|
Name |
Accession |
Description |
Interval |
E-value |
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
6-386 |
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: 768.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 6 RLGTPLSPSATRVMLLGAGELGKEVIIALQRLGVEVIAVDRYPDAPGHQVAHRAHVIDMTDAAALRALVEAERPHLIVPE 85
Cdd:COG0027 3 TIGTPLSPNATKVMLLGSGELGKEVAIELQRLGVEVIAVDRYANAPAMQVAHRSYVIDMLDGDALRALIEREKPDFIVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 86 IEAIATDALAAIEAAGLaEVIPTARATQLTMNREGIRRLAAEELGLATSPYAFADSFDAFSAAVAKIGMPCVVKPVMSSS 165
Cdd:COG0027 83 IEAIATDALVELEAEGF-RVVPTARAVRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 166 GKGQSVVRSEADVKAAWDYAMAGGRVNHGRVIVEGFIDFDYEITQLTVRAIDpatlaTRTYFCEPVGHVQVAGDYVESWQ 245
Cdd:COG0027 162 GKGQSVVRSPADIEAAWEYAQEGGRGGAGRVIVEGFVDFDYEITLLTVRAVD-----GPTHFCEPIGHRQEDGDYRESWQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 246 PQPMSAAALQKSRDIAHKVTEALGGRGLFGVELFVRGDDVWFSEVSPRPHDTGLVTLASQRQSEFELHARAILGLPVD-P 324
Cdd:COG0027 237 PQPMSEAALAKAQEIAKKVTDALGGRGIFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQDLSEFALHARAILGLPVPeI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500215451 325 TLGSPAASAVIYGGLDERGIAFEGVRDALAVPGADLRLFGKPESFVKRRMGVALATGANVDE 386
Cdd:COG0027 317 RLVGPAASAVILAEGESWAPAFDGLAEALAVPGTDLRLFGKPEAYGRRRMGVALATADDVEE 378
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
6-386 |
0e+00 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 750.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 6 RLGTPLSPSATRVMLLGAGELGKEVIIALQRLGVEVIAVDRYPDAPGHQVAHRAHVIDMTDAAALRALVEAERPHLIVPE 85
Cdd:PRK09288 3 RLGTPLSPSATRVMLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSHVIDMLDGDALRAVIEREKPDYIVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 86 IEAIATDALAAIEAAGlAEVIPTARATQLTMNREGIRRLAAEELGLATSPYAFADSFDAFSAAVAKIGMPCVVKPVMSSS 165
Cdd:PRK09288 83 IEAIATDALVELEKEG-FNVVPTARATRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 166 GKGQSVVRSEADVKAAWDYAMAGGRVNHGRVIVEGFIDFDYEITQLTVRAIDPATLatrtyFCEPVGHVQVAGDYVESWQ 245
Cdd:PRK09288 162 GKGQSVVRSPEDIEKAWEYAQEGGRGGAGRVIVEEFIDFDYEITLLTVRAVDGGTH-----FCAPIGHRQEDGDYRESWQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 246 PQPMSAAALQKSRDIAHKVTEALGGRGLFGVELFVRGDDVWFSEVSPRPHDTGLVTLASQRQSEFELHARAILGLPV-DP 324
Cdd:PRK09288 237 PQPMSPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQNLSEFELHARAILGLPIpDI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500215451 325 TLGSPAASAVIYGGLDERGIAFEGVRDALAVPGADLRLFGKPESFVKRRMGVALATGANVDE 386
Cdd:PRK09288 317 RLYSPAASAVILAEGESANPSFDGLAEALAVPGTDVRLFGKPEIRGGRRMGVALATGEDVEE 378
|
|
| purT |
TIGR01142 |
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN ... |
17-386 |
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: 577.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 17 RVMLLGAGELGKEVIIALQRLGVEVIAVDRYPDAPGHQVAHRAHVIDMTDAAALRALVEAERPHLIVPEIEAIATDALAA 96
Cdd:TIGR01142 1 RVLLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSYVINMLDGDALRAVIEREKPDYIVPEIEAIATDALFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 97 IEAAGLaEVIPTARATQLTMNREGIRRLAAEELGLATSPYAFADSFDAFSAAVAKIGMPCVVKPVMSSSGKGQSVVRSEA 176
Cdd:TIGR01142 81 LEKEGY-FVVPNARATKLTMNREGIRRLAAEELGLPTSRYMFADSLDELREAVEKIGYPCVVKPVMSSSGKGQSVVRGPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 177 DVKAAWDYAMAGGRVNHGRVIVEGFIDFDYEITQLTVRAIDPATLatrtyFCEPVGHVQVAGDYVESWQPQPMSAAALQK 256
