|
Name |
Accession |
Description |
Interval |
E-value |
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
1-392 |
0e+00 |
|
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439798 [Multi-domain] Cd Length: 393 Bit Score: 822.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 1 MTRIGTPLSPTATRVLMCGCGELGKEVVIELQRLGVEVIAVDRYANAPAMQVAHRSHVINMLDGAALRAVIEAEKPHFIV 80
Cdd:COG0027 1 MTTIGTPLSPNATKVMLLGSGELGKEVAIELQRLGVEVIAVDRYANAPAMQVAHRSYVIDMLDGDALRALIEREKPDFIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 81 PEIEAIATGTLVELEAEGFTVIPTARAALLTMNREGIRRLAAEELDLPTSPYHFADTFEDYSKAVQDLGFPCVVKPVMSS 160
Cdd:COG0027 81 PEIEAIATDALVELEAEGFRVVPTARAVRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 161 SGKGQSLLRSADDVQKAWDYAQEGGRAGKGRVIIEGFIDFDYEITLLTVRHVGG-TTFCAPVGHRQEKGDYQESWQPQAM 239
Cdd:COG0027 161 SGKGQSVVRSPADIEAAWEYAQEGGRGGAGRVIVEGFVDFDYEITLLTVRAVDGpTHFCEPIGHRQEDGDYRESWQPQPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 240 SPVALAESERVAKAVTEALGGRGLFGVELFIKGDQVWFSEVSPRPHDTGLVTLISQDLSQFALHARAILGLPIPLIRQFG 319
Cdd:COG0027 241 SEAALAKAQEIAKKVTDALGGRGIFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQDLSEFALHARAILGLPVPEIRLVG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785561342 320 PSASAVILVEGQSTQTAFANLGAALSEPDTALRLFGKPEVNGQRRMGVALARDESIEAARAKATRASQAVVVE 392
Cdd:COG0027 321 PAASAVILAEGESWAPAFDGLAEALAVPGTDLRLFGKPEAYGRRRMGVALATADDVEEAREKAREAAAKVKVV 393
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
1-393 |
0e+00 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 798.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 1 MTRIGTPLSPTATRVLMCGCGELGKEVVIELQRLGVEVIAVDRYANAPAMQVAHRSHVINMLDGAALRAVIEAEKPHFIV 80
Cdd:PRK09288 1 MTRLGTPLSPSATRVMLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSHVIDMLDGDALRAVIEREKPDYIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 81 PEIEAIATGTLVELEAEGFTVIPTARAALLTMNREGIRRLAAEELDLPTSPYHFADTFEDYSKAVQDLGFPCVVKPVMSS 160
Cdd:PRK09288 81 PEIEAIATDALVELEKEGFNVVPTARATRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 161 SGKGQSLLRSADDVQKAWDYAQEGGRAGKGRVIIEGFIDFDYEITLLTVRHV-GGTTFCAPVGHRQEKGDYQESWQPQAM 239
Cdd:PRK09288 161 SGKGQSVVRSPEDIEKAWEYAQEGGRGGAGRVIVEEFIDFDYEITLLTVRAVdGGTHFCAPIGHRQEDGDYRESWQPQPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 240 SPVALAESERVAKAVTEALGGRGLFGVELFIKGDQVWFSEVSPRPHDTGLVTLISQDLSQFALHARAILGLPIPLIRQFG 319
Cdd:PRK09288 241 SPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQNLSEFELHARAILGLPIPDIRLYS 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785561342 320 PSASAVILVEGQSTQTAFANLGAALSEPDTALRLFGKPEVNGQRRMGVALARDESIEAARAKATRASQAVVVEL 393
Cdd:PRK09288 321 PAASAVILAEGESANPSFDGLAEALAVPGTDVRLFGKPEIRGGRRMGVALATGEDVEEAREKAKEAASKVKVVG 394
|
|
| purT |
TIGR01142 |
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN ... |
14-392 |
0e+00 |
|
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN (TIGR00639) [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 130212 Cd Length: 380 Bit Score: 667.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 14 RVLMCGCGELGKEVVIELQRLGVEVIAVDRYANAPAMQVAHRSHVINMLDGAALRAVIEAEKPHFIVPEIEAIATGTLVE 93
Cdd:TIGR01142 1 RVLLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSYVINMLDGDALRAVIEREKPDYIVPEIEAIATDALFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 94 LEAEGFTVIPTARAALLTMNREGIRRLAAEELDLPTSPYHFADTFEDYSKAVQDLGFPCVVKPVMSSSGKGQSLLRSADD 173
Cdd:TIGR01142 81 LEKEGYFVVPNARATKLTMNREGIRRLAAEELGLPTSRYMFADSLDELREAVEKIGYPCVVKPVMSSSGKGQSVVRGPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 174 VQKAWDYAQEGGRAGKGRVIIEGFIDFDYEITLLTVRHVGG-TTFCAPVGHRQEKGDYQESWQPQAMSPVALAESERVAK 252
