|
Name |
Accession |
Description |
Interval |
E-value |
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
1-349 |
0e+00 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 516.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 1 MKTSLGLVYGGKSAEHNVSLQTALAVIKALNTEKFDIHPIYITEKGEWVRGARLTEPVSnvkmlQFEQGGSAFSPAALNq 80
Cdd:PRK01966 2 MKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRWYLIDADNMELA-----DDDNDKEDLSLLILP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 81 emfpqeaSQQNEAIDVVFPLLHGPNGEDGTIQGMLELLNIPYVGNGVLASSAGMDKVVMKHLFAQAGLAQAKYAAFLKKD 160
Cdd:PRK01966 76 -------SGGSEEVDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLTRGD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 161 WTrspKESCEQVEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYDRKVVVEEGINGREIEIGVLGNDdPKCS 240
Cdd:PRK01966 149 WE---EASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGND-PKAS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 241 VVGEIAPKTDFYDYKAKYEDGDTDLMIPAIVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTADGEVLINEVNTMPGFT 320
Cdd:PRK01966 225 VPGEIVKPDDFYDYEAKYLDGSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMPGFT 304
|
330 340
....*....|....*....|....*....
gi 504288768 321 PFSMFPLLWKEAGVEYADLIEQLVELAKE 349
Cdd:PRK01966 305 PISMYPKLWEASGLSYPELIDRLIELALE 333
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
6-347 |
1.10e-157 |
|
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: 444.16 E-value: 1.10e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 6 GLVYGGKSAEHNVSLQTALAVIKALNTEKFDIHPIYItekgewvrgarltepvsNVKMLqfeqggsafsPAALNQEmfpq 85
Cdd:COG1181 4 AVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGI-----------------DVEDL----------PAALKEL---- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 86 easqqneAIDVVFPLLHGPNGEDGTIQGMLELLNIPYVGNGVLASSAGMDKVVMKHLFAQAGLAQAKYAAFLKKDWtrsp 165
Cdd:COG1181 53 -------KPDVVFPALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGEL---- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 166 kESCEQVEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYDRKVVVEEGINGREIEIGVLGNDDPKCSVVGEI 245
Cdd:COG1181 122 -ADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGPRALPPIEI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 246 APKTDFYDYKAKYEDGDTDLMIPAIVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTADGEVLINEVNTMPGFTPFSMF 325
Cdd:COG1181 201 VPENGFYDYEAKYTDGGTEYICPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMTPTSLL 280
|
330 340
....*....|....*....|..
gi 504288768 326 PLLWKEAGVEYADLIEQLVELA 347
Cdd:COG1181 281 PKAAAAAGISYEELIERIIELA 302
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
4-347 |
2.06e-154 |
|
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: 436.72 E-value: 2.06e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 4 SLGLVYGGKSAEHNVSLQTALAVIKALNTEKFDIHPIYITEKGEWvrgarltePVSNVKMLQFEQGgsafspaalnqemf 83
Cdd:TIGR01205 1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMGSW--------TYKDLPQLILELG-------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 84 pqeasQQNEAIDVVFPLLHGPNGEDGTIQGMLELLNIPYVGNGVLASSAGMDKVVMKHLFAQAGLAQAKYAaFLKKDWTR 163
Cdd:TIGR01205 59 -----ALLEGIDVVFPVLHGRYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYI-VLTQNRAS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 164 SPKESCEQVEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYDRKVVVEEGINGREIEIGVLGNDD--PKCSV 241
Cdd:TIGR01205 133 ADELECEQVAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEEalPIIEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 242 VGEIapkTDFYDYKAKYEDGDTDLMIPAIVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTADGEVLINEVNTMPGFTP 321
Cdd:TIGR01205 213 VPEI---EGFYDYEAKYLDGSTEYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTIPGMTA 289
|
330 340
....*....|....*....|....*.
