|
Name |
Accession |
Description |
Interval |
E-value |
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
19-369 |
0e+00 |
|
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: 543.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 19 QLGKMMAVSAKQMGYKVAVVDPVKDSPCGQVADIEITAHYNDREAIRKLAEISDIITYEFENIDYDALHWLKDHAYLPQG 98
Cdd:COG0026 1 QLGRMLALAAKRLGYRVHVLDPDPDSPAAQVADEHIVADYDDEEALREFAERCDVVTFEFENVPAEALEALEAEVPVRPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 99 SELLLITQNRETEKKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGYDGKGQFVIKEETQMEQAAVLLEHG 178
Cdd:COG0026 81 PEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRRGGYDGKGQVVIKSAADLEAAWAALGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 179 TCILESWVSFKMELSVIVVRSANGEVSTFPAAENIHHNNILFQSIVPARVEEGIQKKAATLAVKLADELNLVGPLAVEMF 258
Cdd:COG0026 161 PCILEEFVPFERELSVIVARSPDGEVATYPVVENVHRNGILDESIAPARISEALAAEAEEIAKRIAEALDYVGVLAVEFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 259 LTEDGELLVNELAPRPHNSGHYTLDLCETSQFEQHIRAVCGLPLGKTDLLKPGMMVNLLGDEVkLAEEEPELLKE--AKL 336
Cdd:COG0026 241 VTKDGELLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVCGLPLGDTELLSPAVMVNLLGDDW-EDPGWEALLALpgAHL 319
|
330 340 350
....*....|....*....|....*....|...
gi 1036601543 337 YIYGKHEIKKGRKMGHITFMKKPEDDWIQEITN 369
Cdd:COG0026 320 HLYGKKEARPGRKMGHVTVLGDDLEEALERARA 352
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
19-367 |
0e+00 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 530.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 19 QLGKMMAVSAKQMGYKVAVVDPVKDSPCGQVADIEITAHYNDREAIRKLAEISDIITYEFENIDYDALHWLKDHAYLPQG 98
Cdd:PRK06019 12 QLGRMLALAAAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEQCDVITYEFENVPAEALDALAARVPVPPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 99 SELLLITQNRETEKKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGYDGKGQFVIKEETQMEQAAVLLEHG 178
Cdd:PRK06019 92 PDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRRGGYDGKGQWVIRSAEDLEAAWALLGSV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 179 TCILESWVSFKMELSVIVVRSANGEVSTFPAAENIHHNNILFQSIVPARVEEGIQKKAATLAVKLADELNLVGPLAVEMF 258
Cdd:PRK06019 172 PCILEEFVPFEREVSVIVARGRDGEVVFYPLVENVHRNGILRTSIAPARISAELQAQAEEIASRIAEELDYVGVLAVEFF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 259 LTEDGELLVNELAPRPHNSGHYTLDLCETSQFEQHIRAVCGLPLGKTDLLKPGMMVNLLGDEvKLAEEEPELLK--EAKL 336
Cdd:PRK06019 252 VTGDGELLVNEIAPRPHNSGHWTIEACSTSQFEQHLRAILGLPLGTTRLLSPAVMVNLLGDD-WLEPRWDALLAlpGAHL 330
|
330 340 350
....*....|....*....|....*....|.
gi 1036601543 337 YIYGKHEIKKGRKMGHITFMKKPEDDWIQEI 367
Cdd:PRK06019 331 HLYGKAEARPGRKMGHVTVLGDDVEALLAKL 361
|
|
| purK |
TIGR01161 |
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole ... |
19-359 |
1.31e-178 |
|
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: 499.94 E-value: 1.31e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 19 QLGKMMAVSAKQMGYKVAVVDPVKDSPCGQVADIEITAHYNDREAIRKLAEISDIITYEFENIDYDALHWLK-DHAYLPQ 97
Cdd:TIGR01161 9 QLGRMLALAARPLGIKVHVLDPDANSPAVQVADHVVLAPFFDPAAIRELAESCDVITFEFEHVDVEALEKLEaRGVKLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 98 GSELLLITQNRETEKKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGYDGKGQFVIKEETQMEQAAVLLEH 177
Cdd:TIGR01161 89 SPDALAIIQDRLTQKQFLQKLGLPVPPFLVIKDEEELDAALQELGFPVVLKARTGGYDGRGQYRIRNEADLPQAAKELGD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 178 GTCILESWVSFKMELSVIVVRSANGEVSTFPAAENIHHNNILFQSIVPARVEEGIQKKAATLAVKLADELNLVGPLAVEM 257
Cdd:TIGR01161 169 RECIVEEFVPFERELSVIVARSADGETAFYPVVENIHQDGILRYVVAPAAVPDAIQARAEEIARRLMEELGYVGVLAVEM 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 258 FLTEDGELLVNELAPRPHNSGHYTLDLCETSQFEQHIRAVCGLPLGKTDLLKPGMMVNLLG--DEVKLAEEEPELLKEAK 335
Cdd:TIGR01161 249 FVLPDGRLLINELAPRVHNSGHYTLDGCSTSQFEQHLRAILGLPLGSTELLLPSVMVNLLGteDDVIPLWEEILALPGAK 328
|
330 340
....*....|....*....|....
