|
Name |
Accession |
Description |
Interval |
E-value |
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
1-328 |
1.01e-143 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 408.74 E-value: 1.01e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 1 MKNMHVLLLCGGGGSEHEVSLRSANFLEKQLGLLPgIEVTRVEMFAD-RWLSADGRECKL--------GLDKLLSFDSVA 71
Cdd:PRK01966 1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEK-YEVVPIGITKDgRWYLIDADNMELadddndkeDLSLLILPSGGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 72 RPVDYVVPCIHGYPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLT--EQGEASLTEAKA 149
Cdd:PRK01966 80 EEVDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLTrgDWEEASLAEIEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 150 ALaKWGkVFIKAASQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAVKPRELEVAVYQYGDElvATYPGEIcVPQDK 229
Cdd:PRK01966 160 KL-GLP-VFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGNDPK--ASVPGEI-VKPDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 230 FYTYEEKYSSAShTETALKAEgLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEEGEILLNEINTFPGMTSISMFPKL 309
Cdd:PRK01966 235 FYDYEAKYLDGS-AELIIPAD-LSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMPGFTPISMYPKL 312
|
330
....*....|....*....
gi 752543647 310 LEHHGHSFAHYLEQILRKA 328
Cdd:PRK01966 313 WEASGLSYPELIDRLIELA 331
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
4-329 |
8.20e-103 |
|
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: 303.57 E-value: 8.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 4 MHVLLLCGGGGSEHEVSLRSANFLEKQLGLLpGIEVTRVEMfadrwlsaDGREcklgldklLSFDSVARPVDYVVPCIHG 83
Cdd:COG1181 1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKA-GYDVVPIGI--------DVED--------LPAALKELKPDVVFPALHG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 84 YPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLTEqgeASLTEAKAALAKWGK-VFIKAA 162
Cdd:COG1181 64 RGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRR---GELADLEAIEEELGLpLFVKPA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 163 SQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAVKPRELEVAVYQyGDELVATYPGEIcVPQDKFYTYEEKYSSASh 242
Cdd:COG1181 141 REGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLG-NGGPRALPPIEI-VPENGFYDYEAKYTDGG- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 243 TETALKAeGLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEEGEILLNEINTFPGMTSISMFPKLLEHHGHSFAHYLE 322
Cdd:COG1181 218 TEYICPA-RLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMTPTSLLPKAAAAAGISYEELIE 296
|
....*..
gi 752543647 323 QILRKAV 329
Cdd:COG1181 297 RIIELAL 303
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
5-328 |
8.30e-103 |
|
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: 304.21 E-value: 8.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 5 HVLLLCGGGGSEHEVSLRSANFLEKQLGLLpGIEVTRVEMFADRWLSADGRecklgLDKLLSFDSVARPVDYVVPCIHGY 84
Cdd:TIGR01205 1 RVAVLFGGKSAEHEISLVSAAAVLKALRDL-GYDVYPVDIDKMGSWTYKDL-----PQLILELGALLEGIDVVFPVLHGR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 85 PGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLTeQGEASLTEAKAALAK---WGKVFIKA 161
Cdd:TIGR01205 75 YGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLT-QNRASADELECEQVAeplGFPVIVKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 162 ASQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAVKPRELEVAVYQYGDelvATYPGEICVPQDKFYTYEEKYSSAS 241
Cdd:TIGR01205 154 AREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEE---ALPIIEIVPEIEGFYDYEAKYLDGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 242 hTETALKAeGLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEEGEILLNEINTFPGMTSISMFPKLLEHHGHSFAHYL 321
Cdd:TIGR01205 231 -TEYVIPA-PLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTIPGMTAISLFPKAAAAAGIEFSQLV 308
|
....*..
