7.11e-17

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 84.51  E-value: 7.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 542 GATPLDFDVTLGG----VRSSGRVYADGDTFHVFTQGAAETFEW----RNLLAHAGDAEHGGGrLTAPMPGKVIAVLVEP 613
Cdd:PRK09282 462 EGIPTEFKVEVDGekyeVKIEGVKAEGKRPFYLRVDGMPEEVVVeplkEIVVGGRPRASAPGA-VTSPMPGTVVKVKVKE 540

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 736049878 614 GQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGaQLLMMAEG 666
Cdd:PRK09282 541 GDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPG-DVLMEIEP 592
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 591-661 5.13e-16

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 75.67  E-value: 5.13e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736049878 591 AEHGGGRLTAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGAQLL 661
Cdd:PRK05641  80 ASAGENVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
548-664 6.01e-16

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 81.52  E-value: 6.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 548 FDVTLGGVRSSGRVYADGDTFHVFTQGAAETFEwrnLLAHAGDAEHGGGRLTAPMPGKVIAVLVEPGQKVEAGTPLIVME 627
Cdd:PRK14040 480 YTVEVEGKAYVVKVSEGGDISQITPAAPAAAPA---AAAAAAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILE 556

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 736049878 628 AMKMEHTIGAPGPGVVAEVLYGVGDQVADGAQLLMMA 664
Cdd:PRK14040 557 AMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 598-663 1.65e-15

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: 71.48  E-value: 1.65e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736049878  598 LTAPMPGKVIA-----VLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGAQLLMM 663
Cdd:pfam00364   3 IKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 586-665 7.36e-15

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: 78.72  E-value: 7.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   586 AHAGDAEHGGgrltAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVaDGAQLLMMAE 665
Cdd:TIGR01235 1069 ADPGNPAHVG----APMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQI-DAKDLLLVLE 1143
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 588-662 1.27e-14

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 71.08  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 588 AGDAEHGGGRLTAPMPGKV-------IAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGaQL 660
Cdd:COG0511   53 AAAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYG-QP 131


                 ..
gi 736049878 661 LM 662
Cdd:COG0511  132 LF 133
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 591-661 1.01e-11

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 62.52  E-value: 1.01e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736049878 591 AEHGGGRLTAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGAQLL 661
Cdd:PRK06549  57 AAAGADAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 594-665 3.76e-11

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 66.28  E-value: 3.76e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736049878 594 GGGRLTAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGaQLLMMAE 665
Cdd:PRK14042 524 GPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPG-QVLIRVE 594
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 604-654 2.49e-10

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: 56.68  E-value: 2.49e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 736049878 604 GKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQV 654
Cdd:cd06663   14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKV 64
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 598-661 3.07e-10

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 56.33  E-value: 3.07e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736049878 598 LTAPMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGAQLL 661
Cdd:PRK08225   4 VYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLL 67
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 139-320 8.12e-09

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: 58.86  E-value: 8.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   139 QTPAHLHREADRIGYPVLLKASAGGGGKGMRVVERSEDfpaaLASCQREAASSFGNDRVLIEKYLtrPRHVEVQVFGDTH 218
Cdd:TIGR01369  691 TSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEE----LRRYLEEAVAVSPEHPVLIDKYL--EDAVEVDVDAVSD 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   219 GNTVYlfdrdCSVQRRHqkvLEEA-----------PAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGDAFYFME 287
Cdd:TIGR01369  765 GEEVL-----IPGIMEH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIE 836

                          170       180       190
                   ....*....|....*....|....*....|...
gi 736049878   288 MNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEPL 320
Cdd:TIGR01369  837 VNPRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 92-320 1.97e-07

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 54.59  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878   92 AQACHAAGIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDqtPAHLHREADRIGYPVLLKASAGGGGKGMRVV 171
Cdd:PRK12815  647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATD--EEEAFAFAKRIGYPVLIRPSYVIGGQGMAVV 724

