|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-451 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 802.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 1 MFSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAKAVDSYLNVQEVLSAAIVTKAEAIHP 80
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 81 GFGFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLKAA 160
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 161 AGGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVLE 240
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 241 ESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEP 320
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 321 LNVRQEEVVFQGHAIECRINAENPAFHFAPSPGKIQNLLLPaGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFEA 400
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPP-GGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 488239160 401 LMKMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLQEEFLPNWT 451
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEE 450
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-455 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 779.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 1 MFSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAKAVDSYLNVQEVLSAAIVTKAEAIHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 81 GFGFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLkaa 160
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIkas 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 161 aggggkgIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVLE 240
Cdd:COG4770 161 aggggkgMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 241 ESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEP 320
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 321 LNVRQEEVVFQGHAIECRINAENPAFHFAPSPGKIQNLLLPaGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFEA 400
Cdd:COG4770 321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPP-GGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 488239160 401 LMKMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLQEEFLPNWTPETE 455
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAP 454
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-446 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 704.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 1 MFSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAKAVDSYLNVQEVLSAAIVTKAEAIHP 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 81 GFGFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLKAA 160
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 161 AGGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVLE 240
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 241 ESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEP 320
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 321 LNVRQEEVVFQGHAIECRINAENPAFHFAPSPGKIQNLLLPaGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFEA 400
Cdd:PRK05586 321 LSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIP-GGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 488239160 401 LMKMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLQEEF 446
Cdd:PRK05586 400 IQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKL 445
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-443 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 644.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 1 MFSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAKAVDSYLNVQEVLSAAIVTKAEAIHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 81 GFGFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLKAA 160
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 161 AGGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVLE 240
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 241 ESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEP 320
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 321 LNVRQEEVVFQGHAIECRINAENPAfHFAPSPGKIQNLLLPaGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFEA 400
Cdd:PRK06111 321 LSFTQDDIKRSGHAIEVRIYAEDPK-TFFPSPGKITDLTLP-GGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 488239160 401 LMKMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLQ 443
Cdd:PRK06111 399 ISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLT 441
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 639.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 1 MFSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAKAVDSYLNVQEVLSAAIVTKAEAIHP 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 81 GFGFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLKAA 160
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 161 AGGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVLE 240
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 241 ESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDeEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEP 320
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 321 LNVRQEEVVFQGHAIECRINAENPAFHFAPSPGKIQNLLLPaGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFEA 400
Cdd:PRK08654 320 LSFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSP-GGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 488239160 401 LMKMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLQEE 445
Cdd:PRK08654 399 IARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEE 443
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-444 |
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: 622.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 1 MFSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAKAVDSYLNVQEVLSAAIVTKAEAIHP 80
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 81 GFGFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLKAA 160
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 161 AGGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVLE 240
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 241 ESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEP 320
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 321 LNVRQEEVVFQGHAIECRINAENPAFHFAPSPGKIqNLLLPAGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFEA 400
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRI-TRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 488239160 401 LMKMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLQE 444