Cdd:TIGR01142 161 IEKAWEYAQEGARGGAGRVIVEEFIDFDYEITLLTVRHVDGnTTFCAPIGHRQIDGDYHESWQPQEMSEKALEEAQRIAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 253 AVTEALGGRGLFGVELFIKGDQVWFSEVSPRPHDTGLVTLISQDLSQFALHARAILGLPIPLIRQFGPSASAVILVEGQS 332
Cdd:TIGR01142 241 RITDALGGYGLFGVELFVKGDEVIFSEVSPRPHDTGMVTLISQGLSEFALHVRAILGLPIPGIPQLGPAASAVIKAKVTG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 333 TQTAFANLGAALSEPDTALRLFGKPEVNGQRRMGVALARDESIEAARAKATRASQAVVVE 392
Cdd:TIGR01142 321 YSPAFRGLEKALSVPNTQVRLFGKPEAYVGRRLGVALATAKSVEAARERAEEVAHAVEVR 380
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
123-294 |
1.81e-64 |
|
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: 203.25 E-value: 1.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 123 EELDLPTSPYHFADTFEDYSKAVQDLGFPCVVK-PVMSSSGKGQSLLRSADDVQKAWDYAqeggraGKGRVIIEGFIDFD 201
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKaRRGGYDGKGQYVVRSEADLPQAWEEL------GDGPVIVEEFVPFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 202 YEITLLTVRHV-GGTTFCAPVGHRQEKGDYQESWQPQAMSPVALAESERVAKAVTEALGGRGLFGVELFIKGD-QVWFSE 279
Cdd:pfam02222 75 RELSVLVVRSVdGETAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDgDLLINE 154
|
170
....*....|....*
gi 1785561342 280 VSPRPHDTGLVTLIS 294
Cdd:pfam02222 155 LAPRPHNSGHYTLDG 169
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
23-385 |
3.41e-63 |
|
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: 206.08 E-value: 3.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 23 LGKEVVIELQRLGVEVIAVDRYANAPAMQVAHRSHVINMLDGAALRAVieAEKPHFIVPEIEAIATGTLVELEAEGfTVI 102
Cdd:COG0026 2 LGRMLALAAKRLGYRVHVLDPDPDSPAAQVADEHIVADYDDEEALREF--AERCDVVTFEFENVPAEALEALEAEV-PVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 103 PTARAALLTMNRegIR-RLAAEELDLPTSPYHFADTFEDYSKAVQDLGFPCVVKPV-MSSSGKGQSLLRSADDVQKAWDy 180
Cdd:COG0026 79 PGPEALEIAQDR--LLeKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrGGYDGKGQVVIKSAADLEAAWA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 181 aqeggRAGKGRVIIEGFIDFDYEITLLTVRHVGGTTFCAPVGH-RQEKGDYQESWQPQAMSPVALAESERVAKAVTEALG 259
Cdd:COG0026 156 -----ALGGGPCILEEFVPFERELSVIVARSPDGEVATYPVVEnVHRNGILDESIAPARISEALAAEAEEIAKRIAEALD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 260 GRGLFGVELFI-KGDQVWFSEVSPRPHDTGLVTLISQDLSQFALHARAILGLPIPLIRQFGPSASAVILveGQstQTAFA 338
Cdd:COG0026 231 YVGVLAVEFFVtKDGELLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVCGLPLGDTELLSPAVMVNLL--GD--DWEDP 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1785561342 339 NLGAALSEPDTALRLFGKPEVNGQRRMGVALARDESIEAARAKATRA 385
Cdd:COG0026 307 GWEALLALPGAHLHLYGKKEARPGRKMGHVTVLGDDLEEALERARAA 353
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
14-392 |
3.11e-53 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 180.73 E-value: 3.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 14 RVLMCGCGELGKEVVIELQRLGVEVIAVDRYANAPAMQVAHRSHVINMLDGAALRAVieAEKPHFIVPEIEAIATGTLVE 93
Cdd:PRK06019 4 TIGIIGGGQLGRMLALAAAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALREL--AEQCDVITYEFENVPAEALDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 94 LEAEGFtVIPTARAALLTMNREGIRRLAAEeLDLPTSPYHFADTFEDYSKAVQDLGFPCVVKpvmSSS----GKGQSLLR 169
Cdd:PRK06019 82 LAARVP-VPPGPDALAIAQDRLTEKQFLDK-LGIPVAPFAVVDSAEDLEAALADLGLPAVLK---TRRggydGKGQWVIR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 170 SADDVQKAWDyaqeggRAGKGRVIIEGFIDFDYEITLLTVRHVGGTTFCAPVGH-RQEKGDYQESWQPQAMSPVALAESE 248
Cdd:PRK06019 157 SAEDLEAAWA------LLGSVPCILEEFVPFEREVSVIVARGRDGEVVFYPLVEnVHRNGILRTSIAPARISAELQAQAE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 249 RVAKAVTEALGGRGLFGVELFIKGD-QVWFSEVSPRPHDTGLVTLISQDLSQFALHARAILGLPIPLIRQFGPSASAVIL 327