gi 752543647 322 EQILRKA 328
Cdd:TIGR01205 309 ERILELA 315
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
123-325 |
9.44e-54 |
|
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: 174.81 E-value: 9.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 123 LTAIGIPNTPYLFLTEQG-EASLTEAKAALAKWGK--VFIKAASQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAV 199
Cdd:pfam07478 2 LKAAGLPVVPFVTFTRADwKLNPKEWCAQVEEALGypVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 200 KPRELEVAVYQYGDELVATyPGEIcVPQDKFYTYEEKYSSAShTETALKAeGLTQAQADAIHEYALKAFRQLKLTHLSRI 279
Cdd:pfam07478 82 EGREIECAVLGNEDPEVSP-VGEI-VPSGGFYDYEAKYIDDS-AQIVVPA-DLEEEQEEQIQELALKAYKALGCRGLARV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 752543647 280 DFFLTEEGEILLNEINTFPGMTSISMFPKLLEHHGHSFAHYLEQIL 325
Cdd:pfam07478 158 DFFLTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLI 203
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
1-328 |
1.01e-143 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 408.74 E-value: 1.01e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 1 MKNMHVLLLCGGGGSEHEVSLRSANFLEKQLGLLPgIEVTRVEMFAD-RWLSADGRECKL--------GLDKLLSFDSVA 71
Cdd:PRK01966 1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEK-YEVVPIGITKDgRWYLIDADNMELadddndkeDLSLLILPSGGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 72 RPVDYVVPCIHGYPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLT--EQGEASLTEAKA 149
Cdd:PRK01966 80 EEVDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLTrgDWEEASLAEIEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 150 ALaKWGkVFIKAASQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAVKPRELEVAVYQYGDElvATYPGEIcVPQDK 229
Cdd:PRK01966 160 KL-GLP-VFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGNDPK--ASVPGEI-VKPDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 230 FYTYEEKYSSAShTETALKAEgLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEEGEILLNEINTFPGMTSISMFPKL 309
Cdd:PRK01966 235 FYDYEAKYLDGS-AELIIPAD-LSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMPGFTPISMYPKL 312
|
330
....*....|....*....
gi 752543647 310 LEHHGHSFAHYLEQILRKA 328
Cdd:PRK01966 313 WEASGLSYPELIDRLIELA 331
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
4-329 |
8.20e-103 |
|
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: 303.57 E-value: 8.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 4 MHVLLLCGGGGSEHEVSLRSANFLEKQLGLLpGIEVTRVEMfadrwlsaDGREcklgldklLSFDSVARPVDYVVPCIHG 83
Cdd:COG1181 1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKA-GYDVVPIGI--------DVED--------LPAALKELKPDVVFPALHG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 84 YPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLTEqgeASLTEAKAALAKWGK-VFIKAA 162
Cdd:COG1181 64 RGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRR---GELADLEAIEEELGLpLFVKPA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 163 SQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAVKPRELEVAVYQyGDELVATYPGEIcVPQDKFYTYEEKYSSASh 242
Cdd:COG1181 141 REGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLG-NGGPRALPPIEI-VPENGFYDYEAKYTDGG- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 243 TETALKAeGLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEEGEILLNEINTFPGMTSISMFPKLLEHHGHSFAHYLE 322
Cdd:COG1181 218 TEYICPA-RLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMTPTSLLPKAAAAAGISYEELIE 296
|
....*..
gi 752543647 323 QILRKAV 329
Cdd:COG1181 297 RIIELAL 303
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
5-328 |
8.30e-103 |
|
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: 304.21 E-value: 8.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 5 HVLLLCGGGGSEHEVSLRSANFLEKQLGLLpGIEVTRVEMFADRWLSADGRecklgLDKLLSFDSVARPVDYVVPCIHGY 84
Cdd:TIGR01205 1 RVAVLFGGKSAEHEISLVSAAAVLKALRDL-GYDVYPVDIDKMGSWTYKDL-----PQLILELGALLEGIDVVFPVLHGR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 85 PGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLTeQGEASLTEAKAALAK---WGKVFIKA 161
Cdd:TIGR01205 75 YGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLT-QNRASADELECEQVAeplGFPVIVKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 162 ASQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAVKPRELEVAVYQYGDelvATYPGEICVPQDKFYTYEEKYSSAS 241
Cdd:TIGR01205 154 AREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEE---ALPIIEIVPEIEGFYDYEAKYLDGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 242 hTETALKAeGLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEEGEILLNEINTFPGMTSISMFPKLLEHHGHSFAHYL 321
Cdd:TIGR01205 231 -TEYVIPA-PLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTIPGMTAISLFPKAAAAAGIEFSQLV 308
|
....*..
