|
Name |
Accession |
Description |
Interval |
E-value |
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
1-376 |
0e+00 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 547.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 1 MKLHEYQAKEVFADAGIPTPESALATSVDEAVEVADALD-YPVAVKAQVHVGGRGKAGGIKLAENTAEAREAAESILGMD 79
Cdd:PRK00696 1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGgGVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 80 L-------KGYTVDRVLVEEAVDFTNELYVGVTMDRSEGAPVVMVSERGGVDIESVAEEAPEDIVREHVDPSFGLQAYQA 152
Cdd:PRK00696 81 LvthqtgpKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 153 RNAVYDAGIEQDVAGDVAKIVQGVYDLWADSDATEVEINPVMVTSERDVVAADAVMKLDEDALFRQPAFADMEEDAAEDD 232
Cdd:PRK00696 161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 233 LEAKANEYGFDYVRLDGNTGIIGNGAGLVMTTLDLVDYYGGQPANFLDIGGGAKADRVANALDMVFSDENVDSVVFNIFG 312
Cdd:PRK00696 241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501246331 313 GITRGDEVAKGINSALEQFDeIPTPVVVRLAGTNAAEGREILNDD--LVTVEETLEGAVQRAVEYA 376
Cdd:PRK00696 321 GITRCDVIAEGIIAAVKEVG-VTVPLVVRLEGTNVELGKKILAESglNIIAADTLDDAAQKAVEAA 385
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
1-379 |
0e+00 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 545.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 1 MKLHEYQAKEVFADAGIPTPESALATSVDEAVEVADALDY-PVAVKAQVHVGGRGKAGGIKLAENTAEAREAAESILGMD 79
Cdd:COG0045 1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGpPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 80 L-------KGYTVDRVLVEEAVDFTNELYVGVTMDRSEGAPVVMVSERGGVDIESVAEEAPEDIVREHVDPSFGLQAYQA 152
Cdd:COG0045 81 LvthqtgpKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 153 RNAVYDAGIEQDVAGDVAKIVQGVYDLWADSDATEVEINPVMVTSERDVVAADAVMKLDEDALFRQPAFADMEEDAAEDD 232
Cdd:COG0045 161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 233 LEAKANEYGFDYVRLDGNTGIIGNGAGLVMTTLDLVDYYGGQPANFLDIGGGAKADRVANALDMVFSDENVDSVVFNIFG 312
Cdd:COG0045 241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501246331 313 GITRGDEVAKGINSALEQFDeIPTPVVVRLAGTNAAEGREILNDD--LVTVEETLEGAVQRAVEYADEE 379
Cdd:COG0045 321 GITRCDVVAEGIVAALKEVG-LKVPVVVRLEGTNVEEGRKILAESglNIIAADTLEEAAKKAVELAKGA 388
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
1-376 |
1.42e-149 |
|
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]
Pssm-ID: 273396 [Multi-domain] Cd Length: 386 Bit Score: 427.95 E-value: 1.42e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 1 MKLHEYQAKEVFADAGIPTPESALATSVDEAVEVADALDY-PVAVKAQVHVGGRGKAGGIKLAENTAEAREAAESILGMD 79
Cdd:TIGR01016 1 MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAgPVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 80 LK-------GYTVDRVLVEEAVDFTNELYVGVTMDRSEGAPVVMVSERGGVDIESVAEEAPEDIVREHVDPSFGLQAYQA 152
Cdd:TIGR01016 81 LVtnqtdplGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 153 RNAVYDAGIEQDVAGDVAKIVQGVYDLWADSDATEVEINPVMVTSERDVVAADAVMKLDEDALFRQPAFADMEEDAAEDD 232