Cdd:TIGR01142 160 DIEKAWEYAQEGARGGAGRVIVEEFIDFDYEITLLTVRHVDGNTT-----FCAPIGHRQIDGDYHESWQPQEMSEKALEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 257 SRDIAHKVTEALGGRGLFGVELFVRGDDVWFSEVSPRPHDTGLVTLASQRQSEFELHARAILGLPVDPTLG-SPAASAVI 335
Cdd:TIGR01142 235 AQRIAKRITDALGGYGLFGVELFVKGDEVIFSEVSPRPHDTGMVTLISQGLSEFALHVRAILGLPIPGIPQlGPAASAVI 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 500215451 336 YGGLDERGIAFEGVRDALAVPGADLRLFGKPESFVKRRMGVALATGANVDE 386
Cdd:TIGR01142 315 KAKVTGYSPAFRGLEKALSVPNTQVRLFGKPEAYVGRRLGVALATAKSVEA 365
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
26-386 |
4.79e-68 |
|
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: 219.18 E-value: 4.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 26 LGKEVIIALQRLGVEVIAVDRYPDAPGHQVAHRAHVIDMTDAAALRALveAERPHLIVPEIEAIATDALAAIEAAglAEV 105
Cdd:COG0026 2 LGRMLALAAKRLGYRVHVLDPDPDSPAAQVADEHIVADYDDEEALREF--AERCDVVTFEFENVPAEALEALEAE--VPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 106 IPTARATQLTMNRegIR-RLAAEELGLATSPYAFADSFDAFSAAVAKIGMPCVVKPV-MSSSGKGQSVVRSEADVKAAWD 183
Cdd:COG0026 78 RPGPEALEIAQDR--LLeKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrGGYDGKGQVVIKSAADLEAAWA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 184 yamaggRVNHGRVIVEGFIDFDYEITQLTVRAIDPATlatRTYfcePVGH-VQVAGDYVESWQPQPMSAAALQKSRDIAH 262
Cdd:COG0026 156 ------ALGGGPCILEEFVPFERELSVIVARSPDGEV---ATY---PVVEnVHRNGILDESIAPARISEALAAEAEEIAK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 263 KVTEALGGRGLFGVELFVRGDD-VWFSEVSPRPHDTGLVTLASQRQSEFELHARAILGLPV-DPTLGSPAASAVIYGGLD 340
Cdd:COG0026 224 RIAEALDYVGVLAVEFFVTKDGeLLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVCGLPLgDTELLSPAVMVNLLGDDW 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 500215451 341 ERgiafEGVRDALAVPGADLRLFGKPESFVKRRMGVALATGANVDE 386
Cdd:COG0026 304 ED----PGWEALLALPGAHLHLYGKKEARPGRKMGHVTVLGDDLEE 345
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
127-304 |
1.83e-63 |
|
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: 200.94 E-value: 1.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 127 EELGLATSPYAFADSFDAFSAAVAKIGMPCVVK-PVMSSSGKGQSVVRSEADVKAAWDYAmaggrvNHGRVIVEGFIDFD 205
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKaRRGGYDGKGQYVVRSEADLPQAWEEL------GDGPVIVEEFVPFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 206 YEITQLTVRAIDpatlaTRTYFCEPVGHVQVAGDYVESWQPQPMSAAALQKSRDIAHKVTEALGGRGLFGVELFVRGD-D 284
Cdd:pfam02222 75 RELSVLVVRSVD-----GETAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDgD 149
|
170 180
....*....|....*....|
gi 500215451 285 VWFSEVSPRPHDTGLVTLAS 304
Cdd:pfam02222 150 LLINELAPRPHNSGHYTLDG 169
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
21-375 |
1.16e-57 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 192.67 E-value: 1.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 21 LGAGELGKEVIIALQRLGVEVIAVDRYPDAPGHQVAHRAHVIDMTDAAALRALveAERPHLIVPEIEAIATDALAAIEAA 100
Cdd:PRK06019 8 IGGGQLGRMLALAAAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALREL--AEQCDVITYEFENVPAEALDALAAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 101 GLaeVIPTARATQLTMNREGIRRLAAeELGLATSPYAFADSFDAFSAAVAKIGMPCVVKpvmSSS----GKGQSVVRSEA 176