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-453 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 594.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 1 MFSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAKA-VDSYLNVQEVLSAAIVTKAEAIH 79
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHpVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 80 PGFGFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLKA 159
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 160 AAGGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVL 239
Cdd:PRK12999 164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 240 EESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGE 319
Cdd:PRK12999 244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 320 PLN------VRQEEVVFQGHAIECRINAENPAFHFAPSPGKIQNLLLPaGGMGLRVDS-AVYPGYTIPPYYDSMIAKIIV 392
Cdd:PRK12999 324 TLHdleigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSP-GGFGVRLDGgNAFAGAEITPYYDSLLVKLTA 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488239160 393 HGNTRFEALMKMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLQEeflpnwTPE 453
Cdd:PRK12999 403 WGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE------TPE 457
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-453 |
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: 588.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 1 MFSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAK-AVDSYLNVQEVLSAAIVTKAEAIH 79
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKgPVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 80 PGFGFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLKA 159
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 160 AAGGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVL 239
Cdd:COG1038 163 AAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 240 EESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGE 319
Cdd:COG1038 243 EIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 320 PLN------VRQEEVVFQGHAIECRINAENPAFHFAPSPGKIQ---NlllpAGGMGLRVDSA-VYPGYTIPPYYDSMIAK 389
Cdd:COG1038 323 SLDdpeigiPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITayrS----AGGFGIRLDGGnAYTGAVITPYYDSLLVK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239160 390 IIVHGNTRFEALMKMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLQEeflpnwTPE 453
Cdd:COG1038 399 VTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDE------TPE 456
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
4-451 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 553.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 4 KVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAKAVDSYLNVQEVLSAAIVTKAEAIHPGFG 83
Cdd:PRK12833 7 KVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGYG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 84 FLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLKAAAGG 163
Cdd:PRK12833 87 FLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 164 GGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHfGNVIHLGERDCSLQRNNQKVLEESP 243
Cdd:PRK12833 167 GGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDG-ERVVHLFERECSLQRRRQKILEEAP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 244 SVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEE-GDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEPLN 322
Cdd:PRK12833 246 SPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDArGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 323 VRQEEVVFQGHAIECRINAENPAFHFAPSPGKIQNLLLPaGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFEALM 402
Cdd:PRK12833 326 FAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWP-QGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALA 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 488239160 403 KMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLqEEFLPNWT 451
Cdd:PRK12833 405 RAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL-EAWLAEWR 452
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-451 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 552.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 1 MFSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPaKAVDSYLNVQEVLSAAIVTKAEAIHP 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGA-DPLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 81 GFGFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLKAA 160
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 161 AGGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVLE 240
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 241 ESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEP 320
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 321 LNVRQEEVVFQGHAIECRINAENPAFHFAPSPGKIQNLLLPaGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFEA 400
Cdd:PRK07178 320 LSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAP-GGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 488239160 401 LMKMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLQEEflPNWT 451
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESH--PELT 447
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-446 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 530.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 3 SKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAKAVDSYLNVQEVLSAAIVTKAEAIHPGF 82
Cdd:PRK08462 5 KRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 83 GFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLKAAAG 162
Cdd:PRK08462 85 GFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 163 GGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVLEES 242
Cdd:PRK08462 165 GGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 243 PSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEPLn 322
Cdd:PRK08462 245 PAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 323 VRQEEVVFQGHAIECRINAENPAfHFAPSPGKIQNLLLPaGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFEALM 402
Cdd:PRK08462 324 PSQESIKLKGHAIECRITAEDPK-KFYPSPGKITKWIAP-GGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 488239160 403 KMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLQEEF 446
Cdd:PRK08462 402 KMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEHF 445
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
2-442 |
3.88e-177 |
|
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: 528.06 E-value: 3.88e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 2 FSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAKAVDSYLNVQEVLSAAIVTKAEAIHPG 81
