|
Name |
Accession |
Description |
Interval |
E-value |
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
1-306 |
0e+00 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 555.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 1 MADKIAVLLGGTSAEREVSLNSGAAVLAGLREGGVDAHPVDPKEVDVTLLKSMGFQKVFIALHGRGGEDGTLQGMLELIG 80
Cdd:PRK01372 3 MFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAHPIDPGEDIAAQLKELGFDRVFNALHGRGGEDGTIQGLLELLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 81 LPYTGSGVMASAISMDKLRSKLLWQGAGLPVAPWVALTRAEFekglsdeAVTKISALGLPLIVKPSREGSSVGMSKVEEE 160
Cdd:PRK01372 83 IPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREED-------LLAAIDKLGLPLVVKPAREGSSVGVSKVKEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 161 NALQGALALAFQHDEEVLIEKWLSGPEFTVAILGEEILPSIRIQPAGTFYDYEAKYLSDETQYFCPAGLEVEQEAFLQEL 240
Cdd:PRK01372 156 DELQAALELAFKYDDEVLVEKYIKGRELTVAVLGGKALPVIEIVPAGEFYDYEAKYLAGGTQYICPAGLPAEIEAELQEL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507080945 241 VLKAWTALGCKGWGRIDVMLDSDGQFYLLEANTSPGMTSHSLVPMAARQAGLSFSQLVVRILELAD 306
Cdd:PRK01372 236 ALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNTQPGMTSHSLVPMAARAAGISFSELVDRILEDAL 301
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
4-305 |
5.71e-160 |
|
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: 447.63 E-value: 5.71e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 4 KIAVLLGGTSAEREVSLNSGAAVLAGLREGGVDAHPV--DPKEVdVTLLKSMGFQKVFIALHGRGGEDGTLQGMLELIGL 81
Cdd:COG1181 2 RVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIgiDVEDL-PAALKELKPDVVFPALHGRGGEDGTIQGLLELLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 82 PYTGSGVMASAISMDKLRSKLLWQGAGLPVAPWVALTRAEFEkglsdEAVTKISALGLPLIVKPSREGSSVGMSKVEEEN 161
Cdd:COG1181 81 PYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELA-----DLEAIEEELGLPLFVKPAREGSSVGVSKVKNAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 162 ALQGALALAFQHDEEVLIEKWLSGPEFTVAILGE---EILPSIRIQPAGTFYDYEAKYLSDETQYFCPAGLEVEQEAFLQ 238
Cdd:COG1181 156 ELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNggpRALPPIEIVPENGFYDYEAKYTDGGTEYICPARLPEELEERIQ 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507080945 239 ELVLKAWTALGCKGWGRIDVMLDSDGQFYLLEANTSPGMTSHSLVPMAARQAGLSFSQLVVRILELA 305
Cdd:COG1181 236 ELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMTPTSLLPKAAAAAGISYEELIERIIELA 302
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
4-305 |
2.33e-149 |
|
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: 421.31 E-value: 2.33e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 4 KIAVLLGGTSAEREVSLNSGAAVLAGLREGGVDAHPVDPKEV------DVTLL------KSMGFQKVFIALHGRGGEDGT 71
Cdd:TIGR01205 1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMgswtykDLPQLilelgaLLEGIDVVFPVLHGRYGEDGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 72 LQGMLELIGLPYTGSGVMASAISMDKLRSKLLWQGAGLPVAPWVALTR-AEFEKGLSDEAVtkISALGLPLIVKPSREGS 150
Cdd:TIGR01205 81 IQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLTQnRASADELECEQV--AEPLGFPVIVKPAREGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 151 SVGMSKVEEENALQGALALAFQHDEEVLIEKWLSGPEFTVAILG-EEILPSIRIQPAGT-FYDYEAKYLSDETQYFCPAG 228
Cdd:TIGR01205 159 SVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGnEEALPIIEIVPEIEgFYDYEAKYLDGSTEYVIPAP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507080945 229 LEVEQEAFLQELVLKAWTALGCKGWGRIDVMLDSDGQFYLLEANTSPGMTSHSLVPMAARQAGLSFSQLVVRILELA 305