Cdd:PRK06019 86 VP--VPPGPDALAIAQDRLTEKQFLD-KLGIPVAPFAVVDSAEDLEAALADLGLPAVLK---TRRggydGKGQWVIRSAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 177 DVKAAWDyamaggRVNHGRVIVEGFIDFDYEITQLTVRAIDPatlATRTYfcePVGH-VQVAG--DYVESwqPQPMSAAA 253
Cdd:PRK06019 160 DLEAAWA------LLGSVPCILEEFVPFEREVSVIVARGRDG---EVVFY---PLVEnVHRNGilRTSIA--PARISAEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 254 LQKSRDIAHKVTEALGGRGLFGVELFVRGDD-VWFSEVSPRPHDTGLVTLASQRQSEFELHARAILGLPV-DPTLGSPAA 331
Cdd:PRK06019 226 QAQAEEIASRIAEELDYVGVLAVEFFVTGDGeLLVNEIAPRPHNSGHWTIEACSTSQFEQHLRAILGLPLgTTRLLSPAV 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 500215451 332 SAVIYGGLDErgiaFEGVRDALAVPGADLRLFGKPESFVKRRMG 375
Cdd:PRK06019 306 MVNLLGDDWL----EPRWDALLALPGAHLHLYGKAEARPGRKMG 345
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
9-375 |
5.96e-48 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 171.78 E-value: 5.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 9 TPLSPSATRVMLLGAGELGKEVIIALQRLGVEVIAVDRYPDAPGHQVAHRAHVIDMTDAAALRALveAERPHLIVPEIEA 88
Cdd:PLN02948 16 PVHGVSETVVGVLGGGQLGRMLCQAASQMGIKVKVLDPLEDCPASSVAARHVVGSFDDRAAVREF--AKRCDVLTVEIEH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 89 IATDALAAIEAAGLaEVIPTARaTQLTMNREGIRRLAAEELGLATSPYAFADSFDAFSAAVAKIGMPCVVKPV-MSSSGK 167
Cdd:PLN02948 94 VDVDTLEALEKQGV-DVQPKSS-TIRIIQDKYAQKVHFSKHGIPLPEFMEIDDLESAEKAGDLFGYPLMLKSRrLAYDGR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 168 GQSVVRSEADVKAAwdyAMAGGRVNHGrVIVEGFIDFDYEITQLTVRAIDPATLA---TRTYFCEPVGHVQVAgdyvesw 244
Cdd:PLN02948 172 GNAVAKTEEDLSSA---VAALGGFERG-LYAEKWAPFVKELAVMVARSRDGSTRCypvVETIHKDNICHVVEA------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 245 qPQPMSAAALQKSRDIAHKVTEALGGRGLFGVELFVRGD-DVWFSEVSPRPHDTGLVTLASQRQSEFELHARAILGLPV- 322
Cdd:PLN02948 241 -PANVPWKVAKLATDVAEKAVGSLEGAGVFGVELFLLKDgQILLNEVAPRPHNSGHYTIEACYTSQFEQHLRAVLGLPLg 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 500215451 323 DPTLGSPAasAVIYGGLDER------GIAFEGVRDALAVPGADLRLFGKPESFVKRRMG 375
Cdd:PLN02948 320 DTSMKVPA--AIMYNILGEDegeagfRLAHQLMGRALNIPGASVHWYGKPEMRKQRKMG 376
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
70-295 |
9.02e-20 |
|
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: 88.01 E-value: 9.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 70 LRALVEAERPHLIVPEIEAI-ATDALAAIEAAGLAEV--IPTARATQLTMNREGIR-RLAAEELGLATSPYAFADSFDAF 145
Cdd:COG0439 2 IDAIIAAAAELARETGIDAVlSESEFAVETAAELAEElgLPGPSPEAIRAMRDKVLmREALAAAGVPVPGFALVDSPEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 146 SAAVAKIGMPCVVKPVMSSSGKGQSVVRSEADVKAAWDYAMAGGRVN--HGRVIVEGFIDfDYEITqltvraIDPATLAT 223
Cdd:COG0439 82 LAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGspNGEVLVEEFLE-GREYS------VEGLVRDG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500215451 224 RTYFCEPVGHVQVAGDYVES--WQPQPMSAAALQKSRDIAHKVTEALG-GRGLFGVELFVRGDD-VWFSEVSPRPH 295
Cdd:COG0439 155 EVVVCSITRKHQKPPYFVELghEAPSPLPEELRAEIGELVARALRALGyRRGAFHTEFLLTPDGePYLIEINARLG 230
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
17-293 |
8.33e-14 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 71.84 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 17 RVMLLGAGElGKEVIIALQR--LGVEVIAVDRYPDAPGHQVAHRAHVI-DMTDAAALRALVE---AERPHLIVP----EI 86
