|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
45-495 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 821.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 45 ITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 125 YGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVR 204
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 205 GGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 285 APAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 365 PLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPSADmSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:COG4770 322 PFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGP-GVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 186700620 445 SKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQHHKDLLPS 495
Cdd:COG4770 401 ARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAA 451
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
45-488 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 649.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 45 ITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 125 YGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVR 204
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 205 GGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 285 APAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 365 PLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPsADMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:PRK08591 322 SIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPP-GGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 186700620 445 SKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQH 488
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
45-488 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 625.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 45 ITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 125 YGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVR 204
Cdd:PRK06111 82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 205 GGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 285 APAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 365 PLSQEEIPLQGHAFEARIYAEDPdNNFMPGAGPLVHLSTPSADmSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGE-GVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 186700620 445 SKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQH 488
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQ 443
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
47-503 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 590.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 47 KVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPGYG 126
Cdd:PRK08654 4 KILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 127 FLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVRGG 206
Cdd:PRK08654 84 FLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 207 GGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAP 286
Cdd:PRK08654 164 GGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 287 APGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSrHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPL 366
Cdd:PRK08654 244 SPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN-GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 367 SQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPSAdMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSALSK 446
Cdd:PRK08654 323 KQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGG-PGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIAR 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 186700620 447 LRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIpQHHKDLLPSHSTIAKES 503
Cdd:PRK08654 402 MRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFI-EEETTILEEMKRYALEE 457
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
45-488 |
0e+00 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 584.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 45 ITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:COG1038 4 IKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAIHP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 124 GYGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAV 203
Cdd:COG1038 84 GYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 204 RGGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:COG1038 164 AGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 284 EAPAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 363
Cdd:COG1038 244 IAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 364 -------IPlSQEEIPLQGHAFEARIYAEDPDNNFMPGAGplvhlstpsadmstRIET-------GVR-------QGDEV 422
Cdd:COG1038 324 lddpeigIP-SQEDIRLNGYAIQCRITTEDPANNFMPDTG--------------RITAyrsaggfGIRldggnayTGAVI 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186700620 423 SVHYDPMIAKLVVWASDRQSALSKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQH 488
Cdd:COG1038 389 TPYYDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDET 454
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
45-488 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 574.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 45 ITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:PRK12999 5 IKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAIHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 124 GYGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAV 203
Cdd:PRK12999 85 GYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 204 RGGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:PRK12999 165 AGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 284 EAPAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 363
Cdd:PRK12999 245 IAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGAT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 364 I------PLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPSAdmstrieTGVR-------QGDEVSVHYDPMI 430
Cdd:PRK12999 325 LhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGG-------FGVRldggnafAGAEITPYYDSLL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 186700620 431 AKLVVWASDRQSALSKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQH 488
Cdd:PRK12999 398 VKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDET 455
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
46-485 |
0e+00 |
|
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: 574.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 46 TKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPGY 125
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 126 GFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLrEHAGKIGYPVMIKAVRG 205
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGTGLLSSLDEAL-EAAKEIGYPVMLKSTAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 206 GGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEA 285
Cdd:TIGR02712 161 GGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 286 PAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDS-RHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:TIGR02712 241 PAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEaRDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 365 PLSQ--EEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPSAdmsTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQS 442
Cdd:TIGR02712 321 DFASlnISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPDD---VRVDTWVETGTEVSPEYDPMLAKIIVHGSDRED 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 186700620 443 ALSKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFI 485
Cdd:TIGR02712 398 AILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTL 440
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
45-488 |
0e+00 |
|
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: 560.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 45 ITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 125 YGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVR 204
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 205 GGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 285 APAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 365 PLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLsTPSADMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRY-LPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 186700620 445 SKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQH 488
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKK 444
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
45-491 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 558.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 45 ITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 125 YGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVR 204
