|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
47-387 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 617.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 47 STSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDA 126
Cdd:COG4770 117 IAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 127 MLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEF 206
Cdd:COG4770 197 VYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEF 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 207 IMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLV 286
Cdd:COG4770 277 LVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTIT 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 287 HLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGN 366
Cdd:COG4770 357 RLRPP-GGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGD 435
|
330 340
....*....|....*....|.
gi 647569552 367 VHTDFIPQHHKQLLLSRKAAA 387
Cdd:COG4770 436 VDTGFIERELAELLAAAAPEE 456
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
47-375 |
7.63e-168 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 485.46 E-value: 7.63e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 47 STSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDA 126
Cdd:PRK08591 117 VTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 127 MLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEF 206
Cdd:PRK08591 197 VYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEF 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 207 IMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLV 286
Cdd:PRK08591 277 LYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKIT 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 287 HLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGN 366
Cdd:PRK08591 357 RYHPP-GGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGD 435
|
....*....
gi 647569552 367 VHTDFIPQH 375
Cdd:PRK08591 436 YNIHYLEKK 444
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
49-378 |
1.69e-154 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 451.79 E-value: 1.69e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 49 SKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAML 128
Cdd:PRK06111 119 ARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 129 IEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIM 208
Cdd:PRK06111 199 IEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 209 DSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPsNNFMPVAGPLVHL 288
Cdd:PRK06111 279 DEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 289 STPRAdPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVH 368
Cdd:PRK06111 358 TLPGG-EGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYT 436
|
330
....*....|
gi 647569552 369 TDFIPQHHKQ 378
Cdd:PRK06111 437 TGFLTKQLVK 446
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
48-375 |
6.92e-145 |
|
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: 448.37 E-value: 6.92e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 48 TSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAM 127
Cdd:COG1038 121 AARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEV 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 128 LIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFI 207
Cdd:COG1038 201 FLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 208 MDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEK-------IPlSQEEITLQGHAFEARIYAEDPSNNFMP 280
Cdd:COG1038 281 VDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSlddpeigIP-SQEDIRLNGYAIQCRITTEDPANNFMP 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 281 VAGplvhlstpradpstRIET-------GVR-------QGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGL 346
Cdd:COG1038 360 DTG--------------RITAyrsaggfGIRldggnayTGAVITPYYDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGV 425
|
330 340
....*....|....*....|....*....
gi 647569552 347 HTNIDFLLNLSGHPEFEAGNVHTDFIPQH 375
Cdd:COG1038 426 KTNIPFLENVLNHPDFLAGECTTSFIDET 454
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
48-377 |
3.53e-143 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 424.40 E-value: 3.53e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 48 TSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAM 127
Cdd:PRK08654 118 NAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 128 LIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFI 207
Cdd:PRK08654 198 FIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 208 MdSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVH 287
Cdd:PRK08654 278 Y-SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKR 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 288 LSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNV 367
Cdd:PRK08654 357 YRSP-GGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNL 435
|
330
....*....|
gi 647569552 368 HTDFIPQHHK 377
Cdd:PRK08654 436 HTHFIEEETT 445
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
47-377 |
5.34e-143 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 422.20 E-value: 5.34e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 47 STSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDA 126
Cdd:PRK05586 117 SNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDS 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 127 MLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEF 206
Cdd:PRK05586 197 MYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEF 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 207 IMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLV 286
Cdd:PRK05586 277 LLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 287 HLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGN 366
Cdd:PRK05586 357 ELYIP-GGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGT 435
|
330
....*....|.
gi 647569552 367 VHTDFIPQHHK 377
Cdd:PRK05586 436 YDTSFIEKKLV 446
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
55-386 |
1.70e-140 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 436.88 E-value: 1.70e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 55 AAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVD 134
Cdd:PRK12999 129 KAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 135 TPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNF 214
Cdd:PRK12999 209 NPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNF 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 215 CFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI------PLSQEEITLQGHAFEARIYAEDPSNNFMPVAGplvhl 288
Cdd:PRK12999 289 YFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTG----- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 289 stpradpstRIET-------GVR-------QGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLL 354
Cdd:PRK12999 364 ---------RITAyrspggfGVRldggnafAGAEITPYYDSLLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLE 434
|
330 340 350
....*....|....*....|....*....|..