Cdd:TIGR01016 161 REIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDYSQEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 233 LEAKANEYGFDYVRLDGNTGIIGNGAGLVMTTLDLVDYYGGQPANFLDIGGGAKADRVANALDMVFSDENVDSVVFNIFG 312
Cdd:TIGR01016 241 REVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501246331 313 GITRGDEVAKGINSALEQFDeIPTPVVVRLAGTNAAEGREILNDDLVTV--EETLEGAVQRAVEYA 376
Cdd:TIGR01016 321 GITRCDLVAKGLVEALKEVG-VNVPVVVRLEGTNVEEGKKILAESGLNIifATSMEEAAEKAVEAA 385
|
|
| PRK14046 |
PRK14046 |
malate--CoA ligase subunit beta; Provisional |
1-374 |
4.56e-127 |
|
malate--CoA ligase subunit beta; Provisional
Pssm-ID: 237594 [Multi-domain] Cd Length: 392 Bit Score: 370.97 E-value: 4.56e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 1 MKLHEYQAKEVFADAGIPTPESALATSVDEAVEVADALDYPV-AVKAQVHVGGRGKAGGIKLAENTAEAREAAESILGMD 79
Cdd:PRK14046 1 MDIHEYQAKELLASFGVAVPRGALAYSPEQAVYRARELGGWHwVVKAQIHSGARGKAGGIKLCRTYNEVRDAAEDLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 80 L-------KGYTVDRVLVEEAVDFTNELYVGVTMDRSEGAPVVMVSERGGVDIESVAEEAPEDIVREHVDPSFGLQAYQA 152
Cdd:PRK14046 81 LvthqtgpEGKPVQRVYVETADPIERELYLGFVLDRKSERVRVIASARGGMEIEEIAAKEPEAIIQVVVEPAVGLQQFQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 153 RNAVYDAGIEQDVAGDVAKIVQGVYDLWADSDATEVEINPVMVTSERDVVAADAVMKLDEDALFRQPAFADMEEDAAEDD 232
Cdd:PRK14046 161 REIAFGLGLDIKQVSRAVKTIMGCYRAFRDLDATMLEINPLVVTKDDRVLALDAKMSFDDNALFRRPNIAEMRDPSQEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 233 LEAKANEYGFDYVRLDGNTGIIGNGAGLVMTTLDLVDYYGGQPANFLDIGGGAKADRVANALDMVFSDENVDSVVFNIFG 312
Cdd:PRK14046 241 REAQAAEHGLSYVGLDGDIGCIVNGAGLAMATMDMIKLAGGEPANFLDVGGGASPERVAKAFRLVLSDRNVKAILVNIFA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501246331 313 GITRGDEVAKGINSALEQFDeIPTPVVVRLAGTNAAEGREILNDD--LVTVEETLEGAVQRAVE 374
Cdd:PRK14046 321 GINRCDWVAEGVVQAAREVG-IDVPLVVRLAGTNVEEGRKILAESglPIITADTLAEAAEKAVE 383
|
|
| PLN00124 |
PLN00124 |
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional |
3-373 |
1.33e-85 |
|
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional
Pssm-ID: 177736 [Multi-domain] Cd Length: 422 Bit Score: 265.84 E-value: 1.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 3 LHEYQAKEVFADAGIPTPESALATSVDEAVEVADAL---DYPVAVKAQVHVGGRGKA-------GGIKLAEnTAEAREAA 72
Cdd:PLN00124 30 IHEYQGAELMSKYGVNVPKGAAASSLDEVKKALEKMfpdEGEVVVKSQILAGGRGLGtfknglkGGVHIVK-KDKAEELA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 73 ESILGMDL-------KGYTVDRVLVEEAVDFTNELYVGVTMDRSEGAPVVMVSERGGVDIESVAEEAPEDIVREHVDPSF 145
Cdd:PLN00124 109 GKMLGQILvtkqtgpAGKPVNKVYLCEKMSLVNEMYFAILLDRASAGPLIIACSKGGTSIEDLAEKFPEKIIKVPIDIFK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 146 GLQAYQARNAVydAGIEQDVAG--DVAKIVQGVYDLWADSDATEVEINPVMVTSERDVVAADAVMKLDEDALFRQPAFAD 223
Cdd:PLN00124 189 GITDEDAAKVV--DGLAPKVADrnDAIEQVKKLYKLFCKCDCTMVEINPLAETADGQLVAADAKLNFDDNAAFRQKEIFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 224 MEEDAAEDDLEAKANEYGFDYVRLDGNTGIIGNGAGLVMTTLDLVDYYGGQPANFLDIGGGAKADRVANALDMVFSDENV 303