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 205 GGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 285 APAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 365 PLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPSAdMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGG-LGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 186700620 445 SKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQHHKD 491
Cdd:PRK05586 401 QKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKLVD 447
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
45-488 |
3.09e-176 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 511.95 E-value: 3.09e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 45 ITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPsQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP-LAGYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 125 YGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVR 204
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 205 GGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 285 APAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 365 PLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPSADmSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:PRK07178 321 SYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGP-GVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEAL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 186700620 445 SKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQH 488
Cdd:PRK07178 400 DRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESH 443
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
45-488 |
1.79e-170 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 496.19 E-value: 1.79e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 45 ITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 125 YGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVR 204
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 205 GGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 285 APAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 365 PlSQEEIPLQGHAFEARIYAEDPdNNFMPGAGPLVHLSTPsADMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSAL 444
Cdd:PRK08462 324 P-SQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAP-GGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 186700620 445 SKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQH 488
Cdd:PRK08462 401 AKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
43-485 |
6.12e-170 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 495.81 E-value: 6.12e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 43 GSITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIH 122
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 123 PGYGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKA 202
Cdd:PRK12833 83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 203 VRGGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHgNAVYLFERDCSVQRRHQKII 282
Cdd:PRK12833 163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 283 EEAPAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMD-SRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAG 361
Cdd:PRK12833 242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 362 EKIPLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPSADmSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQ 441
Cdd:PRK12833 322 EPLRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGP-GVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 186700620 442 SALSKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFI 485
Cdd:PRK12833 401 AALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
45-517 |
1.89e-162 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 477.00 E-value: 1.89e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 45 ITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQqSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIK-GYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 125 YGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHG-KDQSDQCLREHAGKIGYPVMIKAV 203
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 204 RGGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 284 EAPAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 363
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 364 IPLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLsTPSADMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSA 443
Cdd:PRK08463 321 LDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEY-YPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186700620 444 LSKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQHHKDLLPS---HSTIAKESVCQAALGLILKEKE 517
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKtedRHQENKEEVIAAIAAALKKIRE 476
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
47-488 |
1.93e-160 |
|
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: 493.19 E-value: 1.93e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 47 KVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ---QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLgpiEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 124 GYGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAV 203
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 204 RGGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 284 EAPAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK 363
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 364 IPL------SQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPSAdMSTRIETGVR-QGDEVSVHYDPMIAKLVVW 436
Cdd:TIGR01235 321 LPTpqlgvpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGG-FGIRLDGGNSyAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 186700620 437 ASDRQSALSKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQH 488
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTT 451
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
159-365 |
1.36e-83 |
|
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: 263.40 E-value: 1.36e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 159 KSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLESARREAKKSFNDD 238
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 239 AMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVE 318
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 186700620 319 FIMDSRH-NFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIP 365
Cdd:pfam02786 162 FALDPFSgEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
45-152 |
1.22e-63 |
|
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: 206.57 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 45 ITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 186700620 125 YGFLSENMEFAELCKQEGIIFIGPPSSA 152
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
116-368 |
1.84e-59 |
|
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: 201.25 E-value: 1.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 116 SAAQAIHPGYGF---LSEN----MEFAELCKQEGIIfiGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDqcLR 188
Cdd:COG0439 7 AAAAELARETGIdavLSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEE--AL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 189 EHAGKIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTpRHVEVQVFGdHHGNAVYlf 268
Cdd:COG0439 83 AFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV-RDGEVVV-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 269 erdCSVQRRHQK---IIE---EAPAPgINPEVRRKLGEAAVRAAKAVKYV-GAGTVEFIMDSRHNFYFMEMNTRLQVEH- 340
Cdd:COG0439 159 ---CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLGGEHi 234
|
250 260
....*....|....*....|....*....
gi 186700620 341 -PVTEMITGTDLVEWQLRIAAGEKIPLSQ 368
Cdd:COG0439 235 pPLTELATGVDLVREQIRLALGEPRILDP 263
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
379-487 |
3.86e-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: 164.97 E-value: 3.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 379 EARIYAEDPDNNFMPGAGPLVHLSTPSAdMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSALSKLRYCLHQYNIVG 458
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGG-PGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 186700620 459 LRSNVDFLLRLSGHPEFEAGNVHTDFIPQ 487
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
379-485 |
1.12e-46 |
|
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: 160.66 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 379 EARIYAEDPDNNFMPGAGPLVHLSTPSaDMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSALSKLRYCLHQYNIVG 458
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPG-GPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*..