Cdd:PRK12767 3 NILVTSAGR-RVQLVKALKKslLKGRVIGADISELAPALYFADKFYVVpKVTDPNYIDRLLDickKEKIDLLIPlidpEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 87 EAIAtDALAAIEAAGL------AEVIPTARATQLTMNregirrlAAEELGLATSPYAFADSFDAFSAA--VAKIGMPCVV 158
Cdd:PRK12767 82 PLLA-QNRDRFEEIGVkvlvssKEVIEICNDKWLTYE-------FLKENGIPTPKSYLPESLEDFKAAlaKGELQFPLFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 159 KPVMSSSGKGQSVVRSEADVKAAWDYA---MAGGRVNHGRVIVEGFIDFDYEIT------QLTVRAidpatlatrtyfce 229
Cdd:PRK12767 154 KPRDGSASIGVFKVNDKEELEFLLEYVpnlIIQEFIEGQEYTVDVLCDLNGEVIsivprkRIEVRA-------------- 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500215451 230 pvGHVQ--VAGDYveswqpqpmsaaalQKSRDIAHKVTEALGGRGLFGVELFVRGDDVWFSEVSPR 293
Cdd:PRK12767 220 --GETSkgVTVKD--------------PELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPR 269
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
129-294 |
3.46e-13 |
|
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: 68.11 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 129 LGLATSPYAF---ADSF----DAFSAAVAKIGMPCVVKPVMSSSGKGQSVVRSEADVKAAWDYAmaggRVNHGRVIVEGF 201
Cdd:pfam07478 5 AGLPVVPFVTftrADWKlnpkEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEA----FQYDEKVLVEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 202 IDfdyeitqltVRAIDPATLATRTYFCEPVGHVQVAG---DYVESWQ--------PQPMSAAALQKSRDIAHKVTEALGG 270
Cdd:pfam07478 81 IE---------GREIECAVLGNEDPEVSPVGEIVPSGgfyDYEAKYIddsaqivvPADLEEEQEEQIQELALKAYKALGC 151
|
170 180
....*....|....*....|....*
gi 500215451 271 RGLFGVELFVRGDD-VWFSEVSPRP 294
Cdd:pfam07478 152 RGLARVDFFLTEDGeIVLNEVNTIP 176
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
27-290 |
8.72e-13 |
|
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: 68.59 E-value: 8.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 27 GKEVIIALQRLGVEVIAVDrypdapghqvahrahvidmTDAAALRALVEAERPHLIVPeieaiatdAL-----------A 95
Cdd:COG1181 21 GRAVAAALDKAGYDVVPIG-------------------IDVEDLPAALKELKPDVVFP--------ALhgrggedgtiqG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 96 AIEAAGLAEVIPTARATQLTMNREGIRRLAAEElGLATSPYAFADSFDA--FSAAVAKIGMPCVVKPVMSSSGKGQSVVR 173
Cdd:COG1181 74 LLELLGIPYTGSGVLASALAMDKALTKRVLAAA-GLPTPPYVVLRRGELadLEAIEEELGLPLFVKPAREGSSVGVSKVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 174 SEADVKAAWDYAMAGGRvnhgRVIVEGFID-FDYEItqltvraidpATLATRTYFCEPVGHVQVAG---DYVESWQ---- 245
Cdd:COG1181 153 NAEELAAALEEAFKYDD----KVLVEEFIDgREVTV----------GVLGNGGPRALPPIEIVPENgfyDYEAKYTdggt 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 500215451 246 ----PQPMSAAALQKSRDIAHKVTEALGGRGLFGVELFVRGDD-VWFSEV 290
Cdd:COG1181 219 eyicPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGePYLLEV 268
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
28-294 |
3.69e-12 |
|
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: 66.50 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 28 KEVIIALQRLGVEVIAVDRypdapghqvahRAHVIDMTDAAALRALVEAERPHLIVPEIEAI--ATDALAAIEAAGLAeV 105
Cdd:COG0189 17 KALIEAAQRRGHEVEVIDP-----------DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPPfyGLALLRQLEAAGVP-V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 106 IPTARATQLTMNREGIRRLAAEeLGLATSPYAFADSFDAFSAAVAKIGMPCVVKPVMSSSGKGQSVVRSEADVKAAWDYA 185
Cdd:COG0189 85 VNDPEAIRRARDKLFTLQLLAR-AGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 186 MAGGrvnHGRVIVEGFI----DFDY-------EItqLTVRAIDPATLATRTyfcepvgHVQVAGdyveSWQPQPMSAAAl 254