gi 752543647 322 EQILRKA 328
Cdd:TIGR01205 309 ERILELA 315
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
1-328 |
8.29e-61 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 196.49 E-value: 8.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 1 MKNMHVLLLCGGGGSEHEVSLRS----ANFLEKQlgllpGIEVTRVEMFADRwlsadgrecklgLDKLlsfdsVARPVDY 76
Cdd:PRK01372 2 KMFGKVAVLMGGTSAEREVSLNSgaavLAALREA-----GYDAHPIDPGEDI------------AAQL-----KELGFDR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 77 VVPCIHGYPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLTEQgeaslTEAKAALAKWG- 155
Cdd:PRK01372 60 VFNALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTRE-----EDLLAAIDKLGl 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 156 KVFIKAASQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAVKPRELEVAVYqyGDELVATYpgEIcVPQDKFYTYEE 235
Cdd:PRK01372 135 PLVVKPAREGSSVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVL--GGKALPVI--EI-VPAGEFYDYEA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 236 KYSS--ASHTETAlkaeGLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEEGEILLNEINTFPGMTSISMFPKLLEHH 313
Cdd:PRK01372 210 KYLAggTQYICPA----GLPAEIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNTQPGMTSHSLVPMAARAA 285
|
330
....*....|....*
gi 752543647 314 GHSFAHYLEQILRKA 328
Cdd:PRK01372 286 GISFSELVDRILEDA 300
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
123-325 |
9.44e-54 |
|
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: 174.81 E-value: 9.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 123 LTAIGIPNTPYLFLTEQG-EASLTEAKAALAKWGK--VFIKAASQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAV 199
Cdd:pfam07478 2 LKAAGLPVVPFVTFTRADwKLNPKEWCAQVEEALGypVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 200 KPRELEVAVYQYGDELVATyPGEIcVPQDKFYTYEEKYSSAShTETALKAeGLTQAQADAIHEYALKAFRQLKLTHLSRI 279
Cdd:pfam07478 82 EGREIECAVLGNEDPEVSP-VGEI-VPSGGFYDYEAKYIDDS-AQIVVPA-DLEEEQEEQIQELALKAYKALGCRGLARV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 752543647 280 DFFLTEEGEILLNEINTFPGMTSISMFPKLLEHHGHSFAHYLEQIL 325
Cdd:pfam07478 158 DFFLTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLI 203
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1-328 |
1.04e-40 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 145.74 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 1 MKNmHVLLLCGGGGSEHEVSLRSANFLEKQLGLLPGIEVTRVemFADR----W-----LSADGRECKLGLDKLLSF---- 67
Cdd:PRK14570 1 MKK-NLMLIFGGVSFEHEISLRSAYGIYSALLKLDKYNIYSV--FIDKctgiWylldsVPDPPKLIKRDVLPIVSLipgc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 68 ----DSVARPVDYVVPCIHGYPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYL-------FL 136
Cdd:PRK14570 78 gifvNNKNLEIDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPFIgfrkydyFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 137 TEQGEASltEAKAALAKwgKVFIKAASQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAVKPRELEVAVYqyGDELV 216
