|
Name |
Accession |
Description |
Interval |
E-value |
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
1-343 |
0e+00 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 503.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 1 MAKENVCIVYGGKSAEHDVSILTAQNVLNAIDKERYQIDIIYITNDGAWkkkeniVDTINDIDSLRLIDVEAGEISKLLS 80
Cdd:PRK01966 1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRW------YLIDADNMELADDDNDKEDLSLLIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 81 QGSTGNAYSAVFPLLHGPNGEDGTIQGLFEVLDIPYVGNGVLAASSSMDKLVMKQLFAHRGLPQLPYVSFLRSEYHKYeg 160
Cdd:PRK01966 75 PSGGSEEVDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLTRGDWEEA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 161 nILKLVHDKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEEAFQFDRKLVIEQGIEAREIEVAVLGNDyPETTWPGEVI 240
Cdd:PRK01966 153 -SLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGND-PKASVPGEIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 241 KEVAFYDYKAKYKDGKIKLDIPADLDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTDDNQIFINETNAMPGFTAFSMYP 320
Cdd:PRK01966 231 KPDDFYDYEAKYLDGSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMPGFTPISMYP 310
|
330 340
....*....|....*....|...
gi 1539269555 321 SLWENMGVSYSDLIKKLIELAKE 343
Cdd:PRK01966 311 KLWEASGLSYPELIDRLIELALE 333
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
5-341 |
4.79e-142 |
|
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: 404.49 E-value: 4.79e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 5 NVCIVYGGKSAEHDVSILTAQNVLNAIDKERYQIDIIYItndgawkkkenivDTINDIDSLRLIDVEAgeiskllsqgst 84
Cdd:COG1181 2 RVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGI-------------DVEDLPAALKELKPDV------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 85 gnaysaVFPLLHGPNGEDGTIQGLFEVLDIPYVGNGVLAASSSMDKLVMKQLFAHRGLPQLPYVSFLRSEYhkyegNILK 164
Cdd:COG1181 57 ------VFPALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGEL-----ADLE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 165 LVHDKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEEAFQFDRKLVIEQGIEAREIEVAVLGNDYPETTWPGEVIKEVA 244
Cdd:COG1181 126 AIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGPRALPPIEIVPENG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 245 FYDYKAKYKDGKIKLDIPADLDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTDDNQIFINETNAMPGFTAFSMYPSLWE 324
Cdd:COG1181 206 FYDYEAKYTDGGTEYICPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMTPTSLLPKAAA 285
|
330
....*....|....*..
gi 1539269555 325 NMGVSYSDLIKKLIELA 341
Cdd:COG1181 286 AAGISYEELIERIIELA 302
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
6-341 |
1.91e-124 |
|
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: 360.45 E-value: 1.91e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 6 VCIVYGGKSAEHDVSILTAQNVLNAIDKERYQIDIIYITNDGAWKKKENIVDTINDIDSLRLIDVeageiskllsqgstg 85
Cdd:TIGR01205 2 VAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMGSWTYKDLPQLILELGALLEGIDV--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 86 naysaVFPLLHGPNGEDGTIQGLFEVLDIPYVGNGVLAASSSMDKLVMKQLFAHRGLPQLPYVsFLRSEYHKYEGNILKL 165
Cdd:TIGR01205 67 -----VFPVLHGRYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYI-VLTQNRASADELECEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 166 VHDKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEEAFQFDRKLVIEQGIEAREIEVAVLGND--YPETTWPGEVikeV 243
Cdd:TIGR01205 141 VAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEeaLPIIEIVPEI---E 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 244 AFYDYKAKYKDGKIKLDIPADLDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTDDNQIFINETNAMPGFTAFSMYPSLW 323
Cdd:TIGR01205 218 GFYDYEAKYLDGSTEYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTIPGMTAISLFPKAA 297
|
330
....*....|....*...