gi 1036601543 336 LYIYGKHEIKKGRKMGHITFMKKP 359
Cdd:TIGR01161 329 LHWYGKAEVRPGRKVGHVNLVGSD 352
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
116-283 |
8.01e-84 |
|
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: 252.56 E-value: 8.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 116 QAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGYDGKGQFVIKEETQMEQAAVLLEHGTCILESWVSFKMELSVI 195
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGYDGKGQYVVRSEADLPQAWEELGDGPVIVEEFVPFDRELSVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 196 VVRSANGEVSTFPAAENIHHNNILFQSIVPARVEEGIQKKAATLAVKLADELNLVGPLAVEMFLTEDGELLVNELAPRPH 275
Cdd:pfam02222 81 VVRSVDGETAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAPRPH 160
|
....*...
gi 1036601543 276 NSGHYTLD 283
Cdd:pfam02222 161 NSGHYTLD 168
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
19-369 |
0e+00 |
|
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: 543.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 19 QLGKMMAVSAKQMGYKVAVVDPVKDSPCGQVADIEITAHYNDREAIRKLAEISDIITYEFENIDYDALHWLKDHAYLPQG 98
Cdd:COG0026 1 QLGRMLALAAKRLGYRVHVLDPDPDSPAAQVADEHIVADYDDEEALREFAERCDVVTFEFENVPAEALEALEAEVPVRPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 99 SELLLITQNRETEKKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGYDGKGQFVIKEETQMEQAAVLLEHG 178
Cdd:COG0026 81 PEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRRGGYDGKGQVVIKSAADLEAAWAALGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 179 TCILESWVSFKMELSVIVVRSANGEVSTFPAAENIHHNNILFQSIVPARVEEGIQKKAATLAVKLADELNLVGPLAVEMF 258
Cdd:COG0026 161 PCILEEFVPFERELSVIVARSPDGEVATYPVVENVHRNGILDESIAPARISEALAAEAEEIAKRIAEALDYVGVLAVEFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 259 LTEDGELLVNELAPRPHNSGHYTLDLCETSQFEQHIRAVCGLPLGKTDLLKPGMMVNLLGDEVkLAEEEPELLKE--AKL 336
Cdd:COG0026 241 VTKDGELLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVCGLPLGDTELLSPAVMVNLLGDDW-EDPGWEALLALpgAHL 319
|
330 340 350
....*....|....*....|....*....|...
gi 1036601543 337 YIYGKHEIKKGRKMGHITFMKKPEDDWIQEITN 369
Cdd:COG0026 320 HLYGKKEARPGRKMGHVTVLGDDLEEALERARA 352
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
19-367 |
0e+00 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 530.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 19 QLGKMMAVSAKQMGYKVAVVDPVKDSPCGQVADIEITAHYNDREAIRKLAEISDIITYEFENIDYDALHWLKDHAYLPQG 98
Cdd:PRK06019 12 QLGRMLALAAAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEQCDVITYEFENVPAEALDALAARVPVPPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 99 SELLLITQNRETEKKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGYDGKGQFVIKEETQMEQAAVLLEHG 178
Cdd:PRK06019 92 PDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRRGGYDGKGQWVIRSAEDLEAAWALLGSV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 179 TCILESWVSFKMELSVIVVRSANGEVSTFPAAENIHHNNILFQSIVPARVEEGIQKKAATLAVKLADELNLVGPLAVEMF 258
Cdd:PRK06019 172 PCILEEFVPFEREVSVIVARGRDGEVVFYPLVENVHRNGILRTSIAPARISAELQAQAEEIASRIAEELDYVGVLAVEFF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 259 LTEDGELLVNELAPRPHNSGHYTLDLCETSQFEQHIRAVCGLPLGKTDLLKPGMMVNLLGDEvKLAEEEPELLK--EAKL 336
Cdd:PRK06019 252 VTGDGELLVNEIAPRPHNSGHWTIEACSTSQFEQHLRAILGLPLGTTRLLSPAVMVNLLGDD-WLEPRWDALLAlpGAHL 330
|
330 340 350
....*....|....*....|....*....|.