Cdd:COG0189 164 TELG---SEPVLVQEFIpeedGRDIrvlvvggEP--VAAIRRIPAEGEFRT-------NLARGG----RAEPVELTDEE- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 500215451 255 qksRDIAHKVTEALGGrGLFGVELFVRGDDVWFSEVSPRP 294
Cdd:COG0189 227 ---RELALRAAPALGL-DFAGVDLIEDDDGPLVLEVNVTP 262
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
12-205 |
2.87e-10 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 61.48 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 12 SPSATRVMLLGAGELGKEVIIALQRLGVEVIAVDRYPDAPG-------HQVAHRAHVIDMTD-AAALRALVEAERPHLIV 83
Cdd:COG3919 2 MTMRFRVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAarsryvdEVVVVPDPGDDPEAfVDALLELAERHGPDVLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 84 PEIEAiATDALAAIEAAgLAE--VIPTARATQLT--MNREGIRRLAaEELGLATSPYAFADSFDAFSAAVAKIGMPCVVK 159
Cdd:COG3919 82 PTGDE-YVELLSRHRDE-LEEhyRLPYPDADLLDrlLDKERFYELA-EELGVPVPKTVVLDSADDLDALAEDLGFPVVVK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500215451 160 PVMSSS--------GKGQSVVRSEADVKAAWDYAMAGGrvnhGRVIVEGFIDFD 205
Cdd:COG3919 159 PADSVGydelsfpgKKKVFYVDDREELLALLRRIAAAG----YELIVQEYIPGD 208
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
17-203 |
3.62e-10 |
|
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: 61.17 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 17 RVMLLGAGelGKEVIIAlQRLGVE--VIAVDRYPDAPGHQVAHRAHV--IDMTDAAALRALVEAERPHLIVPEIEAIATD 92
Cdd:TIGR00877 2 KVLVIGNG--GREHALA-WKLAQSplVKYVYVAPGNAGTARLAKNKNvaIEITDIEALVEFAKKKKIDLAIIGPEAPLVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 93 ALA-AIEAAGLAEVIPTARATQLTMNREGIRRLAaEELGLATSPYAFADSFDAFSAAVAKIGMPCVVKPVMSSSGKGQSV 171
Cdd:TIGR00877 79 GLVdALEEAGIPVFGPTKEAAQLEGSKAFAKDFM-KRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIV 157
|
170 180 190
....*....|....*....|....*....|...
gi 500215451 172 VRSEADVKAAWDYAMAGGRVNHG-RVIVEGFID 203
Cdd:TIGR00877 158 AKTNEEAIKAVEDILEQKFGDAGeRVVIEEFLD 190
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
127-293 |
7.02e-09 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 58.06 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 127 EELGLATSPYAFADSFDAFSAAVAKIGMPCVVKPVMSSSGKGQSVVRSEADVKAAwdyaMAGGRVNHGRVIVEGFID-FD 205
Cdd:PRK12815 679 DELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAY----LAENASQLYPILIDQFIDgKE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 206 YEITQLTvraiD--PATLATRTYFCEPVG-HvqvAGDYVESWQPQPMSAAALQKSRDIAHKVTEALGGRGLFGVELFVRG 282
Cdd:PRK12815 755 YEVDAIS----DgeDVTIPGIIEHIEQAGvH---SGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAN 827
|
170
....*....|.
gi 500215451 283 DDVWFSEVSPR 293
Cdd:PRK12815 828 DEIYVLEVNPR 838
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
50-203 |
1.35e-08 |
|
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: 56.17 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 50 APGH----QVAHRaHVIDMTDAAALRALVEAERPHLIVPEIEA-----IAtDALaaiEAAGLAEVIPTARATQLT----- 115
Cdd:COG0151 31 APGNagtaQLAEC-VDIDVTDIEALVAFAKEENIDLVVVGPEAplvagIV-DAF---RAAGIPVFGPSKAAAQLEgskaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 116 ----MNREGIRrlaaeelglaTSPYAFADSFDAFSAAVAKIGMPCVVKPVMSSSGKGQSVVRSEADVKAAWDYAMAGGRV 191
Cdd:COG0151 106 akefMARYGIP----------TAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLEEALAAVDDMLADGKF 175
|
170
....*....|....