Cdd:PRK06019 231 EIASRIAEELDYVGVLAVEFFVTGDgELLVNEIAPRPHNSGHWTIEACSTSQFEQHLRAILGLPLGTTRLLSPAVMVNLL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785561342 328 veGQSTQTAFANlgAALSEPDTALRLFGKPEVNGQRRMGVALARDESIEAARAKATRASQAVVVE 392
Cdd:PRK06019 311 --GDDWLEPRWD--ALLALPGAHLHLYGKAEARPGRKMGHVTVLGDDVEALLAKLEALAPDWAEI 371
|
|
| purK |
TIGR01161 |
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole ... |
15-366 |
3.72e-51 |
|
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, N5-carboxyaminoimidazole ribonucleotide synthetase, which hydrolyzes ATP and converts AIR to N5-CAIR. PurE converts N5-CAIR to CAIR. In the presence of high concentrations of bicarbonate, PurE is reported able to convert AIR to CAIR directly and without ATP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273473 [Multi-domain] Cd Length: 352 Bit Score: 174.83 E-value: 3.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 15 VLMCGCGELGKEVVIELQRLGVEVIAVDRYANAPAMQVAHRSHVINMLDGAALRAVieAEKPHFIVPEIEAIATGTLVEL 94
Cdd:TIGR01161 2 VGILGGGQLGRMLALAARPLGIKVHVLDPDANSPAVQVADHVVLAPFFDPAAIREL--AESCDVITFEFEHVDVEALEKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 95 EAEGFTVIPTARAALLTMNREgIRRLAAEELDLPTSPYHFADTFEDYSKAVQDLGFPCVVKPV-MSSSGKGQSLLRSADD 173
Cdd:TIGR01161 80 EARGVKLFPSPDALAIIQDRL-TQKQFLQKLGLPVPPFLVIKDEEELDAALQELGFPVVLKARtGGYDGRGQYRIRNEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 174 VQKAWDyaqeggRAGKGRVIIEGFIDFDYEITLLTVRHVGGTTFCAPVGHR-QEKGDYQESWQPQAMSPVALAESERVAK 252
Cdd:TIGR01161 159 LPQAAK------ELGDRECIVEEFVPFERELSVIVARSADGETAFYPVVENiHQDGILRYVVAPAAVPDAIQARAEEIAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 253 AVTEALGGRGLFGVELFIKGD-QVWFSEVSPRPHDTGLVTLISQDLSQFALHARAILGLPIPLIRQFGPSASAVIL-VEG 330
Cdd:TIGR01161 233 RLMEELGYVGVLAVEMFVLPDgRLLINELAPRVHNSGHYTLDGCSTSQFEQHLRAILGLPLGSTELLLPSVMVNLLgTED 312
|
330 340 350
....*....|....*....|....*....|....*.
gi 1785561342 331 QSTQTafanLGAALSEPDTALRLFGKPEVNGQRRMG 366
Cdd:TIGR01161 313 DVIPL----WEEILALPGAKLHWYGKAEVRPGRKVG 344
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
6-366 |
5.48e-41 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 152.52 E-value: 5.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 6 TPLSPTATRVLMCGCGELGKEVVIELQRLGVEVIAVDRYANAPAMQVAHRSHVINMLDGAALRAVieAEKPHFIVPEIEA 85
Cdd:PLN02948 16 PVHGVSETVVGVLGGGQLGRMLCQAASQMGIKVKVLDPLEDCPASSVAARHVVGSFDDRAAVREF--AKRCDVLTVEIEH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 86 IATGTLVELEAEGFTVIPTARAaLLTMNREGIRRLAAEELDLPTSPYHFADTFEDYSKAVQDLGFPCVVKPV-MSSSGKG 164
Cdd:PLN02948 94 VDVDTLEALEKQGVDVQPKSST-IRIIQDKYAQKVHFSKHGIPLPEFMEIDDLESAEKAGDLFGYPLMLKSRrLAYDGRG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 165 QSLLRSADDVQKAwdYAQEGGRAgKGrVIIEGFIDFDYEITLLTVRHVGGTTFCAPVG---HRQEKGDYQESwqPQAMSP 241
Cdd:PLN02948 173 NAVAKTEEDLSSA--VAALGGFE-RG-LYAEKWAPFVKELAVMVARSRDGSTRCYPVVetiHKDNICHVVEA--PANVPW 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 242 VALAESERVAKAVTEALGGRGLFGVELFIKGD-QVWFSEVSPRPHDTGLVTLISQDLSQFALHARAILGLPIPLIRQFGP 320
Cdd:PLN02948 247 KVAKLATDVAEKAVGSLEGAGVFGVELFLLKDgQILLNEVAPRPHNSGHYTIEACYTSQFEQHLRAVLGLPLGDTSMKVP 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1785561342 321 SASAV-ILVEGQ---STQTAFANLGAALSEPDTALRLFGKPEVNGQRRMG 366
Cdd:PLN02948 327 AAIMYnILGEDEgeaGFRLAHQLMGRALNIPGASVHWYGKPEMRKQRKMG 376
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
67-314 |
8.13e-22 |
|
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: 93.78 E-value: 8.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 67 LRAVIEAEKPHFIVPEIEAIATGTlveleaeGFTVIPTARAA----LLTMNREGIR--------RLAAEELDLPTSPYHF 134