gi 647569552 355 NLSGHPEFEAGNVHTDFIPQhHKQLLLSRKAA 386
Cdd:PRK12999 435 NVLKHPDFRAGDYTTSFIDE-TPELFDFPKRR 465
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
47-375 |
2.85e-138 |
|
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: 409.92 E-value: 2.85e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 47 STSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDA 126
Cdd:TIGR00514 117 VSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 127 MLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEF 206
Cdd:TIGR00514 197 VYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEF 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 207 IMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLV 286
Cdd:TIGR00514 277 LLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRIT 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 287 HLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGN 366
Cdd:TIGR00514 357 RYLPP-GGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGG 435
|
....*....
gi 647569552 367 VHTDFIPQH 375
Cdd:TIGR00514 436 TNIHYLEKK 444
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
47-375 |
3.76e-127 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 381.40 E-value: 3.76e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 47 STSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDA 126
Cdd:PRK08462 119 SKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 127 MLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEF 206
Cdd:PRK08462 199 MYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEF 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 207 IMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPlSQEEITLQGHAFEARIYAEDPsNNFMPVAGPLV 286
Cdd:PRK08462 279 LLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELP-SQESIKLKGHAIECRITAEDP-KKFYPSPGKIT 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 287 HLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGN 366
Cdd:PRK08462 357 KWIAP-GGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNK 435
|
....*....
gi 647569552 367 VHTDFIPQH 375
Cdd:PRK08462 436 YDTKYLEEH 444
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
38-372 |
8.81e-125 |
|
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: 396.71 E-value: 8.81e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 38 FKWPRP-------LLHsTSKSIMAAAGVPVVEGyHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQ 110
Cdd:TIGR02712 101 FVGPTPeqirkfgLKH-TARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTAGGGGIGMQKCDSAAELAEA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 111 LESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAV 190
Cdd:TIGR02712 179 FETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEETPAPNLPPETRQALLAAAE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 191 RAAKAVNYVGAGTVEFIMDSKHN-FCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQ--EEITLQGHAFEA 267
Cdd:TIGR02712 259 RLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELPDFASlnISLTPRGAAIEA 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 268 RIYAEDPSNNFMPVAGPLVHLSTPRAdpsTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLH 347
Cdd:TIGR02712 339 RVYAENPAKNFQPSPGLLTDVQFPDD---VRVDTWVETGTEVSPEYDPMLAKIIVHGSDREDAILKLHQALAETRVYGIE 415
|
330 340
....*....|....*....|....*
gi 647569552 348 TNIDFLLNLSGHPEFEAGNVHTDFI 372
Cdd:TIGR02712 416 TNLDYLRSILSSETFRSAQVSTRTL 440
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
53-384 |
3.03e-122 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 369.82 E-value: 3.03e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 53 MAAAGVPVVEGYHGEDQS-DQCLKEhARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEK 131
Cdd:PRK07178 122 MIKAGVPVTPGSEGNLADlDEALAE-AERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 132 FVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSK 211
Cdd:PRK07178 201 CIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDAD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 212 HNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTP 291
Cdd:PRK07178 281 GEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAP 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 292 rADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDF 371
Cdd:PRK07178 361 -GGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSF 439
|
330
....*....|...
gi 647569552 372 IPQHHKQLLLSRK 384
Cdd:PRK07178 440 VESHPELTNYSIK 452
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
54-372 |
9.02e-117 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 355.60 E-value: 9.02e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 54 AAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFV 133
Cdd:PRK12833 127 RRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 134 DTPRHVEVQVFGDHHgNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMD-SKH 212
Cdd:PRK12833 207 ARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 213 NFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPR 292
Cdd:PRK12833 286 EFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQ 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 293 AdPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFI 372
Cdd:PRK12833 366 G-PGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
49-380 |
9.22e-115 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 350.65 E-value: 9.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 49 SKSIMAAAGVPVVEGYHG-EDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAM 127
Cdd:PRK08463 118 ARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 128 LIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFI 207
Cdd:PRK08463 198 FMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 208 MDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVH 287
Cdd:PRK08463 278 LDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 288 LsTPRADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNV 367
Cdd:PRK08463 358 Y-YPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYF 436
|
330
....*....|...
