|
Name |
Accession |
Description |
Interval |
E-value |
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
15-318 |
0e+00 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 535.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 15 PKAFGRVAVLFGGKSAEREVSLKSGAMVLQSLLAAGVDAFGIDVGEDLLQRLVEEKIDRAFIILHGRGGEDGSMQGLLEC 94
Cdd:PRK01372 1 PKMFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAHPIDPGEDIAAQLKELGFDRVFNALHGRGGEDGTIQGLLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 95 AGIPYTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIA 174
Cdd:PRK01372 81 LGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 175 AWREAARYDSQVLVEQWISGPEFTVATLRGQVLPAIRLGTPHTFYDYDAKYLASDTRYQVPCGLDEAKERELKELTARAC 254
Cdd:PRK01372 161 ALELAFKYDDEVLVEKYIKGRELTVAVLGGKALPVIEIVPAGEFYDYEAKYLAGGTQYICPAGLPAEIEAELQELALKAY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599606 255 DALGIQGWGRADVMQDAEGRFWLLEVNTAPGMTDHSLVPMAARAAGLDFQQLVLAILADSREAR 318
Cdd:PRK01372 241 RALGCRGWGRVDFMLDEDGKPYLLEVNTQPGMTSHSLVPMAARAAGISFSELVDRILEDALCDR 304
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
19-314 |
2.13e-156 |
|
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: 439.16 E-value: 2.13e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 19 GRVAVLFGGKSAEREVSLKSGAMVLQSLLAAGVDA--FGIDVgEDLLQRLVEEKIDRAFIILHGRGGEDGSMQGLLECAG 96
Cdd:COG1181 1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVvpIGIDV-EDLPAALKELKPDVVFPALHGRGGEDGTIQGLLELLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 97 IPYTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVLASED--DCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIA 174
Cdd:COG1181 80 IPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGElaDLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 175 AWREAARYDSQVLVEQWISGPEFTVATLRG---QVLPAIRLGTPHTFYDYDAKYLASDTRYQVPCGLDEAKERELKELTA 251
Cdd:COG1181 160 ALEEAFKYDDKVLVEEFIDGREVTVGVLGNggpRALPPIEIVPENGFYDYEAKYTDGGTEYICPARLPEELEERIQELAL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599606 252 RACDALGIQGWGRADVMQDAEGRFWLLEVNTAPGMTDHSLVPMAARAAGLDFQQLVLAILADS 314
Cdd:COG1181 240 KAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMTPTSLLPKAAAAAGISYEELIERIIELA 302
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
20-314 |
4.06e-151 |
|
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: 426.32 E-value: 4.06e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 20 RVAVLFGGKSAEREVSLKSGAMVLQSLLAAGVDAFGIDVGE-------DLLQRLVE-----EKIDRAFIILHGRGGEDGS 87
Cdd:TIGR01205 1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKmgswtykDLPQLILElgallEGIDVVFPVLHGRYGEDGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 88 MQGLLECAGIPYTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVL------ASEDDCREAAQRLGFPLIVKPAHEGSSI 161
Cdd:TIGR01205 81 IQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLtqnrasADELECEQVAEPLGFPVIVKPAREGSSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 162 GMAKVGGLDELIAAWREAARYDSQVLVEQWISGPEFTVATLR-GQVLPAIRLGTPHT-FYDYDAKYLASDTRYQVPCGLD 239
Cdd:TIGR01205 161 GVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGnEEALPIIEIVPEIEgFYDYEAKYLDGSTEYVIPAPLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599606 240 EAKERELKELTARACDALGIQGWGRADVMQDAEGRFWLLEVNTAPGMTDHSLVPMAARAAGLDFQQLVLAILADS 314
Cdd:TIGR01205 241 EELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTIPGMTAISLFPKAAAAAGIEFSQLVERILELA 315
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
20-307 |
8.96e-100 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 296.65 E-value: 8.96e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 20 RVAVLFGGKSAEREVSLKSGAMVLQSLLAAG--VDAFGID------VGEDLLQRL------------------VEEKIDR 73
Cdd:PRK01966 5 RVALLFGGRSAEHEVSLVSAKSVLKALDKEKyeVVPIGITkdgrwyLIDADNMELadddndkedlsllilpsgGSEEVDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 74 AFIILHGRGGEDGSMQGLLECAGIPYTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVL----ASEDDCREAAQRLGFP 149
Cdd:PRK01966 85 VFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLtrgdWEEASLAEIEAKLGLP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 150 LIVKPAHEGSSIGMAKVGGLDELIAAWREAARYDSQVLVEQWISGPEFTVATL--RGQVLP--AIRlgTPHTFYDYDAKY 225
Cdd:PRK01966 165 VFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLgnDPKASVpgEIV--KPDDFYDYEAKY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 226 LASDTRYQVPCGLDEAKERELKELTARACDALGIQGWGRADVMQDAEGRFWLLEVNTAPGMTDHSLVPMAARAAGLDFQQ 305
Cdd:PRK01966 243 LDGSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMPGFTPISMYPKLWEASGLSYPE 322
|
..