gi 1539269555 324 ENMGVSYSDLIKKLIELA 341
Cdd:TIGR01205 298 AAAGIEFSQLVERILELA 315
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
136-339 |
2.26e-94 |
|
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: 279.59 E-value: 2.26e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 136 LFAHRGLPQLPYVSFLRSEYHKYEGNILKLVHDKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEEAFQFDRKLVIEQG 215
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 216 IEAREIEVAVLGNDYPETTWPGEVIKEVAFYDYKAKYKDGKIKLDIPADLDEEVQMTLRNMAVEAFKATDCAGLLRADFF 295
Cdd:pfam07478 81 IEGREIECAVLGNEDPEVSPVGEIVPSGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDFF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1539269555 296 VTDDNQIFINETNAMPGFTAFSMYPSLWENMGVSYSDLIKKLIE 339
Cdd:pfam07478 161 LTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
1-343 |
2.03e-83 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 255.42 E-value: 2.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 1 MAKENVCIVYGGKSAEHDVSILTAQNVLNAIDKERYQIDIIyitndgawkkkenivDTINDIdslrlidveageISKLLS 80
Cdd:PRK01372 2 KMFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAHPI---------------DPGEDI------------AAQLKE 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 81 QGstgnaYSAVFPLLHGPNGEDGTIQGLFEVLDIPYVGNGVLAASSSMDKLVMKQLFAHRGLPQLPYVSFLRSEyhkyeg 160
Cdd:PRK01372 55 LG-----FDRVFNALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREE------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 161 nILKLVHDKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEEAFQFDRKLVIEQGIEAREIEVAVLGND-YPettwpgeV 239
Cdd:PRK01372 124 -DLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVLGGKaLP-------V 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 240 IKEVA---FYDYKAKYKDGKIKLDIPADLDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTDDNQIFINETNAMPGFTAF 316
Cdd:PRK01372 196 IEIVPageFYDYEAKYLAGGTQYICPAGLPAEIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNTQPGMTSH 275
|
330 340
....*....|....*....|....*..
gi 1539269555 317 SMYPSLWENMGVSYSDLIKKLIELAKE 343
Cdd:PRK01372 276 SLVPMAARAAGISFSELVDRILEDALC 302
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
3-350 |
1.80e-69 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 221.63 E-value: 1.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 3 KENVCIVYGGKSAEHDVSILTAQNVLNAI-DKERYQIDIIYITN-DGAWKkkenIVDTINDidSLRLIDVEAGEISKLLS 80
Cdd:PRK14570 2 KKNLMLIFGGVSFEHEISLRSAYGIYSALlKLDKYNIYSVFIDKcTGIWY----LLDSVPD--PPKLIKRDVLPIVSLIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 81 Q-GSTGNAYS----AVFPLLHGPNGEDGTIQGLFEVLDIPYVGNGVLAASSSMDKLVMKQLFAHRGLPQLPYVSFLRSEY 155
Cdd:PRK14570 76 GcGIFVNNKNleidVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPFIGFRKYDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 156 HKYEGNILKLVHDKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEEAFQFDRKLVIEQGIEAREIEVAVLGNDYPETTW 235
Cdd:PRK14570 156 FLDKEGIKKDIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIGNEQIKIFT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 236 PGE-VIKEVAFYDYKAKYK---DGKIKLDIPADLDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTDD-NQIFINETNAM 310
Cdd:PRK14570 236 PGEiVVQDFIFYDYDAKYStipGNSIVFNIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKDtGLIYLNEINTI 315
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1539269555 311 PGFTAFSMYPSLWENMGVSYSDLIKKLIELAKEKHEDKKQ 350
Cdd:PRK14570 316 PGFTDISMFAKMCEHDGLQYKSLVDNLIDLAFQSYIKRKK 355
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
3-350 |
1.13e-60 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 208.13 E-value: 1.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 3 KENVCIVYGGKSAEHDVSILTAQNVLNAIDKERYQIDIIYITNDGAWKKKENIVDTINDIDSLRLIDVE-AGEISKLlsq 81
Cdd:PRK14573 451 KLSLGLVCGGKSCEHDISLLSAKNIAKYLSPEFYDVSYFLINRQGLWETVSSLETAIEEDSGKSVLSSEiAQALAKV--- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 82 gstgnaySAVFPLLHGPNGEDGTIQGLFEVLDIPYVGNGVLAASSSMDKLVMKQLFAHRGLPQLPYVSFLRSEYHKYEGN 161
Cdd:PRK14573 528 -------DVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQPLTLAGWKREPEL 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 162 ILKLVHDKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEEAFQFDRKLVIEQG-IEAREIEVAVLGNdypETTW----- 235
Cdd:PRK14573 601 CLAHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEESrLGSREIEVSCLGD---GSSAyviag 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 236 PGEVIKEVAFYDYKAKYK-DGKIKLDIPADLD--EEVQMTLRNMAVEAFKATDCAGLLRADFFVTDDNQIFINETNAMPG 312
Cdd:PRK14573 678 PHERRGSGGFIDYQEKYGlSGKSSAQIVFDLDlsKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMNPIPG 757
|
330 340 350
....*....|....*....|....*....|....*...
