|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
45-396 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 657.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLR------- 357
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRiaagepl 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 --------------------------------------------------------------------------------
Cdd:COG4770 322 pftqediklrghaiecrinaedpargflpspgtitrlrppggpgvrvdsgvyegyeippyydsmiaklivwgpdreeaia 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1958749768 358 ----------IVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQHHKDLLP 396
Cdd:COG4770 402 rmrralaefvIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLA 450
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
45-358 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 543.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749768 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRI 315
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
45-358 |
2.07e-178 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 513.04 E-value: 2.07e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK06111 82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749768 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRI 315
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
47-358 |
1.22e-167 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 487.18 E-value: 1.22e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 47 KVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPGYG 126
Cdd:PRK08654 4 KILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 127 FLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGG 206
Cdd:PRK08654 84 FLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 207 GGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAP 286
Cdd:PRK08654 164 GGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAP 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958749768 287 APGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMdSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:PRK08654 244 SPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKI 314
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
45-358 |
2.60e-167 |
|
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: 507.31 E-value: 2.60e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:COG1038 4 IKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAIHP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 124 GYGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:COG1038 84 GYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:COG1038 164 AGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVE 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958749768 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:COG1038 244 IAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 318
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
45-358 |
8.89e-161 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 490.42 E-value: 8.89e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:PRK12999 5 IKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAIHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 124 GYGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:PRK12999 85 GYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:PRK12999 165 AGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVE 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958749768 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:PRK12999 245 IAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 319
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
45-388 |
1.30e-160 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 467.27 E-value: 1.30e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIV-GLRT 363
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAyGEKL 321
|
330 340 350
....*....|....*....|....*....|.
gi 1958749768 364 NV---DflLRLSGHS---EFEAGNVHTDFIP 388
Cdd:PRK05586 322 SIkqeD--IKINGHSiecRINAEDPKNGFMP 350
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
46-360 |
3.54e-157 |
|
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: 482.22 E-value: 3.54e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 46 TKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPGY 125
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 126 GFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGyHGNDQSDECLKEHAGKIGYPVMIKAIRG 205
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 206 GGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEA 285
Cdd:TIGR02712 161 GGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEET 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749768 286 PAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHN-FYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIVG 360
Cdd:TIGR02712 241 PAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAA 316
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
45-358 |
4.49e-156 |
|
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: 455.76 E-value: 4.49e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749768 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRI 315
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
45-358 |
7.53e-150 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 441.08 E-value: 7.53e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPsQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP-LAGYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQS-DECLKEhAGKIGYPVMIKAI 203
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADlDEALAE-AERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958749768 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRI 314
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
43-360 |
1.30e-140 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 417.23 E-value: 1.30e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 43 GSITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIH 122
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 123 PGYGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKA 202
Cdd:PRK12833 83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 203 IRGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHgNAVYLFERDCSVQRRHQKII 282
Cdd:PRK12833 163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKIL 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958749768 283 EEAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMD-SKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIVG 360
Cdd:PRK12833 242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIAD 320
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
45-358 |
3.18e-138 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 410.29 E-value: 3.18e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749768 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKI 317
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
45-358 |