Cdd:TIGR01205 239 LDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTIPGMTAISLFPKAAAAAGIEFSQLVERILELA 315
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
4-305 |
9.17e-109 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 318.99 E-value: 9.17e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 4 KIAVLLGGTSAEREVSLNSGAAVLAGLREGGVDAHPV-------------DPKEVDVTLLKSMGFQK------------- 57
Cdd:PRK01966 5 RVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIgitkdgrwylidaDNMELADDDNDKEDLSLlilpsggseevdv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 58 VFIALHGRGGEDGTLQGMLELIGLPYTGSGVMASAISMDKLRSKLLWQGAGLPVAPWVALTRAEFEKGLSDEAVTKisaL 137
Cdd:PRK01966 85 VFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLTRGDWEEASLAEIEAK---L 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 138 GLPLIVKPSREGSSVGMSKVEEENALQGALALAFQHDEEVLIEKWLSGPEFTVAILGEEILPSI--RIQPAGTFYDYEAK 215
Cdd:PRK01966 162 GLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGNDPKASVpgEIVKPDDFYDYEAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 216 YLSDETQYFCPAGLEVEQEAFLQELVLKAWTALGCKGWGRIDVMLDSDGQFYLLEANTSPGMTSHSLVPMAARQAGLSFS 295
Cdd:PRK01966 242 YLDGSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMPGFTPISMYPKLWEASGLSYP 321
|
330
....*....|
gi 507080945 296 QLVVRILELA 305
Cdd:PRK01966 322 ELIDRLIELA 331
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
103-303 |
2.13e-101 |
|
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: 295.76 E-value: 2.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 103 LWQGAGLPVAPWVALTRAEFEKGLSDEAVTKISALGLPLIVKPSREGSSVGMSKVEEENALQGALALAFQHDEEVLIEKW 182
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 183 LSGPEFTVAILG---EEILPSIRIQPAGTFYDYEAKYLSDETQYFCPAGLEVEQEAFLQELVLKAWTALGCKGWGRIDVM 259
Cdd:pfam07478 81 IEGREIECAVLGnedPEVSPVGEIVPSGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDFF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 507080945 260 LDSDGQFYLLEANTSPGMTSHSLVPMAARQAGLSFSQLVVRILE 303
Cdd:pfam07478 161 LTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
4-305 |
9.66e-80 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 243.96 E-value: 9.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 4 KIAVLLGGTSAEREVSLNSGAAVLAGLREGGvdaHPVDPKEVDVTLLKSMG----FQKVFIALHGRGGEDGTLQGMLELI 79
Cdd:PRK14571 2 RVALLMGGVSREREISLRSGERVKKALEKLG---YEVTVFDVDEDFLKKVDqlksFDVVFNVLHGTFGEDGTLQAILDFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 80 GLPYTGSGVMASAISMDKLRSKLLWQGAglpvapwvaltrAEFEKGLSDEAVTKISALGLPLIVKPSREGSSVGMSKVEE 159
Cdd:PRK14571 79 GIRYTGSDAFSSMICFDKLLTYRFLKGT------------VEIPDFVEIKEFMKTSPLGYPCVVKPRREGSSIGVFICES 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 160 ENALQGALALAFQHDEEVLIEKWLSGPEFTVAIL----GEEILPSIRIQPAGTFYDYEAKYLSDETQYFCPAGLEVEQEA 235
Cdd:PRK14571 147 DEEFQHALKEDLPRYGSVIVQEYIPGREMTVSILetekGFEVLPILELRPKRRFYDYVAKYTKGETEFILPAPLNPEEER 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 236 FLQELVLKAWTALGCKGWGRIDVMLdSDGQFYLLEANTSPGMTSHSLVPMAARQAGLSFSQLVVRILELA 305
Cdd:PRK14571 227 LVKETALKAFVEAGCRGFGRVDGIF-SDGRFYFLEINTVPGLTELSDLPASAKAGGIEFEELVDIIIKSA 295
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
3-305 |