gi 504288768 322 FSMFPLLWKEAGVEYADLIEQLVELA 347
Cdd:TIGR01205 290 ISLFPKAAAAAGIEFSQLVERILELA 315
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
142-345 |
1.45e-116 |
|
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: 336.21 E-value: 1.45e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 142 LFAQAGLAQAKYAAFLKKDWTRSPKESCEQVEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYDRKVVVEEG 221
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 222 INGREIEIGVLGNDDPKCSVVGEIAPKTDFYDYKAKYEDGDTDLMIPAIVTDEEYATISDMAIKAFKAIDGSGLVRADFF 301
Cdd:pfam07478 81 IEGREIECAVLGNEDPEVSPVGEIVPSGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDFF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504288768 302 LTADGEVLINEVNTMPGFTPFSMFPLLWKEAGVEYADLIEQLVE 345
Cdd:pfam07478 161 LTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
6-350 |
1.28e-98 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 294.33 E-value: 1.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 6 GLVYGGKSAEHNVSLQTALAVIKALNTEKFDIHPIYITEKgewvRGARLTEpvsnvkmlqfeqggsafspaalnqemfpq 85
Cdd:PRK01372 8 AVLMGGTSAEREVSLNSGAAVLAALREAGYDAHPIDPGED----IAAQLKE----------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 86 easqqnEAIDVVFPLLHGPNGEDGTIQGMLELLNIPYVGNGVLASSAGMDKVVMKHLFAQAGLAQAKYAAfLKKDwtrsp 165
Cdd:PRK01372 55 ------LGFDRVFNALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIV-LTRE----- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 166 kESCEQVEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYDRKVVVEEGINGREIEIGVLGNDD-PkcsvVGE 244
Cdd:PRK01372 123 -EDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVLGGKAlP----VIE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 245 IAPKTDFYDYKAKYEDGDTDLMIPAIVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTADGEVLINEVNTMPGFTPFSM 324
Cdd:PRK01372 198 IVPAGEFYDYEAKYLAGGTQYICPAGLPAEIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNTQPGMTSHSL 277
|
330 340
....*....|....*....|....*.
gi 504288768 325 FPLLWKEAGVEYADLIEQLVELAKER 350
Cdd:PRK01372 278 VPMAARAAGISFSELVDRILEDALCD 303
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
2-347 |
6.03e-68 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 217.47 E-value: 6.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 2 KTSLGLVYGGKSAEHNVSLQTALAVIKALNTEKFDIHPIYITEKGEWVRGAR----LTEPVSNVKML---QFEQGGSAFS 74
Cdd:PRK14572 1 MAKIAVFFGGSSTEHSISIRTGCFICATLHTMGHSVKPILLTPDGGWVVPTVyrpsIPDESGNSEDLfleEFQKANGVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 75 PAALNQEMFpqeasqqneaiDVVFPLLHGPNGEDGTIQGMLELLNIPYVGNGVLASSAGMDKVVMKHLFAQAGLAQAKYA 154
Cdd:PRK14572 81 PADISQLDA-----------DIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPFF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 155 AFLKKDWTRSPKESCEQVEQeLGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYDRKVVVEEGINGREIEIGVL-- 232
Cdd:PRK14572 150 ELEKLKYLNSPRKTLLKLES-LGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVLer 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 233 ---GNDDPKCSVVGEIAPKTDFYDYKAKYEDGDTDLMIPAIVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTaDGEVL 309
Cdd:PRK14572 229 yrgGKRNPIALPATEIVPGGEFFDFESKYKQGGSEEITPARISDQEMKRVQELAIRAHESLGCKGYSRTDFIIV-DGEPH 307
|
330 340 350
....*....|....*....|....*....|....*...