4.75e-138 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 410.74 E-value: 4.75e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQqSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIK-GYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHG-NDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958749768 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRI 315
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
47-358 |
3.37e-132 |
|
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: 415.38 E-value: 3.37e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 47 KVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ---QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLgpiEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 124 GYGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958749768 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHI 315
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
159-358 |
3.18e-86 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 267.63 E-value: 3.18e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 159 KSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDD 238
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 239 AMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVE 318
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958749768 319 FIMDSKH-NFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:pfam02786 162 FALDPFSgEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKI 202
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
45-152 |
4.76e-64 |
|
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: 205.80 E-value: 4.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 1958749768 125 YGFLSENMEFAELCKQEGIIFIGPPSTA 152
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
116-359 |
1.66e-63 |
|
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: 210.11 E-value: 1.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 116 SAAQAIHPGYGF---LSEN----MEFAELCKQEGIIfiGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDecLK 188
Cdd:COG0439 7 AAAAELARETGIdavLSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEE--AL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 189 EHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTpRHVEVQVFGdHHGNAVYlf 268
Cdd:COG0439 83 AFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV-RDGEVVV-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 269 erdCSVQRRHQK---IIE---EAPAPgIDPEVRRRLGEAAVRAAKAVNYV-GAGTVEFIMDSKHNFYFMEMNTRLQVEH- 340
Cdd:COG0439 159 ---CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLGGEHi 234
|
250 260
....*....|....*....|
gi 1958749768 341 -PVTEMITGTDLVEWQLRIV 359
Cdd:COG0439 235 pPLTELATGVDLVREQIRLA 254
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
549-612 |
7.72e-25 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 97.87 E-value: 7.72e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749768 549 APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEF 612
Cdd:cd06850 4 APMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
159-334 |
7.99e-24 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 102.11 E-value: 7.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 159 KSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREakksfnDD 238
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 239 AMLIEKFVDtPRHVEVQVFGDHH-----------GNAVYLFErdcsVQRRHQKIIEEAPAPgIDPEVRRRLGEAAVRAAK 307
Cdd:COG1181 170 KVLVEEFID-GREVTVGVLGNGGpralppieivpENGFYDYE----AKYTDGGTEYICPAR-LPEELEERIQELALKAFR 243
|
170 180
....*....|....*....|....*..
gi 1958749768 308 AVNYVGAGTVEFIMDSKHNFYFMEMNT 334
Cdd:COG1181 244 ALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
552-612 |
4.58e-19 |
|
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: 81.72 E-value: 4.58e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958749768 552 TGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEF 612
Cdd:cd06663 13 DGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
536-611 |
1.10e-18 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 83.37 E-value: 1.10e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749768 536 SPVSAEGTQGGTIAPMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVE 611
Cdd:PRK05641 76 APAPASAGENVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIE 151
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
549-602 |
5.53e-18 |
|
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: 88.21 E-value: 5.53e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958749768 549 APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQ 602
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
162-334 |
1.17e-17 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 84.01 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 162 SKSIMAAAGVPVVEGYHGNdqSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARReakksfNDDAML 241
Cdd:PRK01372 102 TKLVWQAAGLPTPPWIVLT--REEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFK------YDDEVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 242 IEKFVDTPrhvEVQ--VFGDH--------HGNAVYLFE----RDCSvqrrhQKIIeeaPApGIDPEVRRRLGEAAVRAAK 307
Cdd:PRK01372 174 VEKYIKGR---ELTvaVLGGKalpvieivPAGEFYDYEakylAGGT-----QYIC---PA-GLPAEIEAELQELALKAYR 241
|
170 180
....*....|....*....|....*..
gi 1958749768 308 AVNYVGAGTVEFIMDSKHNFYFMEMNT 334
Cdd:PRK01372 242 ALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
549-602 |
1.58e-17 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 86.73 E-value: 1.58e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958749768 549 APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQ 602
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQ 1134
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
530-613 |
2.19e-17 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 85.66 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 530 PVPKYLSPVSAEGTQGGTI-APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAP 608
Cdd:PRK09282 507 PLKEIVVGGRPRASAPGAVtSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDV 586
|
....*
gi 1958749768 609 LVEFE 613
Cdd:PRK09282 587 LMEIE 591
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
165-334 |
5.34e-17 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 79.67 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 165 IMAAAGVPVV-------EGYHGNDqsDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREakksfnD 237
Cdd:pfam07478 1 LLKAAGLPVVpfvtftrADWKLNP--KEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 238 DAMLIEKFVDTpRHVEVQVFGDHHGNAVYLFER--DCSVQRRHQKIIEEA-----PApGIDPEVRRRLGEAAVRAAKAVN 310
Cdd:pfam07478 73 EKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALG 150
|
170 180
....*....|....*....|....
gi 1958749768 311 YVGAGTVEFIMDSKHNFYFMEMNT 334
Cdd:pfam07478 151 CRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
536-613 |
8.20e-17 |
|
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: 77.24 E-value: 8.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 536 SPVSAEGTQGGTI-APMTGTI-------EKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHA 607
Cdd:COG0511 51 AAAAAAASGGGAVkSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQ 130
|
....*.