gi 647569552 368 HTDFIPQHHKQLL 380
Cdd:PRK08463 437 DTSYIETHMQELL 449
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
49-375 |
3.79e-111 |
|
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: 359.14 E-value: 3.79e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 49 SKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAML 128
Cdd:TIGR01235 119 ARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 129 IEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIM 208
Cdd:TIGR01235 199 VEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 209 DSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPL------SQEEITLQGHAFEARIYAEDPSNNFMPVA 282
Cdd:TIGR01235 279 DNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTpqlgvpNQEDIRTNGYAIQCRVTTEDPANNFQPDT 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 283 GPLVHLSTPRADpSTRIETGVR-QGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPE 361
Cdd:TIGR01235 359 GRIEAYRSAGGF-GIRLDGGNSyAGAIITPYYDSLLVKVSAWASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPK 437
|
330
....*....|....
gi 647569552 362 FEAGNVHTDFIPQH 375
Cdd:TIGR01235 438 FLDGSYDTRFIDTT 451
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
48-252 |
2.33e-90 |
|
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: 278.03 E-value: 2.33e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 48 TSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAM 127
Cdd:pfam02786 4 LFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNPQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 128 LIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFI 207
Cdd:pfam02786 84 LVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 647569552 208 MDSKH-NFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIP 252
Cdd:pfam02786 164 LDPFSgEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
50-255 |
1.14e-60 |
|
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: 202.41 E-value: 1.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 50 KSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLI 129
Cdd:COG0439 59 REALAAAGVPVPGFALVDSPEE--ALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 130 EKFVDTpRHVEVQVFGdHHGNAVYlferdCSVQRRHQK---IIE---EAPAPgIKSEVRKKLGEAAVRAAKAVNYV-GAG 202
Cdd:COG0439 137 EEFLEG-REYSVEGLV-RDGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAF 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 647569552 203 TVEFIMDSKHNFCFMEMNTRLQVEH--PVTEMITGTDLVEWQLRIAAGEKIPLSQ 255
Cdd:COG0439 209 HTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEPRILDP 263
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
266-372 |
1.02e-49 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 167.59 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 266 EARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVG 345
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFP-GGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*..
gi 647569552 346 LHTNIDFLLNLSGHPEFEAGNVHTDFI 372
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
266-374 |
1.12e-49 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 167.67 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 266 EARIYAEDPSNNFMPVAGPLVHLSTPrADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVG 345
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 647569552 346 LHTNIDFLLNLSGHPEFEAGNVHTDFIPQ 374
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
534-597 |
6.86e-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: 6.86e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647569552 534 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 597
Cdd:cd06850 4 APMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
531-597 |
1.33e-23 |
|
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: 94.43 E-value: 1.33e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647569552 531 GPLAPM------TGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 597
Cdd:cd06663 1 TILIPDlaqhlgDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
48-221 |
2.13e-21 |
|
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: 95.17 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 48 TSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfnDDAM 127
Cdd:COG1181 98 LTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DDKV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 128 LIEKFVDtPRHVEVQVFGDHH-----------GNAVYLFErdcsVQRRHQKIIEEAPAPgIKSEVRKKLGEAAVRAAKAV 196
Cdd:COG1181 172 LVEEFID-GREVTVGVLGNGGpralppieivpENGFYDYE----AKYTDGGTEYICPAR-LPEELEERIQELALKAFRAL 245
|
170 180
....*....|....*....|....*
gi 647569552 197 NYVGAGTVEFIMDSKHNFCFMEMNT 221
Cdd:COG1181 246 GCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
515-596 |
2.66e-19 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 84.91 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 515 PVPKYLSSVSSQETQGGP---LAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRH 591
Cdd:PRK05641 67 PTPVAPAAPAPAPASAGEnvvTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTG 146
|
....*
gi 647569552 592 TPLVE 596
Cdd:PRK05641 147 QPLIE 151
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
534-587 |
8.87e-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: 87.83 E-value: 8.87e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 647569552 534 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQ 587
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
515-598 |
1.07e-17 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 86.82 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 515 PVPKYLSSVSSQETQGGPL-APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTP 593
Cdd:PRK09282 507 PLKEIVVGGRPRASAPGAVtSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDV 586
|
....*
gi 647569552 594 LVEFE 598
Cdd:PRK09282 587 LMEIE 591
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
534-587 |
2.23e-17 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 86.35 E-value: 2.23e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 647569552 534 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQ 587
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQ 1134
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
52-221 |
1.42e-16 |
|
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: 78.51 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 52 IMAAAGVPVV-------EGYHgEDQSDQCLKEHARrIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfnD 124
Cdd:pfam07478 1 LLKAAGLPVVpfvtftrADWK-LNPKEWCAQVEEA-LGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 125 DAMLIEKFVDTpRHVEVQVFGDHHGNAVYLFER--DCSVQRRHQKIIEEA-----PApGIKSEVRKKLGEAAVRAAKAVN 197
Cdd:pfam07478 73 EKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALG 150
|
170 180
....*....|....*....|....