gi 504288768 310 INEVNTMPGFTPFSMFPLLWKEAGVEYADLIEQLVELA 347
Cdd:PRK14572 308 ILETNTLPGMTETSLIPQQAKAAGINMEEVFTDLIEIG 345
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1-355 |
1.50e-66 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 214.31 E-value: 1.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 1 MKTSLGLVYGGKSAEHNVSLQTALAVIKAL-NTEKFDIHPIYITE-KGEWVRGARLTEPVSNVK-----MLQFEQGGSAF 73
Cdd:PRK14570 1 MKKNLMLIFGGVSFEHEISLRSAYGIYSALlKLDKYNIYSVFIDKcTGIWYLLDSVPDPPKLIKrdvlpIVSLIPGCGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 74 SpaalnqemfpqeaSQQNEAIDVVFPLLHGPNGEDGTIQGMLELLNIPYVGNGVLASSAGMDKVVMKHLFAQAGLAQAKY 153
Cdd:PRK14570 81 V-------------NNKNLEIDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 154 AAFLKKDWTRSPKESCEQVEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYDRKVVVEEGINGREIEIGVLG 233
Cdd:PRK14570 148 IGFRKYDYFLDKEGIKKDIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 234 NDDPKCSVVGEIAPKT-DFYDYKAKYE--DGDTDLM-IPAIVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTAD-GEV 308
Cdd:PRK14570 228 NEQIKIFTPGEIVVQDfIFYDYDAKYStiPGNSIVFnIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKDtGLI 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 504288768 309 LINEVNTMPGFTPFSMFPLLWKEAGVEYADLIEQLVELAKERHAEKQ 355
Cdd:PRK14570 308 YLNEINTIPGFTDISMFAKMCEHDGLQYKSLVDNLIDLAFQSYIKRK 354
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
2-361 |
4.70e-65 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 220.46 E-value: 4.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 2 KTSLGLVYGGKSAEHNVSLQTALAVIKALNTEKFDIHPIYITEKGEWvrgarltEPVSNVKMLQFE-QGGSAFSPaalnq 80
Cdd:PRK14573 451 KLSLGLVCGGKSCEHDISLLSAKNIAKYLSPEFYDVSYFLINRQGLW-------ETVSSLETAIEEdSGKSVLSS----- 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 81 emfpqEASQQNEAIDVVFPLLHGPNGEDGTIQGMLELLNIPYVGNGVLASSAGMDKVVMKHLFAQAGLAQAKYAAFLKKD 160
Cdd:PRK14573 519 -----EIAQALAKVDVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQPLTLAG 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 161 WTRSPKESCEQVEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYDRKVVVEEGING-REIEIGVLGnDDPKC 239
Cdd:PRK14573 594 WKREPELCLAHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEESRLGsREIEVSCLG-DGSSA 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 240 SVVGEIAPK---TDFYDYKAKYE-DG--------DTDLmipaivTDEEYATISDMAIKAFKAIDGSGLVRADFFLTADGE 307
Cdd:PRK14573 673 YVIAGPHERrgsGGFIDYQEKYGlSGkssaqivfDLDL------SKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGN 746
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 504288768 308 VLINEVNTMPGFTPFSMFPLLWKEAGVEYADLIEQLVELAKERHAEKQLIKHTF 361
Cdd:PRK14573 747 FWLSEMNPIPGMTEASPFLTAFVRKGWTYEQIVHQLIIDGLHKFDQRQRLISTF 800
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
5-347 |
2.91e-51 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 172.70 E-value: 2.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 5 LGLVYGGKSAEHNVSLQTALAVIKALNTEKFDIHPIYITEKgewvrgarltepvsnvkmlqfeqggsafspaalnqemFP 84
Cdd:PRK14571 3 VALLMGGVSREREISLRSGERVKKALEKLGYEVTVFDVDED-------------------------------------FL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 85 QEASQQNEaIDVVFPLLHGPNGEDGTIQGMLELLNIPYVGNGVLASSAGMDKVvMKHLFAQAGLAQAKYAaFLKKDWTRS 164
Cdd:PRK14571 46 KKVDQLKS-FDVVFNVLHGTFGEDGTLQAILDFLGIRYTGSDAFSSMICFDKL-LTYRFLKGTVEIPDFV-EIKEFMKTS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 165 PkesceqveqeLGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYDRKVVVEEGINGREIEIGVLG-NDDPKCSVVG 243
Cdd:PRK14571 123 P----------LGYPCVVKPRREGSSIGVFICESDEEFQHALKEDLPRYGSVIVQEYIPGREMTVSILEtEKGFEVLPIL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 244 EIAPKTDFYDYKAKYEDGDTDLMIPAIVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTaDGEVLINEVNTMPGFTPFS 323
Cdd:PRK14571 193 ELRPKRRFYDYVAKYTKGETEFILPAPLNPEEERLVKETALKAFVEAGCRGFGRVDGIFS-DGRFYFLEINTVPGLTELS 271
|
330 340
....*....|....*....|....