gi 1539269555 313 FTAFSMYPSLWENMGVSYSDLIKKLIELAKEKHEDKKQ 350
Cdd:PRK14573 758 MTEASPFLTAFVRKGWTYEQIVHQLIIDGLHKFDQRQR 795
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
1-341 |
1.09e-54 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 182.80 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 1 MAKenVCIVYGGKSAEHDVSILTAQNVLNAIDKERYQIDIIYITNDGAWkkkenIVDTINDIdslrLIDVEAGEISKLLS 80
Cdd:PRK14572 1 MAK--IAVFFGGSSTEHSISIRTGCFICATLHTMGHSVKPILLTPDGGW-----VVPTVYRP----SIPDESGNSEDLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 81 QG-STGNAYS-----------AVFPLLHGPNGEDGTIQGLFEVLDIPYVGNGVLAASSSMDKLVMKQLFAHRGLPQLPYV 148
Cdd:PRK14572 70 EEfQKANGVSepadisqldadIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPFF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 149 SFLRSEY-HKYEGNILKLvhDKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEEAFQFDRKLVIEQGIEAREIEVAVL- 226
Cdd:PRK14572 150 ELEKLKYlNSPRKTLLKL--ESLGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVLe 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 227 ----GNDYPETTWPGEVIKEVAFYDYKAKYKDGKIKLDIPADLDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTdDNQI 302
Cdd:PRK14572 228 ryrgGKRNPIALPATEIVPGGEFFDFESKYKQGGSEEITPARISDQEMKRVQELAIRAHESLGCKGYSRTDFIIV-DGEP 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 1539269555 303 FINETNAMPGFTAFSMYPSLWENMGVSYSDLIKKLIELA 341
Cdd:PRK14572 307 HILETNTLPGMTETSLIPQQAKAAGINMEEVFTDLIEIG 345
|
|
| Dala_Dala_lig_N |
pfam01820 |
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the ... |
5-118 |
8.25e-45 |
|
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: 149.68 E-value: 8.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 5 NVCIVYGGKSAEHDVSILTAQNVLNAIDKERYQIDIIYITNDGAWKKKENIVDTINDIDSLRLIDVEAGEISKLLSQGST 84
Cdd:pfam01820 1 KVAVLFGGRSSEHEVSLVSARSVLKALDKEKYEVIPIGITKDGRLGEAALRELASDDGLLLEVDDAPDGGPAGLLFGPNV 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1539269555 85 GNAYSA---VFPLLHGPNGEDGTIQGLFEVLDIPYVG 118
Cdd:pfam01820 81 LELLIEvdvVFPVLHGPNGEDGTLQGLLELAGIPYVG 117
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
1-342 |
7.13e-41 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 145.20 E-value: 7.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 1 MAKENVCIVYGGKSAEHDVSILTAQNVLNAIDKERYqidiiyitndgawkkkenivDTINdidslrlIDVEAGE-ISKLL 79
Cdd:PRK14569 1 MKNEKIVVLYGGDSPEREVSLKSGKAVLDSLISQGY--------------------DAVG-------VDASGKElVAKLL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 80 SQGStgnaySAVFPLLHGPNGEDGTIQGLFEVLDIPYVGNGVLAASSSMDKLVMKQLFAHRGLPQlPYVSFLRSeyhkye 159
Cdd:PRK14569 54 ELKP-----DKCFVALHGEDGENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPT-PMAKFLTD------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 160 gnilKLVH-DKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEEAFQFDrKLVIEQGIEAREIEVAVLGNDYPETTWpge 238
Cdd:PRK14569 122 ----KLVAeDEISFPVAVKPSSGGSSIATFKVKSIQELKHAYEEASKYG-EVMIEQWVTGKEITVAIVNDEVYSSVW--- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 239 VIKEVAFYDYKAKYKdGKIKLDIPADLDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTDDNQIFINETNAMPGFTAFSM 318
Cdd:PRK14569 194 IEPQNEFYDYESKYS-GKSIYHSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEINSSPGMTDNSL 272
|
330 340
....*....|....*....|....