gi 15599606 306 LV 307
Cdd:PRK01966 323 LI 324
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
20-315 |
7.11e-79 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 242.27 E-value: 7.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 20 RVAVLFGGKSAEREVSLKSGAMVLQSLLAAGVDAFGIDV-GEDLLQRLVEEKIDRAFIILHGRGGEDGSMQGLLECAGIP 98
Cdd:PRK14569 5 KIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAVGVDAsGKELVAKLLELKPDKCFVALHGEDGENGRVSALLEMLEIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 99 YTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVLAsedDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWRE 178
Cdd:PRK14569 85 HTSSSMKSSVITMDKMISKEILMHHRMPTPMAKFLT---DKLVAEDEISFPVAVKPSSGGSSIATFKVKSIQELKHAYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 179 AARYdSQVLVEQWISGPEFTVATLRGQVLPAIRLGTPHTFYDYDAKYlASDTRYQVPCGLDEAKERELKELTARACDALG 258
Cdd:PRK14569 162 ASKY-GEVMIEQWVTGKEITVAIVNDEVYSSVWIEPQNEFYDYESKY-SGKSIYHSPSGLCEQKELEVRQLAKKAYDLLG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599606 259 IQGWGRADVMQDAEGRFWLLEVNTAPGMTDHSLVPMAARAAGLDFQQLVLAILADSR 315
Cdd:PRK14569 240 CSGHARVDFIYDDRGNFYIMEINSSPGMTDNSLSPKSAAAEGVDFDSFVKRIIEQAQ 296
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
119-311 |
7.49e-75 |
|
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: 228.74 E-value: 7.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 119 VWLSLGLPTPDYAVLASEDD-------CREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWREAARYDSQVLVEQW 191
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTRADWklnpkewCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 192 ISGPEFTVATL---RGQVLPAIRLGTPHTFYDYDAKYLASDTRYQVPCGLDEAKERELKELTARACDALGIQGWGRADVM 268
Cdd:pfam07478 81 IEGREIECAVLgneDPEVSPVGEIVPSGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDFF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15599606 269 QDAEGRFWLLEVNTAPGMTDHSLVPMAARAAGLDFQQLVLAIL 311
Cdd:pfam07478 161 LTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLI 203
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
20-311 |
4.14e-72 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 225.09 E-value: 4.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 20 RVAVLFGGKSAEREVSLKSGAMVLQSLLAAGVDAFGIDVGEDLLQRLVE-EKIDRAFIILHGRGGEDGSMQGLLECAGIP 98
Cdd:PRK14571 2 RVALLMGGVSREREISLRSGERVKKALEKLGYEVTVFDVDEDFLKKVDQlKSFDVVFNVLHGTFGEDGTLQAILDFLGIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 99 YTGSGVLASALAMDKLRTKRVwLSLGLPTPDYAVLASEDDcreaAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWRE 178
Cdd:PRK14571 82 YTGSDAFSSMICFDKLLTYRF-LKGTVEIPDFVEIKEFMK----TSPLGYPCVVKPRREGSSIGVFICESDEEFQHALKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 179 A-ARYDSqVLVEQWISGPEFTVATLRG----QVLPAIRLGTPHTFYDYDAKYLASDTRYQVPCGLDEAKERELKELTARA 253
Cdd:PRK14571 157 DlPRYGS-VIVQEYIPGREMTVSILETekgfEVLPILELRPKRRFYDYVAKYTKGETEFILPAPLNPEEERLVKETALKA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599606 254 CDALGIQGWGRAD-VMQDaeGRFWLLEVNTAPGMTDHSLVPMAARAAGLDFQQLVLAIL 311
Cdd:PRK14571 236 FVEAGCRGFGRVDgIFSD--GRFYFLEINTVPGLTELSDLPASAKAGGIEFEELVDIII 292
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
20-306 |
4.40e-48 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 164.31 E-value: 4.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 20 RVAVLFGGKSAEREVSLKSGAMVLQSLLAAGVDA----------------------FGIDVGEDLLQRLVEEK------- 70
Cdd:PRK14572 3 KIAVFFGGSSTEHSISIRTGCFICATLHTMGHSVkpilltpdggwvvptvyrpsipDESGNSEDLFLEEFQKAngvsepa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 71 ------IDRAFIILHGRGGEDGSMQGLLECAGIPYTGSGVLASALAMDKLRTKRVWLSLGLP-TPDYAV--LASEDDCRE 141
Cdd:PRK14572 83 disqldADIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKvAPFFELekLKYLNSPRK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 142 AAQRL---GFPLIVKPAHEGSSIGMAKVGGLDELIAAWREAARYDSQVLVEQWISGPEFTVATL---RGQ-----VLPAI 210
Cdd:PRK14572 163 TLLKLeslGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVLeryRGGkrnpiALPAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 211 RLGTPHTFYDYDAKYLASDTRYQVPCGLDEAKERELKELTARACDALGIQGWGRADVMQdAEGRFWLLEVNTAPGMTDHS 290
Cdd:PRK14572 243 EIVPGGEFFDFESKYKQGGSEEITPARISDQEMKRVQELAIRAHESLGCKGYSRTDFII-VDGEPHILETNTLPGMTETS 321
|
330
....*....|....*.