Cdd:TIGR02712 1 FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 82 FGFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGsTGVLSTVEEALEIADRIGYPVMLKAAA 161
Cdd:TIGR02712 81 YGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 162 GGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVLEE 241
Cdd:TIGR02712 160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 242 SPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEE-GDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEP 320
Cdd:TIGR02712 240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEArDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 321 LNVRQ--EEVVFQGHAIECRINAENPAFHFAPSPGKIQNLLLPAggmGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRF 398
Cdd:TIGR02712 320 PDFASlnISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPD---DVRVDTWVETGTEVSPEYDPMLAKIIVHGSDRE 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 488239160 399 EALMKMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFL 442
Cdd:TIGR02712 397 DAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTL 440
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-449 |
6.90e-169 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 483.55 E-value: 6.90e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 1 MFSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGpAKAVDSYLNVQEVLSAAIVTKAEAIHP 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIG-TDPIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 81 GFGFLSENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGVLS-TVEEALEIADRIGYPVMLKA 159
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSeSMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 160 AAGGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVL 239
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 240 EESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGE 319
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 320 PLNVRQEEVVFQGHAIECRINAENPAFHFAPSPGKIQNlLLPAGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFE 399
Cdd:PRK08463 320 ILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITE-YYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 488239160 400 ALMKMQRALSEFITEGIITNAEFQMDLISHPAVIAGDYSTAFLQ---EEFLPN 449
Cdd:PRK08463 399 AVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIEthmQELLEK 451
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
116-322 |
3.11e-73 |
|
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: 229.50 E-value: 3.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 116 KINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPVMLKAAAGGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGND 195
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 196 DMYLEKIIYPARHIEVQILGDHFGNVIHLGERDCSLQRNNQKVLEESPSVVISQSKREALGDAAVRAAKAVNYENAGTIE 275
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488239160 276 FLMD-EEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEPLN 322
Cdd:pfam02786 162 FALDpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-109 |
3.24e-61 |
|
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: 194.63 E-value: 3.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 2 FSKVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAICIGPAKAVDSYLNVQEVLSAAIVTKAEAIHPG 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 488239160 82 FGFLSENSRFASMCEECNITFIGPKSAT 109
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
62-320 |
4.32e-56 |
|
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: 187.00 E-value: 4.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 62 NVQEVLSA-AIVTKAEAIHpgfGFLSEN----SRFASMCEECNITfiGPKSATIDAMGNKINARQLMQEANVPViPGSTg 136
Cdd:COG0439 1 DIDAIIAAaAELARETGID---AVLSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 137 VLSTVEEALEIADRIGYPVMLKAAAGGGGKGIRKVQSKEELPQHFSSAQQEAAAAFGNDDMYLEKIIyPARHIEVQILGD 216
Cdd:COG0439 74 LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFL-EGREYSVEGLVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 217 HfGNVIHlgerdCSLQRNNQK---VLE---ESPSvVISQSKREALGDAAVRAAKAVNYEN-AGTIEFLMDEEGDFYFMEM 289
Cdd:COG0439 153 D-GEVVV-----CSITRKHQKppyFVElghEAPS-PLPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYLIEI 225
|
250 260 270
....*....|....*....|....*....|...
gi 488239160 290 NTRIQVEH--PVTEMVTGIDLVKKQVEIAAGEP 320
Cdd:COG0439 226 NARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-444 |
6.16e-54 |
|
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: 175.76 E-value: 6.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 336 ECRINAENPAFHFAPSPGKIQNLLLPaGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFEALMKMQRALSEFITEG 415
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 488239160 416 IITNAEFQMDLISHPAVIAGDYSTAFLQE 444
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-442 |
1.02e-53 |
|
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: 175.29 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 336 ECRINAENPAFHFAPSPGKIQNLLLPaGGMGLRVDSAVYPGYTIPPYYDSMIAKIIVHGNTRFEALMKMQRALSEFITEG 415
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFP-GGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*..
gi 488239160 416 IITNAEFQMDLISHPAVIAGDYSTAFL 442
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
4-321 |
2.53e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 64.95 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 4 KVLIANRGEIAVRIIRACRELGIQTVAIYSEADAEALHTQLADEAIcigpakAVDSYLNVQEVLSAAIVTKAEAIHPGF- 82
Cdd:COG3919 7 RVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVV------VVPDPGDDPEAFVDALLELAERHGPDVl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 83 --------GFLSEN-SRFASmceecNITFIGPKSATIDAMGNKINARQLMQEANVPViPGsTGVLSTVEEALEIADRIGY 153
Cdd:COG3919 81 iptgdeyvELLSRHrDELEE-----HYRLPYPDADLLDRLLDKERFYELAEELGVPV-PK-TVVLDSADDLDALAEDLGF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 154 PVML--------KAAAGGGGKGIRKVQSKEELpqhfsSAQQEAAAAFGNDDMYLEKIIYPARHIE-VQILGDHFGNVIHL 224
Cdd:COG3919 154 PVVVkpadsvgyDELSFPGKKKVFYVDDREEL-----LALLRRIAAAGYELIVQEYIPGDDGEMRgLTAYVDRDGEVVAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 225 GERdcslqrnnQKVLEESP----SVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEE-GDFYFMEMNTRIQVEHPv 299
Cdd:COG3919 229 FTG--------RKLRHYPPaggnSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRdGEYKLIEINPRFWRSLY- 299
|
330 340
....*....|....*....|....