gi 1958749768 608 PLVEFE 613
Cdd:COG0511 131 PLFVIE 136
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
159-334 |
9.69e-16 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 78.62 E-value: 9.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 159 KSTSKSIMAAAGVPVVEGY--HGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREakksfn 236
Cdd:PRK01966 124 KILTKRLLAAAGIPVAPYVvlTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEY------ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 237 DDAMLIEKFVDtPRHVEVqvfgdhhgnAVYLFERDCSV------------------QRRHQKIIeeaPAPgIDPEVRRRL 298
Cdd:PRK01966 198 DRKVLVEQGIK-GREIEC---------AVLGNDPKASVpgeivkpddfydyeakylDGSAELII---PAD-LSEELTEKI 263
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958749768 299 GEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNT 334
Cdd:PRK01966 264 RELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
127-336 |
2.66e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 74.96 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 127 FLSENMEfaELckQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRG- 205
Cdd:COG3919 90 LLSRHRD--EL--EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADD--LDALAEDLGFPVVVKPADSv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 206 -------GGGKGMRIIRSEKEFQEQLESARREakksfnDDAMLIEKFVDTPRHVEVQVFG--DHHGNAVYLFerdcsVQR 276
Cdd:COG3919 164 gydelsfPGKKKVFYVDDREELLALLRRIAAA------GYELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF-----TGR 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749768 277 RHQkiieEAPAPG-----IDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHN-FYFMEMNTRL 336
Cdd:COG3919 233 KLR----HYPPAGgnsaaRESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGeYKLIEINPRF 294
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
528-600 |
5.18e-14 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 74.97 E-value: 5.18e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749768 528 GIPVPKYLSPVSAEGTQGGTI-APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEG 600
Cdd:PRK14040 507 PAAAPAAAAAAAPAAAAGEPVtAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEG 580
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
163-319 |
8.76e-13 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 70.10 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 163 KSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGG-GGKGMRIIRSEKEFQEqlesarreAKKSFNDDAML 241
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLED--LEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADLEA--------AWAALGGGPCI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 242 IEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHqkIIEE--APApGIDPEVRRRLGEAAVRAAKAVNYVGAGTV 317
Cdd:COG0026 164 LEEFVPFERELSVIVARSPDGEVATypVVE---NVHRNG--ILDEsiAPA-RISEALAAEAEEIAKRIAEALDYVGVLAV 237
|
..
gi 1958749768 318 EF 319
Cdd:COG0026 238 EF 239
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
549-612 |
1.89e-12 |
|
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: 62.62 E-value: 1.89e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958749768 549 APMTGT-----IEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEF 612
Cdd:pfam00364 5 SPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
132-333 |
9.79e-12 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 66.12 E-value: 9.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 132 MEFAELCKQEGIIFIGPPStAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGM 211
Cdd:COG0189 71 LALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPPTLVTRDPDD--LRAFLEELGGPVVLKPLDGSGGRGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 212 RIIRSEKEFQEQLesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVF--GdhhGNAVYLFER-----DCSVQRRHQKIIEE 284
Cdd:COG0189 148 FLVEDEDALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVLvvG---GEPVAAIRRipaegEFRTNLARGGRAEP 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958749768 285 APapgIDPEVRrrlgEAAVRAAKAV--NYVGagtVEFIMDsKHNFYFMEMN 333
Cdd:COG0189 220 VE---LTDEER----ELALRAAPALglDFAG---VDLIED-DDGPLVLEVN 259
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
508-610 |
1.98e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 61.75 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 508 KF-ILLDNTIYLFSME---GSIEVGIPVPKYLSPVSAEGTQGGTI-----------------APMTGTIEKVFVKAGDRV 566