Cdd:PRK14570 158 DKEGIKK--DIKEVLGY--PVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVI--GNEQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 217 ATY-PGEICVPQDKFYTYEEKYSSASHTETALKAEG-LTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEE-GEILLNE 293
Cdd:PRK14570 232 KIFtPGEIVVQDFIFYDYDAKYSTIPGNSIVFNIPAhLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKDtGLIYLNE 311
|
330 340 350
....*....|....*....|....*....|....*
gi 752543647 294 INTFPGMTSISMFPKLLEHHGHSFAHYLEQILRKA 328
Cdd:PRK14570 312 INTIPGFTDISMFAKMCEHDGLQYKSLVDNLIDLA 346
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
2-329 |
3.63e-40 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 149.97 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 2 KNMHVLLLCGGGGSEHEVSLRSANFLEKQLGLlpgiEVTRVEMFA-DR---WLSADGRECKLGLDKLLS-FDS-VARP-- 73
Cdd:PRK14573 450 KKLSLGLVCGGKSCEHDISLLSAKNIAKYLSP----EFYDVSYFLiNRqglWETVSSLETAIEEDSGKSvLSSeIAQAla 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 74 -VDYVVPCIHGYPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLTEQG---EASLTEAKA 149
Cdd:PRK14573 526 kVDVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQPLTLAGwkrEPELCLAHI 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 150 ALAKWGKVFIKAASQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKA-VKPRELEVAVyqYGDELVATY---PGEICv 225
Cdd:PRK14573 606 VEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEESrLGSREIEVSC--LGDGSSAYViagPHERR- 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 226 PQDKFYTYEEKYSSASHTETALKAE-GLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEEGEILLNEINTFPGMTSIS 304
Cdd:PRK14573 683 GSGGFIDYQEKYGLSGKSSAQIVFDlDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMNPIPGMTEAS 762
|
330 340
....*....|....*....|....*
gi 752543647 305 MFPKLLEHHGHSFahylEQILRKAV 329
Cdd:PRK14573 763 PFLTAFVRKGWTY----EQIVHQLI 783
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
4-329 |
4.12e-33 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 124.16 E-value: 4.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 4 MHVLLLCGGGGSEHEVSLRSANFLEKQLGLLpGIEVTRVEMfADRWLSAdgrecklgLDKLLSFDSVARpvdyvvpCIHG 83
Cdd:PRK14571 1 MRVALLMGGVSREREISLRSGERVKKALEKL-GYEVTVFDV-DEDFLKK--------VDQLKSFDVVFN-------VLHG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 84 YPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTA-IGIPNtpYLFLTEQGEASlteakaalaKWG-KVFIKA 161
Cdd:PRK14571 64 TFGEDGTLQAILDFLGIRYTGSDAFSSMICFDKLLTYRFLKGtVEIPD--FVEIKEFMKTS---------PLGyPCVVKP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 162 ASQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAVKPRELEVAVYQYGdELVATYPGEICVPQDKFYTYEEKYSSAs 241
Cdd:PRK14571 133 RREGSSIGVFICESDEEFQHALKEDLPRYGSVIVQEYIPGREMTVSILETE-KGFEVLPILELRPKRRFYDYVAKYTKG- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 242 HTETALKAEgLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLtEEGEILLNEINTFPGMTSISMFPKLLEHHGHSFAHYL 321
Cdd:PRK14571 211 ETEFILPAP-LNPEEERLVKETALKAFVEAGCRGFGRVDGIF-SDGRFYFLEINTVPGLTELSDLPASAKAGGIEFEELV 288
|
....*...