gi 647569552 198 YVGAGTVEFIMDSKHNFCFMEMNT 221
Cdd:pfam07478 151 CRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
49-221 |
6.76e-16 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 78.61 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 49 SKSIMAAAGVPVVEGYHGEDQSDQCLKEHarRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARReakksfNDDAML 128
Cdd:PRK01372 102 TKLVWQAAGLPTPPWIVLTREEDLLAAID--KLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFK------YDDEVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 129 IEKFVDTPrhvEVQ--VFGDH--------HGNAVYLFE----RDCSvqrrhQKIIeeaPApGIKSEVRKKLGEAAVRAAK 194
Cdd:PRK01372 174 VEKYIKGR---ELTvaVLGGKalpvieivPAGEFYDYEakylAGGT-----QYIC---PA-GLPAEIEAELQELALKAYR 241
|
170 180
....*....|....*....|....*..
gi 647569552 195 AVNYVGAGTVEFIMDSKHNFCFMEMNT 221
Cdd:PRK01372 242 ALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
534-598 |
4.99e-15 |
|
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: 72.24 E-value: 4.99e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647569552 534 APMTGTI-------EKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 598
Cdd:COG0511 65 SPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
534-597 |
5.18e-15 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 69.94 E-value: 5.18e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647569552 534 APMTGT-----IEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEF 597
Cdd:pfam00364 5 SPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
513-585 |
1.38e-14 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 76.89 E-value: 1.38e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647569552 513 DIPVPKYLSSVSSQETQGGPL-APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREG 585
Cdd:PRK14040 507 PAAAPAAAAAAAPAAAAGEPVtAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEG 580
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
52-252 |
4.79e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 74.19 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 52 IMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRG--------GGGKGMRIVRSEQEFQEQLESARREakksfn 123
Cdd:COG3919 124 LAEELGVPVPKTVVLDSADD--LDALAEDLGFPVVVKPADSvgydelsfPGKKKVFYVDDREELLALLRRIAAA------ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 124 DDAMLIEKFVDTPRHVEVQVFG--DHHGNAVYLFerdcsVQRRHQkiieEAPAPG-----IKSEVRKKLGEAAVRAAKAV 196
Cdd:COG3919 196 GYELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF-----TGRKLR----HYPPAGgnsaaRESVDDPELEEAARRLLEAL 266
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 647569552 197 NYVGAGTVEFIMDSKHN-FCFMEMNTRL--QVEHPVtemITGTDLVEWQLRIAAGEKIP 252
Cdd:COG3919 267 GYHGFANVEFKRDPRDGeYKLIEINPRFwrSLYLAT---AAGVNFPYLLYDDAVGRPLE 322
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
48-221 |
6.77e-14 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 73.23 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 48 TSKSIMAAAGVPVVEGY--HGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREakksfnDD 125
Cdd:PRK01966 126 LTKRLLAAAGIPVAPYVvlTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEY------DR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 126 AMLIEKFVDtPRHVEVqvfgdhhgnAVYLFERDCSV------------------QRRHQKIIeeaPAPgIKSEVRKKLGE 187
Cdd:PRK01966 200 KVLVEQGIK-GREIEC---------AVLGNDPKASVpgeivkpddfydyeakylDGSAELII---PAD-LSEELTEKIRE 265
|
170 180 190
....*....|....*....|....*....|....
gi 647569552 188 AAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNT 221
Cdd:PRK01966 266 LAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
50-206 |
1.57e-12 |
|
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: 69.33 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 50 KSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEQEFQeqlesarrEAKKSFNDDAML 128
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLED--LEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADLE--------AAWAALGGGPCI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 129 IEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHqkIIEE--APApGIKSEVRKKLGEAAVRAAKAVNYVGAGTV 204
Cdd:COG0026 164 LEEFVPFERELSVIVARSPDGEVATypVVE---NVHRNG--ILDEsiAPA-RISEALAAEAEEIAKRIAEALDYVGVLAV 237
|
..