5.11e-69 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 216.47 E-value: 5.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 3 DKIAVLLGGTSAEREVSLNSGAAVLAGLREGGVDAHPVDP--KEVDVTLLKsMGFQKVFIALHGRGGEDGTLQGMLELIG 80
Cdd:PRK14569 4 EKIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAVGVDAsgKELVAKLLE-LKPDKCFVALHGEDGENGRVSALLEMLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 81 LPYTGSGVMASAISMDKLRSKLLWQGAGLPVApwvaltraeFEKGLSDEAVTKiSALGLPLIVKPSREGSSVGMSKVEEE 160
Cdd:PRK14569 83 IKHTSSSMKSSVITMDKMISKEILMHHRMPTP---------MAKFLTDKLVAE-DEISFPVAVKPSSGGSSIATFKVKSI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 161 NALQGALALAFQHDEeVLIEKWLSGPEFTVAILGEEILPSIRIQPAGTFYDYEAKYlSDETQYFCPAGLEVEQEAFLQEL 240
Cdd:PRK14569 153 QELKHAYEEASKYGE-VMIEQWVTGKEITVAIVNDEVYSSVWIEPQNEFYDYESKY-SGKSIYHSPSGLCEQKELEVRQL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507080945 241 VLKAWTALGCKGWGRIDVMLDSDGQFYLLEANTSPGMTSHSLVPMAARQAGLSFSQLVVRILELA 305
Cdd:PRK14569 231 AKKAYDLLGCSGHARVDFIYDDRGNFYIMEINSSPGMTDNSLSPKSAAAEGVDFDSFVKRIIEQA 295
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
4-305 |
2.92e-67 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 213.61 E-value: 2.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 4 KIAVLLGGTSAEREVSLNSGAAVLAGLREGGVDAHPV-----------------DPKEVDVT------------------ 48
Cdd:PRK14572 3 KIAVFFGGSSTEHSISIRTGCFICATLHTMGHSVKPIlltpdggwvvptvyrpsIPDESGNSedlfleefqkangvsepa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 49 LLKSMGFQKVFIALHGRGGEDGTLQGMLELIGLPYTGSGVMASAISMDKLRSKLLWQGAGLPVAPWVALTRAEFEKGlSD 128
Cdd:PRK14572 83 DISQLDADIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPFFELEKLKYLNS-PR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 129 EAVTKISALGLPLIVKPSREGSSVGMSKVEEENALQGALALAFQHDEEVLIEKWLSGPEFTVAILG-------EEI-LPS 200
Cdd:PRK14572 162 KTLLKLESLGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVLEryrggkrNPIaLPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 201 IRIQPAGTFYDYEAKYLSDETQYFCPAGLEVEQEAFLQELVLKAWTALGCKGWGRIDVMLdSDGQFYLLEANTSPGMTSH 280
Cdd:PRK14572 242 TEIVPGGEFFDFESKYKQGGSEEITPARISDQEMKRVQELAIRAHESLGCKGYSRTDFII-VDGEPHILETNTLPGMTET 320
|
330 340
....*....|....*....|....*
gi 507080945 281 SLVPMAARQAGLSFSQLVVRILELA 305
Cdd:PRK14572 321 SLIPQQAKAAGINMEEVFTDLIEIG 345
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1-305 |
2.99e-43 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 151.91 E-value: 2.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 1 MADKIAVLLGGTSAEREVSLNSGAAVLAGLRE--------------GGV----DAHPVDPKEVD------VTLL------ 50
Cdd:PRK14570 1 MKKNLMLIFGGVSFEHEISLRSAYGIYSALLKldkyniysvfidkcTGIwyllDSVPDPPKLIKrdvlpiVSLIpgcgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 51 ---KSMGFQKVFIALHGRGGEDGTLQGMLELIGLPYTGSGVMASAISMDKLRSKLLWQGAGLPVAPWVALTRAEFEkgLS 127
Cdd:PRK14570 81 vnnKNLEIDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPFIGFRKYDYF--LD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 128 DEAVTK--ISALGLPLIVKPSREGSSVGMSKVEEENALQGALALAFQHDEEVLIEKWLSGPEFTVAILGEEilpSIRIQP 205
Cdd:PRK14570 159 KEGIKKdiKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIGNE---QIKIFT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 206 AG-------TFYDYEAKYLS---DETQYFCPAGLEVEQEAFLQELVLKAWTALGCKGWGRIDVMLDSD-GQFYLLEANTS 274
Cdd:PRK14570 236 PGeivvqdfIFYDYDAKYSTipgNSIVFNIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKDtGLIYLNEINTI 315
|
330 340 350
....*....|....*....|....*....|.