gi 504288768 324 MFPLLWKEAGVEYADLIEQLVELA 347
Cdd:PRK14571 272 DLPASAKAGGIEFEELVDIIIKSA 295
|
|
| Dala_Dala_lig_N |
pfam01820 |
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the ... |
5-124 |
4.96e-46 |
|
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: 153.14 E-value: 4.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 5 LGLVYGGKSAEHNVSLQTALAVIKALNTEKFDIHPIYITEKGEWVRGARLTEPVSNVKMLQFEQGGSAFSPAALNQEMFP 84
Cdd:pfam01820 2 VAVLFGGRSSEHEVSLVSARSVLKALDKEKYEVIPIGITKDGRLGEAALRELASDDGLLLEVDDAPDGGPAGLLFGPNVL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 504288768 85 QEAsqqnEAIDVVFPLLHGPNGEDGTIQGMLELLNIPYVG 124
Cdd:pfam01820 82 ELL----IEVDVVFPVLHGPNGEDGTLQGLLELAGIPYVG 117
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
2-348 |
2.63e-32 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 122.86 E-value: 2.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 2 KTSLGLVYGGKSAEHNVSLQTALAVIKALNTEKFDIHPIYITEKgEWVrgarltepvsnVKMLQFEQggsafspaalnqe 81
Cdd:PRK14569 3 NEKIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAVGVDASGK-ELV-----------AKLLELKP------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 82 mfpqeasqqneaiDVVFPLLHGPNGEDGTIQGMLELLNIPYVGNGVLASSAGMDKVVMKHLFAQAGLAqAKYAAFLKKDW 161
Cdd:PRK14569 58 -------------DKCFVALHGEDGENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMP-TPMAKFLTDKL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 162 TRspkesceqvEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYDrKVVVEEGINGREIEIGVLgNDDPKCSV 241
Cdd:PRK14569 124 VA---------EDEISFPVAVKPSSGGSSIATFKVKSIQELKHAYEEASKYG-EVMIEQWVTGKEITVAIV-NDEVYSSV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 242 VgeIAPKTDFYDYKAKYEdGDTDLMIPAIVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTADGEVLINEVNTMPGFTP 321
Cdd:PRK14569 193 W--IEPQNEFYDYESKYS-GKSIYHSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEINSSPGMTD 269
|
330 340
....*....|....*....|....*..