Cdd:COG0439 2 IDAIIAAAAELARETGIDAVLSES-------EFAVETAAELAeelgLPGPSPEAIRamrdkvlmREALAAAGVPVPGFAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 135 ADTFEDYSKAVQDLGFPCVVKPVMSSSGKGQSLLRSADDVQKAWDYAQEGGRAGK--GRVIIEGFIDfDYEITLLTVRHV 212
Cdd:COG0439 75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSpnGEVLVEEFLE-GREYSVEGLVRD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 213 GGTTFCAPVGHRQEKGDYQES--WQPQAMSPVALAESERVAKAVTEALG-GRGLFGVELFI-KGDQVWFSEVSPRPHDTG 288
Cdd:COG0439 154 GEVVVCSITRKHQKPPYFVELghEAPSPLPEELRAEIGELVARALRALGyRRGAFHTEFLLtPDGEPYLIEINARLGGEH 233
|
250 260
....*....|....*....|....*...
gi 1785561342 289 LVTLI--SQDLSQFALHARAILGLPIPL 314
Cdd:COG0439 234 IPPLTelATGVDLVREQIRLALGEPRIL 261
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
25-284 |
4.91e-14 |
|
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: 71.90 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 25 KEVVIELQRLGVEVIAVDryANAPAMQVAHRSHVINMLDGAALRAVIEAEKPHFIvpeieaiATGTLVELEAEGFTVIPT 104
Cdd:COG0189 17 KALIEAAQRRGHEVEVID--PDDLTLDLGRAPELYRGEDLSEFDAVLPRIDPPFY-------GLALLRQLEAAGVPVVND 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 105 ARAALLTMNREGIRRLAAEeLDLPTSPYHFADTFEDYSKAVQDLGFPCVVKPVMSSSGKGQSLLRSADDvqkAWDYAQEG 184
Cdd:COG0189 88 PEAIRRARDKLFTLQLLAR-AGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDA---LESILEAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 185 GRAGKGRVIIEGFI----DFDYEITLltvrhVGGTTFCA-----PVGHRQEKGDYQESWQPQAMSPvalaESERVAKAVT 255
Cdd:COG0189 164 TELGSEPVLVQEFIpeedGRDIRVLV-----VGGEPVAAirripAEGEFRTNLARGGRAEPVELTD----EERELALRAA 234
|
250 260
....*....|....*....|....*....
gi 1785561342 256 EALGGrGLFGVELFIKGDQVWFSEVSPRP 284
Cdd:COG0189 235 PALGL-DFAGVDLIEDDDGPLVLEVNVTP 262
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
9-284 |
8.26e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 72.27 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 9 SPTATRVLMCGCGELGKEVVIELQRLGVEVIAVDRYANAPAMQ--VAHRSHVI-NMLDG-----AALRAVIEAEKPHFIV 80
Cdd:COG3919 2 MTMRFRVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARsrYVDEVVVVpDPGDDpeafvDALLELAERHGPDVLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 81 P----EIEAIATgTLVELEAEgfTVIPTARAALLT--MNREGIRRLAaEELDLPTSPYHFADTFEDYSKAVQDLGFPCVV 154
Cdd:COG3919 82 PtgdeYVELLSR-HRDELEEH--YRLPYPDADLLDrlLDKERFYELA-EELGVPVPKTVVLDSADDLDALAEDLGFPVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 155 KPVMSSS--------GKGQSLLRSADDVQKAWDYAQEGGragkGRVIIEGFI--DFDYEITLLTVRHVGGTTFCAPVGH- 223
Cdd:COG3919 158 KPADSVGydelsfpgKKKVFYVDDREELLALLRRIAAAG----YELIVQEYIpgDDGEMRGLTAYVDRDGEVVATFTGRk 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785561342 224 -RQekgdyqesWQPQ-----AMSPVALAESERVAKAVTEALGGRGLFGVELFI--KGDQVWFSEVSPRP 284
Cdd:COG3919 234 lRH--------YPPAggnsaARESVDDPELEEAARRLLEALGYHGFANVEFKRdpRDGEYKLIEINPRF 294
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
107-284 |
1.95e-13 |
|
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273498 [Multi-domain] Cd Length: 315 Bit Score: 70.39 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 107 AALLTMNREGIRRLAAEeLDLPTSPY------HFADTFEDYSKAVQDLGFPCVVKPVMSSSGKGQSLLRSADDVQKAWDY 180
Cdd:TIGR01205 99 ASALSMDKLLTKLLWKA-LGLPTPDYivltqnRASADELECEQVAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 181 AQEGGRagkgRVIIEGFIDfDYEITLLTVRHVGGTTFCAPVGHRQEKGDYQESWQ--------PQAMSPVALAESERVAK 252
Cdd:TIGR01205 178 AFEYDE----EVLVEQFIK-GRELEVSILGNEEALPIIEIVPEIEGFYDYEAKYLdgsteyviPAPLDEELEEKIKELAL 252
|
170 180 190
....*....|....*....|....*....|...