gi 1036601543 337 YIYGKHEIKKGRKMGHITFMKKPEDDWIQEI 367
Cdd:PRK06019 331 HLYGKAEARPGRKMGHVTVLGDDVEALLAKL 361
|
|
| purK |
TIGR01161 |
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole ... |
19-359 |
1.31e-178 |
|
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: 499.94 E-value: 1.31e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 19 QLGKMMAVSAKQMGYKVAVVDPVKDSPCGQVADIEITAHYNDREAIRKLAEISDIITYEFENIDYDALHWLK-DHAYLPQ 97
Cdd:TIGR01161 9 QLGRMLALAARPLGIKVHVLDPDANSPAVQVADHVVLAPFFDPAAIRELAESCDVITFEFEHVDVEALEKLEaRGVKLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 98 GSELLLITQNRETEKKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGYDGKGQFVIKEETQMEQAAVLLEH 177
Cdd:TIGR01161 89 SPDALAIIQDRLTQKQFLQKLGLPVPPFLVIKDEEELDAALQELGFPVVLKARTGGYDGRGQYRIRNEADLPQAAKELGD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 178 GTCILESWVSFKMELSVIVVRSANGEVSTFPAAENIHHNNILFQSIVPARVEEGIQKKAATLAVKLADELNLVGPLAVEM 257
Cdd:TIGR01161 169 RECIVEEFVPFERELSVIVARSADGETAFYPVVENIHQDGILRYVVAPAAVPDAIQARAEEIARRLMEELGYVGVLAVEM 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 258 FLTEDGELLVNELAPRPHNSGHYTLDLCETSQFEQHIRAVCGLPLGKTDLLKPGMMVNLLG--DEVKLAEEEPELLKEAK 335
Cdd:TIGR01161 249 FVLPDGRLLINELAPRVHNSGHYTLDGCSTSQFEQHLRAILGLPLGSTELLLPSVMVNLLGteDDVIPLWEEILALPGAK 328
|
330 340
....*....|....*....|....
gi 1036601543 336 LYIYGKHEIKKGRKMGHITFMKKP 359
Cdd:TIGR01161 329 LHWYGKAEVRPGRKVGHVNLVGSD 352
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
19-354 |
1.72e-101 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 311.61 E-value: 1.72e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 19 QLGKMMAVSAKQMGYKVAVVDPVKDSPCGQVADIEITAHYNDREAIRKLAEISDIITYEFENIDYDALHWLKDhaylpQG 98
Cdd:PLN02948 32 QLGRMLCQAASQMGIKVKVLDPLEDCPASSVAARHVVGSFDDRAAVREFAKRCDVLTVEIEHVDVDTLEALEK-----QG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 99 ------SELLLITQNRETEKKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGYDGKGQFVIKEETQMEQAA 172
Cdd:PLN02948 107 vdvqpkSSTIRIIQDKYAQKVHFSKHGIPLPEFMEIDDLESAEKAGDLFGYPLMLKSRRLAYDGRGNAVAKTEEDLSSAV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 173 VLL---EHGTCIlESWVSFKMELSVIVVRSANGEVSTFPAAENIHHNNILFQSIVPARVEEGIQKKAATLAVKLADELNL 249
Cdd:PLN02948 187 AALggfERGLYA-EKWAPFVKELAVMVARSRDGSTRCYPVVETIHKDNICHVVEAPANVPWKVAKLATDVAEKAVGSLEG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 250 VGPLAVEMFLTEDGELLVNELAPRPHNSGHYTLDLCETSQFEQHIRAVCGLPLGKTDLLKPG-MMVNLLGDevklAEEEP 328
Cdd:PLN02948 266 AGVFGVELFLLKDGQILLNEVAPRPHNSGHYTIEACYTSQFEQHLRAVLGLPLGDTSMKVPAaIMYNILGE----DEGEA 341
|
330 340 350
....*....|....*....|....*....|....*...