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  172 eRSEdfpAALASCQREAASSfgNDRVLIEKYLTrPRHVEVQVFGDthGNTVYL---FDrdcsvqrrHqkvLEEA------ 242
Cdd:PRK12815  725 -YDE---PALEAYLAENASQ--LYPILIDQFID-GKEYEVDAISD--GEDVTIpgiIE--------H---IEQAgvhsgd 784

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  243 -----PAPGLHDDVRQAMGEAAVAAARAVGYVGAGTVEFIMTGDAFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAG 317
Cdd:PRK12815  785 siavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLG 864


                  ...
gi 736049878  318 EPL 320
Cdd:PRK12815  865 KSL 867
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 604-664 1.64e-06

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 46.21  E-value: 1.64e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736049878 604 GKVIAVLVEPGQKVEAGTPLIVMEAMK--MEhtIGAPGPGVVAEVLYGVGDQVADGAQLLMMA 664
Cdd:COG0508   17 GTIVEWLVKEGDTVKEGDPLAEVETDKatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 604-663 4.23e-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: 49.87  E-value: 4.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  604 GKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGAQLLMM 663
Cdd:TIGR01348  14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATL 73
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 604-663 3.60e-05

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 46.74  E-value: 3.60e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736049878 604 GKVIAVLVEPGQKVEAGTPLIVMEAMK--MEhtIGAPGPGVVAEVLYGVGDQVADGAQLLMM 663
Cdd:PRK11855  16 VEVIEWLVKEGDTVEEDQPLVTVETDKatME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVI 75
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 604-663 7.46e-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: 7.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  604 GKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGAQLLMM 663
Cdd:TIGR01348 130 VTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTL 189
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 598-626 8.54e-05

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: 40.86  E-value: 8.54e-05
                         10        20
                 ....*....|....*....|....*....
gi 736049878 598 LTAPMPGKVIAVLVEPGQKVEAGTPLIVM 626
Cdd:cd06850   39 VTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 599-627 1.12e-04

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: 42.57  E-value: 1.12e-04
                         10        20
                 ....*....|....*....|....*....
gi 736049878 599 TAPMPGKVIAVLVEPGQKVEAGTPLIVME 627
Cdd:COG0511  108 EAPVSGTVVEILVENGQPVEYGQPLFVIE 136
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 148-418 1.71e-04

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 44.84  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 148 ADRIGYPVLLKASAGGGGKGMRVVERSEDFPAALASCQREAASSFgndrvLIEKYLTRPRHvEVQVFGDTHGNTVylfdr 227
Cdd:PRK02186 138 LDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTRAA-----LVQAYVEGDEY-SVETLTVARGHQV----- 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 228 dCSVQRRHQ-------KVLEEAPAPgLHDDVRQAMGEAAVAAARAVGY-VGAGTVEFIMTGDAFYFMEMNTRLQVEH-PV 298
Cdd:PRK02186 207 -LGITRKHLgppphfvEIGHDFPAP-LSAPQRERIVRTVLRALDAVGYaFGPAHTELRVRGDTVVIIEINPRLAGGMiPV 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 299 T-EMVTGLDLVEWQLRVAAGEPlplQQHELRVQGH-AIEARLyaenPARGflpstGTLRHLRLPDGVEFAiGAPVRVDSG 376
Cdd:PRK02186 285 LlEEAFGVDLLDHVIDLHLGVA---AFADPTAKRYgAIRFVL----PARS-----GVLRGLLFLPDDIAA-RPELRFHPL 351

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 736049878 377 VREGDAITP---FYDPmiAKLIVHGADRAEALGRMLRALRACEVV 418
Cdd:PRK02186 352 KQPGDALRLegdFRDR--IAAVVCAGDHRDSVAAAAERAVAGLSI 394
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
23-321 2.13e-04