gi 1785561342 253 AVTEALGGRGLFGVELFI-KGDQVWFSEVSPRP 284
Cdd:TIGR01205 253 KAYKALGCRGLARVDFFLdEEGEIYLNEINTIP 285
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
24-280 |
8.14e-12 |
|
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: 65.51 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 24 GKEVVIELQRLGVEVIAVDryanapamqvahrshvinmLDGAALRAVIEAEKPHFIVPeieaIATGTLVE-------LEA 96
Cdd:COG1181 21 GRAVAAALDKAGYDVVPIG-------------------IDVEDLPAALKELKPDVVFP----ALHGRGGEdgtiqglLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 97 EGftvIP----TARAALLTMNREGIRRLAAEElDLPTSPYHF--ADTFEDYSKAVQDLGFPCVVKPVMSSSGKGQSLLRS 170
Cdd:COG1181 78 LG---IPytgsGVLASALAMDKALTKRVLAAA-GLPTPPYVVlrRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 171 ADDVQKAWDYAQEGGRagkgRVIIEGFID-FDYEITLLTvrhvGGTTFCAPVGHRQEKG---DYQESWQPQA-------- 238
Cdd:COG1181 154 AEELAAALEEAFKYDD----KVLVEEFIDgREVTVGVLG----NGGPRALPPIEIVPENgfyDYEAKYTDGGteyicpar 225
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1785561342 239 MSPVALAESERVAKAVTEALGGRGLFGVELFIKGD-QVWFSEV 280
Cdd:COG1181 226 LPEELEERIQELALKAFRALGCRGYARVDFRLDEDgEPYLLEV 268
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
70-312 |
9.91e-11 |
|
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: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 70 VIEAEKPHFIVPEIEA-IATGTLVELEAEGFTVIPTARAAL-LTMNREGIRRLAaEELDLPTSPYHFADTFEDYSKAVQD 147
Cdd:TIGR01369 624 IIELEKPEGVIVQFGGqTPLNLAKALEEAGVPILGTSPESIdRAEDREKFSELL-DELGIPQPKWKTATSVEEAVEFASE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 148 LGFPCVVKPVMSSSGKGQSLLRSADDVQKawdYAQEGGRAGKGR-VIIEGFIDFDYEITLLTVRHvGGTTFCAPVGHRQE 226
Cdd:TIGR01369 703 IGYPVLVRPSYVLGGRAMEIVYNEEELRR---YLEEAVAVSPEHpVLIDKYLEDAVEVDVDAVSD-GEEVLIPGIMEHIE 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 227 K-----GDYQESWQPQAMSPVALAESERVAKAVTEALGGRGLFGVELFIKGDQVWFSEVSPRPHDTglVTLISQDLS-QF 300
Cdd:TIGR01369 779 EagvhsGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRT--VPFVSKATGvPL 856
|
250
....*....|...