gi 1036601543 329 EL------------LKEAKLYIYGKHEIKKGRKMGHIT 354
Cdd:PLN02948 342 GFrlahqlmgralnIPGASVHWYGKPEMRKQRKMGHIT 379
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
116-283 |
8.01e-84 |
|
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: 252.56 E-value: 8.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 116 QAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGYDGKGQFVIKEETQMEQAAVLLEHGTCILESWVSFKMELSVI 195
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGYDGKGQYVVRSEADLPQAWEELGDGPVIVEEFVPFDRELSVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 196 VVRSANGEVSTFPAAENIHHNNILFQSIVPARVEEGIQKKAATLAVKLADELNLVGPLAVEMFLTEDGELLVNELAPRPH 275
Cdd:pfam02222 81 VVRSVDGETAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAPRPH 160
|
....*...
gi 1036601543 276 NSGHYTLD 283
Cdd:pfam02222 161 NSGHYTLD 168
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
20-351 |
4.43e-37 |
|
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: 137.95 E-value: 4.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 20 LGKMMAVSAKQMGYKVAVVDPVKDSPCGQVAD----IEITahynDREAIRKLAEIS--DIITYEFENIDYDALHWLKDha 93
Cdd:COG0027 23 LGKEVAIELQRLGVEVIAVDRYANAPAMQVAHrsyvIDML----DGDALRALIEREkpDFIVPEIEAIATDALVELEA-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 94 ylpQGSELL------LITQNREtekkAIQ--AA---GCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGYdGKGQFVI 162
Cdd:COG0027 97 ---EGFRVVptaravRLTMNRE----GIRrlAAeelGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSSS-GKGQSVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 163 KEETQMEQA---AVllEHG-----TCILESWVSFKMELSVIVVRSANGEVSTFPAAENIHHNNILFQSIVPARVEEGIQK 234
Cdd:COG0027 169 RSPADIEAAweyAQ--EGGrggagRVIVEGFVDFDYEITLLTVRAVDGPTHFCEPIGHRQEDGDYRESWQPQPMSEAALA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 235 KAATLAVKLADELNLVGPLAVEMFLTEDgELLVNELAPRPHNSGHYTL---DLcetSQFEQHIRAVCGLPLGKTDLLKPG 311
Cdd:COG0027 247 KAQEIAKKVTDALGGRGIFGVELFVKGD-EVYFSEVSPRPHDTGMVTLisqDL---SEFALHARAILGLPVPEIRLVGPA 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1036601543 312 ----MMVNLLGDEVKLAEEEPEL-LKEAKLYIYGKHEIKKGRKMG 351
Cdd:COG0027 323 asavILAEGESWAPAFDGLAEALaVPGTDLRLFGKPEAYGRRRMG 367
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
20-351 |
4.82e-36 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 135.26 E-value: 4.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 20 LGKMMAVSAKQMGYKVAVVDPVKDSPCGQVAD----IEITahynDREAIRKL--AEISDIITYEFENIDYDALHWLKDha 93
Cdd:PRK09288 23 LGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHrshvIDML----DGDALRAVieREKPDYIVPEIEAIATDALVELEK-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 94 ylpQGSELL------LITQNREtekkAIQ--AA---GCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGyDGKGQFVI 162
Cdd:PRK09288 97 ---EGFNVVptaratRLTMNRE----GIRrlAAeelGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS-SGKGQSVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 163 KEETQMEQA---AVllEHG-----TCILESWVSFKMELSVIVVRSANGEVStFPAAenIHHNnilfQ-------SIVPAR 227
Cdd:PRK09288 169 RSPEDIEKAweyAQ--EGGrggagRVIVEEFIDFDYEITLLTVRAVDGGTH-FCAP--IGHR----QedgdyreSWQPQP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 228 VEEGIQKKAATLAVKLADELNLVGPLAVEMFLTEDgELLVNELAPRPHNSGHYTL---DLcetSQFEQHIRAVCGLPLGK 304