gi 15599606 291 LVPMAARAAGLDFQQL 306
Cdd:PRK14572 322 LIPQQAKAAGINMEEV 337
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
14-307 |
6.35e-43 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 157.29 E-value: 6.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 14 DPKAFGrVAVLFGGKSAEREVSLKSGAMVLQSL----------------LAAGVDAFGIDVGED---------LLQRLve 68
Cdd:PRK14573 448 EPKKLS-LGLVCGGKSCEHDISLLSAKNIAKYLspefydvsyflinrqgLWETVSSLETAIEEDsgksvlsseIAQAL-- 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 69 EKIDRAFIILHGRGGEDGSMQGLLECAGIPYTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVLA------SEDDC-RE 141
Cdd:PRK14573 525 AKVDVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQPLTlagwkrEPELClAH 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 142 AAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWREAARYDSQVLVEQWISGP-EFTVATLrGQVLPAIRLGTPHT--- 217
Cdd:PRK14573 605 IVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEESRLGSrEIEVSCL-GDGSSAYVIAGPHErrg 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 218 ---FYDYDAKY-LASDTRYQVPCGLD---EAKEReLKELTARACDALGIQGWGRADVMQDAEGRFWLLEVNTAPGMTDHS 290
Cdd:PRK14573 684 sggFIDYQEKYgLSGKSSAQIVFDLDlskESQEQ-VLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMNPIPGMTEAS 762
|
330
....*....|....*..
gi 15599606 291 LVPMAARAAGLDFQQLV 307
Cdd:PRK14573 763 PFLTAFVRKGWTYEQIV 779
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
96-316 |
5.03e-38 |
|
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: 135.77 E-value: 5.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 96 GIPYTGsgvLASALAM-DKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIA 174
Cdd:COG0439 40 GLPGPS---PEAIRAMrDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 175 AWREAARY------DSQVLVEQWISGPEFTVATL--RGQVLPAI---RLGTPHTFYdydakylasDTRYQVPCGLDEAKE 243
Cdd:COG0439 117 ALAEARAEakagspNGEVLVEEFLEGREYSVEGLvrDGEVVVCSitrKHQKPPYFV---------ELGHEAPSPLPEELR 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599606 244 RELKELTARACDALGIQ-GWGRADVMQDAEGRFWLLEVNT-APGmtDHsLVPMAARAAGLDFQQLVLAILADSRE 316
Cdd:COG0439 188 AEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINArLGG--EH-IPPLTELATGVDLVREQIRLALGEPR 259
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
70-307 |
1.35e-33 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 126.48 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 70 KIDRAFIILHGRGGEDGSMQGLLECAGIPYTGSGVLASALAMDKLRTKRVWLSLGLP--------TPDYaVLASEDDCRE 141
Cdd:PRK14570 87 EIDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPlvpfigfrKYDY-FLDKEGIKKD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 142 AAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWREAARYDSQVLVEQWISGPEFTVATLRGQvlpAIRLGTP------ 215
Cdd:PRK14570 166 IKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIGNE---QIKIFTPgeivvq 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 216 -HTFYDYDAKYL---ASDTRYQVPCGLDEAKERELKELTARACDALGIQGWGRAD-VMQDAEGRFWLLEVNTAPGMTDHS 290
Cdd:PRK14570 243 dFIFYDYDAKYStipGNSIVFNIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDfLIEKDTGLIYLNEINTIPGFTDIS 322
|
250
....*....|....*..
gi 15599606 291 LVPMAARAAGLDFQQLV 307
Cdd:PRK14570 323 MFAKMCEHDGLQYKSLV 339
|
|
| Dala_Dala_lig_N |
pfam01820 |
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the ... |
20-102 |
1.82e-27 |
|
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4 which is thought to be involved in substrate binding. 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). This domain is structurally related to the PreATP-grasp domain.