Cdd:PLN00124 267 LRDTSQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGSPANFLDVGGNASEQQVVEAFKILTSDDKV 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501246331 304 DSVVFNIFGGITRGDEVAKGINSALEQFDeIPTPVVVRLAGTNAAEGREILND---DLVTVEEtLEGAVQRAV 373
Cdd:PLN00124 347 KAILVNIFGGIMKCDVIASGIVNAAKQVG-LKVPLVVRLEGTNVDQGKRILKEsgmTLITAED-LDDAAEKAV 417
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
2-192 |
1.70e-74 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 229.84 E-value: 1.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 2 KLHEYQAKEVFADAGIPTPESALATSVDEAVEVADALDYPVAV-KAQVHVGGRGKAGGIKLAENTAEAREAAESILGMDL 80
Cdd:pfam08442 1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVvKAQVLAGGRGKAGGVKLAKSPEEAKEVAKEMLGKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 81 K-------GYTVDRVLVEEAVDFTNELYVGVTMDRSEGAPVVMVSERGGVDIESVAEEAPEDIVREHVDPSFGLQAYQAR 153
Cdd:pfam08442 81 VtkqtgpdGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKGLTPYQAR 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 501246331 154 NAVYDAGIEQDVAGDVAKIVQGVYDLWADSDATEVEINP 192
Cdd:pfam08442 161 EIAFKLGLPGELIKQAADIIKKLYKLFVEYDATLVEINP 199
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
3-214 |
7.99e-22 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 97.12 E-value: 7.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 3 LHEYQAKEVFADAGIPTPESALATSVDEAVEVADALDYPVAVKAQ----VHvggrgK--AGGIKLA-ENTAEAREAAESI 75
Cdd:COG1042 488 LTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVspdiLH-----KsdVGGVRLNlRDAEAVRAAFEEI 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 76 LGmDLKGY----TVDRVLVEEAVDFTNELYVGVTMDRSEGaPVVMVSErGGVDIE-----SVA------EEAPEDIVREH 140
Cdd:COG1042 563 LA-RVRAArpdaRIDGVLVQPMVPGGVELIVGVKRDPVFG-PVIMFGL-GGIFVEvlkdvALRlpplneALAREMIRELR 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501246331 141 VDPsfGLQAYQARNAVydagieqDVAGdVAKIVQGVYDL-WADSDATEVEINPVMVtSERDVVAADAVMKLDEDA 214
Cdd:COG1042 640 AAK--LLRGYRGRPPA-------DLDA-LADVLVRLSQLaADLPEILELDINPLLV-VPEGVVAVDARIRLAPPA 703
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
3-210 |
2.55e-20 |
|
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: 88.30 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 3 LHEYQAKEVFADAGIPTPESALATSVDEAVEVADALDYPVAVKAQ----VHvggRGKAGGIKLAENTAEA-REAAESIL- 76
Cdd:pfam13549 10 LTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVspdiLH---KSDVGGVRLNLRSAEAvRAAYEEILe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 77 --GMDLKGYTVDRVLVEEAVDFTNELYVGVTMDRSEGaPVVMVSErGGVDIE-----SVA-----EEAPEDIVREhvdps 144
Cdd:pfam13549 87 rvRRYRPDARIEGVLVQPMAPGGRELIVGVTRDPQFG-PVIMFGL-GGIAVEvlkdvAFRlpplnMTLAREMIRR----- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501246331 145 fgLQAYQARNAVydAGIEQDVAGDVAKIVQGVYDLWADSDA-TEVEINPVMVtSERDVVAADAVMKL 210
Cdd:pfam13549 160 --TRAYKLLKGY--RGEPPADLDALEDVLVRVSQLVIDFPEiRELDINPLLA-DEDGVVALDARIRL 221
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
256-372 |
8.69e-16 |
|
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilize ATP others use GTP.