gi 507080945 275 PGMTSHSLVPMAARQAGLSFSQLVVRILELA 305
Cdd:PRK14570 316 PGFTDISMFAKMCEHDGLQYKSLVDNLIDLA 346
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
5-298 |
1.04e-39 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 147.66 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 5 IAVLLGGTSAEREVSLNSGAAVLAGL-------------REG--------------GVDAHPVDPK------EVDVtllk 51
Cdd:PRK14573 454 LGLVCGGKSCEHDISLLSAKNIAKYLspefydvsyflinRQGlwetvssletaieeDSGKSVLSSEiaqalaKVDV---- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 52 smgfqkVFIALHGRGGEDGTLQGMLELIGLPYTGSGVMASAISMDKLRSKLLWQGAGLPVAPWVALTRAeFEKGLSDEAV 131
Cdd:PRK14573 530 ------VLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQPLTLA-GWKREPELCL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 132 TKI-SALGLPLIVKPSREGSSVGMSKVEEENALQGALALAFQHDEEVLIEK-WLSGPEFTVAILGEEILPSIRIQP---- 205
Cdd:PRK14573 603 AHIvEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEEsRLGSREIEVSCLGDGSSAYVIAGPherr 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 206 -AGTFYDYEAKY-----LSDETQYfcPAGLEVEQEAFLQELVLKAWTALGCKGWGRIDVMLDSDGQFYLLEANTSPGMTS 279
Cdd:PRK14573 683 gSGGFIDYQEKYglsgkSSAQIVF--DLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMNPIPGMTE 760
|
330
....*....|....*....
gi 507080945 280 HSLVPMAARQAGLSFSQLV 298
Cdd:PRK14573 761 ASPFLTAFVRKGWTYEQIV 779
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
80-302 |
1.18e-27 |
|
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: 108.04 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 80 GLPYTGSGvmASAISMDKLRSKLLWQGAGLPVAPWVALTRAEfekglsdEAVTKISALGLPLIVKPSREGSSVGMSKVEE 159
Cdd:COG0439 40 GLPGPSPE--AIRAMRDKVLMREALAAAGVPVPGFALVDSPE-------EALAFAEEIGYPVVVKPADGAGSRGVRVVRD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 160 ENALQGALALA------FQHDEEVLIEKWLSGPEFTVAILGEE-----ILPSIRIQPAGTFYdyeakylsdETQYFCPAG 228
Cdd:COG0439 111 EEELEAALAEAraeakaGSPNGEVLVEEFLEGREYSVEGLVRDgevvvCSITRKHQKPPYFV---------ELGHEAPSP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507080945 229 LEVEQEAFLQELVLKAWTALG-CKGWGRIDVMLDSDGQFYLLEANT-SPGMTSHSLVPMAarqAGLSFSQLVVRIL 302
Cdd:COG0439 182 LPEELRAEIGELVARALRALGyRRGAFHTEFLLTPDGEPYLIEINArLGGEHIPPLTELA---TGVDLVREQIRLA 254
|
|
| Dala_Dala_lig_N |
pfam01820 |
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the ... |
4-86 |
6.47e-26 |
|
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: 99.22 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 4 KIAVLLGGTSAEREVSLNSGAAVLAGLREGGVDAHPV-------------------DPKEVDVTLLKSMGFQK------- 57
Cdd:pfam01820 1 KVAVLFGGRSSEHEVSLVSARSVLKALDKEKYEVIPIgitkdgrlgeaalrelasdDGLLLEVDDAPDGGPAGllfgpnv 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 507080945 58 ---------VFIALHGRGGEDGTLQGMLELIGLPYTGS 86
Cdd:pfam01820 81 lellievdvVFPVLHGPNGEDGTLQGLLELAGIPYVGS 118
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
90-303 |
7.26e-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: 64.58 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 90 ASAISMDKLRSKLLWQGAGLPVAPWVALTRAefekglsDEAVTKISALGLPLIVKPSREGSSVGMSKVEEENALQGALAL 169
Cdd:COG0189 90 AIRRARDKLFTLQLLARAGIPVPPTLVTRDP-------DDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 170 AFQH-DEEVLIEKWL---SGPEFTVAILGEEILPSIRIQPA-GTFYDYEAKYLSDETQyfcpaglEVEQEafLQELVLKA 244
Cdd:COG0189 163 LTELgSEPVLVQEFIpeeDGRDIRVLVVGGEPVAAIRRIPAeGEFRTNLARGGRAEPV-------ELTDE--ERELALRA 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507080945 245 WTALGCkGWGRIDVMLDSDGqFYLLEANTSPGmtshslVPMAARQAGLSFSQLVVRILE 303