Pssm-ID: 460346 [Multi-domain] Cd Length: 118 Bit Score: 103.45 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 20 RVAVLFGGKSAEREVSLKSGAMVLQSLLAAG--VDAFGID----VGEDLLQRL--------------------------- 66
Cdd:pfam01820 1 KVAVLFGGRSSEHEVSLVSARSVLKALDKEKyeVIPIGITkdgrLGEAALRELasddglllevddapdggpagllfgpnv 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 15599606 67 --VEEKIDRAFIILHGRGGEDGSMQGLLECAGIPYTGS 102
Cdd:pfam01820 81 leLLIEVDVVFPVLHGPNGEDGTLQGLLELAGIPYVGS 118
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
106-309 |
3.75e-16 |
|
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: 77.29 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 106 ASALAMDKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWRE-AARYDS 184
Cdd:COG0189 90 AIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEAlTELGSE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 185 QVLVEQWI---SGPEFTVATLRGQVLPAI-RLGTPHTFYDydakYLASDTRYQvPCGLDEakerELKELTARACDALGIq 260
Cdd:COG0189 170 PVLVQEFIpeeDGRDIRVLVVGGEPVAAIrRIPAEGEFRT----NLARGGRAE-PVELTD----EERELALRAAPALGL- 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15599606 261 GWGRADVMQDAEGrFWLLEVNTAPGmtdhslVPMAARAAGLDFQQLVLA 309
Cdd:COG0189 240 DFAGVDLIEDDDG-PLVLEVNVTPG------FRGLERATGVDIAEAIAD 281
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
97-303 |
7.64e-16 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 77.28 E-value: 7.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 97 IPYTGSGVLASAlaMDKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGG-------- 168
Cdd:COG3919 104 LPYPDADLLDRL--LDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPADSVGYDELSFPGKkkvfyvdd 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 169 LDELIAAWREAARYDSQVLVEQWISGP---EFTVATL---RGQVLPA----IRLGTPHTFydydakylasdtryQVPCGL 238
Cdd:COG3919 182 REELLALLRRIAAAGYELIVQEYIPGDdgeMRGLTAYvdrDGEVVATftgrKLRHYPPAG--------------GNSAAR 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599606 239 DEAKERELKELTARACDALGIQGWGRADVMQDAE-GRFWLLEVNTAPGMTdhslVPMAArAAGLDF 303
Cdd:COG3919 248 ESVDDPELEEAARRLLEALGYHGFANVEFKRDPRdGEYKLIEINPRFWRS----LYLAT-AAGVNF 308
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
106-263 |
5.74e-13 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 68.63 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 106 ASALAMDKLRTKRvwLS---LGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWREA--- 179
Cdd:PRK09288 107 ATRLTMNREGIRR--LAaeeLGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPEDIEKAWEYAqeg 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 180 ARYDSQ-VLVEQWIsgP---EFTVATLRgQVLPAIRLGTP--HTFYDYDakYLASdtrYQvPCGLDEAKERELKELTARA 253
Cdd:PRK09288 185 GRGGAGrVIVEEFI--DfdyEITLLTVR-AVDGGTHFCAPigHRQEDGD--YRES---WQ-PQPMSPAALEEAQEIAKKV 255
|
170
....*....|
gi 15599606 254 CDALGiqGWG 263
Cdd:PRK09288 256 TDALG--GRG 263
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
102-216 |
1.20e-12 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 68.26 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 102 SGVLASALAMDKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPA---H-EGSSIGmakVGGLDELIAAWR 177
Cdd:PRK14016 204 TSAIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLdgnHgRGVTVN---ITTREEIEAAYA 280
|
90 100 110
....*....|....*....|....*....|....*....
gi 15599606 178 EAARYDSQVLVEQWISGPEFTVATLRGQVLPAIRLGTPH 216
Cdd:PRK14016 281 VASKESSDVIVERYIPGKDHRLLVVGGKLVAAARREPPH 319
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
106-192 |
1.08e-11 |
|
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: 64.71 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 106 ASALAM--DKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGss-iGMAKVGGLDELIAAWREAARy 182
Cdd:COG0026 81 PEALEIaqDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRRGGydgkGQVVIKSAADLEAAWAALGG- 159
|
90
....*....|
gi 15599606 183 dSQVLVEQWI 192
Cdd:COG0026 160 -GPCILEEFV 168
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
106-263 |
1.39e-11 |
|
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: 64.76 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 106 ASALAMDKLRTKRvwLS---LGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWREA--- 179
Cdd:COG0027 107 AVRLTMNREGIRR--LAaeeLGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPADIEAAWEYAqeg 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 180 ARYDSQ-VLVEQWIsgpEF-------TVATLRGQV--LPAIrlGtpHTFYDYDakYLASdtrYQvPCGLDEAKERELKEL 249
Cdd:COG0027 185 GRGGAGrVIVEGFV---DFdyeitllTVRAVDGPThfCEPI--G--HRQEDGD--YRES---WQ-PQPMSEAALAKAQEI 251
|
170
....*....|....