Cdd:PRK06549 4 KFkITIDGKEYLVEMEeigAPAQAAAPAQPASTPVPVPTEASPQVeaqapqpaaaagadampSPMPGTILKVLVAVGDQV 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958749768 567 KAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLV 610
Cdd:PRK06549 84 TENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
165-353 |
2.77e-11 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 66.92 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 165 IMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESArreakkSFNDDAMLIEK 244
Cdd:PRK12815 677 LLDELGLPHVPGLTATDEEE--AFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAEN------ASQLYPILIDQ 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 245 FVDTpRHVEVQVFGDhhGNAVYL---FErdcsvqrrHqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVN 310
Cdd:PRK12815 749 FIDG-KEYEVDAISD--GEDVTIpgiIE--------H---IEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLG 814
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958749768 311 YVGAGTVEFIMDSKhNFYFMEMNTRLQVEHPVTEMITGTDLVE 353
Cdd:PRK12815 815 FRGIMNIQFVLAND-EIYVLEVNPRASRTVPFVSKATGVPLAK 856
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
132-335 |
1.34e-10 |
|
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: 64.13 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 132 MEFAELCKQEGIIFIGPPSTAI-----RDMgikstSKSIMAAAGVPVVEGYHGNDQsDECLKEhAGKIGYPVMIKAIRGG 206
Cdd:COG0458 88 VELEEAGILEGVKILGTSPDAIdlaedREL-----FKELLDKLGIPQPKSGTATSV-EEALAI-AEEIGYPVIVRPSYVL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 207 GGKGMRIIRSEKEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLferdCSVQrrHqkiIEEA- 285
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLE----RALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAg 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 286 ----------PAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKhNFYFMEMNTR 335
Cdd:COG0458 228 vhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDG-RVYVIEVNPR 286
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
163-319 |
4.19e-10 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 61.71 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 163 KSIMAAAGVPVVEgYHG-NDQSDecLKEHAGKIGYPVMIKAIRGG-GGKGMRIIRSEKEFQEqlesarreAKKSFNDDAM 240
Cdd:PRK06019 105 KQFLDKLGIPVAP-FAVvDSAED--LEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEA--------AWALLGSVPC 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 241 LIEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHQKIIEEAPAPgIDPEVRRRLGEAAVRAAKAVNYVGAGTVE 318
Cdd:PRK06019 174 ILEEFVPFEREVSVIVARGRDGEVVFypLVE---NVHRNGILRTSIAPAR-ISAELQAQAEEIASRIAEELDYVGVLAVE 249
|
.
gi 1958749768 319 F 319
Cdd:PRK06019 250 F 250
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
182-358 |
5.26e-10 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 62.71 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 182 QSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHH 261
Cdd:TIGR01369 691 TSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGE 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 262 GNAVY-LFErdcsvqrrHqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSkHNFYF 329
Cdd:TIGR01369 767 EVLIPgIME--------H---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYV 834
|
170 180
....*....|....*....|....*....
gi 1958749768 330 MEMNTRLQVEHPVTEMITGTDLVEWQLRI 358
Cdd:TIGR01369 835 IEVNPRASRTVPFVSKATGVPLAKLAVRV 863
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
167-319 |
8.98e-10 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 58.03 E-value: 8.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 167 AAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGG-GGKGMRIIRSEkefqEQLESARREAKksfnDDAMLIEKF 245
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEE--LIEAGQELGYPCVVKARRGGyDGKGQYVVRSE----ADLPQAWEELG----DGPVIVEEF 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749768 246 VDTPRHVEVQVFGDHHGnAVYLFErdcSVQRRHQK---IIEEAPAPgIDPEVRRRLGEAAVRAAKAVNYVGAGTVEF 319
Cdd:pfam02222 71 VPFDRELSVLVVRSVDG-ETAFYP---VVETIQEDgicRLSVAPAR-VPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
548-613 |
6.29e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 52.87 E-value: 6.29e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749768 548 IAPMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEFE 613
Cdd:PRK08225 5 YASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
356-389 |
5.62e-08 |
|
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: 50.95 E-value: 5.62e-08
10 20 30
....*....|....*....|....*....|....