Pssm-ID: 395434 [Multi-domain] Cd Length: 128 Bit Score: 73.06 E-value: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 256 NGAGLVMTTLDLVDYYGGQPANFLDIGGGAKA-DRVANALDMVFSDENVDSVVFNIFGGITRGDEVAKGINSALEQFDEI 334
Cdd:pfam00549 3 NGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTpTTRIDALKLEAADPEVKVILLDIVLGYGACEDPAGGLLKAIKEARAR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 501246331 335 PTPVVVRLAGTNA-----AEGREILNDDLVTVEETLEGAVQRA 372
Cdd:pfam00549 83 ELPVVARVCGTEAdpqgrSGQAKALAESGVLIASSNNQALRAA 125
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
6-95 |
3.40e-12 |
|
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: 66.05 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 6 YQAKEVFADAGIPTPESALATSVDEAVEVADALDYPVAVKAQVHVGGRgkagGIKLAENTAEAREAAESILGMDLKGYTV 85
Cdd:COG0439 56 VLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSR----GVRVVRDEEELEAALAEARAEAKAGSPN 131
|
90
....*....|
gi 501246331 86 DRVLVEEAVD 95
Cdd:COG0439 132 GEVLVEEFLE 141
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
8-95 |
6.82e-09 |
|
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: 56.95 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 8 AKEVFADAGIPTPESALATSVDEAVEVADALDYPVAVKAQvhvggrGKAG--GIKLAENTAEAREAAESILGMDLKGYTV 85
Cdd:COG0151 106 AKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKAD------GLAAgkGVVVAETLEEALAAVDDMLADGKFGDAG 179
|
90
....*....|
gi 501246331 86 DRVLVEEAVD 95
Cdd:COG0151 180 ARVVIEEFLE 189
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
8-95 |
8.95e-09 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 54.98 E-value: 8.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 8 AKEVFADAGIPTPESALATSVDEAVEVADALDYPVAV-KAQVHVGGRGkaggIKLAENTAEAREAAESILGMDLKGYTVD 86
Cdd:pfam01071 6 AKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVvKADGLAAGKG----VIVASSNEEAIKAVDEILEQKKFGEAGE 81
|
....*....
gi 501246331 87 RVLVEEAVD 95
Cdd:pfam01071 82 TVVIEEFLE 90
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
9-94 |
9.19e-09 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 57.32 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 9 KEVFADA----GIPTPESALATSVDEAVEVADALDYPVAVKAQVHVGGRGkaGGIklAENTAEAREAAESILGMDlkgyT 84
Cdd:TIGR01369 128 RELFREAmkeiGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFTLGGTG--GGI--AYNREELKEIAERALSAS----P 199
|
90
....*....|
gi 501246331 85 VDRVLVEEAV 94
Cdd:TIGR01369 200 INQVLVEKSL 209
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
13-129 |
3.35e-08 |
|
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: 52.64 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 13 ADAGIPTPESALATSVDEAVEVADALDYPVAVKAQVHvGGRGKagGIKLAENTAEAREAAESILGMdlkgytvdRVLVEE 92
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRG-GYDGK--GQYVVRSEADLPQAWEELGDG--------PVIVEE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 501246331 93 AVDFTNELYVGVTMDRsEGA----PVVMVSERGGVDIESVA 129
Cdd:pfam02222 70 FVPFDRELSVLVVRSV-DGEtafyPVVETIQEDGICRLSVA 109
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
9-94 |
5.18e-08 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 55.10 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 9 KEVFADAGIPTPESALATSVDEAVEVADALDYPVAVKAQVHVGGRGkaGGIklAENTAEAREAAESilGMDLKgyTVDRV 88
Cdd:PRK05294 133 KEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVIIRPSFTLGGTG--GGI--AYNEEELEEIVER--GLDLS--PVTEV 204
|
....*.
gi 501246331 89 LVEEAV 94
Cdd:PRK05294 205 LIEESL 210
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
7-95 |
7.57e-08 |
|
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: 52.31 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 7 QAKEVFADAGIPTPES--ALATSVDEAVEVADALDYPVAVKAQVHVGGRgkagGIKLAENTAEAREAAESILGMDLKGYT 84
Cdd:pfam02786 4 LFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGL----GMGIARNEEELAELFALALAEAPAAFG 79
|
90
....*....|.
gi 501246331 85 VDRVLVEEAVD 95
Cdd:pfam02786 80 NPQVLVEKSLK 90
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
8-95 |
1.48e-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: 52.42 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 8 AKEVFADAGIPTPESALATSVDEAV--EVADALDYPVAVKAqVHvggrgkAG---GIKLAENTAEAREAAESILGMDlkg 82
Cdd:COG1181 99 TKRVLAAAGLPTPPYVVLRRGELADleAIEEELGLPLFVKP-AR------EGssvGVSKVKNAEELAAALEEAFKYD--- 168
|
90
....*....|...
gi 501246331 83 ytvDRVLVEEAVD 95
Cdd:COG1181 169 ---DKVLVEEFID 178
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
9-95 |
1.62e-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: 49.88 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 9 KEVFADAGIPTPESALATSVDEAVEVADALDYPVAVKAqVHV-GGRGkaGGIklAENTAEAREAAESILGMDLKGytvdR 87
Cdd:COG0458 119 KELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRP-SYVlGGRG--MGI--VYNEEELEEYLERALKVSPDH----P 189
|
....*...