gi 504288768 322 FSMFPLLWKEAGVEYADLIEQLVELAK 348
Cdd:PRK14569 270 NSLSPKSAAAEGVDFDSFVKRIIEQAQ 296
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
116-347 |
3.98e-28 |
|
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: 110.35 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 116 ELLNIPyvGNGVLASSAGMDKVVMKHLFAQAGLAQAKYAAFlkkdwtrSPKESCEQVEQELGYPCFVKPANLGSSVGISK 195
Cdd:COG0439 37 EELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALV-------DSPEEALAFAEEIGYPVVVKPADGAGSRGVRV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 196 CRNREELQKAFELA------FQYDRKVVVEEGINGREIEI-GVLGNDDPK-CSVVGEIaPKTDFYdykakYEDGDTdlmI 267
Cdd:COG0439 108 VRDEEELEAALAEAraeakaGSPNGEVLVEEFLEGREYSVeGLVRDGEVVvCSITRKH-QKPPYF-----VELGHE---A 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 268 PAIVTDEEYATISDMAIKAFKAID-GSGLVRADFFLTADGEVLINEVNT-MPGftpfSMFPLLWKEA-GVeyaDLIEQLV 344
Cdd:COG0439 179 PSPLPEELRAEIGELVARALRALGyRRGAFHTEFLLTPDGEPYLIEINArLGG----EHIPPLTELAtGV---DLVREQI 251
|
...
gi 504288768 345 ELA 347
Cdd:COG0439 252 RLA 254
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
144-313 |
3.86e-17 |
|
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: 78.06 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 144 AQAGLAQAKYaaflkkdWTRSPKESCEQVEQELGYPCFVKPANLGSS-VGISKCRNREELQKAFELAFqyDRKVVVEEGI 222
Cdd:pfam02222 1 QKLGLPTPRF-------MAAESLEELIEAGQELGYPCVVKARRGGYDgKGQYVVRSEADLPQAWEELG--DGPVIVEEFV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 223 NgREIEIGVLGNDDPKcsvvGEIApktdFYD-YKAKYEDGDTDLMI-PAIVTDEEYATISDMAIKAFKAIDGSGLVRADF 300
Cdd:pfam02222 72 P-FDRELSVLVVRSVD----GETA----FYPvVETIQEDGICRLSVaPARVPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
170
....*....|...
gi 504288768 301 FLTADGEVLINEV 313
Cdd:pfam02222 143 FVTEDGDLLINEL 155
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
123-349 |
1.10e-16 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 79.93 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 123 VGNGVLASSAG-----MDKVVMKHLFAQAGLAQAKyaAFLKKDwtrspKESCEQV--EQELGYPCFVKPANLGSSVGISK 195
Cdd:PRK12767 94 IGVKVLVSSKEvieicNDKWLTYEFLKENGIPTPK--SYLPES-----LEDFKAAlaKGELQFPLFVKPRDGSASIGVFK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 196 CRNREELqkafELAFQYDRKVVVEEGINGREIEIGVLgnDDPKCSVVGEIAPKtdfydyKAKYEDGDTDlmiPAIVtdEE 275
Cdd:PRK12767 167 VNDKEEL----EFLLEYVPNLIIQEFIEGQEYTVDVL--CDLNGEVISIVPRK------RIEVRAGETS---KGVT--VK 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504288768 276 YATISDMAIKAFKAIDGSGLVRADFFLTaDGEVLINEVNtmPGF---TPFSMfpllwkEAGVEYADLIEQLVELAKE 349
Cdd:PRK12767 230 DPELFKLAERLAEALGARGPLNIQCFVT-DGEPYLFEIN--PRFgggYPLSY------MAGANEPDWIIRNLLGGEN 297
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
114-319 |
1.90e-13 |
|
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: 69.97 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 114 MLELLNIPYVgNGVLASSAGMDKVVMKHLFAQAGLAQAKYAaflkkdWTRSPkESCEQVEQELGYPCFVKPANLGSSVGI 193
Cdd:COG0189 76 QLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTL------VTRDP-DDLRAFLEELGGPVVLKPLDGSGGRGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 194 SKCRNREELQKAFELAFQYDRKVV-VEEGI---NGREIEIGVLGNDdpkcsVVGEIAPKTDFYDYKAKYEDGDTdlMIPA 269