gi 647569552 205 EF 206
Cdd:COG0026 238 EF 239
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
52-251 |
1.76e-11 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 67.30 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 52 IMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESArreakkSFNDDAMLIEK 131
Cdd:PRK12815 677 LLDELGLPHVPGLTATDEEE--AFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAEN------ASQLYPILIDQ 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 132 FVDTpRHVEVQVFGDhhGNAVYL---FErdcsvqrrHqkiIEEA-----------PAPGIKSEVRKKLGEAAVRAAKAVN 197
Cdd:PRK12815 749 FIDG-KEYEVDAISD--GEDVTIpgiIE--------H---IEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLG 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 647569552 198 YVGAGTVEFIMDSKhNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKI 251
Cdd:PRK12815 815 FRGIMNIQFVLAND-EIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSL 867
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
24-338 |
4.00e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 66.02 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 24 PLPPSRATYLWRKSFKwprplLHSTsksiMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRS 103
Cdd:PRK02186 95 PAANTEAIRTCRDKKR-----LART----LRDHGIDVPRTHALALRAV--ALDALDGLTYPVVVKPRMGSGSVGVRLCAS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 104 EQEFQEQLESARREAKKSFnddamLIEKFVDTPRHvEVQVFGDHHGNAVYlferdcSVQRRHQ-------KIIEEAPAPg 176
Cdd:PRK02186 164 VAEAAAHCAALRRAGTRAA-----LVQAYVEGDEY-SVETLTVARGHQVL------GITRKHLgppphfvEIGHDFPAP- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 177 IKSEVRKKLGEAAVRAAKAVNY-VGAGTVEFIMdSKHNFCFMEMNTRLQVEH-PVT-EMITGTDLVEWQLRIAAGE---- 249
Cdd:PRK02186 231 LSAPQRERIVRTVLRALDAVGYaFGPAHTELRV-RGDTVVIIEINPRLAGGMiPVLlEEAFGVDLLDHVIDLHLGVaafa 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 250 ----------KIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPlVHLSTPRADPSTRIETGVRQGDE---VSVHYDPM 316
Cdd:PRK02186 310 dptakrygaiRFVLPARSGVLRGLLFLPDDIAARPELRFHPLKQP-GDALRLEGDFRDRIAAVVCAGDHrdsVAAAAERA 388
|
330 340
....*....|....*....|....*....
gi 647569552 317 IAKLVV-------WAADRQAALTKLRYSL 338
Cdd:PRK02186 389 VAGLSIdigdaarAAALNDAGAGAARPGL 417
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
54-206 |
1.03e-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: 60.73 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 54 AAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEqefqEQLESARREAKksfnDDAMLIEKF 132
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEE--LIEAGQELGYPCVVKARRGGyDGKGQYVVRSE----ADLPQAWEELG----DGPVIVEEF 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647569552 133 VDTPRHVEVQVFGDHHGnAVYLFErdcSVQRRHQK---IIEEAPAPgIKSEVRKKLGEAAVRAAKAVNYVGAGTVEF 206
Cdd:pfam02222 71 VPFDRELSVLVVRSVDG-ETAFYP---VVETIQEDgicRLSVAPAR-VPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
534-598 |
1.51e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 57.10 E-value: 1.51e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647569552 534 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 598
Cdd:PRK08225 6 ASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
534-595 |
1.67e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 59.06 E-value: 1.67e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647569552 534 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLV 595
Cdd:PRK06549 66 SPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
75-251 |
1.88e-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: 64.25 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 75 KEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY- 153
Cdd:TIGR01369 697 VEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPg 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 154 LFErdcsvqrrHqkiIEEA-----------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSkHNFCFMEMNTR 222
Cdd:TIGR01369 773 IME--------H---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPR 840
|
170 180
....*....|....*....|....*....
gi 647569552 223 LQVEHPVTEMITGTDLVEWQLRIAAGEKI 251
Cdd:TIGR01369 841 ASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
50-206 |
4.52e-10 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 61.71 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 50 KSIMAAAGVPVVEgYHG-EDQSDqcLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEQEFQeqlesarrEAKKSFNDDAM 127
Cdd:PRK06019 105 KQFLDKLGIPVAP-FAVvDSAED--LEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLE--------AAWALLGSVPC 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 128 LIEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHQKIIEEAPAPgIKSEVRKKLGEAAVRAAKAVNYVGAGTVE 205
Cdd:PRK06019 174 ILEEFVPFEREVSVIVARGRDGEVVFypLVE---NVHRNGILRTSIAPAR-ISAELQAQAEEIASRIAEELDYVGVLAVE 249
|
.