gi 752543647 322 EQILRKAV 329
Cdd:PRK14571 289 DIIIKSAF 296
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
1-328 |
1.25e-25 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 103.99 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 1 MKNMHVLLLCGGGGSEHEVSLRSANFLEKQLgLLPGIEVTRVEmfadrwlsADGRECklgLDKLLSFDSvarpvDYVVPC 80
Cdd:PRK14569 1 MKNEKIVVLYGGDSPEREVSLKSGKAVLDSL-ISQGYDAVGVD--------ASGKEL---VAKLLELKP-----DKCFVA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 81 IHGYPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLTEQgeasLTEAKAALAKwgkVFIK 160
Cdd:PRK14569 64 LHGEDGENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPTPMAKFLTDK----LVAEDEISFP---VAVK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 161 AASQGSSVGCYSASNEADLVKGIADAFGYSEqVLIEKAVKPRELEVAVYQygDELVATYPGEicvPQDKFYTYEEKYSSA 240
Cdd:PRK14569 137 PSSGGSSIATFKVKSIQELKHAYEEASKYGE-VMIEQWVTGKEITVAIVN--DEVYSSVWIE---PQNEFYDYESKYSGK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 241 S--HTETalkaeGLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEEGEILLNEINTFPGMTSISMFPKLLEHHGHSFA 318
Cdd:PRK14569 211 SiyHSPS-----GLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEINSSPGMTDNSLSPKSAAAEGVDFD 285
|
330
....*....|
gi 752543647 319 HYLEQILRKA 328
Cdd:PRK14569 286 SFVKRIIEQA 295
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
6-308 |
1.08e-24 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 102.29 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 6 VLLLCGGGGSEHEVSLRSANFLEKQLGLLpGIEVTRVEMFAD-RWL----------SADGRECKLGLDKLLSFDSVARP- 73
Cdd:PRK14572 4 IAVFFGGSSTEHSISIRTGCFICATLHTM-GHSVKPILLTPDgGWVvptvyrpsipDESGNSEDLFLEEFQKANGVSEPa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 74 ------VDYVVPCIHGYPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLtEQGEaSLTEA 147
Cdd:PRK14572 83 disqldADIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPFFEL-EKLK-YLNSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 148 KAALAKWGK----VFIKAASQGSSVGCYSASNEADLVKGIADAFGYSEQVLIEKAVKPRELEVAV---YQYGD-ELVATY 219
Cdd:PRK14572 161 RKTLLKLESlgfpQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVlerYRGGKrNPIALP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 220 PGEIcVPQDKFYTYEEKYSS-ASHTETALKaegLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTeEGEILLNEINTFP 298
Cdd:PRK14572 241 ATEI-VPGGEFFDFESKYKQgGSEEITPAR---ISDQEMKRVQELAIRAHESLGCKGYSRTDFIIV-DGEPHILETNTLP 315
|
330
....*....|
gi 752543647 299 GMTSISMFPK 308
Cdd:PRK14572 316 GMTETSLIPQ 325
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
99-296 |
4.77e-19 |
|
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: 84.92 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 99 GLPylGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLTeqgeaSLTEAKAALAKWG-KVFIKAASQGSSVGCYSASNEA 177
Cdd:COG0439 40 GLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVD-----SPEEALAFAEEIGyPVVVKPADGAGSRGVRVVRDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 178 DL------VKGIADAFGYSEQVLIEKAVKPRELEVAVYQYGDELVatypgeICVPQDKFYT----YEEKYSSASHtetal 247
Cdd:COG0439 113 ELeaalaeARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVV------VCSITRKHQKppyfVELGHEAPSP----- 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 752543647 248 kaegLTQAQADAIHEYALKAFRQLKLTH-LSRIDFFLTEEGEILLNEINT 296
Cdd:COG0439 182 ----LPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYLIEINA 227
|
|
| Dala_Dala_lig_N |
pfam01820 |
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the ... |
5-105 |
1.86e-16 |
|