Cdd:COG0189 148 FLVEDEDALESILEALTELGSEPVlVQEFIpeeDGRDIRVLVVGGE-----PVAAIRRIPAEGEFRTNLARGGR--AEPV 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504288768 270 IVTDEEYatisDMAIKAFKAIdGSGLVRADFFLTADGEVLInEVNTMPGF 319
Cdd:COG0189 221 ELTDEER----ELALRAAPAL-GLDFAGVDLIEDDDGPLVL-EVNVTPGF 264
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
135-313 |
3.13e-12 |
|
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: 67.02 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 135 DKVVMKHLFAQAGLAQAKYAAFlkkdwtRSPkESCEQVEQELGYPCFVKPANLGss-vGISKCRNREELQKAFELAFQyd 213
Cdd:COG0026 89 DRLLEKAFLAELGIPVAPFAAV------DSL-EDLEAAIAELGLPAVLKTRRGGydgkGQVVIKSAADLEAAWAALGG-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 214 RKVVVEEGIN-GREIeigvlgnddpkcSVV------GEIApktdFYD----YkakYEDGDTDLMI-PAIVTDEEYATISD 281
Cdd:COG0026 160 GPCILEEFVPfEREL------------SVIvarspdGEVA----TYPvvenV---HRNGILDESIaPARISEALAAEAEE 220
|
170 180 190
....*....|....*....|....*....|..
gi 504288768 282 MAIKAFKAIDGSGLVRADFFLTADGEVLINEV 313
Cdd:COG0026 221 IAKRIAEALDYVGVLAVEFFVTKDGELLVNEI 252
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
135-315 |
8.57e-10 |
|
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: 58.08 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 135 DKVVMKHLFAQAGLAQAKYAAflkkdwtrSPKESCEQ---VEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQ 211
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTA--------GPVETEEEalaAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 212 ------YDRKVVVEEGING-REIEIGVLGNDDPKCSVVGEIapktdfyDYKAKYEDGDTDLMIPAI-VTDEEYATISDMA 283
Cdd:pfam02786 73 eapaafGNPQVLVEKSLKGpKHIEYQVLRDAHGNCITVCNR-------ECSDQRRTQKSIEVAPSQtLTDEERQMLREAA 145
|
170 180 190
....*....|....*....|....*....|...
gi 504288768 284 IKAFKAIDGSGLVRADFFLTAD-GEVLINEVNT 315
Cdd:pfam02786 146 VKIARHLGYVGAGTVEFALDPFsGEYYFIEMNT 178
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
167-313 |
8.52e-09 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 56.68 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 167 ESCEQVEQELGYPCFVKPAnLGSSV-GISKCRNREELQKAFELAFQYDR----KVVVEEGINgREIEIGVLgnddpkcsV 241
Cdd:PRK09288 139 EELRAAVEEIGYPCVVKPV-MSSSGkGQSVVRSPEDIEKAWEYAQEGGRggagRVIVEEFID-FDYEITLL--------T 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 242 VGEIAPKTDF----------YDYKAKYEdgdtdlmiPAIVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTADgEVLIN 311
Cdd:PRK09288 209 VRAVDGGTHFcapighrqedGDYRESWQ--------PQPMSPAALEEAQEIAKKVTDALGGRGLFGVELFVKGD-EVYFS 279
|
..
gi 504288768 312 EV 313
Cdd:PRK09288 280 EV 281
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
176-318 |
7.05e-08 |
|
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: 51.52 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 176 LGYPCFVKPANLGSSVGISKCRNREELQKAFE--------LAFQYDRKVV------VEEGINGREIEIGVLGNDDPKcSV 241
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAaireeieqWKEMYPEAVVdggsflVEEYIEGEEFAVDAYFDENGE-PV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 242 VGEIAPKtDFYDYKAKYedgDTDLMIPAIVTDEEYATISDMAIKAFKAIdgsGL----VRADFFLTADGEVLINEVNTMP 317
Cdd:pfam13535 80 ILNILKH-DFASSEDVS---DRIYVTSASIIRETQAAFTEFLKRINALL---GLknfpVHIELRVDEDGQIIPIEVNPLR 152
|
.