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 44.15  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  23 RLGIASVAVYSDADANAKHVAACDEAVHIGGSAAADSYLrIERIIEAARATGAQAIHPGY----GFLSENEDFAqachAA 98
Cdd:COG3919   26 EAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGDDPEAF-VDALLELAERHGPDVLIPTGdeyvELLSRHRDEL----EE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878  99 GIAFIGPPVDAIAAMGSKAAAKALMHAAAVPLVPGYHGDDqtPAHLHREADRIGYPVLLKAS-----AGGGGKGMRVVER 173
Cdd:COG3919  101 HYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDS--ADDLDALAEDLGFPVVVKPAdsvgyDELSFPGKKKVFY 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 174 SEDFPAALASCQREAASSFgndRVLIEKYLTRPRHVEVQVFG--DTHGNTVYLFdrdcSVQRRHQK--------VLEEAP 243
Cdd:COG3919  179 VDDREELLALLRRIAAAGY---ELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF----TGRKLRHYppaggnsaARESVD 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 244 APGLHDDVRQAMGEAavaaaravGYVGAGTVEFI--MTGDAFYFMEMNTRLQVEHPvteMVT--GLDLVEWQLRVAAGEP 319
Cdd:COG3919  252 DPELEEAARRLLEAL--------GYHGFANVEFKrdPRDGEYKLIEINPRFWRSLY---LATaaGVNFPYLLYDDAVGRP 320


                 ..
gi 736049878 320 LP 321
Cdd:COG3919  321 LE 322
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 604-666 2.57e-04

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 44.22  E-value: 2.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736049878 604 GKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGAqLLMMAEG 666
Cdd:PRK11854  15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGA-LIMIFES 76
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 604-665 3.32e-04

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 43.84  E-value: 3.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736049878 604 GKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGAqLLMMAE 665
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGS-LIMVFE 178
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 604-661 3.84e-04

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 43.45  E-value: 3.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 736049878 604 GKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADGAQLL 661
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIM 276
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 604-661 5.02e-04

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 43.27  E-value: 5.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049878 604 GKVIAVLVEPGQKVEAGTPLIVMEAMK--MEhtIGAPGPGVVAEVLYGVGDQVADGAQLL 661
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKatME--IPSPVAGVVKEIKVKVGDKVSVGSLLV 190
PRK05889 PRK05889
biotin/lipoyl-binding carrier protein;
600-657 5.91e-04

biotin/lipoyl-binding carrier protein;


Pssm-ID: 180306 [Multi-domain]  Cd Length: 71  Bit Score: 38.64  E-value: 5.91e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 736049878 600 APMPGKVIAVLVEPGQKVEAGTPLIVMEAMKMEHTIGAPGPGVVAEVLYGVGDQVADG 657
Cdd:PRK05889   7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAG 64
PylC COG2232
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ...
 267-343 1.92e-03

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: 41.06  E-value: 1.92e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736049878 267 GYVGAGTVEFIMTGDAFYFMEMNTRLQVEHPVTEMVTGLDLVEWQLRVAAGEpLPLQQHEL--RVQGHAIearLYAENP 343
Cdd:COG2232  238 GLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRGE-LPEVPRPKprRVAAKAI---LYAPRD 312
PLN02735 PLN02735
carbamoyl-phosphate synthase
 148-222 3.83e-03

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 40.53  E-value: 3.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736049878  148 ADRIGYPVLLKASAGGGGKGMRVVERSEDFPAALascqrEAASSFGNDR-VLIEKYLTRPRHVEVQVFGDTHGNTV 222
Cdd:PLN02735  733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYL-----ETAVEVDPERpVLVDKYLSDATEIDVDALADSEGNVV 803
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 148-222 9.73e-03

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: 39.09  E-value: 9.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736049878 148 ADRIGYPVLLKASAGGGGKGMRVVERSEDFPAALascqREAASSFGNDRVLIEKYLTRPRHVEVQVFGDTHGNTV 222
Cdd:COG0458  145 AEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYL----ERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVI 215
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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