gi 500215451 192 -NHG-RVIVEGFID 203
Cdd:COG0151 176 gDAGaRVVIEEFLE 189
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
117-293 |
1.59e-08 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 56.93 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 117 NREGIRRLAaEELGLATSPYAFADSFDAFSAAVAKIGMPCVVKPVMSSSGKGQSVVRSEADVKAAWDYAMAGGrVNHGrV 196
Cdd:TIGR01369 669 DREKFSELL-DELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVS-PEHP-V 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 197 IVEGFIDFDYEITqltvraIDPATLATRTYFCEPVGHVQVAG----DYVESWQPQPMSAAALQKSRDIAHKVTEALGGRG 272
Cdd:TIGR01369 746 LIDKYLEDAVEVD------VDAVSDGEEVLIPGIMEHIEEAGvhsgDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKG 819
|
170 180
....*....|....*....|.
gi 500215451 273 LFGVELFVRGDDVWFSEVSPR 293
Cdd:TIGR01369 820 LMNIQFAVKDGEVYVIEVNPR 840
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
27-272 |
4.78e-08 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 53.96 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 27 GKEVIIALQRLGVEVIAVDrypdaPGHQVAHRahvidmtdaaalralVEAERPhlivpeieAIATDAL-----------A 95
Cdd:PRK01372 25 GAAVLAALREAGYDAHPID-----PGEDIAAQ---------------LKELGF--------DRVFNALhgrggedgtiqG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 96 AIEAAGlaevIP-T---ARATQLTMNREgIRRLAAEELGLATSPYAFADSFDAFSAAVAKIGMPCVVKPVMSSSGKGQSV 171
Cdd:PRK01372 77 LLELLG----IPyTgsgVLASALAMDKL-RTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 172 VRSEADVKAAWDYAMAGGrvnhGRVIVEGFIDFDyEIT-------QLTVRAIDPAT---------LATRT-YFCepvghv 234
Cdd:PRK01372 152 VKEEDELQAALELAFKYD----DEVLVEKYIKGR-ELTvavlggkALPVIEIVPAGefydyeakyLAGGTqYIC------ 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 500215451 235 qvagdyveswqPQPMSAAALQKSRDIAHKVTEALGGRG 272
Cdd:PRK01372 221 -----------PAGLPAEIEAELQELALKAYRALGCRG 247
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
83-385 |
8.98e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 54.47 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 83 VPEIEAIATDALAAIEAAglAEV-----IPTARATQLTMNREGIR---RLAAEELGLatsPYAFADSFDAFSA-AVAKIG 153
Cdd:PRK02186 68 LDGVAGIMSSSEYFIEVA--SEVarrlgLPAANTEAIRTCRDKKRlarTLRDHGIDV---PRTHALALRAVALdALDGLT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 154 MPCVVKPVMSSSGKGQSVVRSEADvkaAWDYAMAGGRVNHGRVIVEGFIDFD-YEITQLTVRAIDPATLATRTYFCEPVG 232
Cdd:PRK02186 143 YPVVVKPRMGSGSVGVRLCASVAE---AAAHCAALRRAGTRAALVQAYVEGDeYSVETLTVARGHQVLGITRKHLGPPPH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 233 HVQVAGDYveswqPQPMSAAALQKSRDIAHKVTEALGGRglFG---VELFVRGDDVWFSEVSPRPHDtGLVTLASQRQ-- 307
Cdd:PRK02186 220 FVEIGHDF-----PAPLSAPQRERIVRTVLRALDAVGYA--FGpahTELRVRGDTVVIIEINPRLAG-GMIPVLLEEAfg 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 308 -SEFELHARAILGLPVDPTLGSPAASAV---------IYGGL----DERGIAFEGVRDALAVPGADLRLFGkpeSFvKRR 373
Cdd:PRK02186 292 vDLLDHVIDLHLGVAAFADPTAKRYGAIrfvlparsgVLRGLlflpDDIAARPELRFHPLKQPGDALRLEG---DF-RDR 367
|
330
....*....|..
gi 500215451 374 MGVALATGANVD 385
Cdd:PRK02186 368 IAAVVCAGDHRD 379
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
114-294 |
5.28e-07 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 50.89 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 114 LTMNREGIRRLAAEeLGLATSPYAFADSFDA----FSAAVAKIGMPCVVKPVMSSSGKGQSVVRSEADVKAAWDYAMAGG 189
Cdd:PRK01966 120 LSMDKILTKRLLAA-AGIPVAPYVVLTRGDWeeasLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 190 RvnhgRVIVEGFIDfDYEITqLTVRAIDPATLatrtyfcePVGHVQVAGD-------YVE-SWQ---PQPMSAAALQKSR 258
Cdd:PRK01966 199 R----KVLVEQGIK-GREIE-CAVLGNDPKAS--------VPGEIVKPDDfydyeakYLDgSAEliiPADLSEELTEKIR 264
|
170 180 190
....*....|....*....|....*....|....*..