Cdd:COG0189 234 APALGL-DFAGVDLIEDDDG-PLVLEVNVTPG------FRGLERATGVDIAEAIADYLE 284
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
96-273 |
2.17e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 64.23 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 96 DKLRSKLLWQGAGLPVAPWValtraefEKGLSD--EAVTKISALGLPLIVKPSREGSSVGMSKVEEENALQGAL------ 167
Cdd:PRK08654 115 SKINAKKLMKKAGVPVLPGT-------EEGIEDieEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIestqsi 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 168 -ALAFQhDEEVLIEKWLSGP---EFTvaILGEEILPSIRIqpagtfYDYEA------KYLSDETQyfCPAGLEvEQEAFL 237
Cdd:PRK08654 188 aQSAFG-DSTVFIEKYLEKPrhiEIQ--ILADKHGNVIHL------GDRECsiqrrhQKLIEEAP--SPIMTP-ELRERM 255
|
170 180 190
....*....|....*....|....*....|....*.
gi 507080945 238 QELVLKAWTALGCKGWGRIDvMLDSDGQFYLLEANT 273
Cdd:PRK08654 256 GEAAVKAAKAINYENAGTVE-FLYSNGNFYFLEMNT 290
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
80-303 |
1.13e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 61.68 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 80 GLPYTGSGVMASAISMDKLRSKLLWQGAGLPVAPWV--ALTRAEFEKGLSDEavtkisaLGLPLIVKPSREGSSVGMSKV 157
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKE-------IGYPVILKAAAGGGGRGMRVV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 158 EEENALQGAL------ALAFQHDEEVLIEKWLSGPE-FTVAILGEEILPSIRIQPAGTFYDYEAKYLSDETqyfcPA-GL 229
Cdd:PRK08462 174 EDESDLENLYlaaeseALSAFGDGTMYMEKFINNPRhIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEES----PAvVL 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507080945 230 EVEQEAFLQELVLKAWTALGCKGWGRIDVMLDSDGQFYLLEANTSPgMTSHSLVPMAarqAGLSFSQLVVRILE 303
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRL-QVEHTVSEMV---SGLDLIEWMIKIAE 319
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
96-273 |
5.03e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 60.04 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 96 DKLRSKLLWQGAGLPVAPWValtraefEKGLSD--EAVTKISALGLPLIVKPSREGSSVGMSKVEEENALQGALAL---- 169
Cdd:PRK06111 115 SKIEARRAMQAAGVPVVPGI-------TTNLEDaeEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESnkkr 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 170 --AFQHDEEVLIEKWLSGPEftvailgeeilpSIRIQPAGTFYDYeAKYLSDETqyfC-------------PA-GLEVEQ 233
Cdd:PRK06111 188 aaNFFGNGEMYIEKYIEDPR------------HIEIQLLADTHGN-TVYLWERE---CsvqrrhqkvieeaPSpFLDEET 251
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 507080945 234 EAFLQELVLKAWTALGCKGWGRIDVMLDSDGQFYLLEANT 273
Cdd:PRK06111 252 RKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNT 291
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
85-272 |
1.14e-08 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 55.28 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 85 GSGVMAS-----AISMDKLRSKLLWQGAGLPVAP-WVALTRAEFEKGLsdeavtKISALGLPLIVKPSREGSSVGMSKVE 158
Cdd:PRK12767 95 GVKVLVSskeviEICNDKWLTYEFLKENGIPTPKsYLPESLEDFKAAL------AKGELQFPLFVKPRDGSASIGVFKVN 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 159 EENALQgalaLAFQHDEEVLIEKWLSGPEFTVAIL----GE--EILPSIRIQP-AG------TFYDYEakylsdetqyfc 225
Cdd:PRK12767 169 DKEELE----FLLEYVPNLIIQEFIEGQEYTVDVLcdlnGEviSIVPRKRIEVrAGetskgvTVKDPE------------ 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 507080945 226 pagleveqeafLQELVLKAWTALGCKGWGRIDVMLDsDGQFYLLEAN 272
Cdd:PRK12767 233 -----------LFKLAERLAEALGARGPLNIQCFVT-DGEPYLFEIN 267
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
137-272 |
3.64e-07 |
|