gi 15599606 250 TARACDALGiqGWG 263
Cdd:COG0027 252 AKKVTDALG--GRG 263
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
106-258 |
3.20e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 64.10 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 106 ASALAMDKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWREAARYDS- 184
Cdd:PRK02186 101 AIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTr 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 185 QVLVEQWISGPEFTVATL---RGQVLPAI---RLGTPHTFYDydakyLASDtryqVPCGLDEAKERELKELTARACDALG 258
Cdd:PRK02186 181 AALVQAYVEGDEYSVETLtvaRGHQVLGItrkHLGPPPHFVE-----IGHD----FPAPLSAPQRERIVRTVLRALDAVG 251
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
101-281 |
3.88e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 62.98 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 101 GSGVLAS-----ALAMDKLRTKRVWLSLGLPTPDYAVLASEDDCREA--AQRLGFPLIVKPAHEGSSIGMAKVGGLDELi 173
Cdd:PRK12767 95 GVKVLVSskeviEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEEL- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 174 aawREAARYDSQVLVEQWISGPEFTVATLR---GQVL---PAIRLGTphtfydydakyLASDTrYQVPCGLDEakerELK 247
Cdd:PRK12767 174 ---EFLLEYVPNLIIQEFIEGQEYTVDVLCdlnGEVIsivPRKRIEV-----------RAGET-SKGVTVKDP----ELF 234
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15599606 248 ELTARACDALG------IQGWgradvmqDAEGRFWLLEVN 281
Cdd:PRK12767 235 KLAERLAEALGargplnIQCF-------VTDGEPYLFEIN 267
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
123-261 |
7.05e-11 |
|
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: 59.96 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 123 LGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGSS-IGMAKVGGLDELIAAWREAAryDSQVLVEQWIS-GPEFTVA 200
Cdd:pfam02222 3 LGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGYDgKGQYVVRSEADLPQAWEELG--DGPVIVEEFVPfDRELSVL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599606 201 TLR---GQVL--PAIrlGTPHTFYDYDAKYlasdtryqVPCGLDEAKERELKELTARACDALGIQG 261
Cdd:pfam02222 81 VVRsvdGETAfyPVV--ETIQEDGICRLSV--------APARVPQAIQAEAQDIAKRLVDELGGVG 136
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
95-309 |
5.83e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 60.04 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 95 AGIPYTGSGVLASALAMDKLRTKRVWLSLGLPT---PDYAvLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDE 171
Cdd:PRK06111 98 EGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVvpgITTN-LEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 172 LIAAW----REAARY--DSQVLVEQWISGP---EFtvatlrgQVLpAIRLGtpHTFYDYDaKYLASDTRYQ-----VPC- 236
Cdd:PRK06111 177 LTKAFesnkKRAANFfgNGEMYIEKYIEDPrhiEI-------QLL-ADTHG--NTVYLWE-RECSVQRRHQkvieeAPSp 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599606 237 GLDEAKERELKELTARACDALGIQGWGRADVMQDAEGRFWLLEVNTAPgMTDHslvPMAARAAGLDF--QQLVLA 309
Cdd:PRK06111 246 FLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRL-QVEH---PVTEEITGIDLveQQLRIA 316
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
146-281 |
6.61e-10 |
|
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: 56.91 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 146 LGFPLIVKPAHEGSSIGMAKVGGLDELIAA----------WREaaRYDSQV------LVEQWISGPEFTV-ATLRGQVLP 208
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAfaaireeieqWKE--MYPEAVvdggsfLVEEYIEGEEFAVdAYFDENGEP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599606 209 AIRLGTPHTFydYDAKYLaSDTRYQVPCGLDEAKERELKELTARACDALGI-QGWGRADVMQDAEGRFWLLEVN 281
Cdd:pfam13535 79 VILNILKHDF--ASSEDV-SDRIYVTSASIIRETQAAFTEFLKRINALLGLkNFPVHIELRVDEDGQIIPIEVN 149
|
|
| LysX_arch |
TIGR02144 |
Lysine biosynthesis enzyme LysX; The family of proteins found in this equivalog include the ... |
91-284 |
1.80e-09 |
|
Lysine biosynthesis enzyme LysX; The family of proteins found in this equivalog include the characterized LysX from Thermus thermophilus, which is part of a well-organized lysine biosynthesis gene cluster. LysX is believed to carry out an ATP-dependent acylation of the amino group of alpha-aminoadipate in the prokaryotic version of the fungal AAA lysine biosynthesis pathway. No species having a sequence in this equivalog contains the elements of the more common diaminopimelate lysine biosythesis pathway, and none has been shown to be a lysine auxotroph. These sequences have mainly recieved the name of the related enzyme, "ribosomal protein S6 modification protein RimK". RimK has been characterized in E. coli, and acts by ATP-dependent condensation of S6 with glutamate residues.