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: 74.18 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 5 HVLLLCGGGGSEHEVSLRSAN----------------FLEKQLGLlpGIEVTRVEMFADRWLSADGRECK---LGLDKLL 65
Cdd:pfam01820 1 KVAVLFGGRSSEHEVSLVSARsvlkaldkekyevipiGITKDGRL--GEAALRELASDDGLLLEVDDAPDggpAGLLFGP 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 752543647 66 SFDSVARPVDYVVPCIHGYPGETGDLQSFLELAGLPYLGC 105
Cdd:pfam01820 79 NVLELLIEVDVVFPVLHGPNGEDGTLQGLLELAGIPYVGS 118
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
59-296 |
5.00e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 53.95 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 59 LGLDKLLSFDSVARPVDYVVP--C--IH---GYPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNT 131
Cdd:PRK07178 51 IGADPLAGYLNPRRLVNLAVEtgCdaLHpgyGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 132 PYlflTEQGEASLTEAKAALAKWG-KVFIKAASQGSSVG---CYSA----SNEADLVKGIADAFGYSEqVLIEKA-VKPR 202
Cdd:PRK07178 131 PG---SEGNLADLDEALAEAERIGyPVMLKATSGGGGRGirrCNSReeleQNFPRVISEATKAFGSAE-VFLEKCiVNPK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 203 ELEVAVyqygdelVATYPGEIcvpqdkFYTYEEKYSSASHTETALK---AEGLTQAQADAIHEYALKAFRQLKLTHLSRI 279
Cdd:PRK07178 207 HIEVQI-------LADSHGNV------VHLFERDCSIQRRNQKLIEiapSPQLTPEQRAYIGDLAVRAAKAVGYENAGTV 273
|
250
....*....|....*..
gi 752543647 280 DFFLTEEGEILLNEINT 296
Cdd:PRK07178 274 EFLLDADGEVYFMEMNT 290
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
127-294 |
2.05e-06 |
|
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: 47.25 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 127 GIPNTPYLFLTeqgeaSLTEAKAALAKWGKVF-IKAASQGSS-VGCYSASNEADLVKGIADAFGysEQVLIEKAVK-PRE 203
Cdd:pfam02222 4 GLPTPRFMAAE-----SLEELIEAGQELGYPCvVKARRGGYDgKGQYVVRSEADLPQAWEELGD--GPVIVEEFVPfDRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 204 LEVAVYQYGDELVATYPGEICVPQDKfyTYEEKYSSASHTETALKaegltQAQadaihEYALKAFRQLKLTHLSRIDFFL 283
Cdd:pfam02222 77 LSVLVVRSVDGETAFYPVVETIQEDG--ICRLSVAPARVPQAIQA-----EAQ-----DIAKRLVDELGGVGVFGVELFV 144
|
170
....*....|.
gi 752543647 284 TEEGEILLNEI 294
Cdd:pfam02222 145 TEDGDLLINEL 155
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
98-296 |
4.56e-06 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 48.21 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 98 AGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYlflTEQGEASLTEAKAALAKWG-KVFIKAASQGSSVGCYSASNE 176
Cdd:PRK12999 102 AGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPG---SEGPIDDIEEALEFAEEIGyPIMLKASAGGGGRGMRIVRSE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 177 ADLVKGIADA-------FGYSEqVLIEKAV-KPRELEVAVyqYGDELvatypGEIcvpqdkFYTYEEKYS-SASH---TE 244
Cdd:PRK12999 179 EELEEAFERAkreakaaFGNDE-VYLEKYVeNPRHIEVQI--LGDKH-----GNV------VHLYERDCSvQRRHqkvVE 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 752543647 245 TAlKAEGLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEEGEILLNEINT 296
Cdd:PRK12999 245 IA-PAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNP 295
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
82-296 |
7.09e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 47.44 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 82 HGYPGETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPylflTEQGE-ASLTEAKAALAKWG-KVFI 159
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVP----GSDGVvASLDAALEVAARIGyPLMI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 160 KAASQGSSVGCYSASNEADLVKGI-------ADAFGySEQVLIEKAV-KPRELEVAVYQYGDELVATYPGEICVPQDKFY 231