gi 186700620 459 LRSNVDFLLRLSGHPEFEAGNVHTDFI 485
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
647-710 |
9.10e-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: 9.10e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186700620 647 APMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEF 710
Cdd:cd06850 4 APMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
650-710 |
1.14e-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: 83.65 E-value: 1.14e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186700620 650 TGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEF 710
Cdd:cd06663 13 DGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
634-709 |
1.30e-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: 1.30e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186700620 634 SPVSAEGAQGGTIAPMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVE 709
Cdd:PRK05641 76 APAPASAGENVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIE 151
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
647-700 |
5.72e-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: 88.98 E-value: 5.72e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 186700620 647 APMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQ 700
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
647-700 |
2.03e-17 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 87.12 E-value: 2.03e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 186700620 647 APMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQ 700
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQ 1134
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
628-711 |
6.43e-17 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 84.51 E-value: 6.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 628 PVPKYLSPVSAEGAQGGTI-APMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAP 706
Cdd:PRK09282 507 PLKEIVVGGRPRASAPGAVtSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDV 586
|
....*
gi 186700620 707 LVEFE 711
Cdd:PRK09282 587 LMEIE 591
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
147-334 |
7.20e-17 |
|
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: 82.08 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 147 GPPSSAI-RDmgiKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLE 225
Cdd:COG1181 86 GVLASALaMD---KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 226 SARREakksfnDDAMLIEKFVDtPRHVEVQVFGDHH-----------GNAVYLFErdcsVQRRHQKIIEEAPAPgINPEV 294
Cdd:COG1181 163 EAFKY------DDKVLVEEFID-GREVTVGVLGNGGpralppieivpENGFYDYE----AKYTDGGTEYICPAR-LPEEL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 186700620 295 RRKLGEaavraakavkYV----------GAGTVEFIMDSRHNFYFMEMNT 334
Cdd:COG1181 231 EERIQE----------LAlkafralgcrGYARVDFRLDEDGEPYLLEVNT 270
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
634-711 |
8.01e-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: 77.63 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 634 SPVSAEGAQGGTI-APMTGTI-------EKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHA 705
Cdd:COG0511 51 AAAAAAASGGGAVkSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQ 130
|
....*.
gi 186700620 706 PLVEFE 711
Cdd:COG0511 131 PLFVIE 136
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
626-698 |
4.93e-14 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 75.35 E-value: 4.93e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186700620 626 GIPVPKYLSPVSAEGAQGGTI-APMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEG 698
Cdd:PRK14040 507 PAAAPAAAAAAAPAAAAGEPVtAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEG 580
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
647-710 |
5.79e-13 |
|
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: 64.54 E-value: 5.79e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186700620 647 APMTGT-----IEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEF 710
Cdd:pfam00364 5 SPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
127-365 |
9.39e-12 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 67.26 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 127 FLSENMEfaELckQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDqcLREHAGKIGYPVMIKAVRG- 205
Cdd:COG3919 90 LLSRHRD--EL--EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADD--LDALAEDLGFPVVVKPADSv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 206 -------GGGKGMRIVRSEREFQEQLESARREakksfnDDAMLIEKFVDTPRHVEVQVFG--DHHGNAVYLFerdcSVQR 276
Cdd:COG3919 164 gydelsfPGKKKVFYVDDREELLALLRRIAAA------GYELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF----TGRK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 277 RHQK--------IIEEAPAPGINPEVRRKLGEAAvraakavkYVGAGTVEFIMDSRHN-FYFMEMNTRL--QVEHPVtem 345
Cdd:COG3919 234 LRHYppaggnsaARESVDDPELEEAARRLLEALG--------YHGFANVEFKRDPRDGeYKLIEINPRFwrSLYLAT--- 302
|
250 260
....*....|....*....|
gi 186700620 346 ITGTDLVEWQLRIAAGEKIP 365
Cdd:COG3919 303 AAGVNFPYLLYDDAVGRPLE 322
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
603-708 |
1.36e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 62.52 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 603 RKSKfILLDNTVHLFSMEgsiEVGIPV------------------------PKYLSPVSAEGAQGGTiAPMTGTIEKVFV 658
Cdd:PRK06549 3 RKFK-ITIDGKEYLVEME---EIGAPAqaaapaqpastpvpvpteaspqveAQAPQPAAAAGADAMP-SPMPGTILKVLV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 186700620 659 KAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLV 708
Cdd:PRK06549 78 AVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
165-334 |
2.23e-11 |
|
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: 63.87 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 165 IMAAAGVPVV-------EGYHgKDQSDQCLREHAgKIGYPVMIKAVRGGGGKGMRIVRSErefqEQLESARREAKKsfND 237
Cdd:pfam07478 1 LLKAAGLPVVpfvtftrADWK-LNPKEWCAQVEE-ALGYPVFVKPARLGSSVGVSKVESR----EELQAAIEEAFQ--YD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 238 DAMLIEKFVDTpRHVEVQVFGDHHGNAVYLFER--DCSVQRRHQKIIEEA-----PApGINPEVRRKLGEAAVRAAKAVK 310
Cdd:pfam07478 73 EKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALG 150
|
170 180
....*....|....*....|....