gi 488239160 300 teMVT--GIDLVKKQVEIAAGEPL 321
Cdd:COG3919 300 --LATaaGVNFPYLLYDDAVGRPL 321
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
96-322 |
7.47e-11 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 64.61 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 96 EECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTGvlSTVEEALEIADRIGYPVMLKAAAGGGGKGIRKVQSKE 175
Cdd:PRK12815 651 EEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTA--TDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEP 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 176 ELPQHFSSAQqeaaaafGNDDMYLEKIIYPARHIEVQILGD-----------HFGNV-IHLGERDCSLqrnnqkvleesP 243
Cdd:PRK12815 729 ALEAYLAENA-------SQLYPILIDQFIDGKEYEVDAISDgedvtipgiieHIEQAgVHSGDSIAVL-----------P 790
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239160 244 SVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDeEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEPLN 322
Cdd:PRK12815 791 PQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLA-NDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLA 868
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
96-321 |
1.59e-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: 63.48 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 96 EECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGSTgvLSTVEEALEIADRIGYPVMLKAAAGGGGKGIRKVQSKE 175
Cdd:TIGR01369 650 EEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKT--ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 176 ELPQHFSSAQQEAAAAFGNDDMYLEKiiypARHIEVQILGDHfGNV-------------IHLGERDCSLqrnnqkvlees 242
Cdd:TIGR01369 728 ELRRYLEEAVAVSPEHPVLIDKYLED----AVEVDVDAVSDG-EEVlipgimehieeagVHSGDSTCVL----------- 791
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239160 243 PSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDeEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEPL 321
Cdd:TIGR01369 792 PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
18-321 |
5.04e-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: 55.39 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 18 IRACRELGIQTVAIYSEadaeaLHTQLADEAIcigpAKAVdsYLnvqEVLSAAIVTK------AEAIHPGFGF------- 84
Cdd:TIGR01369 33 CKALKEEGYRVILVNSN-----PATIMTDPEM----ADKV--YI---EPLTPEAVEKiiekerPDAILPTFGGqtalnla 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 85 --LSEnsrfASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGstGVLSTVEEALEIADRIGYPVMlkaaag 162
Cdd:TIGR01369 99 veLEE----SGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIAHSVEEALAAAKEIGYPVI------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 163 gggkgIRK-----------VQSKEElpqhFSSAQQEAAAAFGNDDMYLEKIIYPARHIEVQILGDHFGNVI--------- 222
Cdd:TIGR01369 167 -----VRPaftlggtgggiAYNREE----LKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCItvcnmenfd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 223 ----HLGERdcslqrnnqkvLEESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMD-EEGDFYFMEMNTRIQVEH 297
Cdd:TIGR01369 238 pmgvHTGDS-----------IVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNpDSGRYYVIEVNPRVSRSS 306
|
330 340
....*....|....*....|....
gi 488239160 298 PVTEMVTGIDLVKKQVEIAAGEPL 321
Cdd:TIGR01369 307 ALASKATGYPIAKVAAKLAVGYTL 330
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
122-291 |
9.51e-08 |
|
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: 52.32 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 122 LMQEANVPVIP-----GSTGVLSTVEEALEIADRIGYPVMLKAAAGGGGKGIRKVQSKEELPQHFSSAQqeaaaafgndd 196
Cdd:pfam07478 1 LLKAAGLPVVPfvtftRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAF----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 197 MYLEKIIYP----ARHIEVQILGDHFGNVIHLGER--DCSLQRNNQKVLEESPSVVI----SQSKREALGDAAVRAAKAV 266
Cdd:pfam07478 70 QYDEKVLVEegieGREIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSAQIVVpadlEEEQEEQIQELALKAYKAL 149
|
170 180
....*....|....*....|....*
gi 488239160 267 NYENAGTIEFLMDEEGDFYFMEMNT 291
Cdd:pfam07478 150 GCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
96-156 |