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: 49.20 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 137 LGLPLIVKPSREGSSVGMSKVEEENALQGALA--------LAFQHDEEV------LIEKWLSGPEFTV-AILGEEILPSI 201
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAaireeieqWKEMYPEAVvdggsfLVEEYIEGEEFAVdAYFDENGEPVI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507080945 202 riqpAGTFY--DYEAKYLSDeTQYFCPAGLEVEQEAFLQELVLKAWTALGCK-GWGRIDVMLDSDGQFYLLEAN 272
Cdd:pfam13535 81 ----LNILKhdFASSEDVSD-RIYVTSASIIRETQAAFTEFLKRINALLGLKnFPVHIELRVDEDGQIIPIEVN 149
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
76-302 |
3.82e-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: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 76 LELIGLPYTGSGVMASAISMDKLRSKLLWQGAGLPVAPWVALTRAEfekglsdEAVTKISALGLPLIVKPSREGSSVGMS 155
Cdd:TIGR01369 649 LEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVE-------EAVEFASEIGYPVLVRPSYVLGGRAME 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 156 KVEEENALQGALALAFQHDEE--VLIEKWLS-GPEFTVAIL--GEEIL-PSI--RIQPAGTfydyeakYLSDETQYFCPA 227
Cdd:TIGR01369 722 IVYNEEELRRYLEEAVAVSPEhpVLIDKYLEdAVEVDVDAVsdGEEVLiPGImeHIEEAGV-------HSGDSTCVLPPQ 794
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507080945 228 GLEVEQEAFLQELVLKAWTALGCKGWGRIDVMLDsDGQFYLLEANTSPGMTshslVPMAARQAGLSFSQLVVRIL 302
Cdd:TIGR01369 795 TLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVNPRASRT----VPFVSKATGVPLAKLAVRVM 864
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
76-302 |
4.24e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 51.51 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 76 LELIGLPYTGSGVMASAISMDKLRSKLLWQGAGLPVAPWVALTRAEfekglsdEAVTKISALGLPLIVKPSREGSSVGMS 155
Cdd:PRK12815 650 LEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEE-------EAFAFAKRIGYPVLIRPSYVIGGQGMA 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 156 KVEEENALQGALALAFQHDEEVLIEKWLSGPEFTVAIL--GEEI-LPSI--RIQPAGTfydyeakYLSDETQYFCPAGLE 230
Cdd:PRK12815 723 VVYDEPALEAYLAENASQLYPILIDQFIDGKEYEVDAIsdGEDVtIPGIieHIEQAGV-------HSGDSIAVLPPQSLS 795
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507080945 231 VEQEAFLQELVLKAWTALGCKGWGRIDVMLDsDGQFYLLEANTSPGMTshslVPMAARQAGLSFSQLVVRIL 302
Cdd:PRK12815 796 EEQQEKIRDYAIKIAKKLGFRGIMNIQFVLA-NDEIYVLEVNPRASRT----VPFVSKATGVPLAKLATKVL 862
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
96-273 |
5.88e-06 |
|
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: 46.14 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 96 DKLRSKLLWQGAGLPVAPWVALTRAEFEkglsdEAVTKISALGLPLIVKPSREGSSVGMSKVEEENALQGALALAFQH-- 173
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEE-----EALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEap 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 174 ----DEEVLIEKWLSGP---EFTV--------AILG--EEILP-----SIRIQPAGTfydyeakyLSDETQyfcpaglev 231
Cdd:pfam02786 76 aafgNPQVLVEKSLKGPkhiEYQVlrdahgncITVCnrECSDQrrtqkSIEVAPSQT--------LTDEER--------- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 507080945 232 eQEafLQELVLKAWTALGCKGWGRIDVMLDSD-GQFYLLEANT 273
Cdd:pfam02786 139 -QM--LREAAVKIARHLGYVGAGTVEFALDPFsGEYYFIEMNT 178
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
86-194 |
1.92e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.92 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 86 SGVMASAISMDKLRSKLLWQGAGLPVAPWVALTRAEfekglsdEAVTKISALGLPLIVKPS-----ReGSSVGMSKVEEe 160
Cdd:PRK14016 204 TSAIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAE-------DAWEAAEEIGYPVVVKPLdgnhgR-GVTVNITTREE- 274
|
90 100 110
....*....|....*....|....*....|....