gi 186700620 311 YVGAGTVEFIMDSRHNFYFMEMNT 334
Cdd:pfam07478 151 CRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
162-334 |
1.67e-10 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 62.82 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 162 SKSIMAAAGVPVVEGYHGKDQSDQCLREHagKIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLESARReakksfNDDAML 241
Cdd:PRK01372 102 TKLVWQAAGLPTPPWIVLTREEDLLAAID--KLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFK------YDDEVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 242 IEKFVDTPrhvEVQ--VFGDH--------HGNAVYLFE----RDCSvqrrhQKIIeeaPApGINPEVRRKLGEAAVRAAK 307
Cdd:PRK01372 174 VEKYIKGR---ELTvaVLGGKalpvieivPAGEFYDYEakylAGGT-----QYIC---PA-GLPAEIEAELQELALKAYR 241
|
170 180
....*....|....*....|....*..
gi 186700620 308 AVKYVGAGTVEFIMDSRHNFYFMEMNT 334
Cdd:PRK01372 242 ALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
142-334 |
1.20e-09 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 60.52 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 142 GIIFIGPP--SSAirdMGI-KSTSKSIMAAAGVPVVEGY--HGKDQSDQCLREHAGKIGYPVMIKAVRGGGGKGMRIVRS 216
Cdd:PRK01966 107 GIPYVGCGvlASA---LSMdKILTKRLLAAAGIPVAPYVvlTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKN 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 217 EREFQEQLESARREakksfnDDAMLIEKFVDtPRHVEVqvfgdhhgnAVYLFERDCSV------------------QRRH 278
Cdd:PRK01966 184 EEELAAALDLAFEY------DRKVLVEQGIK-GREIEC---------AVLGNDPKASVpgeivkpddfydyeakylDGSA 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186700620 279 QKIIeeaPAPgINPEVRRKLGEAAVRAakavkY--VGAG---TVEFIMDSRHNFYFMEMNT 334
Cdd:PRK01966 248 ELII---PAD-LSEELTEKIRELAIKA-----FkaLGCSglaRVDFFLTEDGEIYLNEINT 299
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
646-711 |
3.05e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 53.64 E-value: 3.05e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186700620 646 IAPMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEFE 711
Cdd:PRK08225 5 YASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
165-364 |
6.35e-09 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 59.60 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 165 IMAAAGVPVVEGyhGKDQSDQCLREHAGKIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLESArreakkSFNDDAMLIEK 244
Cdd:PRK12815 677 LLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAEN------ASQLYPILIDQ 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 245 FVDTpRHVEVQVFGDhhGNAVYL---FErdcsvqrrHqkiIEEA-----------PAPGINPEVRRKLGEAAVRAAKAVK 310
Cdd:PRK12815 749 FIDG-KEYEVDAISD--GEDVTIpgiIE--------H---IEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLG 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 186700620 311 YVGAGTVEFIMDSRhNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:PRK12815 815 FRGIMNIQFVLAND-EIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSL 867
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
132-257 |
5.88e-08 |
|
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: 54.95 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 132 MEFAELCKQEGIIFIGPPSsAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDqcLREHAGKIGYPVMIKAVRGGGGKGM 211
Cdd:COG0189 71 LALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPPTLVTRDPDD--LRAFLEELGGPVVLKPLDGSGGRGV 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 186700620 212 RIVRSEREFQEQLesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVF 257
Cdd:COG0189 148 FLVEDEDALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVL 188
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
188-364 |
8.81e-08 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 55.78 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 188 REHAGKIGYPVMIKAVRGGGGKGMRIVRSErefqEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY- 266
Cdd:TIGR01369 697 VEFASEIGYPVLVRPSYVLGGRAMEIVYNE----EELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPg 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 267 LFErdcsvqrrHqkiIEEA-----------PAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSrHNFYFMEMNTR 335
Cdd:TIGR01369 773 IME--------H---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPR 840
|
170 180
....*....|....*....|....*....