Pssm-ID: 273994 [Multi-domain] Cd Length: 280 Bit Score: 57.79 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 91 LLECAGIPytgsgVLASALAM----DKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAhEGSSIGM-AK 165
Cdd:TIGR02144 67 LLEALGVP-----VINSSHAIeacgDKIFTYLKLAKAGVPTPRTYLAFDREAALKAAEALGYPVVLKPV-IGSWGRLvAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 166 VGGLDEL--IAAWREAARyDSQV---LVEQWISGPE--FTVATLRGQVLPAIrlgtphtfYDYDAKYLASDTR--YQVPC 236
Cdd:TIGR02144 141 VRDRDEAeaLLEHKEVLG-GSQLklfYIQEYINKPGrdIRVFVIGDEAIAAI--------YRYSNHWRTNTARggKAEPC 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15599606 237 GLDEakerELKELTARACDALGIqGWGRADVMQDAEGRFWLLEVNTAP 284
Cdd:TIGR02144 212 PLDE----EIEELAVKAAEAVGG-GVVAIDIFESKERGLLVNEVNHVP 254
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
122-194 |
6.13e-09 |
|
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: 56.81 E-value: 6.13e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599606 122 SLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWREAARY--DSQVLVEQWISG 194
Cdd:COG0458 124 KLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLERALKVspDHPVLIDESLLG 198
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
112-299 |
7.36e-09 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 55.00 E-value: 7.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 112 DKLRTKRVWLSLGLPT-PDYAVLA-SEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWREA------ARYD 183
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTvPGTAGPVeTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALAlaeapaAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 184 SQVLVEQWISGP-EFTVATLRGQVLPAIRLGTPHTFydyDAKYlASDTRYQVPC-GLDEAKERELKELTARACDALGIQG 261
Cdd:pfam02786 81 PQVLVEKSLKGPkHIEYQVLRDAHGNCITVCNRECS---DQRR-TQKSIEVAPSqTLTDEERQMLREAAVKIARHLGYVG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15599606 262 WGRADVMQDAE-GRFWLLEVNT--------APGMTDHSLVPMAARAA 299
Cdd:pfam02786 157 AGTVEFALDPFsGEYYFIEMNTrlqvehalAEKATGYDLAKEAAKIA 203
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
60-199 |
3.79e-08 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 54.59 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 60 EDLLQRLVEEKIDraFIILhGRGGEDGS--MQGLLEcAGIPYTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVLASED 137
Cdd:PRK12815 620 EDVLNVAEAENIK--GVIV-QFGGQTAInlAKGLEE-AGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEE 695
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599606 138 DCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWREAARYDSQVLVEQWISGPEFTV 199
Cdd:PRK12815 696 EAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPILIDQFIDGKEYEV 757
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
66-316 |
1.71e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 52.34 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 66 LVEE--KIDRAFIIlhgRGGEDGSM--QGLLECAGIPYTGSGVLASAlAMDKLRTKRVWLSLGLPTPDYAVLASEDDCR- 140
Cdd:PRK07206 62 LVEFlrKLGPEAII---AGAESGVElaDRLAEILTPQYSNDPALSSA-RRNKAEMINALAEAGLPAARQINTADWEEAEa 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 141 --EAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWR----EAARYD---SQVLVEQWISGPEFTVAT--LRGQVLPA 209
Cdd:PRK07206 138 wlRENGLIDRPVVIKPLESAGSDGVFICPAKGDWKHAFNailgKANKLGlvnETVLVQEYLIGTEYVVNFvsLDGNHLVT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 210 -------IRLGTPHTFYDYDAKYLASDTRYQvpcgldeakerELKELTARACDALGIQ-GWGRADVMQDAEGRFwLLEVN 281
Cdd:PRK07206 218 eivryhkTSLNSGSTVYDYDEFLDYSEPEYQ-----------ELVDYTKQALDALGIKnGPAHAEVMLTADGPR-LIEIG 285
|
250 260 270
....*....|....*....|....*....|....*.
gi 15599606 282 TAPgmtDHSLVPMAARAA-GLDFQQLVLAILADSRE 316
Cdd:PRK07206 286 ARL---DGGLHPDVARLAtGDSQLDATVESLADPDV 318
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
108-193 |
3.68e-07 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 50.92 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 108 ALAMDKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGss-iGMAKVGGLDELIAAWREAAryDSQV 186
Cdd:PRK06019 96 AIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRRGGydgkGQWVIRSAEDLEAAWALLG--SVPC 173
|
....*..