gi 507080945 161 naLQGALALAFQHDEEVLIEKWLSGPEFTVAILG 194
Cdd:PRK14016 275 --IEAAYAVASKESSDVIVERYIPGKDHRLLVVG 306
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
96-273 |
2.38e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 45.48 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 96 DKLRSKLLWQGAGLPVAPwvaltRAEFEKGLSDEAVTKISALGLPLIVKPSREGSSVGMSKVEEENALQGALAL------ 169
Cdd:PRK07178 114 DKTEARRAMIKAGVPVTP-----GSEGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRviseat 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 170 -AFQhDEEVLIEKWLSGPE-FTVAILGE-----------------------EILPSIRIQPagtfydyeakylsdetqyf 224
Cdd:PRK07178 189 kAFG-SAEVFLEKCIVNPKhIEVQILADshgnvvhlferdcsiqrrnqkliEIAPSPQLTP------------------- 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 507080945 225 cpaglevEQEAFLQELVLKAWTALGCKGWGRIDVMLDSDGQFYLLEANT 273
Cdd:PRK07178 249 -------EQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNT 290
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
92-149 |
5.15e-05 |
|
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: 44.29 E-value: 5.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 507080945 92 AISMDKLRSKLLWQGAGLPVAPWVALTRAEfekglsdEAVTKISALGLPLIVKPSREG 149
Cdd:COG0026 85 EIAQDRLLEKAFLAELGIPVAPFAAVDSLE-------DLEAAIAELGLPAVLKTRRGG 135
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-273 |
9.18e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 43.59 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 1 MADKiAVLLGGTSAEREVsLNSgAAVLAGLREGGVDA-HPvdpkevdvtllkSMGFQkvfialhgrgGEDGTLQGMLELI 79
Cdd:PRK12833 47 MADE-AVHIGPSHAAKSY-LNP-AAILAAARQCGADAiHP------------GYGFL----------SENAAFAEAVEAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 80 GLPYTGSGVMASAISMDKLRSKLLWQGAGLPVAPWVALTRAEFekglsDEAVTKISALGLPLIVKPSREGSSVGMSKVEE 159
Cdd:PRK12833 102 GLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASL-----DAALEVAARIGYPLMIKAAAGGGGRGIRVAHD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 160 ENALQGALALAFQH------DEEVLIEKWLS-GPEFTVAILGEEilpsiriQPAGTFYDYEAKYLSDETQYFCPA---GL 229
Cdd:PRK12833 177 AAQLAAELPLAQREaqaafgDGGVYLERFIArARHIEVQILGDG-------ERVVHLFERECSLQRRRQKILEEApspSL 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 507080945 230 EVEQEAFLQELVLKAWTALGCKGWGRIDVMLD-SDGQFYLLEANT 273
Cdd:PRK12833 250 TPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNT 294
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
92-149 |
9.89e-05 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.60 E-value: 9.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 507080945 92 AISMDKLRSKLLWQGAGLPVAPWVALTRAEfekglsdEAVTKISALGLPLIVKPSREG 149
Cdd:PRK06019 96 AIAQDRLTEKQFLDKLGIPVAPFAVVDSAE-------DLEAALADLGLPAVLKTRRGG 146
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
95-185 |
1.95e-04 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 42.94 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 95 MDKLrskllwqgaGLPVAPWVALTRAEfekglsdEAVTKISALGLPLIVKPS--REGSsvGMSKVEEENALQGALALAFQ 172
Cdd:COG0458 122 LDKL---------GIPQPKSGTATSVE-------EALAIAEEIGYPVIVRPSyvLGGR--GMGIVYNEEELEEYLERALK 183
|
90
....*....|....*
gi 507080945 173 H--DEEVLIEKWLSG 185
Cdd:COG0458 184 VspDHPVLIDESLLG 198
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
79-249 |
3.19e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 42.14 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 79 IGLPytGSGVMASAISMDKLRSKLLWQGAGLPVA-PWVALTRAEFEKGLSdeavtkisALGLPLIVKPSREGSSVGMSKV 157
Cdd:PRK02186 92 LGLP--AANTEAIRTCRDKKRLARTLRDHGIDVPrTHALALRAVALDALD--------GLTYPVVVKPRMGSGSVGVRLC 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 158 E-EENALQGALALAFQHDEEVLIEKWLSGPEFTVAIL----GEEILPSIR--IQPAGTFYdyeakylsdETQYFCPAGLE 230
Cdd:PRK02186 162 AsVAEAAAHCAALRRAGTRAALVQAYVEGDEYSVETLtvarGHQVLGITRkhLGPPPHFV---------EIGHDFPAPLS 232
|
170
....*....|....*....