gi 186700620 336 LQVEHPVTEMITGTDLVEWQLRIAAGEKI 364
Cdd:TIGR01369 841 ASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
651-710 |
3.29e-07 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 48.14 E-value: 3.29e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186700620 651 GTIEKVFVKAGDRVKAGDSLMVMIAMK--MEhtIKAPKDGRIKKVFFSEGAQANRHAPLVEF 710
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
167-247 |
3.84e-07 |
|
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: 50.72 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 167 AAAGVPVVEGYHGKDQSDqcLREHAGKIGYPVMIKAVRGG-GGKGMRIVRSErefqEQLESARREAKksfnDDAMLIEKF 245
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEE--LIEAGQELGYPCVVKARRGGyDGKGQYVVRSE----ADLPQAWEELG----DGPVIVEEF 70
|
..
gi 186700620 246 VD 247
Cdd:pfam02222 71 VP 72
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
132-265 |
3.95e-07 |
|
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: 53.34 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 132 MEFAELCKQEGIIFIGPPSSAI-----RDMgikstSKSIMAAAGVPVVEGYHGKDQSDqcLREHAGKIGYPVMIKA--VR 204
Cdd:COG0458 88 VELEEAGILEGVKILGTSPDAIdlaedREL-----FKELLDKLGIPQPKSGTATSVEE--ALAIAEEIGYPVIVRPsyVL 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186700620 205 GGggKGMRIVRSEREFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 265
Cdd:COG0458 161 GG--RGMGIVYNEEELEEYLE----RALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVI 215
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
147-435 |
7.29e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 52.93 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 147 GPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDqcLREHAGKIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLES 226
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAV--ALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 227 ARREAKKSFnddamLIEKFVDTPRHvEVQVFGDHHGNAVYlferdcSVQRRHQ-------KIIEEAPAPGINPEVRRKLG 299
Cdd:PRK02186 174 LRRAGTRAA-----LVQAYVEGDEY-SVETLTVARGHQVL------GITRKHLgppphfvEIGHDFPAPLSAPQRERIVR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 300 EAAVRAAKAVKYVGAGTVEFIMdSRHNFYFMEMNTRLQVEH-PVT-EMITGTDLVEWQLRIAAGE--------------K 363
Cdd:PRK02186 242 TVLRALDAVGYAFGPAHTELRV-RGDTVVIIEINPRLAGGMiPVLlEEAFGVDLLDHVIDLHLGVaafadptakrygaiR 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186700620 364 IPLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPlVHLSTPSADMSTRIETGVRQGDE---VSVHYDPMIAKLVV 435
Cdd:PRK02186 321 FVLPARSGVLRGLLFLPDDIAARPELRFHPLKQP-GDALRLEGDFRDRIAAVVCAGDHrdsVAAAAERAVAGLSI 394
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
148-247 |
1.31e-06 |
|
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: 51.23 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 148 PPSSAIR---DmgiKSTSKSIMAAAGVPVVEGYHGKDQSDqcLREHAGKIGYPVMIKAVRGG-GGKGMRIVRSErefqEQ 223
Cdd:COG0026 79 PGPEALEiaqD---RLLEKAFLAELGIPVAPFAAVDSLED--LEAAIAELGLPAVLKTRRGGyDGKGQVVIKSA----AD 149
|
90 100
....*....|....*....|....
gi 186700620 224 LEsarrEAKKSFNDDAMLIEKFVD 247
Cdd:COG0026 150 LE----AAWAALGGGPCILEEFVP 169
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
150-246 |
3.82e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 50.15 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 150 SSAI-----RDmgiKSTSKSIMAAAGVPVVEGyhGKDQSDQCLREHAGKIGYPVMIKAVRGGGGKGMRI-VRSErefqEQ 223
Cdd:PRK14016 204 TSAIavdiaCD---KELTKRLLAAAGVPVPEG--RVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTR----EE 274
|
90 100
....*....|....*....|...