Cdd:PRK09288 240 MSPAALEEAQEIAKKVTDALGGRGLFGVELFVKGD-EVYFSEVSPRPHDTGMVTLisqNL---SEFELHARAILGLPIPD 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1036601543 305 TDLLKPGMMVNLLGDE---------VKLAEEEPellkEAKLYIYGKHEIKKGRKMG 351
Cdd:PRK09288 316 IRLYSPAASAVILAEGesanpsfdgLAEALAVP----GTDVRLFGKPEIRGGRRMG 367
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
112-301 |
6.37e-14 |
|
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: 71.06 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 112 KKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTcRGGYDGKGQFVIKEETQMEQA--------AVLLEHGTCILE 183
Cdd:COG0439 59 REALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKP-ADGAGSRGVRVVRDEEELEAAlaearaeaKAGSPNGEVLVE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 184 SWVSfKMELSV--------IVVRSANGEVSTFPAAENIHHnnilfqsIVPARVEEGIQKKAATLAVKLADELNLV-GPLA 254
Cdd:COG0439 138 EFLE-GREYSVeglvrdgeVVVCSITRKHQKPPYFVELGH-------EAPSPLPEELRAEIGELVARALRALGYRrGAFH 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1036601543 255 VEMFLTEDGELLVNELAPRPhnSGHYTLDLCE----TSQFEQHIRAVCGLP 301
Cdd:COG0439 210 TEFLLTPDGEPYLIEINARL--GGEHIPPLTElatgVDLVREQIRLALGEP 258
|
|
| PurK_C |
pfam17769 |
Phosphoribosylaminoimidazole carboxylase C-terminal domain; This entry represents the ... |
313-355 |
3.52e-13 |
|
Phosphoribosylaminoimidazole carboxylase C-terminal domain; This entry represents the C-terminal domain of the PurK enzyme.
Pssm-ID: 436029 [Multi-domain] Cd Length: 56 Bit Score: 63.73 E-value: 3.52e-13
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1036601543 313 MVNLLGDEVKLAEEEPELLKEAKLYIYGKHEIKKGRKMGHITF 355
Cdd:pfam17769 3 MVNLLGEELGEGLEELLAIPGAHLHLYGKEEARPGRKMGHVTV 45
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
112-269 |
4.54e-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: 66.28 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 112 KKAIQAAGCEVAPYSIVNTKD--ELKQGVQELGLPAVLKTCRGGyDGKGQFVIKEETQMEQA-AVLLEHGTCIL-ESWVS 187
Cdd:COG1181 100 KRVLAAAGLPTPPYVVLRRGElaDLEAIEEELGLPLFVKPAREG-SSVGVSKVKNAEELAAAlEEAFKYDDKVLvEEFID 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 188 fKMELSVIVVrsANGEVSTFPAAENIHHNNIL-FQS---------IVPARVEEGIQKKAATLAVKLADELNLVGpLA-VE 256
Cdd:COG1181 179 -GREVTVGVL--GNGGPRALPPIEIVPENGFYdYEAkytdggteyICPARLPEELEERIQELALKAFRALGCRG-YArVD 254
|
170
....*....|...
gi 1036601543 257 MFLTEDGELLVNE 269
Cdd:COG1181 255 FRLDEDGEPYLLE 267
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
116-274 |
2.04e-09 |
|
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: 56.94 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 116 QAAGCEVAPYSIV-------NTKDELKQGVQELGLPAVLKTCRGGyDGKGQFVIKEETQMEQAAVL-LEH-GTCILESWV 186
Cdd:pfam07478 3 KAAGLPVVPFVTFtradwklNPKEWCAQVEEALGYPVFVKPARLG-SSVGVSKVESREELQAAIEEaFQYdEKVLVEEGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 187 SFK-MELSVIvvrsANGEVSTFPAAE--------NIHHNNIL--FQSIVPARVEEGIQKKAATLAVKLADELNLVGPLAV 255
Cdd:pfam07478 82 EGReIECAVL----GNEDPEVSPVGEivpsggfyDYEAKYIDdsAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARV 157
|
170
....*....|....*....