gi 501246331 88 VLVEEAVD 95
Cdd:COG0458 190 VLIDESLL 197
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
2-100 |
2.05e-06 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 49.30 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 2 KLHEyqaKEVFADAGIPTPESALATSVDEAVEVADALDYPVAVKAQVHvGGRGKagGIKLAENTAEAREAAESILGMDLk 81
Cdd:COG0026 90 RLLE---KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRRG-GYDGK--GQVVIKSAADLEAAWAALGGGPC- 162
|
90
....*....|....*....
gi 501246331 82 gytvdrvLVEEAVDFTNEL 100
Cdd:COG0026 163 -------ILEEFVPFEREL 174
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
8-75 |
1.19e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 47.29 E-value: 1.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501246331 8 AKEVFADAGIP----TPESAlaTSVDEAVEVADALDYPVAVKAQvhVGGRGKagGIKLAENTAEAREAAESI 75
Cdd:PRK08654 119 AKKLMKKAGVPvlpgTEEGI--EDIEEAKEIAEEIGYPVIIKAS--AGGGGI--GMRVVYSEEELEDAIEST 184
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
8-92 |
1.58e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 46.26 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 8 AKEVFADAGIPTPESALATSVDEAVEVADALDYPVAVKAqVHvggRGKAGGIKLAENTAEAREAAESILGMDlkgytvDR 87
Cdd:PRK01372 102 TKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP-AR---EGSSVGVSKVKEEDELQAALELAFKYD------DE 171
|
....*
gi 501246331 88 VLVEE 92
Cdd:PRK01372 172 VLVEK 176
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
8-74 |
1.86e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 46.33 E-value: 1.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501246331 8 AKEVFADAGIPT-PESA-LATSVDEAVEVADALDYPVAVKAQVHVGGRgkagGIKLAENTAEAREAAES 74
Cdd:PRK08591 119 AKATMKKAGVPVvPGSDgPVDDEEEALAIAKEIGYPVIIKATAGGGGR----GMRVVRTEAELEKAFSM 183
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
7-95 |
2.22e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 46.67 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 7 QAKEVFADAGIPT-PESA-LATSVDEAVEVADALDYPVAVKAQVHVGGRgkagGIKLAENTAEAREAAESILGMDLKGYT 84
Cdd:PRK12999 122 AARNAAIKAGVPViPGSEgPIDDIEEALEFAEEIGYPIMLKASAGGGGR----GMRIVRSEEELEEAFERAKREAKAAFG 197
|
90
....*....|.
gi 501246331 85 VDRVLVEEAVD 95
Cdd:PRK12999 198 NDEVYLEKYVE 208
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
14-54 |
6.08e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 45.09 E-value: 6.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 501246331 14 DAGIPTPESALATSVDEAVEVADALDYPVAVKAQVHVGGRG 54
Cdd:PRK05294 679 KLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRA 719
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
9-91 |
7.33e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 44.76 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 9 KEVFADAGIPTPESALATSVDEAVEVADALDYPVAVKAQVHVGGRGKAGGIKLAENTAEAREAAESIlgmdlkgytVDRV 88
Cdd:PRK14016 219 KRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVNITTREEIEAAYAVASKE---------SSDV 289
|
...
gi 501246331 89 LVE 91
Cdd:PRK14016 290 IVE 292
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
13-139 |
7.45e-05 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 44.53 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 13 ADAGIPTPESALATSVDEAVEVADALDYPVAVKAQ-----VHVGGRGKAGGIKlAENTAEAREAAESILGMDlkgytvDR 87
Cdd:COG3919 126 EELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPAdsvgyDELSFPGKKKVFY-VDDREELLALLRRIAAAG------YE 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501246331 88 VLVEEAV--DFTNELYVGVTMDRsEGAPVVMVSER----------GGVDIESVAEEAPEDIVRE 139
Cdd:COG3919 199 LIVQEYIpgDDGEMRGLTAYVDR-DGEVVATFTGRklrhyppaggNSAARESVDDPELEEAARR 261
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
7-94 |
1.14e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 43.94 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 7 QAKEVFADAGIP-TP--ESALATsVDEAVEVADALDYPVAVKAQVHVGGRgkagGIKLAENTAEAREAAESILGMDLKGY 83
Cdd:PRK07178 117 EARRAMIKAGVPvTPgsEGNLAD-LDEALAEAERIGYPVMLKATSGGGGR----GIRRCNSREELEQNFPRVISEATKAF 191
|
90
....*....|.