gi 186700620 224 LESARREAKKSFNDdaMLIEKFV 246
Cdd:PRK14016 275 IEAAYAVASKESSD--VIVERYI 295
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
87-365 |
1.02e-05 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 48.34 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 87 MADEAYSIgpaPSQQSYLAMEKIIQVAKSSAAQAIHPGY----GFLSENM-EFAElckqEGIIFIGPPSSAIRDMGIKST 161
Cdd:PRK12767 42 FADKFYVV---PKVTDPNYIDRLLDICKKEKIDLLIPLIdpelPLLAQNRdRFEE----IGVKVLVSSKEVIEICNDKWL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 162 SKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVRGGGGKGMRIVRSErefqEQLESARREAKKsfnddaML 241
Cdd:PRK12767 115 TYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDK----EELEFLLEYVPN------LI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 242 IEKFVDTPRhVEVQVFGDHHGNAVYLFER----------DCSVQRRHQKIIEEApapginPEVRRKLGeaavraakavkY 311
Cdd:PRK12767 185 IQEFIEGQE-YTVDVLCDLNGEVISIVPRkrievragetSKGVTVKDPELFKLA------ERLAEALG-----------A 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 186700620 312 VGAGTVEFIMDSRhNFYFMEMNTRLQVEHPVTEMiTGTDLVEWQLRIAAGEKIP 365
Cdd:PRK12767 247 RGPLNIQCFVTDG-EPYLFEINPRFGGGYPLSYM-AGANEPDWIIRNLLGGENE 298
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
634-711 |
1.07e-05 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 48.95 E-value: 1.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186700620 634 SPVSAEGAQGGTIAPMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEFE 711
Cdd:PRK14042 517 SSVNNKIGPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
163-266 |
2.22e-05 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 47.45 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 163 KSIMAAAGVPVVEgYHG-KDQSDqcLREHAGKIGYPVMIKAVRGG-GGKGMRIVRSErefqEQLEsarrEAKKSFNDDAM 240
Cdd:PRK06019 105 KQFLDKLGIPVAP-FAVvDSAED--LEAALADLGLPAVLKTRRGGyDGKGQWVIRSA----EDLE----AAWALLGSVPC 173
|
90 100
....*....|....*....|....*.
gi 186700620 241 LIEKFVDTPRHVEVQVFGDHHGNAVY 266
Cdd:PRK06019 174 ILEEFVPFEREVSVIVARGRDGEVVF 199
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
651-714 |
2.37e-05 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 47.51 E-value: 2.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186700620 651 GTIEKVFVKAGDRVKAGDSLM-VMI--AMkMEhtIKAPKDGRIKKVFFSEGAQANRHAPLVEFEEEE 714
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVtVETdkAT-ME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
188-256 |
4.32e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 47.01 E-value: 4.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186700620 188 REHAGKIGYPVMikaVRGG---GGKGMRIVRSErefqEQLESARREAKKSFNDDAMLIEKFVDtpRHVEVQV 256
Cdd:PRK05294 697 LEVAEEIGYPVL---VRPSyvlGGRAMEIVYDE----EELERYMREAVKVSPDHPVLIDKFLE--GAIEVDV 759
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
149-257 |
6.24e-05 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 45.42 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 149 PSSAIRDMGIKSTSKSIMAAAGVPV-VEGYHGKDQSDQCLREHagkIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLESA 227
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLpRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHF 155
|
90 100 110
....*....|....*....|....*....|
gi 186700620 228 RREAKKSfndDAMLIEKFVDTPRHVEVQVF 257
Cdd:TIGR00768 156 EQLNGPQ---NLFLVQEYIKKPGGRDIRVF 182
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
651-715 |
1.12e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 45.58 E-value: 1.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186700620 651 GTIEKVFVKAGDRVKAGDSLM-VMI--AMkMEhtIKAPKDGRIKKVFFSEGAQANRHAPLVEFEEEES 715
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLItVETdkAT-ME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
87-265 |
5.63e-04 |
|
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: 43.45 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 87 MADEAYsIGPAPSQqsylAMEKIIQVAKssaAQAIHPGYG---FLSENMEFAEL--CKQEGIIFIGPPSSAIRDMGIKST 161
Cdd:TIGR01369 59 MADKVY-IEPLTPE----AVEKIIEKER---PDAILPTFGgqtALNLAVELEESgvLEKYGVEVLGTPVEAIKKAEDREL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 162 SKSIMAAAGVPVVEGY--HGKDQSdqclREHAGKIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLESARREAKKsfndDA 239
Cdd:TIGR01369 131 FREAMKEIGEPVPESEiaHSVEEA----LAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQ 202
|
170 180
....*....|....*....|....*.