6.05e-07 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 52.02 E-value: 6.05e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488239160 96 EECNITFIGPKSATIDAMGNKINARQLMQEANVPVIPGstGVLSTVEEALEIADRIGYPVM 156
Cdd:PRK05294 109 EKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVI 167
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
77-291 |
6.43e-07 |
|
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: 50.88 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 77 AIHpgfGFLSENSRFASMCEECNITFIGPKSATIdAMG-NKINARQLMQEANVPVIPGSTGVLSTVEEALEIADRIGYPV 155
Cdd:COG1181 60 ALH---GRGGEDGTIQGLLELLGIPYTGSGVLAS-ALAmDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 156 MLkaaaggggkgIRKVQSKEELPQHFssaqqeaAAAFGNDDMYL-EKIIyPARHIEVQILGDHFGNVIHLGERD-----C 229
Cdd:COG1181 136 FVkparegssvgVSKVKNAEELAAAL-------EEAFKYDDKVLvEEFI-DGREVTVGVLGNGGPRALPPIEIVpengfY 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239160 230 SLQ--RNNQKVLEESPSvVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNT 291
Cdd:COG1181 208 DYEakYTDGGTEYICPA-RLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
15-156 |
1.48e-06 |
|
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: 50.65 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 15 VRIIRACRELGIQTVAI----------YSEADAealhtqladeaICIGPakavdsyLNVQEVLSAAIVTKAEAIHPGFG- 83
Cdd:COG0458 19 VQACKALREEGYEVILVnsnpetvstdYDTADR-----------LYFEP-------LTVEDVLDIIEKEKPDGVIVQFGg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 84 --------FLSENSRFAsmceecNITFIGPKSATIDamgnKINAR----QLMQEANVPVIPGstGVLSTVEEALEIADRI 151
Cdd:COG0458 81 qtalnlavELEEAGILE------GVKILGTSPDAID----LAEDRelfkELLDKLGIPQPKS--GTATSVEEALAIAEEI 148
|
....*
gi 488239160 152 GYPVM 156
Cdd:COG0458 149 GYPVI 153
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
99-322 |
1.53e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 50.93 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 99 NITFIGPKSATIDAMGNKINARQLMQEANVPVIPGstGVLSTVEEALEIADRIGYPVMLKAAAGGGGKGIRKVQSKEELP 178
Cdd:PLN02735 686 NVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 179 QHFSSAQQEAAAAFGNDDMYLEKiiypARHIEVQILGDHFGNV-------------IHLGERDCSLqrnnqkvleesPSV 245
Cdd:PLN02735 764 TYLETAVEVDPERPVLVDKYLSD----ATEIDVDALADSEGNVviggimehieqagVHSGDSACSL-----------PTQ 828
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239160 246 VISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEHPVTEMVTGIDLVKKQVEIAAGEPLN 322
Cdd:PLN02735 829 TIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSLK 905
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
112-291 |
6.65e-06 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 47.80 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 112 AMgNKINARQLMQEANVPVIPGStgVLSTVEEALEIADRIGYPVMLKAAAGGGGKGIRKVQSKEELPQHFssaqqeaAAA 191
Cdd:PRK01372 96 AM-DKLRTKLVWQAAGLPTPPWI--VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAAL-------ELA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 192 FGNDDMYL-EKIIyPARHIEVQILGDHFGNVIHLgerdCSLQRN---NQKVLEES-----PSvVISQSKREALGDAAVRA 262
Cdd:PRK01372 166 FKYDDEVLvEKYI-KGRELTVAVLGGKALPVIEI----VPAGEFydyEAKYLAGGtqyicPA-GLPAEIEAELQELALKA 239
|
170 180
....*....|....*....|....*....
gi 488239160 263 AKAVNYENAGTIEFLMDEEGDFYFMEMNT 291
Cdd:PRK01372 240 YRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
119-155 |
1.09e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 44.73 E-value: 1.09e-04
10 20 30
....*....|....*....|....*....|....*..
gi 488239160 119 ARQLMQEANVPVIPgsTGVLSTVEEALEIADRIGYPV 155
Cdd:COG1042 493 AKALLAAYGIPVVP--TRLARSAEEAVAAAEEIGYPV 527
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
121-156 |
4.32e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 42.78 E-value: 4.32e-04
10 20 30
....*....|....*....|....*....|....*.
gi 488239160 121 QLMQEANVPVIPGstGVLSTVEEALEIADRIGYPVM 156
Cdd:PRK05294 675 KLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVL 708
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
119-157 |
7.01e-04 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 40.92 E-value: 7.01e-04
10 20 30
....*....|....*....|....*....|....*....