gi 647569552 206 F 206
Cdd:PRK06019 250 F 250
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
50-210 |
7.04e-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: 61.82 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 50 KSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKA--VRGGggKGMRIVRSEQEFQEQLEsarrEAKKSFNDDAM 127
Cdd:COG0458 119 KELLDKLGIPQPKSGTATSVEE--ALAIAEEIGYPVIVRPsyVLGG--RGMGIVYNEEELEEYLE----RALKVSPDHPV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 128 LIEKFVDTPRHVEVQVFGDHHGNAVYLferdCSVQrrHqkiIEEA-----------PAPGIKSEVRKKLGEAAVRAAKAV 196
Cdd:COG0458 191 LIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARAL 261
|
170
....*....|....
gi 647569552 197 NYVGAGTVEFIMDS 210
Cdd:COG0458 262 GVVGLCNIQFAVDD 275
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
26-220 |
9.27e-10 |
|
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: 59.95 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 26 PPSRATYLWRKSFKW-------PRPLLHSTSK----SIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGGG 94
Cdd:COG0189 66 PPFYGLALLRQLEAAgvpvvndPEAIRRARDKlftlQLLARAGIPVPPTLVTRDPDD--LRAFLEELGGPVVLKPLDGSG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 95 GKGMRIVRSEQEFQEQLesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVF--GdhhGNAVYLFERDcsVQRRHQKIIEEA 172
Cdd:COG0189 144 GRGVFLVEDEDALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVLvvG---GEPVAAIRRI--PAEGEFRTNLAR 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 647569552 173 PAPGIKSEVRKKLGEAAVRAAKAV--NYVGagtVEFIMDsKHNFCFMEMN 220
Cdd:COG0189 214 GGRAEPVELTDEERELALRAAPALglDFAG---VDLIED-DDGPLVLEVN 259
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
512-597 |
1.33e-09 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 54.72 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 512 IDIPVPKYLSSVSSqetqggplapmtGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRH 591
Cdd:cd06849 1 TEIKMPDLGESMTE------------GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVG 68
|
....*.
gi 647569552 592 TPLVEF 597
Cdd:cd06849 69 QVIAVI 74
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
49-240 |
7.18e-08 |
|
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: 54.27 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 49 SKSIMAAAGVPVVEG--YHGEDQSDQCLKEharrIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSfndDA 126
Cdd:TIGR00768 92 SHQLLAKAGIPLPRTglAGSPEEALKLIEE----IGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQLNGPQ---NL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 127 MLIEKFVDTPRHVEVQVF--GDHHGNAVYL-----FERDCSVQRRHQKIieeapapgiksEVRKKLGEAAVRAAKAVNyV 199
Cdd:TIGR00768 165 FLVQEYIKKPGGRDIRVFvvGDEVVAAIYRitsghWRSNLARGGKAEPC-----------SLTEEIEELAIKAAKALG-L 232
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 647569552 200 GAGTVEFIMdSKHNFCFMEMNTRLQVEHpvTEMITGTDLVE 240
Cdd:TIGR00768 233 DVAGVDLLE-SEDGLLVNEVNANPEFKN--SVKTTGVNIAG 270
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
536-608 |
7.26e-08 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 54.80 E-value: 7.26e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647569552 536 MT-GTIEKVFVKAGDKVKAGDSLMVM----IAMKMEhtikSPKDGTVKKVFYREGAQANRHTPLVEFEEEESDKRESE 608
Cdd:PRK11856 14 MTeGEIVEWLVKVGDTVKEGQPLAEVetdkATVEIP----SPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEAAAA 87
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
57-252 |
9.22e-08 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 54.12 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 57 GVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEqefqEQLESARREAKKsfnddaMLIEKFVDTP 136
Cdd:PRK12767 123 GIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDK----EELEFLLEYVPN------LIIQEFIEGQ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 137 RhVEVQVFGDHHGNAVYLFERdcsvqRRHQKIIEEApapgIKSEVRK--KLGEAAVRAAKAVNYVGAGTVEFIMDSKhNF 214
Cdd:PRK12767 193 E-YTVDVLCDLNGEVISIVPR-----KRIEVRAGET----SKGVTVKdpELFKLAERLAEALGARGPLNIQCFVTDG-EP 261
|
170 180 190
....*....|....*....|....*....|....*...