gi 186700620 240 MLIEKFVDTPRHVEVQVFGDHHGNAV 265
Cdd:TIGR01369 203 VLVEKSLAGWKEIEYEVMRDSNDNCI 228
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
648-707 |
6.11e-04 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 42.52 E-value: 6.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186700620 648 PMTGTI-------EKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPL 707
Cdd:PLN02983 203 PMAGTFyrspapgEPPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPL 269
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
651-715 |
1.75e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 41.53 E-value: 1.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186700620 651 GTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEFEEEES 715
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
187-247 |
1.77e-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: 41.26 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186700620 187 LREHAGKIGYPVMIKAVRGGGGKGMRIVRSErefqEQLESARREAKKS--FNDDAMLIEKFVD 247
Cdd:COG0027 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----ADIEAAWEYAQEGgrGGAGRVIVEGFVD 199
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
645-673 |
1.86e-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: 41.60 E-value: 1.86e-03
10 20 30
....*....|....*....|....*....|
gi 186700620 645 TI-APMTGTIEKVFVKAGDRVKAGDSLMVM 673
Cdd:COG1038 1115 TItAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
647-698 |
2.02e-03 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 37.48 E-value: 2.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 186700620 647 APMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEG 698
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVG 58
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
148-256 |
2.51e-03 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 41.20 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 148 PPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDqsDQCLREHAGKIGYPVMIKAVRGG-GGKGMRIVRSErefqEQLES 226
Cdd:PLN02948 111 PKSSTIRIIQDKYAQKVHFSKHGIPLPEFMEIDD--LESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTE----EDLSS 184
|
90 100 110
....*....|....*....|....*....|
gi 186700620 227 ArrEAKKSFNDDAMLIEKFVDTPRHVEVQV 256
Cdd:PLN02948 185 A--VAALGGFERGLYAEKWAPFVKELAVMV 212
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
194-267 |
2.82e-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: 39.19 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 194 IGYPVMIKAVRGGGGKGMRIVRSEREFQEQLESARRE--------AKKSFNDDAMLIEKFVDTPrHVEVQVFGDHHGNAV 265
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEieqwkemyPEAVVDGGSFLVEEYIEGE-EFAVDAYFDENGEPV 79
|
..
gi 186700620 266 YL 267
Cdd:pfam13535 80 IL 81
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
647-673 |
3.62e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.89 E-value: 3.62e-03
10 20
....*....|....*....|....*..
gi 186700620 647 APMTGTIEKVFVKAGDRVKAGDSLMVM 673
Cdd:PRK12999 1118 APVDGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
187-233 |
4.26e-03 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 40.12 E-value: 4.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 186700620 187 LREHAGKIGYPVMIKAVRGGGGKGMRIVRSErefqEQLESARREAKK 233
Cdd:PRK09288 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----EDIEKAWEYAQE 183
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
191-265 |
4.83e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 40.53 E-value: 4.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186700620 191 AGKIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLESARREAKksfnDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 265
Cdd:PLN02735 733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDP----ERPVLVDKYLSDATEIDVDALADSEGNVV 803
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
647-673 |
5.30e-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: 39.54 E-value: 5.30e-03
10 20
....*....|....*....|....*..
gi 186700620 647 APMTGTIEKVFVKAGDRVKAGDSLMVM 673
Cdd:COG0845 28 ARVSGRVEEVLVDEGDRVKKGQVLARL 54
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
135-247 |
5.49e-03 |
|
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: 39.61 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186700620 135 AELCKQEGI--IFIGP--P-----SSAIRDMGI---------------KSTSKSIMAAAGVPVVEgYHGKDQSDQCLrEH 190
Cdd:COG0151 55 VAFAKEENIdlVVVGPeaPlvagiVDAFRAAGIpvfgpskaaaqlegsKAFAKEFMARYGIPTAA-YRVFTDLEEAL-AY 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186700620 191 AGKIGYPVMIKAVRGGGGKGMRIVRSEREfqeqlesARREAKKSFNDDAM-------LIEKFVD 247
Cdd:COG0151 133 LEEQGAPIVVKADGLAAGKGVVVAETLEE-------ALAAVDDMLADGKFgdagarvVIEEFLE 189
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
635-673 |
5.56e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 39.65 E-value: 5.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 186700620 635 PVSAEGAQGGTI----APMTGTIEKVFVKAGDRVKAGDSLMVM 673
Cdd:COG1566 34 PVTADGRVEARVvtvaAKVSGRVTEVLVKEGDRVKKGQVLARL 76
|
|
| |