gi 488239160 119 ARQLMQEANVPVIPgsTGVLSTVEEALEIADRIGYPVML 157
Cdd:pfam13549 15 AKALLAAYGIPVVP--TRLARSPEEAVAAAEEIGYPVVL 51
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
16-311 |
7.02e-04 |
|
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: 41.46 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 16 RIIRACRELGIQTVAIyseadaealhtQLADEAICIGPAKAVDSYLNVQEVlsAAIVTKAEAIHPGFGFLSensrfasMC 95
Cdd:COG0189 18 ALIEAAQRRGHEVEVI-----------DPDDLTLDLGRAPELYRGEDLSEF--DAVLPRIDPPFYGLALLR-------QL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 96 EECNITFIGPkSATIDAMGNKINARQLMQEANVPVIPgsTGVLSTVEEALEIADRIGYPVMLKAAAGGGGKGIRKVQSKE 175
Cdd:COG0189 78 EAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPVPP--TLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 176 ELPQHFSSAQQEaaaafGNDDMYLEKIIY--PARHIEVQILGdhfGNVIHLGERDCSLQ--RNNQKVLEESPSVVISqsk 251
Cdd:COG0189 155 ALESILEALTEL-----GSEPVLVQEFIPeeDGRDIRVLVVG---GEPVAAIRRIPAEGefRTNLARGGRAEPVELT--- 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 252 rEALGDAAVRAAKAVNYENAGtIEFLMDEEGdFYFMEMNTRIQVEHpvTEMVTGIDLVKK 311
Cdd:COG0189 224 -DEERELALRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVTPGFRG--LERATGVDIAEA 278
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
96-157 |
8.62e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 41.88 E-value: 8.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239160 96 EECNITFIGPKSATIDaMGNKINA-RQLMQEANVPVipGSTGVLSTVEEALEIADRIGYPVML 157
Cdd:PRK12815 109 EQYGVELLGTNIEAIQ-KGEDRERfRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIV 168
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
78-290 |
1.11e-03 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 41.34 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 78 IHPGFGflsENSRFASMCEECNITFIGPkSATIDAMG-NKINARQLMQEANVPVIPGSTGVLSTVEEALE-----IADRI 151
Cdd:PRK14573 534 LHGPFG---EDGTMQGFLEIIGKPYTGP-SLAFSAIAmDKVLTKRFASDVGVPVVPYQPLTLAGWKREPElclahIVEAF 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 152 GYPVMLKAAAGGGGKGIRKVQSKEELPQHFSSAQQEaaaafgNDDMYLEKIIYPARHIEVQILGDHFGN--VIHLGERdC 229
Cdd:PRK14573 610 SFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLY------DTDVFVEESRLGSREIEVSCLGDGSSAyvIAGPHER-R 682
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488239160 230 SLQR----------NNQKVLEESPSVVISQSKREALGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMN 290
Cdd:PRK14573 683 GSGGfidyqekyglSGKSSAQIVFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMN 753
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
115-157 |
1.48e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 40.91 E-value: 1.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488239160 115 NKINARQLMQEANVPVIPGstGVLSTVEEALEIADRIGYPVML 157
Cdd:PRK14016 214 DKELTKRLLAAAGVPVPEG--RVVTSAEDAWEAAEEIGYPVVV 254
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
87-316 |
8.22e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 38.12 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 87 ENSRFASMCEECNITFIGPKSATIDAMGNKINARQLMQEANVPvipgsTGVLSTVEEALEIADRIGYPVMLKAAAGGGGK 166
Cdd:PRK14569 70 ENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMP-----TPMAKFLTDKLVAEDEISFPVAVKPSSGGSSI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 167 GIRKVQSKEELPQHFSSAQQeaaaafgNDDMYLEKIIyPARHIEVQILGDHFGNVI---HLGERDCSLQRNNQKVLEESP 243
Cdd:PRK14569 145 ATFKVKSIQELKHAYEEASK-------YGEVMIEQWV-TGKEITVAIVNDEVYSSVwiePQNEFYDYESKYSGKSIYHSP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239160 244 SVVISQSKREaLGDAAVRAAKAVNYENAGTIEFLMDEEGDFYFMEMNTRIQVEH----PVTEMVTGID---LVKKQVEIA 316
Cdd:PRK14569 217 SGLCEQKELE-VRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEINSSPGMTDnslsPKSAAAEGVDfdsFVKRIIEQA 295
|
|
| |