gi 1539269555 319 YPSLWENMGVSYSDLIKKLIELAK 342
Cdd:PRK14569 273 SPKSAAAEGVDFDSFVKRIIEQAQ 296
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
6-344 |
6.80e-40 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 142.65 E-value: 6.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 6 VCIVYGGKSAEHDVSILTAQNVLNAIDKERYQIDIIYItndgawkkKENIVDTINDIDSlrlidveageiskllsqgstg 85
Cdd:PRK14571 3 VALLMGGVSREREISLRSGERVKKALEKLGYEVTVFDV--------DEDFLKKVDQLKS--------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 86 naYSAVFPLLHGPNGEDGTIQGLFEVLDIPYVGNGVLAASSSMDKLVMKQLFahRGLPQLPYVSFLRsEYHKYEgnilkl 165
Cdd:PRK14571 54 --FDVVFNVLHGTFGEDGTLQAILDFLGIRYTGSDAFSSMICFDKLLTYRFL--KGTVEIPDFVEIK-EFMKTS------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 166 vhdKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEEAFQFDRKLVIEQGIEAREIEVAVLG-NDYPETTWPGEVIKEVA 244
Cdd:PRK14571 123 ---PLGYPCVVKPRREGSSIGVFICESDEEFQHALKEDLPRYGSVIVQEYIPGREMTVSILEtEKGFEVLPILELRPKRR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 245 FYDYKAKYKDGKIKLDIPADLDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTdDNQIFINETNAMPGFTAFSMYPSLWE 324
Cdd:PRK14571 200 FYDYVAKYTKGETEFILPAPLNPEEERLVKETALKAFVEAGCRGFGRVDGIFS-DGRFYFLEINTVPGLTELSDLPASAK 278
|
330 340
....*....|....*....|
gi 1539269555 325 NMGVSYSDLIKKLIELAKEK 344
Cdd:PRK14571 279 AGGIEFEELVDIIIKSAFLK 298
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
110-309 |
1.45e-20 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 89.55 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 110 EVLDIPyvGNGVLAASSSMDKLVMKQLFAHRGLPQLPYVSfLRSEYHkyegniLKLVHDKLEYPVFVKPANLGSSVGISK 189
Cdd:COG0439 37 EELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFAL-VDSPEE------ALAFAEEIGYPVVVKPADGAGSRGVRV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 190 CNNEEELKNGIEEA------FQFDRKLVIEQGIEAREIEVAVLGNDypettwpGEVIkevaFYDYKAKYKDGK----IKL 259
Cdd:COG0439 108 VRDEEELEAALAEAraeakaGSPNGEVLVEEFLEGREYSVEGLVRD-------GEVV----VCSITRKHQKPPyfveLGH 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1539269555 260 DIPADLDEEVQMTLRNMAVEAFKAtdcAGLLR----ADFFVTDDNQIFINETNA 309
Cdd:COG0439 177 EAPSPLPEELRAEIGELVARALRA---LGYRRgafhTEFLLTPDGEPYLIEINA 227
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
125-344 |
3.54e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 63.36 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 125 SSSMDKLVMKQLFAHRGLPQLPyvSFLRSEYhkyEGNILKLVHDKLEYPVFVKPANLGSSVGISKCNNEEELKNgieeAF 204
Cdd:PRK12767 107 EICNDKWLTYEFLKENGIPTPK--SYLPESL---EDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEF----LL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 205 QFDRKLVIEQGIEAREIEVAVLgNDYP-----------ETTWPGEVIKEVAFYDYKakykdgkikldipadldeevqmtL 273