gi 507080945 231 VEQEAFLQELVLKAWTALG 249
Cdd:PRK02186 233 APQRERIVRTVLRALDAVG 251
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
140-198 |
8.14e-04 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 41.07 E-value: 8.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507080945 140 PLIVKPSREGSSVGMSKVEEENAL---QGALALAFQHDEEVLIEKWLSGPEFTVAILGEEIL 198
Cdd:PRK02471 526 AIVVKPKSTNFGLGISIFKEPASLedyEKALEIAFREDSSVLVEEFIVGTEYRFFVLDGKVE 587
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
105-182 |
1.09e-03 |
|
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: 39.16 E-value: 1.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507080945 105 QGAGLPVAPWVALTRAefekglsDEAVTKISALGLPLIVKPSREGSS-VGMSKVEEENALQGALALAFqhDEEVLIEKW 182
Cdd:pfam02222 1 QKLGLPTPRFMAAESL-------EELIEAGQELGYPCVVKARRGGYDgKGQYVVRSEADLPQAWEELG--DGPVIVEEF 70
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
96-194 |
2.27e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 39.74 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 96 DKLRSKLLWQGAGLPVAPWValtraefEKGLSD--EAVTKISALGLPLIVKPSREGSSVGMSKVEEENALQGAL------ 167
Cdd:PRK12999 119 DKVAARNAAIKAGVPVIPGS-------EGPIDDieEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFerakre 191
|
90 100 110
....*....|....*....|....*....|
gi 507080945 168 ALAFQHDEEVLIEKWLSGP---EftVAILG 194
Cdd:PRK12999 192 AKAAFGNDEVYLEKYVENPrhiE--VQILG 219
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
96-194 |
3.97e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 38.91 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 96 DKLRSKLLWQGAGLPVAPWValtraefEKGLSD-EAVTKISA-LGLPLIVKPSREGSSVGMSKVEEENALQGALAL---- 169
Cdd:COG1038 118 DKVAARAAAIEAGVPVIPGT-------EGPVDDlEEALAFAEeIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESarre 190
|
90 100 110
....*....|....*....|....*....|.
gi 507080945 170 ---AFQhDEEVLIEKWLSGP---EftVAILG 194
Cdd:COG1038 191 akaAFG-DDEVFLEKYIERPkhiE--VQILG 218
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
132-272 |
4.85e-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: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 132 TKISALGLPLIVKPSREGSSVGMSKVEEENALQGALalafqhdEEVLIEKWLSGPEFTVAIL--GEEILP----SIRIQP 205
Cdd:pfam02655 25 EELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFI-------ENVLVQEFIEGEPLSVSLLsdGEKALPlsvnRQYIDN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080945 206 AGTFYDY---EAKYLSDETQyfcpaglEVEQEAflQELVLKawtALGCKGWGRIDVMLdSDGQFYLLEAN 272
Cdd:pfam02655 98 GGSGFVYagnVTPSRTELKE-------EIIELA--EEVVEC---LPGLRGYVGVDLVL-KDNEPYVIEVN 154
|
|
| |