gi 647569552 215 CFMEMNTRLQVEHPVTEMiTGTDLVEWQLRIAAGEKIP 252
Cdd:PRK12767 262 YLFEINPRFGGGYPLSYM-AGANEPDWIIRNLLGGENE 298
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
538-597 |
1.05e-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: 49.29 E-value: 1.05e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647569552 538 GTIEKVFVKAGDKVKAGDSLM-VMIAmK--MEhtIKSPKDGTVKKVFYREGAQANRHTPLVEF 597
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAeVETD-KatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
50-133 |
1.28e-07 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 54.78 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 50 KSIMAAAGVPVVEGY--HGEDQsdqcLKEHARRIGYPVMIKAVRGGGGKGMRI-VRSEqefqEQLESARREAKKSFNDda 126
Cdd:PRK14016 219 KRLLAAAGVPVPEGRvvTSAED----AWEAAEEIGYPVVVKPLDGNHGRGVTVnITTR----EEIEAAYAVASKESSD-- 288
|
....*..
gi 647569552 127 MLIEKFV 133
Cdd:PRK14016 289 VIVERYI 295
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
538-602 |
2.38e-07 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 53.67 E-value: 2.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647569552 538 GTIEKVFVKAGDKVKAGDSLM-VMI--AMkMEhtIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEES 602
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLItVETdkAT-ME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
538-601 |
5.75e-07 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 52.52 E-value: 5.75e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647569552 538 GTIEKVFVKAGDKVKAGDSLM-VMI--AMkMEhtIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEE 601
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVtVETdkAT-ME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
515-594 |
1.02e-06 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 50.61 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 515 PVPKYLSSVSSQETqggPL-APMTGTI-------EKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGA 586
Cdd:PLN02983 185 ASPPPAKAPKSSHP---PLkSPMAGTFyrspapgEPPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGK 261
|
....*...
gi 647569552 587 QANRHTPL 594
Cdd:PLN02983 262 PVSVDTPL 269
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
521-598 |
1.29e-06 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 51.26 E-value: 1.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647569552 521 SSVSSQETQGGPLAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFE 598
Cdd:PRK14042 517 SSVNNKIGPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
78-200 |
2.19e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 50.87 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 78 ARRIGYPVMikaVRGG---GGKGMRIVRSEQEfqeqLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDhhGNAVYL 154
Cdd:PRK05294 700 AEEIGYPVL---VRPSyvlGGRAMEIVYDEEE----LERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GEDVLI 770
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647569552 155 ---FErdcsvqrrHqkiIEEApapGIKS--------------EVRKKLGEAAVRAAKAVNYVG 200
Cdd:PRK05294 771 ggiME--------H---IEEA---GVHSgdsacslppqtlseEIIEEIREYTKKLALELNVVG 819
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
50-223 |
3.66e-05 |
|
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: 46.92 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 50 KSIMAAAGVPVVEGYHGEDQsDQCLkEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKsfndDAMLI 129
Cdd:TIGR01369 132 REAMKEIGEPVPESEIAHSV-EEAL-AAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVLV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 130 EKFVDTPRHVEVQVFGDHHGNAVYLferdCSVQR-----RHQ-KIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGT 203
Cdd:TIGR01369 206 EKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCN 281
|
170 180
....*....|....*....|.
gi 647569552 204 VEFIMDSK-HNFCFMEMNTRL 223
Cdd:TIGR01369 282 VQFALNPDsGRYYVIEVNPRV 302
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
57-238 |
1.11e-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: 43.26 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 57 GVPVVEGYHGEDQSDQCLKEHARRigYPVMIKAVRGGGGKGMRIVRSEQEFqEQLESARREakksfnddAMLIEKFVDTP 136
Cdd:pfam08443 17 GPPNTRLAWYPEDAEQFIEQIKRQ--FPVIVKSIYGSQGIGVFLAEDEQKL-RQTLSATNE--------QILVQEFIAEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 137 --RHVEVQVFGDHHGNAVYLFERDCSVQRRHQKiieeaPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGtVEfIMDSKHNF 214
Cdd:pfam08443 86 nnEDIRCLVVGDQVVGALHRQSNEGDFRSNLHR-----GGVGEKYQLSQEETELAIKAAQAMQLDVAG-VD-LLRQKRGL 158
|
170 180
....*....|....*....|....