gi 1958749768 356 LRIVGLRTNVDFLLRLSGHSEFEAGNVHTDFIPQ 389
Cdd:pfam02785 75 FRIEGVKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
147-336 |
5.84e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 56.01 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 147 GPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLES 226
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAV--ALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 227 ARREAKKSFnddamLIEKFVDTPRHvEVQVFGDHHGNAVYlferdcSVQRRHQ-------KIIEEAPAPgIDPEVRRRLG 299
Cdd:PRK02186 174 LRRAGTRAA-----LVQAYVEGDEY-SVETLTVARGHQVL------GITRKHLgppphfvEIGHDFPAP-LSAPQRERIV 240
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958749768 300 EAAVRAAKAVNY-VGAGTVEFIMdSKHNFYFMEMNTRL 336
Cdd:PRK02186 241 RTVLRALDAVGYaFGPAHTELRV-RGDTVVIIEINPRL 277
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
163-246 |
2.73e-07 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 53.62 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 163 KSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGMRI-IRSEkefqEQLESARREAKKSFNDdaML 241
Cdd:PRK14016 219 KRLLAAAGVPVPEGRVVTSAED--AWEAAEEIGYPVVVKPLDGNHGRGVTVnITTR----EEIEAAYAVASKESSD--VI 290
|
....*
gi 1958749768 242 IEKFV 246
Cdd:PRK14016 291 VERYI 295
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
87-365 |
4.90e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 52.19 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 87 MADEAYSIgpaPSQQSYLAMEKIIQVAKSSAAQAIHPGY----GFLSENM-EFAElckqEGIIFIGPPSTAIRDMGIKST 161
Cdd:PRK12767 42 FADKFYVV---PKVTDPNYIDRLLDICKKEKIDLLIPLIdpelPLLAQNRdRFEE----IGVKVLVSSKEVIEICNDKWL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 162 SKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEkefqEQLESARREAKKsfnddaML 241
Cdd:PRK12767 115 TYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDK----EELEFLLEYVPN------LI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 242 IEKFVDTPRhVEVQVFGDHHGNAVylferdCSVQRRHQKIIEEAPAPGI---DPEVRrrlgEAAVRAAKAVNYVGAGTVE 318
Cdd:PRK12767 185 IQEFIEGQE-YTVDVLCDLNGEVI------SIVPRKRIEVRAGETSKGVtvkDPELF----KLAERLAEALGARGPLNIQ 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958749768 319 FIMDSKhNFYFMEMNTRLQVEHPVTEMiTGTDLVEWQLRIVGLRTNV 365
Cdd:PRK12767 254 CFVTDG-EPYLFEINPRFGGGYPLSYM-AGANEPDWIIRNLLGGENE 298
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
553-612 |
7.56e-07 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 46.98 E-value: 7.56e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958749768 553 GTIEKVFVKAGDRVKAGDALMVMIAMK--MEhtIKAPKDGRIKKVFFSEGAQANRHAPLVEF 612
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
87-336 |
4.19e-06 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 50.00 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 87 MADEAYsIGPAPSQqsylAMEKIIQVAKssaAQAIHPGYG-----FLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKST 161
Cdd:TIGR01369 59 MADKVY-IEPLTPE----AVEKIIEKER---PDAILPTFGgqtalNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDREL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 162 SKSIMAAAGVPVVEGYHGNDQsDECLkEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKKsfndDAML 241
Cdd:TIGR01369 131 FREAMKEIGEPVPESEIAHSV-EEAL-AAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 242 IEKFVDTPRHVEVQVFGDHHGNAVYLferdCSVQR-----RHQ-KIIEEAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:TIGR01369 205 VEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGC 280
|
250 260
....*....|....*....|..