gi 15599606 187 LVEQWIS 193
Cdd:PRK06019 174 ILEEFVP 180
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
92-194 |
3.71e-07 |
|
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: 51.54 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 92 LECAGIPYTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDE 171
Cdd:TIGR01369 649 LEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEE 728
|
90 100
....*....|....*....|....*
gi 15599606 172 LIAAWREAARYDSQ--VLVEQWISG 194
Cdd:TIGR01369 729 LRRYLEEAVAVSPEhpVLIDKYLED 753
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
63-194 |
4.72e-07 |
|
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: 51.15 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 63 LQRLVE-EKIDRafiILHGRGGEDG-------SMQGLLECAGIPYTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVLA 134
Cdd:TIGR01369 73 VEKIIEkERPDA---ILPTFGGQTAlnlavelEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAH 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599606 135 SEDDCREAAQRLGFPLIVKPAH----EGSSIgmakVGGLDELIAAWREA--ARYDSQVLVEQWISG 194
Cdd:TIGR01369 150 SVEEALAAAKEIGYPVIVRPAFtlggTGGGI----AYNREELKEIAERAlsASPINQVLVEKSLAG 211
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
92-292 |
5.47e-07 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 50.04 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 92 LECAGIPYTGSGVlASALAMDKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAhEGS-SIGMAKVGGLD 170
Cdd:TIGR00768 69 LESLGVPVINSSD-AILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPV-FGSwGRGVSLARDRQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 171 E---LIAAWREAARYDSQVLVEQWISGPE------FTVAtlrGQVLPAIrlgtpHTFYDYDAKYLASDTRYQVPCGLDEa 241
Cdd:TIGR00768 147 AaesLLEHFEQLNGPQNLFLVQEYIKKPGgrdirvFVVG---DEVVAAI-----YRITSGHWRSNLARGGKAEPCSLTE- 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15599606 242 kerELKELTARACDALGIQGWGrADVMQDAEGrFWLLEVNTAPGMTDHSLV 292
Cdd:TIGR00768 218 ---EIEELAIKAAKALGLDVAG-VDLLESEDG-LLVNEVNANPEFKNSVKT 263
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
89-194 |
6.25e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 51.12 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 89 QGLLECAGIPYTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAH--EGSSIGMAKv 166
Cdd:PRK12815 105 DGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPIIVRPAYtlGGTGGGIAE- 183
|
90 100 110
....*....|....*....|....*....|
gi 15599606 167 gGLDELIAAWREAARYD--SQVLVEQWISG 194
Cdd:PRK12815 184 -NLEELEQLFKQGLQASpiHQCLLEESIAG 212
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
110-282 |
2.42e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 48.83 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 110 AM-DKLRTKRVWLSLGLP----TPDyaVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWR------E 178
Cdd:PRK08654 112 AMgSKINAKKLMKKAGVPvlpgTEE--GIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIEstqsiaQ 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 179 AARYDSQVLVEQWISGP---EFtvatlrgQVLpAIRLGtpHTFYDYDaKYLASDTRYQ-----VPCGL--DEAKEReLKE 248
Cdd:PRK08654 190 SAFGDSTVFIEKYLEKPrhiEI-------QIL-ADKHG--NVIHLGD-RECSIQRRHQklieeAPSPImtPELRER-MGE 257
|
170 180 190
....*....|....*....|....*....|....
gi 15599606 249 LTARACDALGIQGWGRADVMQDaEGRFWLLEVNT 282
Cdd:PRK08654 258 AAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNT 290
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
96-282 |
3.13e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 48.20 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 96 GIPYTGSGVLASALAMDKLRTKRVWLSLGLPT---PDYAvLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDEL 172
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVipgSDGA-LKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 173 ----IAAWREA--ARYDSQVLVEQWISGPE-FTVATLRGQVLPAIRLGTPHTFYDYDAKYLASDTRYQVpcgLDEAKERE 245
Cdd:PRK08462 180 enlyLAAESEAlsAFGDGTMYMEKFINNPRhIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVV---LDEKTRER 256
|
170 180 190
....*....|....*....|....*....|....*..
gi 15599606 246 LKELTARACDALGIQGWGRADVMQDAEGRFWLLEVNT 282
Cdd:PRK08462 257 LHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNT 293
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
95-282 |
1.31e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 46.67 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 95 AGIPYTGSGvlASALAM--DKLRTKRVWLSLGLPT-PDYAVLA-SEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLD 170
Cdd:PRK12999 102 AGITFIGPT--AEVLRLlgDKVAARNAAIKAGVPViPGSEGPIdDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 171 ELIAAWREAARY------DSQVLVEQWISGP---EFtvatlrgQVLpAIRLGTPHTFYDYDakylAS-DTRYQ-----VP 235
Cdd:PRK12999 180 ELEEAFERAKREakaafgNDEVYLEKYVENPrhiEV-------QIL-GDKHGNVVHLYERD----CSvQRRHQkvveiAP 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15599606 236 C-GLDEAKERELKELTARACDALGIQGWGRADVMQDAEGRFWLLEVNT 282
Cdd:PRK12999 248 ApGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNP 295
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
112-282 |
1.99e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 45.95 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 112 DKLRTKRVWLSLGLPT-P--DyAVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWR------EAARY 182
Cdd:PRK08591 115 DKVTAKATMKKAGVPVvPgsD-GPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSmaraeaKAAFG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 183 DSQVLVEQWISGP---EFtvatlrgQVLP-----AIRLGTphtfydydakylaSDT----RYQ-------VPcGLDEAKE 243
Cdd:PRK08591 194 NPGVYMEKYLENPrhiEI-------QVLAdghgnAIHLGE-------------RDCslqrRHQkvleeapSP-AITEELR 252
|
170 180 190
....*....|....*....|....*....|....*....
gi 15599606 244 RELKELTARACDALGIQGWGRADVMQDAEGRFWLLEVNT 282
Cdd:PRK08591 253 RKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNT 291
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
112-195 |
8.10e-05 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 44.30 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 112 DKLRTKRVWLSLGLPT-PDYAVL-ASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLDELIAAWREAARY------D 183
Cdd:COG1038 118 DKVAARAAAIEAGVPViPGTEGPvDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREakaafgD 197
|
90
....*....|..