gi 501246331 84 TVDRVLVEEAV 94
Cdd:PRK07178 192 GSAEVFLEKCI 202
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
2-100 |
1.29e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.60 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 2 KLHEyqaKEVFADAGIPTPESALATSVDEAVEVADALDYPVAVKAQVHvGGRGKagGIKLAENTAEAREAAESILGMDLk 81
Cdd:PRK06019 101 RLTE---KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRRG-GYDGK--GQWVIRSAEDLEAAWALLGSVPC- 173
|
90
....*....|....*....
gi 501246331 82 gytvdrvLVEEAVDFTNEL 100
Cdd:PRK06019 174 -------ILEEFVPFEREV 185
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
7-70 |
1.92e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 43.20 E-value: 1.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501246331 7 QAKEVFADAGIPT-PESA-LATSVDEAVEVADALDYPVAVKAQVHVGGRgkagGIKLAENTAEARE 70
Cdd:PRK12833 121 RARRTARRAGVPTvPGSDgVVASLDAALEVAARIGYPLMIKAAAGGGGR----GIRVAHDAAQLAA 182
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
7-74 |
2.15e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 43.09 E-value: 2.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501246331 7 QAKEVFADAGIPT---PESALAtSVDEAVEVADALDYPVAVKAQVHVGGRgkagGIKLAENTAEAREAAES 74
Cdd:PRK06111 118 EARRAMQAAGVPVvpgITTNLE-DAEEAIAIARQIGYPVMLKASAGGGGI----GMQLVETEQELTKAFES 183
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
16-109 |
5.03e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 42.26 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 16 GIPTPESALATSVDEAVEVADALDYPVAVKAQVHVGGRGkaGGIklaentAEAREAAESILGMDLKGYTVDRVLVEEAVD 95
Cdd:PRK12815 140 GEPVPESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTG--GGI------AENLEELEQLFKQGLQASPIHQCLLEESIA 211
|
90
....*....|....
gi 501246331 96 FTNELYVGVTMDRS 109
Cdd:PRK12815 212 GWKEIEYEVMRDRN 225
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
2-217 |
5.67e-04 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 41.68 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 2 KLHEYQAKEVFAD-----AGIPTP-ESALATSVDEAVEVADALDY----PVAVKAQVHVGGRGKAGGIKLAENTAEAREA 71
Cdd:PLN02235 5 KIREYDSKRLLKEhlkrlAGIDLPiRSAQVTESTDFNELANKEPWlsstKLVVKPDMLFGKRGKSGLVALNLDLAQVATF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 72 AESILGMDL-----KGyTVDRVLVEEAVDFTNELYVGVTMDRSeGAPVVMvSERGGVDIESvaeeaPEDIVREHVDPSfG 146
Cdd:PLN02235 85 VKERLGKEVemggcKG-PITTFIVEPFVPHDQEFYLSIVSDRL-GCSISF-SECGGIEIEE-----NWDKVKTIFLPT-E 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501246331 147 LQAYQARNAVYDAGIEQDVAGDVAKIVQGVYDLWADSDATEVEINP-VMVTSERdvVAADAVMKLDEDALFR 217
Cdd:PLN02235 156 APLTSEICAPLIATLPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPfTLVDGEP--YPLDMRGELDDTAAFK 225
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
7-54 |
6.34e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 41.65 E-value: 6.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 501246331 7 QAKEVFADAG---IPTPESALAtSVDEAVEVADALDYPVAVKAQVHVGGRG 54
Cdd:PRK08462 120 KAKEVMKRAGvpvIPGSDGALK-SYEEAKKIAKEIGYPVILKAAAGGGGRG 169
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
7-74 |
1.03e-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: 41.22 E-value: 1.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 7 QAKEVFADAGIPTPES--ALATSVDEAVEVADALDYPVAVKAQVHVGGRgkagGIKLAENTAEAREAAES 74
Cdd:COG1038 121 AARAAAIEAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAAAGGGGR----GMRVVRSEEELEEAFES 186
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
6-109 |
1.11e-03 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 40.81 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 6 YQAKEVFADAGIPTPESALATSVDEAVEVADALDYPVAVKAQ-VHVGGRGKAggikLAENTAEAREAAESILGMDLKGYt 84