gi 1958749768 316 TVEFIMDSK-HNFYFMEMNTRL 336
Cdd:TIGR01369 281 NVQFALNPDsGRYYVIEVNPRV 302
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
536-613 |
5.96e-06 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 49.33 E-value: 5.96e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749768 536 SPVSAEGTQGGTIAPMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEFE 613
Cdd:PRK14042 517 SSVNNKIGPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
553-616 |
7.54e-05 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 45.58 E-value: 7.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749768 553 GTIEKVFVKAGDRVKAGDALM-VMI--AMkMEhtIKAPKDGRIKKVFFSEGAQANRHAPLVEFEEEE 616
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVtVETdkAT-ME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
188-313 |
1.21e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 45.47 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 188 KEHAGKIGYPVMIkaiRGG---GGKGMRIIRSEKEfqeqLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDhhGNA 264
Cdd:PRK05294 697 LEVAEEIGYPVLV---RPSyvlGGRAMEIVYDEEE----LERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GED 767
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958749768 265 VYL---FErdcsvqrrHqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVNYVG 313
Cdd:PRK05294 768 VLIggiME--------H---IEEAgvhsgdsacslPPQTLSEEIIEEIREYTKKLALELNVVG 819
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
148-315 |
1.55e-04 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 44.67 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 148 PPSTAIRDMGIKSTSKSIMAAAGVPVVEgyHGNDQSDECLKEHAGKIGYPVMIKAIRGG-GGKGMRIIRSEKEfqeqLES 226
Cdd:PLN02948 111 PKSSTIRIIQDKYAQKVHFSKHGIPLPE--FMEIDDLESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTEED----LSS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 227 ArrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV-Y-LFErdcSVQRRHQKIIEEAPAPgIDPEVRRRLGEAAVR 304
Cdd:PLN02948 185 A--VAALGGFERGLYAEKWAPFVKELAVMVARSRDGSTRcYpVVE---TIHKDNICHVVEAPAN-VPWKVAKLATDVAEK 258
|
170
....*....|.
gi 1958749768 305 AAKAVNyvGAG 315
Cdd:PLN02948 259 AVGSLE--GAG 267
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
553-613 |
2.25e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 44.04 E-value: 2.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749768 553 GTIEKVFVKAGDRVKAGDALM-VMI--AMkMEhtIKAPKDGRIKKVFFSEGAQANRHAPLVEFE 613
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLItVETdkAT-ME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
550-609 |
3.19e-04 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 42.90 E-value: 3.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749768 550 PMTGTI-------EKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPL 609
Cdd:PLN02983 203 PMAGTFyrspapgEPPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPL 269
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
159-351 |
4.33e-04 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 41.72 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 159 KSTSKSIMAAAGVPV-VEGYHGNDQSDECLKEHAGKiGYPVMIKAIRGGGGKGMRIIRSEKEFqEQLESARREAkksfnd 237
Cdd:pfam08443 4 KAKSHQLLAKHGIGPpNTRLAWYPEDAEQFIEQIKR-QFPVIVKSIYGSQGIGVFLAEDEQKL-RQTLSATNEQ------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 238 daMLIEKFVDTP--RHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPApGIDPEVRrrlgEAAVRAAKAVNYVGAG 315
Cdd:pfam08443 76 --ILVQEFIAEAnnEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKY-QLSQEET----ELAIKAAQAMQLDVAG 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958749768 316 tVEfIMDSKHNFYFMEMNTRLQVEHpvTEMITGTDL 351
Cdd:pfam08443 149 -VD-LLRQKRGLLVCEVNSSPGLEG--IEKTLGINI 180
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
537-575 |
5.14e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.73 E-value: 5.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1958749768 537 PVSAEGTQGGTI----APMTGTIEKVFVKAGDRVKAGDALMVM 575
Cdd:COG1566 34 PVTADGRVEARVvtvaAKVSGRVTEVLVKEGDRVKKGQVLARL 76
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
135-336 |
7.33e-04 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 42.31 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 135 AELCKQEGI--IFIGP--P-----STAIRDMGI---------------KSTSKSIMAAAGVPVVEgYHGNDQSDEClKEH 190
Cdd:COG0151 55 VAFAKEENIdlVVVGPeaPlvagiVDAFRAAGIpvfgpskaaaqlegsKAFAKEFMARYGIPTAA-YRVFTDLEEA-LAY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 191 AGKIGYPVMIKAIRGGGGKGMRIIRSEKEfqeqlesARREAKKSFNDDAM-------LIEKFVDTPRhVEVQVFGDhhGN 263
Cdd:COG0151 133 LEEQGAPIVVKADGLAAGKGVVVAETLEE-------ALAAVDDMLADGKFgdagarvVIEEFLEGEE-ASLFALTD--GK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 264 AVYLFE--RDcsvqrrHqKIIEE-------------APAPGIDPEVRRRLGEAAVR------AAKAVNYVG---AGtvef 319
Cdd:COG0151 203 TVLPLPtaQD------H-KRAGDgdtgpntggmgaySPAPVVTEELLEKIMEEIIEptvagmAAEGIPYRGvlyAG---- 271
|
250
....*....|....*..