Cdd:PRK12833 161 KAAAGGGGRGIRVAHDAAQLAAELplaqreaQAAFG-DGGVYLERFIaRARHIEVQILGDGERVVHLFERECSLQRRRQK 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752543647 232 TYEEKYSSAshtetalkaegLTQAQADAIHEYALKAFRQLKLTHLSRIDF-FLTEEGEILLNEINT 296
Cdd:PRK12833 240 ILEEAPSPS-----------LTPAQRDALCASAVRLARQVGYRGAGTLEYlFDDARGEFYFIEMNT 294
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
95-299 |
2.21e-05 |
|
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: 45.32 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 95 LELAGLPYLGcDAEASKVCFNKITTKLWLTAIGIPnTPYLFLTEqgeaSLTEAKAALAKWG-KVFIKAA--SQGSSVgcY 171
Cdd:COG0189 77 LEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIP-VPPTLVTR----DPDDLRAFLEELGgPVVLKPLdgSGGRGV--F 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 172 SASNEADLVKGIADAFGYSEQVLI--EKAVKPRELEVAVYQYGDELVATYpgeicvpqdkfytyeEKYSSASHTETALKA 249
Cdd:COG0189 149 LVEDEDALESILEALTELGSEPVLvqEFIPEEDGRDIRVLVVGGEPVAAI---------------RRIPAEGEFRTNLAR 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 752543647 250 EGLTQAQA--DAIHEYALKAFRQLKLtHLSRIDFFLTEEGeILLNEINTFPG 299
Cdd:COG0189 214 GGRAEPVEltDEERELALRAAPALGL-DFAGVDLIEDDDG-PLVLEVNVTPG 263
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
98-296 |
4.81e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 44.63 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 98 AGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYlflTEQGEASLTEAKAALAKWG-KVFIKAASQGSSVGCYSASNE 176
Cdd:PRK06111 98 EGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPG---ITTNLEDAEEAIAIARQIGyPVMLKASAGGGGIGMQLVETE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 177 ADLVKGI-------ADAFGYSEqVLIEKAV-KPRELEVAVY--QYGDelvATYPGEI-CVPQDKfytyEEKYssashTET 245
Cdd:PRK06111 175 QELTKAFesnkkraANFFGNGE-MYIEKYIeDPRHIEIQLLadTHGN---TVYLWEReCSVQRR----HQKV-----IEE 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 752543647 246 AlKAEGLTQAQADAIHEYALKAFRQLKLTHLSRIDFFLTEEGEILLNEINT 296
Cdd:PRK06111 242 A-PSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNT 291
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
95-301 |
9.19e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 41.11 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 95 LELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPYLFLTeqgeaSLTEAKAALAKWG-KVFIKAASQGSSVGCYSA 173
Cdd:PRK12815 650 LEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTAT-----DEEEAFAFAKRIGyPVLIRPSYVIGGQGMAVV 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 174 SNEADLVKGIADAFGYSEQVLIEKAVKPRELEV-AVYQYGDELVATYPGEIcvpqdkfytyEEKYSSASHTETALKAEGL 252
Cdd:PRK12815 725 YDEPALEAYLAENASQLYPILIDQFIDGKEYEVdAISDGEDVTIPGIIEHI----------EQAGVHSGDSIAVLPPQSL 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 752543647 253 TQAQADAIHEYALKAFRQLKLTHLSRIDFFLtEEGEILLNEINTFPGMT 301
Cdd:PRK12815 795 SEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVLEVNPRASRT 842
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
81-208 |
2.98e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 39.01 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752543647 81 IHgyPG-----ETGDLQSFLELAGLPYLGCDAEASKVCFNKITTKLWLTAIGIPNTPylflTEQGE-ASLTEAKAALAKW 154
Cdd:PRK08591 78 IH--PGygflsENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP----GSDGPvDDEEEALAIAKEI 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752543647 155 G-KVFIKAASQGSSVGCYSASNEADLVKGIA-------DAFGySEQVLIEKAV-KPRELEVAV 208
Cdd:PRK08591 152 GyPVIIKATAGGGGRGMRVVRTEAELEKAFSmaraeakAAFG-NPGVYMEKYLeNPRHIEIQV 213
|
|
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