gi 647569552 215 CFMEMNTRLQVEhpVTEMITGTDL 238
Cdd:pfam08443 159 LVCEVNSSPGLE--GIEKTLGINI 180
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
538-602 |
6.15e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 42.68 E-value: 6.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647569552 538 GTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEES 602
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
534-585 |
6.55e-04 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 38.64 E-value: 6.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 647569552 534 APMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREG 585
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVG 58
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
78-222 |
7.91e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.46 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 78 ARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKksfnDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYlfer 157
Cdd:PLN02735 733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDP----ERPVLVDKYLSDATEIDVDALADSEGNVVI---- 804
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647569552 158 dCSVQRRhqkiIEEA-----------PAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTR 222
Cdd:PLN02735 805 -GGIMEH----IEQAgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR 875
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
50-202 |
8.87e-04 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 42.35 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 50 KSIMAAAGVPVVEgyHGEDQSDQCLKEHARRIGYPVMIKAVRGG-GGKGMRIVRSEQEfqeqLESArrEAKKSFNDDAML 128
Cdd:PLN02948 126 KVHFSKHGIPLPE--FMEIDDLESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTEED----LSSA--VAALGGFERGLY 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647569552 129 IEKFVDTPRHVEVQVFGDHHGNAV-Y-LFErdcSVQRRHQKIIEEAPAPgIKSEVRKKLGEAAVRAAKAVNyvGAG 202
Cdd:PLN02948 198 AEKWAPFVKELAVMVARSRDGSTRcYpVVE---TIHKDNICHVVEAPAN-VPWKVAKLATDVAEKAVGSLE--GAG 267
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
81-154 |
1.25e-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: 39.96 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 81 IGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARRE--------AKKSFNDDAMLIEKFVDTPrHVEVQVFGDHHGNAV 152
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEieqwkemyPEAVVDGGSFLVEEYIEGE-EFAVDAYFDENGEPV 79
|
..
gi 647569552 153 YL 154
Cdd:pfam13535 80 IL 81
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
74-134 |
1.27e-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: 41.65 E-value: 1.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647569552 74 LKEHARRIGYPVMIKAVRGGGGKGMRIVRSEqefqEQLESARREAKKS--FNDDAMLIEKFVD 134
Cdd:COG0027 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----ADIEAAWEYAQEGgrGGAGRVIVEGFVD 199
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
534-560 |
1.70e-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: 1.70e-03
10 20
....*....|....*....|....*..
gi 647569552 534 APMTGTIEKVFVKAGDKVKAGDSLMVM 560
Cdd:COG1038 1118 APRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
533-560 |
2.26e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 41.28 E-value: 2.26e-03
10 20
....*....|....*....|....*...
gi 647569552 533 LAPMTGTIEKVFVKAGDKVKAGDSLMVM 560
Cdd:PRK12999 1117 TAPVDGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
49-134 |
3.49e-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: 40.00 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647569552 49 SKSIMAAAGVPVVEGYHGEDQSDqcLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEfqeqlesARREAKKSFNDDAM- 127
Cdd:COG0151 106 AKEFMARYGIPTAAYRVFTDLEE--ALAYLEEQGAPIVVKADGLAAGKGVVVAETLEE-------ALAAVDDMLADGKFg 176
|
90
....*....|...
gi 647569552 128 ------LIEKFVD 134
Cdd:COG0151 177 dagarvVIEEFLE 189
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
74-120 |
4.15e-03 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 39.74 E-value: 4.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 647569552 74 LKEHARRIGYPVMIKAVRGGGGKGMRIVRSEqefqEQLESARREAKK 120
Cdd:PRK09288 141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----EDIEKAWEYAQE 183
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
534-560 |
6.34e-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: 39.16 E-value: 6.34e-03
10 20
....*....|....*....|....*..
gi 647569552 534 APMTGTIEKVFVKAGDKVKAGDSLMVM 560
Cdd:COG0845 28 ARVSGRVEEVLVDEGDRVKKGQVLARL 54
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
534-560 |
9.21e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 38.49 E-value: 9.21e-03
10 20
....*....|....*....|....*..
gi 647569552 534 APMTGTIEKVFVKAGDKVKAGDSLMVM 560
Cdd:COG1566 50 AKVSGRVTEVLVKEGDRVKKGQVLARL 76
|
|
| |