gi 500215451 259 DIAHKVTEALGGRGLFGVELFVRGD-DVWFSEVSPRP 294
Cdd:PRK01966 265 ELAIKAFKALGCSGLARVDFFLTEDgEIYLNEINTMP 301
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
246-336 |
1.09e-06 |
|
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: 50.30 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 246 PQPMSAAALQKSRDIAHKVTEALGGRGLFGVELFVRGDDVWFSEVSPRPhdTGLVTL--ASQRQSEFELHARAILG-LP- 321
Cdd:COG2232 215 PLALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRP--QASLDLyeDATGGNLFDAHLRACRGeLPe 292
|
90
....*....|....*.
gi 500215451 322 -VDPTLGSPAASAVIY 336
Cdd:COG2232 293 vPRPKPRRVAAKAILY 308
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
10-208 |
3.61e-06 |
|
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: 49.23 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 10 PLSPSATRVMLLGAGEL-----------GKEVIIALQRLGVEVIAVDRYP-----DapgHQVAHRAHVIDMTdAAALRAL 73
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIvigqaaefdysGSQACKALKEEGYRVILVNSNPatimtD---PEMADKVYIEPLT-PEAVEKI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 74 VEAERPHLIVPEIE-------AIATDALAAIEAAGLaEVIPT-ARATQLTMNREGIRRlAAEELGLATSPYAFADSFDAF 145
Cdd:TIGR01369 77 IEKERPDAILPTFGgqtalnlAVELEESGVLEKYGV-EVLGTpVEAIKKAEDRELFRE-AMKEIGEPVPESEIAHSVEEA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500215451 146 SAAVAKIGMPCVVKPVMSSSGKGQSVVRSEADVKAAWDYAMAGGRVNhgRVIVE----GFIDFDYEI 208
Cdd:TIGR01369 155 LAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPIN--QVLVEkslaGWKEIEYEV 219
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
139-206 |
2.50e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 46.30 E-value: 2.50e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 139 ADSFDAFSAAVAKIGMPCVVKPVMSSSGKGQSV-VRSEADVKAAWDYAMAGGRvnhgRVIVEGFID-FDY 206
Cdd:PRK14016 235 VTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESS----DVIVERYIPgKDH 300
|
|
| RmlD_sub_bind |
pfam04321 |
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ... |
18-83 |
8.05e-05 |
|
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.
Pssm-ID: 427865 [Multi-domain] Cd Length: 284 Bit Score: 44.19 E-value: 8.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500215451 18 VMLLGA-GELGKEVIIALQRLGVEVIAVDRYPdapghqvahrahvIDMTDAAALRALVEAERPHLIV 83
Cdd:pfam04321 1 ILITGAnGQLGTELRRLLAERGIEVVALTRAE-------------LDLTDPEAVARLLREIKPDVVV 54
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
24-202 |
1.80e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 43.59 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 24 GELGKEVIIALQRLGVEVIAVdrYPDAPGHQVAHRahvidMTDAAALRALVEAERPHLIVPEIEAIATDALA-------- 95
Cdd:PRK12833 14 GEIAVRIIRAARELGMRTVAA--CSDADRDSLAAR-----MADEAVHIGPSHAAKSYLNPAAILAAARQCGAdaihpgyg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 96 ----------AIEAAGLAEVIPTARATQlTMNREGIRRLAAEELGLATSPYAFA--DSFDAFSAAVAKIGMPCVVKPVMS 163
Cdd:PRK12833 87 flsenaafaeAVEAAGLIFVGPDAQTIR-TMGDKARARRTARRAGVPTVPGSDGvvASLDAALEVAARIGYPLMIKAAAG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500215451 164 SSGKGQSVVRSEADVKAAWDYAM--AGGRVNHGRVIVEGFI 202
Cdd:PRK12833 166 GGGRGIRVAHDAAQLAAELPLAQreAQAAFGDGGVYLERFI 206
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
22-105 |
1.91e-04 |
|
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: 42.67 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 22 GAGELGKEVIIALQRLGVEVIAVDRYPDAPGHQVAHRAHVI--DMTDAAALRALVEAERPHLIVPeIEAIATDALAAIEA 99
Cdd:pfam01370 6 ATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTARLADLRFVegDLTDRDALEKLLADVRPDAVIH-LAAVGGVGASIEDP 84
|
....*.