gi 1785561342 301 A-LHARAILGLPI 312
Cdd:TIGR01369 857 AkLAVRVMLGKKL 869
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
125-306 |
1.91e-10 |
|
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: 60.02 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 125 LDLPTSPY-------HFADTFEDYSKAVQDLGFPCVVKPVMSSSGKGQSLLRSADDVQKAWDYAQEGGRagkgRVIIEGF 197
Cdd:pfam07478 5 AGLPVVPFvtftradWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDE----KVLVEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 198 IDFDyEItllTVRHVGGTTF-CAPVGHRQEKG---DYQESWQP---QAMSPVALAESER-----VAKAVTEALGGRGLFG 265
Cdd:pfam07478 81 IEGR-EI---ECAVLGNEDPeVSPVGEIVPSGgfyDYEAKYIDdsaQIVVPADLEEEQEeqiqeLALKAYKALGCRGLAR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1785561342 266 VELFIKGD-QVWFSEVSPRPHDTglvtlisqDLSQFALHARA 306
Cdd:pfam07478 157 VDFFLTEDgEIVLNEVNTIPGFT--------SISMFPKLAAA 190
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
14-283 |
7.69e-10 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 59.51 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 14 RVLMCGCGElGKEVVIELQR--LGVEVIAVDRYANAPAMQVAHRSHVINML-DGAALRAVIE---AEKPHFIVP----EI 83
Cdd:PRK12767 3 NILVTSAGR-RVQLVKALKKslLKGRVIGADISELAPALYFADKFYVVPKVtDPNYIDRLLDickKEKIDLLIPlidpEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 84 EAIATGTlVELEAEGFT-------VIPTARAALLTMNRegirrLAAEELDLPTS--PYHFADTFEDYSKAvqDLGFPCVV 154
Cdd:PRK12767 82 PLLAQNR-DRFEEIGVKvlvsskeVIEICNDKWLTYEF-----LKENGIPTPKSylPESLEDFKAALAKG--ELQFPLFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 155 KPVMSSSGKGQSLLRSADDVQKAWDYAQEggragkgrVIIEGFIDfDYEITL------------------LTVRhvGGTT 216
Cdd:PRK12767 154 KPRDGSASIGVFKVNDKEELEFLLEYVPN--------LIIQEFIE-GQEYTVdvlcdlngevisivprkrIEVR--AGET 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785561342 217 FCAPVGHRQEKGDYqeswqpqamspvalaeservAKAVTEALGGRGLFGVELFIKGDQVWFSEVSPR 283
Cdd:PRK12767 223 SKGVTVKDPELFKL--------------------AERLAEALGARGPLNIQCFVTDGEPYLFEINPR 269
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
70-283 |
4.06e-09 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 58.44 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 70 VIEAEKPHFIVPEIEA-IATGTLVELEAEGFTVIPTARAALLTM-NREGIRRLAaEELDLPTSPYHFADTFEDYSKAVQD 147
Cdd:PRK12815 625 VAEAENIKGVIVQFGGqTAINLAKGLEEAGLTILGTSPDTIDRLeDRDRFYQLL-DELGLPHVPGLTATDEEEAFAFAKR 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 148 LGFPCVVKPVMSSSGKGQSLLRSADDVQKAWDYAQEGGRAgkgrVIIEGFID-FDYEITLLTVrhvGGTTFCAPVGHRQE 226
Cdd:PRK12815 704 IGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENASQLYP----ILIDQFIDgKEYEVDAISD---GEDVTIPGIIEHIE 776
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785561342 227 K-----GDYQESWQPQAMSPVALAESERVAKAVTEALGGRGLFGVELFIKGDQVWFSEVSPR 283
Cdd:PRK12815 777 QagvhsGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPR 838
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
63-225 |
6.17e-09 |
|
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273315 [Multi-domain] Cd Length: 422 Bit Score: 57.32 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 63 DGAALRAVIEAEKPHFIVPEIEA-IATGTLVELEAEGFTVI-PTARAALLTMNREGIRRLAaEELDLPTSPYHFADTFED 140
Cdd:TIGR00877 52 DIEALVEFAKKKKIDLAIIGPEApLVLGLVDALEEAGIPVFgPTKEAAQLEGSKAFAKDFM-KRYGIPTAEYEVFTDPEE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 141 YSKAVQDLGFPCVVKPVMSSSGKGQSLlrsADDVQKAWDYAQE----GGRAGKGRVIIEGFIDFDyEITLLTVrhVGGTT 216
Cdd:TIGR00877 131 AKSYIQEKGAPIVVKADGLAAGKGVIV---AKTNEEAIKAVEDileqKFGDAGERVVIEEFLDGE-EFSLLAF--VDGKT 204
|
....*....
gi 1785561342 217 FcAPVGHRQ 225
Cdd:TIGR00877 205 V-IPMPPAQ 212
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
32-327 |
7.12e-08 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 53.77 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 32 QRLGVEVIAVDRYANAPAMQVAHRSHVINMLDG--------AALRAVIEAEKPHFIVPeieaiatGTLVEleaegftvip 103
Cdd:COG2232 22 RRAGYRVYAVDLFADLDTRALAERWVRLDAESCgfdledlpAALLELAAADDPDGLVY-------GSGFE---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 104 tARAALLTMNREGIRRL--AAEELDLPTSPYHFADTFEDY-------SKAVQDLGFPCVVKPVMSSSGKGQSLLRSADDV 174
Cdd:COG2232 85 -NFPELLERLARRLPLLgnPPEVVRRVKDPLRFFALLDELgiphpetRFEPPPDPGPWLVKPIGGAGGWHIRPADSEAPP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 175 QKAWdYAQE--GGR-------AGKGRVIIEGFidfdyeiTLLTVRHVGGT--TFCAPVGhrqekgdyqeswqPQAMSPVA 243
Cdd:COG2232 164 APGR-YFQRyvEGTpasvlflADGSDARVLGF-------NRQLIGPAGERpfRYGGNIG-------------PLALPPAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 244 LAESERVAKAVTEALGGRGLFGVELFIKGDQVWFSEVSPRPhdTGLVTLISQDLSQ--FALHARAILG-LPIPLIRQFGP 320
Cdd:COG2232 223 AEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRP--QASLDLYEDATGGnlFDAHLRACRGeLPEVPRPKPRR 300
|
....*..