Cdd:PLN02948 123 YAQKVHFSKHGIPLPEFMEIDDLESAEKAGDLFGYPLMLKSRrLAYDGRGNA----VAKTEEDLSSAVAALGGFERGLY- 197
|
90 100
....*....|....*....|....*
gi 501246331 85 vdrvlVEEAVDFTNELYVGVTMDRS 109
Cdd:PLN02948 198 -----AEKWAPFVKELAVMVARSRD 217
|
|
| LysX_arch |
TIGR02144 |
Lysine biosynthesis enzyme LysX; The family of proteins found in this equivalog include the ... |
13-72 |
1.31e-03 |
|
Lysine biosynthesis enzyme LysX; The family of proteins found in this equivalog include the characterized LysX from Thermus thermophilus, which is part of a well-organized lysine biosynthesis gene cluster. LysX is believed to carry out an ATP-dependent acylation of the amino group of alpha-aminoadipate in the prokaryotic version of the fungal AAA lysine biosynthesis pathway. No species having a sequence in this equivalog contains the elements of the more common diaminopimelate lysine biosythesis pathway, and none has been shown to be a lysine auxotroph. These sequences have mainly recieved the name of the related enzyme, "ribosomal protein S6 modification protein RimK". RimK has been characterized in E. coli, and acts by ATP-dependent condensation of S6 with glutamate residues.
Pssm-ID: 273994 [Multi-domain] Cd Length: 280 Bit Score: 40.07 E-value: 1.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501246331 13 ADAGIPTPESALATSVDEAVEVADALDYPVAVKAQVHVGGR--GKAGGIKLAENTAEAREAA 72
Cdd:TIGR02144 96 AKAGVPTPRTYLAFDREAALKAAEALGYPVVLKPVIGSWGRlvAKVRDRDEAEALLEHKEVL 157
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
10-78 |
1.43e-03 |
|
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: 39.92 E-value: 1.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501246331 10 EVFADAGIPTPESALATSVDEAVEVADALDYPVAVKaqVHVGGRGKagGIKLAENTAEAREAAESILGM 78
Cdd:COG0189 102 QLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLK--PLDGSGGR--GVFLVEDEDALESILEALTEL 166
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
9-94 |
1.99e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 40.53 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 9 KEVFADA----GIPTPESALATSVDEAVEVADAL-DYPVAVKAQVHVGGRGkaGGIklaentAEAREAAESILGMDLKGY 83
Cdd:PLN02735 145 RELFKQAmekiGLKTPPSGIATTLDECFEIAEDIgEFPLIIRPAFTLGGTG--GGI------AYNKEEFETICKAGLAAS 216
|
90
....*....|.
gi 501246331 84 TVDRVLVEEAV 94
Cdd:PLN02735 217 ITSQVLVEKSL 227
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
8-156 |
2.83e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 39.70 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246331 8 AKEVFADAG---IPTPESALATSvDEAVEVADALDYPVAVKAQVHVGGRgkagGIKLAENTAEAREAAESILGMDLKGYT 84
Cdd:PRK05586 119 AREIMIKAGvpvVPGSEGEIENE-EEALEIAKEIGYPVMVKASAGGGGR----GIRIVRSEEELIKAFNTAKSEAKAAFG 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501246331 85 VDRVLVEEAVDFTNELYVGVTMDRSEGapVVMVSERggvDI------ESVAEEAPEDIVREHVDPSFGLQAYQARNAV 156
Cdd:PRK05586 194 DDSMYIEKFIENPKHIEFQILGDNYGN--VVHLGER---DCslqrrnQKVLEEAPSPVMTEELRKKMGEIAVKAAKAV 266
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
16-54 |
6.72e-03 |
|
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: 38.83 E-value: 6.72e-03
10 20 30
....*....|....*....|....*....|....*....
gi 501246331 16 GIPTPESALATSVDEAVEVADALDYPVAVKAQVHVGGRG 54
Cdd:TIGR01369 681 GIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRA 719
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
11-76 |
9.03e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 38.29 E-value: 9.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501246331 11 VFADAGIPTPESALATSVDEAVEVADALDYPVAVKAqvhVGGRGKAgGIKLAENTAEAREAAESIL 76
Cdd:PRK02186 114 TLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKP---RMGSGSV-GVRLCASVAEAAAHCAALR 175
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