gi 500215451 100 AGLAEV 105
Cdd:pfam01370 85 EDFIEA 90
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
17-132 |
7.51e-04 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 41.12 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 17 RVMLLGA-GELGKEVIIALQRLGVEVIAVDRYPD-APGHQVAHRAHVI--DMTDAAALRALVEaerphlivpEIEAIatd 92
Cdd:COG0451 1 RILVTGGaGFIGSHLARRLLARGHEVVGLDRSPPgAANLAALPGVEFVrgDLRDPEALAAALA---------GVDAV--- 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 500215451 93 alaaIEAAGLAEVIPTARATQLTMNREGIRRL--AAEELGLA 132
Cdd:COG0451 69 ----VHLAAPAGVGEEDPDETLEVNVEGTLNLleAARAAGVK 106
|
|
| Zn_ADH7 |
cd08261 |
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ... |
17-110 |
9.15e-04 |
|
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
Pssm-ID: 176222 [Multi-domain] Cd Length: 337 Bit Score: 41.02 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 17 RVMLLGAGELGKEVIIALQRLGVEVIAVDRYPD----APGHQVAHRAHVIDMTDAAALRALVEAERPHLIvpeIEaiATD 92
Cdd:cd08261 162 TVLVVGAGPIGLGVIQVAKARGARVIVVDIDDErlefARELGADDTINVGDEDVAARLRELTDGEGADVV---ID--ATG 236
|
90
....*....|....*...
gi 500215451 93 ALAAIEAAgLAEVIPTAR 110
Cdd:cd08261 237 NPASMEEA-VELVAHGGR 253
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
127-297 |
1.39e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 40.92 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 127 EELGLATSPYAFADSFDAFSAAVAKIGMPCVVKPVMSSSGKGQSVVRSEADVKAAWDYAMaggRVNHGR-VIVEGFIDfd 205
Cdd:PLN02735 711 NELKIEQPKGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAV---EVDPERpVLVDKYLS-- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500215451 206 yEITQLTVRAIdpatlatrtyfCEPVGHVQVAG--DYVE-----------SWQPQPMSAAALQKSRDIAHKVTEALGGRG 272
Cdd:PLN02735 786 -DATEIDVDAL-----------ADSEGNVVIGGimEHIEqagvhsgdsacSLPTQTIPSSCLATIRDWTTKLAKRLNVCG 853
|
170 180
....*....|....*....|....*.
gi 500215451 273 LFGVELFV-RGDDVWFSEVSPRPHDT 297
Cdd:PLN02735 854 LMNCQYAItPSGEVYIIEANPRASRT 879
|
|
| 2-Hacid_dh_11 |
cd12175 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ... |
6-54 |
3.43e-03 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240652 [Multi-domain] Cd Length: 311 Bit Score: 39.09 E-value: 3.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 500215451 6 RLGTPLSPSAT-----RVMLLGAGELGKEVIIALQRLGVEVIAVDRYPDAPGHQ 54
Cdd:cd12175 128 RWGRPEGRPSRelsgkTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRDPEAEE 181
|
|
| SerA |
COG0111 |
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ... |
17-50 |
4.69e-03 |
|
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439881 [Multi-domain] Cd Length: 314 Bit Score: 38.64 E-value: 4.69e-03
10 20 30
....*....|....*....|....*....|....
gi 500215451 17 RVMLLGAGELGKEVIIALQRLGVEVIAVDRYPDA 50
Cdd:COG0111 142 TVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPKP 175
|
|
| 2-Hacid_dh_C |
pfam02826 |
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ... |
17-69 |
7.85e-03 |
|
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.
Pssm-ID: 427007 [Multi-domain] Cd Length: 178 Bit Score: 37.09 E-value: 7.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 500215451 17 RVMLLGAGELGKEVIIALQRLGVEVIAVDRYPDAPGHQVAHRAHVIDMTDAAA 69
Cdd:pfam02826 38 TVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLA 90
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
17-73 |
9.03e-03 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 37.74 E-value: 9.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 500215451 17 RVMLLGAGELGKEVIIALQRLGVEVIAVDRYPDAPGHQVAHRAHVI--DMTDAAALRAL 73
Cdd:COG0569 97 HVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIvgDATDEEVLEEA 155
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
152-203 |
9.03e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 36.88 E-value: 9.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500215451 152 IGMPCVVKPVMSSSGKGQSVVRSEADVKAA----------WDYAMAGGRVNHGRVIVEGFID 203
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAfaaireeieqWKEMYPEAVVDGGSFLVEEYIE 62
|
|
| |