gi 15599606 184 SQVLVEQWISGP 195
Cdd:COG1038 198 DEVFLEKYIERP 209
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
93-310 |
2.06e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 42.82 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 93 ECAGIPYTGSGVLASALAMDKLRTKRVWLSLGLPT--PDYAVLASEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVGGLD 170
Cdd:PRK12833 99 EAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTvpGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 171 ELIA----AWREA--ARYDSQVLVEQWISGPEFTVATLRGQVLPAIRLgtphtfydYDAKYLASDTRYQV-----PCGLD 239
Cdd:PRK12833 179 QLAAelplAQREAqaAFGDGGVYLERFIARARHIEVQILGDGERVVHL--------FERECSLQRRRQKIleeapSPSLT 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599606 240 EAKERELKELTARACDALGIQGWGRADVMQDAE-GRFWLLEVNTAPgMTDHslvPMAARAAGLDFQQLVLAI 310
Cdd:PRK12833 251 PAQRDALCASAVRLARQVGYRGAGTLEYLFDDArGEFYFIEMNTRI-QVEH---PVTEAITGIDLVQEMLRI 318
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
66-203 |
3.11e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.46 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 66 LVEEKID--RAFIILHGRGGEDG-------SMQGLLECAGIPYTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVLASE 136
Cdd:PLN02735 89 LVEQVIAkeRPDALLPTMGGQTAlnlavalAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTL 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599606 137 DDCREAAQRLG-FPLIVKPAHE--GSSIGMAKVGGLDELIAAWREAARYDSQVLVEQWISG-PEFTVATLR 203
Cdd:PLN02735 169 DECFEIAEDIGeFPLIIRPAFTlgGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGwKEYELEVMR 239
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
110-194 |
7.23e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 41.24 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 110 AMDKLrtkrvwlslGLPTPDYAVLASEDDCREAAQRLGFPLIVKPAHE--GSSIGMAKvgGLDELIAAWRE--AARYDSQ 185
Cdd:PRK05294 135 AMKKI---------GLPVPRSGIAHSMEEALEVAEEIGYPVIIRPSFTlgGTGGGIAY--NEEELEEIVERglDLSPVTE 203
|
....*....
gi 15599606 186 VLVEQWISG 194
Cdd:PRK05294 204 VLIEESLLG 212
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
92-154 |
1.48e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 40.47 E-value: 1.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599606 92 LECAGIPYTGSGVLASALAMDKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKP 154
Cdd:PRK05294 649 LEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRP 711
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
106-215 |
2.16e-03 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 39.91 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 106 ASALAMD-KLRTKRVWLSLGLPTPdyavlASED-DCREAAQRlGFPLI------VKPAHEGSSIGMA---KVGGLDELIA 174
Cdd:PRK02471 481 ISPLIMEnKVVTKKILAEAGFPVP-----AGDEfTSLEEALA-DYSLFadkaivVKPKSTNFGLGISifkEPASLEDYEK 554
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15599606 175 AWREAARYDSQVLVEQWISGPEFTVATLRGQVLpAIRLGTP 215
Cdd:PRK02471 555 ALEIAFREDSSVLVEEFIVGTEYRFFVLDGKVE-AVLLRVP 594
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
110-202 |
4.63e-03 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 36.98 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 110 AMDKLRTKRVWLSLGLPTPdyavlasEDDCREAAQRLGFPLIVKPAHEGSSIGMAKVggldeliAAWREAARYDSQVLVE 189
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTP-------ETLQAEELLREEKKYVVKPRDGCGGEGVRKV-------ENGREDEAFIENVLVQ 66
|
90
....*....|...
gi 15599606 190 QWISGPEFTVATL 202
Cdd:pfam02655 67 EFIEGEPLSVSLL 79
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
112-193 |
6.70e-03 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 38.12 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 112 DKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIVKP---AHEGSsiGMAKVGGLDELIAAWREAARYDSQVLV 188
Cdd:PLN02948 121 DKYAQKVHFSKHGIPLPEFMEIDDLESAEKAGDLFGYPLMLKSrrlAYDGR--GNAVAKTEEDLSSAVAALGGFERGLYA 198
|
....*
gi 15599606 189 EQWIS 193
Cdd:PLN02948 199 EKWAP 203
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
112-202 |
8.40e-03 |
|
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: 36.88 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599606 112 DKLRTKRVWLSLGLPTPDYAVLASEDDCREAAQRLGFPLIV-KP----AHEGSSIGMAKvgglDELIAAWREA------A 180
Cdd:pfam01071 2 SKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVvKAdglaAGKGVIVASSN----EEAIKAVDEIleqkkfG 77
|
90 100
....*....|....*....|..
gi 15599606 181 RYDSQVLVEQWISGPEFTVATL 202
Cdd:pfam01071 78 EAGETVVIEEFLEGEEVSVLAF 99
|
|
| |