Cdd:PRK12767 178 EYVPNLIIQEFIEGQEYTVDVL-CDLNgevisivprkrIEVRAGETSKGVTVKDPE-----------------------L 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1539269555 274 RNMAVEAFKATDCAGLLRADFFVTDDnQIFINETNamPGF---TAFSMYpslwenMGVSYSDLIKKLIELAKEK 344
Cdd:PRK12767 234 FKLAERLAEALGARGPLNIQCFVTDG-EPYLFEIN--PRFgggYPLSYM------AGANEPDWIIRNLLGGENE 298
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
108-313 |
7.30e-09 |
|
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: 56.10 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 108 LFEVLDIPYVgNGVLAASSSMDKLVMKQLFAHRGLPqLPYVSFLRSEyhkyegNILKLVHDKLEYPVFVKPANLGSSVGI 187
Cdd:COG0189 76 QLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIP-VPPTLVTRDP------DDLRAFLEELGGPVVLKPLDGSGGRGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 188 SKCNNEEELKNGIEEAFQFDRKLVIEQ----GIEAREIEVAVLGndypettwpGEVikeVAFYDYKAKYKDGKIKLD--- 260
Cdd:COG0189 148 FLVEDEDALESILEALTELGSEPVLVQefipEEDGRDIRVLVVG---------GEP---VAAIRRIPAEGEFRTNLArgg 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1539269555 261 --IPADLDEEVqmtlRNMAVEAFKATDcAGLLRADFFVTDDNqIFINETNAMPGF 313
Cdd:COG0189 216 raEPVELTDEE----RELALRAAPALG-LDFAGVDLIEDDDG-PLVLEVNVTPGF 264
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
163-306 |
3.34e-08 |
|
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: 52.64 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 163 LKLVHDKLEYPVFVKPANLGSS-VGISKCNNEEELKNGIEEAFqfDRKLVIEQGIEArEIEVAVLGndypETTWPGEVik 241
Cdd:pfam02222 19 LIEAGQELGYPCVVKARRGGYDgKGQYVVRSEADLPQAWEELG--DGPVIVEEFVPF-DRELSVLV----VRSVDGET-- 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539269555 242 evAFYD-YKAKYKDGKIKLDI-PADLDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTDDNQIFINE 306
Cdd:pfam02222 90 --AFYPvVETIQEDGICRLSVaPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINE 154
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
129-308 |
8.19e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 53.49 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 129 DKLVMKQLFAHRGLPQLPYVSFLRSEYHKyegnILKLVHDkLEYPVFVKPANLGSSVGISKCNNEEELKNGIE----EAF 204
Cdd:PRK06111 115 SKIEARRAMQAAGVPVVPGITTNLEDAEE----AIAIARQ-IGYPVMLKASAGGGGIGMQLVETEQELTKAFEsnkkRAA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 205 QF--DRKLVIEQGIE-AREIEVAVLGNDYPETTWPGEvikevafYDYKAKYKDGKIKLDIPAD-LDEEVQMTLRNMAVEA 280
Cdd:PRK06111 190 NFfgNGEMYIEKYIEdPRHIEIQLLADTHGNTVYLWE-------RECSVQRRHQKVIEEAPSPfLDEETRKAMGERAVQA 262
|
170 180
....*....|....*....|....*...