gi 1036601543 256 EMFLTEDGELLVNELAPRP 274
Cdd:pfam07478 158 DFFLTEDGEIVLNEVNTIP 176
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
112-265 |
4.65e-06 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 47.80 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 112 KKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGyDGKGQFVIKEETQMEQAAVL-LEHGTCIL-ESWVSfK 189
Cdd:PRK01372 103 KLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREG-SSVGVSKVKEEDELQAALELaFKYDDEVLvEKYIK-G 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 190 MELSVIVVrsaNGEVstFPAAEnIHHNNILF-----------QSIVPARVEEGIQKKAATLAVKLADELNLVGPLAVEMF 258
Cdd:PRK01372 181 RELTVAVL---GGKA--LPVIE-IVPAGEFYdyeakylaggtQYICPAGLPAEIEAELQELALKAYRALGCRGWGRVDFM 254
|
....*..
gi 1036601543 259 LTEDGEL 265
Cdd:PRK01372 255 LDEDGKP 261
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
104-273 |
7.53e-05 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 44.99 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 104 ITQNRETEKKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLktcRGGY--DGKGQFVIKEETQMEQ-----AAVLLE 176
Cdd:TIGR01369 666 RAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLV---RPSYvlGGRAMEIVYNEEELRRyleeaVAVSPE 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 177 HGTCIlESWVSFKMELSVIVVrSANGEVSTFPAAENIH----HNNILFQSIVPARVEEGIQKKAATLAVKLADELNLVGP 252
Cdd:TIGR01369 743 HPVLI-DKYLEDAVEVDVDAV-SDGEEVLIPGIMEHIEeagvHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGL 820
|
170 180
....*....|....*....|.
gi 1036601543 253 LAVEmFLTEDGELLVNELAPR 273
Cdd:TIGR01369 821 MNIQ-FAVKDGEVYVIEVNPR 840
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
104-269 |
2.16e-04 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 42.80 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 104 ITQNRETEKKAIQAAGCEVAPYSIVNTKDELKQGVQE----LGLPAVLKTCRGG-----YdgkgqfVIKEETQMEQA-AV 173
Cdd:PRK01966 120 LSMDKILTKRLLAAAGIPVAPYVVLTRGDWEEASLAEieakLGLPVFVKPANLGssvgiS------KVKNEEELAAAlDL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 174 LLEHGTCIL-ESWVSFKmELSVIVVRSaNGEVStfPAAENIHHNNIL-FQS---------IVPARVEEGIQKKAATLAVK 242
Cdd:PRK01966 194 AFEYDRKVLvEQGIKGR-EIECAVLGN-DPKAS--VPGEIVKPDDFYdYEAkyldgsaelIIPADLSEELTEKIRELAIK 269
|
170 180
....*....|....*....|....*...
gi 1036601543 243 LADELNLVGpLA-VEMFLTEDGELLVNE 269
Cdd:PRK01966 270 AFKALGCSG-LArVDFFLTEDGEIYLNE 296
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
104-178 |
5.77e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 42.07 E-value: 5.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036601543 104 ITQNRETEKKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLKTCRGGYdGKGQFV-IKEETQMEQA-AVLLEHG 178
Cdd:PRK14016 211 IACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNH-GRGVTVnITTREEIEAAyAVASKES 286
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
104-273 |
4.18e-03 |
|
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: 39.09 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 104 ITQNRETEKKAIQAAGCEVAPYSIVNTKDELKQGVQELGLPAVLktcRGGY--DGKGQFVIKEETQMEQAA--------- 172
Cdd:COG0458 111 LAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIV---RPSYvlGGRGMGIVYNEEELEEYLeralkvspd 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601543 173 --VLLEHGtciLESWVsfkmELSVIVVRSANGEVSTFPAAENI-----HHNNilfqSIV--PARV--EEGIQK-KAATLa 240
Cdd:COG0458 188 hpVLIDES---LLGAK----EIEVDVVRDGEDNVIIVGIMEHIepagvHSGD----SICvaPPQTlsDKEYQRlRDATL- 255
|
170 180 190
....*....|....*....|....*....|...
gi 1036601543 241 vKLADELNLVGPLAVEmFLTEDGELLVNELAPR 273
Cdd:COG0458 256 -KIARALGVVGLCNIQ-FAVDDGRVYVIEVNPR 286
|
|
| |