gi 1958749768 320 IMDSKHNFYFMEMNTRL 336
Cdd:COG0151 272 LMITADGPKVLEFNVRF 288
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
547-575 |
1.29e-03 |
|
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: 41.99 E-value: 1.29e-03
10 20 30
....*....|....*....|....*....|
gi 1958749768 547 TI-APMTGTIEKVFVKAGDRVKAGDALMVM 575
Cdd:COG1038 1115 TItAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
191-335 |
1.29e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.07 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 191 AGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKksfnDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYlfer 270
Cdd:PLN02735 733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDP----ERPVLVDKYLSDATEIDVDALADSEGNVVI---- 804
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749768 271 dCSVQRRhqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNTR 335
Cdd:PLN02735 805 -GGIMEH----IEQAgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR 875
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
549-575 |
2.41e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 41.28 E-value: 2.41e-03
10 20
....*....|....*....|....*..
gi 1958749768 549 APMTGTIEKVFVKAGDRVKAGDALMVM 575
Cdd:PRK12999 1118 APVDGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
549-600 |
2.63e-03 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 36.71 E-value: 2.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1958749768 549 APMTGTIEKVFVKAGDRVKAGDALMVMIAMKMEHTIKAPKDGRIKKVFFSEG 600
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVG 58
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
549-575 |
2.71e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 40.31 E-value: 2.71e-03
10 20
....*....|....*....|....*..
gi 1958749768 549 APMTGTIEKVFVKAGDRVKAGDALMVM 575
Cdd:COG0845 28 ARVSGRVEEVLVDEGDRVKKGQVLARL 54
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
191-334 |
3.19e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 40.04 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 191 AGKIGYPVMIKAIRGGGGKGMRIIRSekefQEQLESARREAKKSfndDAMLIEKFVdTPRHVEVQVFGDHHGNAVYLFER 270
Cdd:PRK14569 126 EDEISFPVAVKPSSGGSSIATFKVKS----IQELKHAYEEASKY---GEVMIEQWV-TGKEITVAIVNDEVYSSVWIEPQ 197
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749768 271 DCSVQRRHQ---KIIEEAPApGIDPEVRRRLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFYFMEMNT 334
Cdd:PRK14569 198 NEFYDYESKysgKSIYHSPS-GLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEINS 263
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
187-247 |
4.07e-03 |
|
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439798 [Multi-domain] Cd Length: 393 Bit Score: 39.72 E-value: 4.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958749768 187 LKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEkefqEQLESARREAKKS--FNDDAMLIEKFVD 247
Cdd:COG0027 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----ADIEAAWEYAQEGgrGGAGRVIVEGFVD 199
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
547-575 |
8.07e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 34.73 E-value: 8.07e-03
10 20 30
....*....|....*....|....*....|
gi 1958749768 547 TIAPMT-GTIEKVFVKAGDRVKAGDALMVM 575
Cdd:pfam13533 4 KIASPVsGKVVAVNVKEGQQVKKGDVLATL 33
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
194-267 |
8.07e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 37.65 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749768 194 IGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARRE--------AKKSFNDDAMLIEKFVDTPrHVEVQVFGDHHGNAV 265
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEieqwkemyPEAVVDGGSFLVEEYIEGE-EFAVDAYFDENGEPV 79
|
..
gi 1958749768 266 YL 267
Cdd:pfam13535 80 IL 81
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
183-233 |
8.77e-03 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 38.96 E-value: 8.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958749768 183 SDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEkefqEQLESARREAKK 233
Cdd:PRK09288 137 SLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----EDIEKAWEYAQE 183
|
|
| |