gi 1539269555 281 FKATDCAGLLRADFFVTDDNQIFINETN 308
Cdd:PRK06111 263 AKAIGYTNAGTIEFLVDEQKNFYFLEMN 290
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
129-319 |
9.29e-06 |
|
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: 46.57 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 129 DKLVMKQLFAHRGLPQlP--YVSFlrseyhkyEGNILKLVHDKLEYPVFVKPANLGSSVGISKCNNEEELKNGIE--EAF 204
Cdd:TIGR00768 88 DKFLSHQLLAKAGIPL-PrtGLAG--------SPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEhfEQL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 205 QFDRKLVIEQGI----EAREIEVAVLGNDYP---ETTWPGEVIKEVAfydykakyKDGKIKldiPADLDEEVqmtlRNMA 277
Cdd:TIGR00768 159 NGPQNLFLVQEYikkpGGRDIRVFVVGDEVVaaiYRITSGHWRSNLA--------RGGKAE---PCSLTEEI----EELA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1539269555 278 VEAFKAT--DCAGLlraDFFVTDDNQIfINETNAMPGFTAFSMY 319
Cdd:TIGR00768 224 IKAAKALglDVAGV---DLLESEDGLL-VNEVNANPEFKNSVKT 263
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
158-355 |
1.16e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 47.01 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 158 YEGNI------LKLVhDKLEYPVFVKPANLGSSVGISKCNNEEELKNGIE------EAFQFDRKLVIEQGIEA-REIEVA 224
Cdd:PRK05586 134 SEGEIeneeeaLEIA-KEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNtakseaKAAFGDDSMYIEKFIENpKHIEFQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 225 VLGNDYPETTWPGEvikevafYDYKAKYKDGKIKLDIPAD-LDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTDDNQIF 303
Cdd:PRK05586 213 ILGDNYGNVVHLGE-------RDCSLQRRNQKVLEEAPSPvMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFY 285
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1539269555 304 INETNampgfTAFSMYPSLWENM-GVsysDLIKKLIELAKEKHEDKKQNKYKI 355
Cdd:PRK05586 286 FMEMN-----TRIQVEHPITEMItGV---DLVKEQIKIAYGEKLSIKQEDIKI 330
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
129-306 |
1.52e-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: 46.22 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 129 DKLVMKQLFAHRGLPQLPYVSFlrseyhKYEGNILKLVhDKLEYPVFVKPANLGss-vGISKCNNEEELkngiEEAFQF- 206
Cdd:COG0026 89 DRLLEKAFLAELGIPVAPFAAV------DSLEDLEAAI-AELGLPAVLKTRRGGydgkGQVVIKSAADL----EAAWAAl 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 207 -DRKLVIEQGIE-AREIEV-AVLGNDypettwpgeviKEVAFYD----YkakYKDGkIkLD---IPADLDEEVQMTLRNM 276
Cdd:COG0026 158 gGGPCILEEFVPfERELSViVARSPD-----------GEVATYPvvenV---HRNG-I-LDesiAPARISEALAAEAEEI 221
|
170 180 190
....*....|....*....|....*....|
gi 1539269555 277 AVEAFKATDCAGLLRADFFVTDDNQIFINE 306
Cdd:COG0026 222 AKRIAEALDYVGVLAVEFFVTKDGELLVNE 251
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
172-312 |
9.50e-05 |
|
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: 42.27 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 172 YPVFVKPANLGSSVGISKCNNEEELKNGI----EEAFQF----------DRKLVIEQGIEAREIEVAVLgndYPETTWPg 237
Cdd:pfam13535 3 YPCVIKPSVGFFSVGVYKINNREEWKAAFaairEEIEQWkemypeavvdGGSFLVEEYIEGEEFAVDAY---FDENGEP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 238 eVIKEVAFYDYkAKYKDGKIKLDI-PADLDEEVQMTLRNMAVEAFKAtdcAGL----LRADFFVTDDNQIFINETNAMPG 312
Cdd:pfam13535 79 -VILNILKHDF-ASSEDVSDRIYVtSASIIRETQAAFTEFLKRINAL---LGLknfpVHIELRVDEDGQIIPIEVNPLRF 153
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
113-308 |
1.76e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 43.19 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 113 DIPYVGNGVLAASSSMDKLVMKQLFAHRGLPQLPYVSFLRSEYHKyegniLKLVHDKLEYPVFVKPANLGSSVGISKCNN 192
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEE-----AKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 193 EEELKNGI-------EEAFQfDRKLVIEQGIE-AREIEVAVLGNDYpettwpGEVIkEVAFYDYKAKYKDGKIKLDIPAD 264