gi 1785561342 321 SASAVIL 327
Cdd:COG2232 301 VAAKAIL 307
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
59-199 |
1.79e-07 |
|
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: 52.71 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 59 INMLDGAALRAVIEAEKPHFIVPEIEA-IATGtLV-ELEAEGFTVI-PTARAALLT---------MNREGIrrlaaeeld 126
Cdd:COG0151 46 IDVTDIEALVAFAKEENIDLVVVGPEApLVAG-IVdAFRAAGIPVFgPSKAAAQLEgskafakefMARYGI--------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 127 lPTSPYHfadTFEDYSKA---VQDLGFPCVVKPVMSSSGKGqslLRSADDVQKAWDYAQE---GGRAGKG--RVIIEGFI 198
Cdd:COG0151 116 -PTAAYR---VFTDLEEAlayLEEQGAPIVVKADGLAAGKG---VVVAETLEEALAAVDDmlaDGKFGDAgaRVVIEEFL 188
|
.
gi 1785561342 199 D 199
Cdd:COG0151 189 E 189
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
102-283 |
1.65e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 50.23 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 102 IPTARAALLTMNREGIR---RLAAEELDLPTSpyHFADTFEDYSKAVQDLGFPCVVKPVMSSSGKGQSLLRSADDvqkAW 178
Cdd:PRK02186 94 LPAANTEAIRTCRDKKRlarTLRDHGIDVPRT--HALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAE---AA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 179 DYAQEGGRAGKGRVIIEGFIDFD-YEITLLTV---RHVGGTT--FCAPVGHRQEKG-DYQeswqpqamSPVALAESERVA 251
Cdd:PRK02186 169 AHCAALRRAGTRAALVQAYVEGDeYSVETLTVargHQVLGITrkHLGPPPHFVEIGhDFP--------APLSAPQRERIV 240
|
170 180 190
....*....|....*....|....*....|....*.
gi 1785561342 252 KAVTEALGGRGL-FG---VELFIKGDQVWFSEVSPR 283
Cdd:PRK02186 241 RTVLRALDAVGYaFGpahTELRVRGDTVVIIEINPR 276
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
135-202 |
1.96e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 49.77 E-value: 1.96e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 135 ADTFEDYSKAVQDLGFPCVVKPVMSSSGKGQSL-LRSADDVQKAWDYAQEGGRAgkgrVIIEGFID-FDY 202
Cdd:PRK14016 235 VTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESSD----VIVERYIPgKDH 300
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
127-205 |
1.07e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 46.64 E-value: 1.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785561342 127 LPTSPYHFADTFEDYSKAVQDLGFPCVVKPVMSSSGKGQSLLRSADDVQKAWDYAQEGGragkGRVIIEGFIDFDyEIT 205
Cdd:PRK01372 111 LPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKYD----DEVLVEKYIKGR-ELT 184
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
123-225 |
1.17e-04 |
|
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: 42.65 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 123 EELDLPTSPYhfaDTFEDYSKA---VQDLGFP-CVVKPVMSSSGKGQSLlrsADDVQKAWDYAQE------GGRAGKgRV 192
Cdd:pfam01071 11 KRYGIPTAEY---ETFTDPEEAksyIQEAGFPaIVVKADGLAAGKGVIV---ASSNEEAIKAVDEileqkkFGEAGE-TV 83
|
90 100 110
....*....|....*....|....*....|...
gi 1785561342 193 IIEGFIDfDYEITLLTVrhVGGTTFcAPVGHRQ 225
Cdd:pfam01071 84 VIEEFLE-GEEVSVLAF--VDGKTV-KPLPPAQ 112
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
70-283 |
1.76e-04 |
|
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: 43.71 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 70 VIEAEKPHFIVPeieaiatgTL---------VELEAEGF----TVIPTARAAL-LTMNREGIRRLAaEELDLPTSPYHFA 135
Cdd:COG0458 65 IIEKEKPDGVIV--------QFggqtalnlaVELEEAGIlegvKILGTSPDAIdLAEDRELFKELL-DKLGIPQPKSGTA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 136 DTFEDYSKAVQDLGFPCVVKP--VMSSSGKGQsllrsADDVQKAWDYAQEGGRA-GKGRVIIEGFID----FDYEItllt 208
Cdd:COG0458 136 TSVEEALAIAEEIGYPVIVRPsyVLGGRGMGI-----VYNEEELEEYLERALKVsPDHPVLIDESLLgakeIEVDV---- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 209 VRHVGGTTFCA-------PVG-HrqeKGDYQESWQPQAMSPVALAESERVAKAVTEALGGRGLFGVELFIKGDQVWFSEV 280
Cdd:COG0458 207 VRDGEDNVIIVgimehiePAGvH---SGDSICVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEV 283
|
...
gi 1785561342 281 SPR 283
Cdd:COG0458 284 NPR 286
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
103-199 |
4.97e-04 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 42.03 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 103 PTARAALLTMNREGIRRLAaEELDLPTSPYhfaDTFEDYSKA---VQDLGFPCVVKPVMSSSGKGQSLLRSADDVQKAWD 179
Cdd:PLN02257 92 PSAEAAALEGSKNFMKDLC-DKYKIPTAKY---ETFTDPAAAkkyIKEQGAPIVVKADGLAAGKGVVVAMTLEEAYEAVD 167
|
90 100
....*....|....*....|...
gi 1785561342 180 ---YAQEGGRAGkGRVIIEGFID 199
Cdd:PLN02257 168 smlVKGAFGSAG-SEVVVEEFLD 189
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
13-211 |
7.42e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 41.55 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 13 TRVLMCGCGELGKEVVIELQRLGVEVIAVDRYANAPAMQV--AHRSHVInmldGAA--------LRAVIEAEKphfiVPE 82
Cdd:PRK06111 3 QKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVkmADEAYLI----GGPrvqesylnLEKIIEIAK----KTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 83 IEAI--ATGTLVE-------LEAEGFTVIPTARAALLTMNREGIRRLAAEELDLPTSP-YHFA-DTFEDYSKAVQDLGFP 151
Cdd:PRK06111 75 AEAIhpGYGLLSEnasfaerCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPgITTNlEDAEEAIAIARQIGYP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785561342 152 CVVKPVMSSSGKGQSLLRSADDVQKAWDYAQEGGRA--GKGRVIIEGFIDF--DYEITLLTVRH 211
Cdd:PRK06111 155 VMLKASAGGGGIGMQLVETEQELTKAFESNKKRAANffGNGEMYIEKYIEDprHIEIQLLADTH 218
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
110-199 |
2.23e-03 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 39.72 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 110 LTMNREGIRRLAAEeLDLPTSPYHF----ADTFEDYSKAVQDLGFPCVVKPVMSSSGKGQSLLRSADDVQKAWDYAQEGG 185
Cdd:PRK01966 120 LSMDKILTKRLLAA-AGIPVAPYVVltrgDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYD 198
|
90
....*....|....
gi 1785561342 186 RagkgRVIIEGFID 199
Cdd:PRK01966 199 R----KVLVEQGIK 208
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
7-204 |
2.43e-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: 39.98 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 7 PLSPTATRVLMCGCGEL-----------GKEVVIELQRLGVEVIAVDryANAPAMQVAHR-SHVINM--LDGAALRAVIE 72
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIvigqaaefdysGSQACKALKEEGYRVILVN--SNPATIMTDPEmADKVYIepLTPEAVEKIIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561342 73 AEKPHFIVPEI---EAIATGTLVE----LEAEGFTVIPTARAAL-LTMNREGIRRlAAEELDLPTSPYHFADTFEDYSKA 144
Cdd:TIGR01369 79 KERPDAILPTFggqTALNLAVELEesgvLEKYGVEVLGTPVEAIkKAEDRELFRE-AMKEIGEPVPESEIAHSVEEALAA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785561342 145 VQDLGFPCVVKPVMSSSGKGQSLLRSADDVQKAwdyAQEGGRAGK-GRVIIE----GFIDFDYEI 204
Cdd:TIGR01369 158 AKEIGYPVIVRPAFTLGGTGGGIAYNREELKEI---AERALSASPiNQVLVEkslaGWKEIEYEV 219
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
21-80 |
6.80e-03 |
|
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.
Pssm-ID: 396097 [Multi-domain] Cd Length: 238 Bit Score: 37.66 E-value: 6.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785561342 21 GELGKEVVIELQRLGVEVIAVDRYANAPAMQVAHRSHVI--NMLDGAALRAVIEAEKPHFIV 80
Cdd:pfam01370 8 GFIGSHLVRRLLEKGYEVIGLDRLTSASNTARLADLRFVegDLTDRDALEKLLADVRPDAVI 69
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