Cdd:PRK08462 176 ESDLENLYlaaeseaLSAFG-DGTMYMEKFINnPRHIEVQILGDKH------GNVI-HVGERDCSLQRRHQKLIEESPAV 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1539269555 265 -LDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTDDNQIFINETN 308
Cdd:PRK08462 248 vLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMN 292
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
129-319 |
4.22e-04 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 40.95 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 129 DKLVMKQLFAHRGLPqlPYVSFLRSEYHKYEGNILKLvhdKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEeafQFDR 208
Cdd:pfam08443 3 DKAKSHQLLAKHGIG--PPNTRLAWYPEDAEQFIEQI---KRQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLS---ATNE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 209 KLVIEQGI---EAREIEVAVLGNdypettwpgEVikeVAFYDYKAKYKDGKIKLDI-----PADLDEEvqmtLRNMAVEA 280
Cdd:pfam08443 75 QILVQEFIaeaNNEDIRCLVVGD---------QV---VGALHRQSNEGDFRSNLHRggvgeKYQLSQE----ETELAIKA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1539269555 281 FKAT--DCAGLlraDFFVTDDNQIFInETNAMPGFTAFSMY 319
Cdd:pfam08443 139 AQAMqlDVAGV---DLLRQKRGLLVC-EVNSSPGLEGIEKT 175
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
159-308 |
7.28e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 41.24 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 159 EGNILKLVH-----DKLEYPVFVKPANLGSSVGISKCNNEEELKNG----IEEAFQ-FDRKLV-IEQGI-EAREIEVAVL 226
Cdd:PRK07178 134 EGNLADLDEalaeaERIGYPVMLKATSGGGGRGIRRCNSREELEQNfprvISEATKaFGSAEVfLEKCIvNPKHIEVQIL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 227 GNDYpettwpGEVIkEVAFYDYKAKYKDGK-IKLDIPADLDEEVQMTLRNMAVEAFKATDCAGLLRADFFVTDDNQIFIN 305
Cdd:PRK07178 214 ADSH------GNVV-HLFERDCSIQRRNQKlIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFM 286
|
...
gi 1539269555 306 ETN 308
Cdd:PRK07178 287 EMN 289
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
168-226 |
9.02e-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: 41.02 E-value: 9.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1539269555 168 DKLEYPVFVKPA-NL-GSSVGIskCNNEEELKNGIEEAFQF--DRKLVIEQGIE-AREIEVAVL 226
Cdd:COG0458 146 EEIGYPVIVRPSyVLgGRGMGI--VYNEEELEEYLERALKVspDHPVLIDESLLgAKEIEVDVV 207
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
164-230 |
9.73e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 40.74 E-value: 9.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539269555 164 KLVHDKLEYPVFVKPANLGSSVGISKCNNEEELKNGIE-------EAFQfDRKLVIEQGIE-AREIEVAVLGNDY 230
Cdd:PRK08654 145 KEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIEstqsiaqSAFG-DSTVFIEKYLEkPRHIEIQILADKH 218
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
172-309 |
1.71e-03 |
|
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: 39.21 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 172 YPVFVKPANLGSSVGISKCNNEEELKNGIEEAFQ------FDRKLVIEQGIEA-REIEVAVLGNDYPETTWPGEVikeva 244
Cdd:pfam02786 39 YPVIIKAAFGGGGLGMGIARNEEELAELFALALAeapaafGNPQVLVEKSLKGpKHIEYQVLRDAHGNCITVCNR----- 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539269555 245 fyDYKAKYKDGKIKLDIPADL--DEEVQMtLRNMAVEAFKATDCAGLLRADFFV-TDDNQIFINETNA 309
Cdd:pfam02786 114 --ECSDQRRTQKSIEVAPSQTltDEERQM-LREAAVKIARHLGYVGAGTVEFALdPFSGEYYFIEMNT 178
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
168-247 |
7.84e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 38.20 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539269555 168 DKLEYPVFVKPANLGSSVGISKCNNEEELKNGIEEA-------FQFDRkLVIEQGIE-AREIEVAVLGNDYpettwpGEV 239
Cdd:PRK12999 153 EEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAkreakaaFGNDE-VYLEKYVEnPRHIEVQILGDKH------GNV 225
|
....*...
gi 1539269555 240 ikeVAFYD 247
Cdd:PRK12999 226 ---VHLYE 230
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