gi 504288768 318 G 318
Cdd:pfam13535 153 F 153
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
139-314 |
9.39e-08 |
|
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: 53.73 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 139 MKHLFAQAGLAQAKYAAFlkkdwtRSPKESCEQVEqELGYPCFVKPA-NL-GSSVGIskCRNREELQKAFELAFQY--DR 214
Cdd:COG0458 118 FKELLDKLGIPQPKSGTA------TSVEEALAIAE-EIGYPVIVRPSyVLgGRGMGI--VYNEEELEEYLERALKVspDH 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 215 KVVVEEGING-REIEIGVL--GNDDpkCSVVGEIapktdfydykakyED--------GDTDLMIPAI-VTDEEYATISDM 282
Cdd:COG0458 189 PVLIDESLLGaKEIEVDVVrdGEDN--VIIVGIM-------------EHiepagvhsGDSICVAPPQtLSDKEYQRLRDA 253
|
170 180 190
....*....|....*....|....*....|..
gi 504288768 283 AIKAFKAIDGSGLVRADFFLtADGEVLINEVN 314
Cdd:COG0458 254 TLKIARALGVVGLCNIQFAV-DDGRVYVIEVN 284
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
167-313 |
1.35e-07 |
|
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439798 [Multi-domain] Cd Length: 393 Bit Score: 52.82 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 167 ESCEQVEQELGYPCFVKPAnLGSSV-GISKCRNREELQKAFELAFQYDR----KVVVEEGINgREIEIGVLgnddpkcsV 241
Cdd:COG0027 139 EELRAAVEEIGYPCVVKPV-MSSSGkGQSVVRSPADIEAAWEYAQEGGRggagRVIVEGFVD-FDYEITLL--------T 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 242 VGEIAPKTDF----------YDYKAKYEdgdtdlmiPAIVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTADgEVLIN 311
Cdd:COG0027 209 VRAVDGPTHFcepighrqedGDYRESWQ--------PQPMSEAALAKAQEIAKKVTDALGGRGIFGVELFVKGD-EVYFS 279
|
..
gi 504288768 312 EV 313
Cdd:COG0027 280 EV 281
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
174-315 |
3.65e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 51.64 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 174 QELGYPCFVKPANLGSSVGISKCRNREELQKAFEL-------AFQyDRKVVVEEGI-NGREIEIGVLGND--------DP 237
Cdd:PRK07178 148 ERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRviseatkAFG-SAEVFLEKCIvNPKHIEVQILADShgnvvhlfER 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 238 KCSV------VGEIAPKTDfydykakyedgdtdlmipaiVTDEEYATISDMAIKAFKAID--GSGLVraDFFLTADGEVL 309
Cdd:PRK07178 227 DCSIqrrnqkLIEIAPSPQ--------------------LTPEQRAYIGDLAVRAAKAVGyeNAGTV--EFLLDADGEVY 284
|
....*.
gi 504288768 310 INEVNT 315
Cdd:PRK07178 285 FMEMNT 290
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
135-312 |
1.20e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 49.77 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 135 DKVVMKHLFAQAGLAQAKYAAFlkkdwtRSPKEScEQVEQELGYPCFVKPANLGss-vGISKCRNREELQKAFELAFQYD 213
Cdd:PRK06019 100 DRLTEKQFLDKLGIPVAPFAVV------DSAEDL-EAALADLGLPAVLKTRRGGydgkGQWVIRSAEDLEAAWALLGSVP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 214 rkVVVEEGIN-GREIE-IGVLGNDdpkcsvvGEIApktdFYD----YkakYEDGDTDLMI-PAIVTDEEYATISDMAIKA 286
Cdd:PRK06019 173 --CILEEFVPfEREVSvIVARGRD-------GEVV----FYPlvenV---HRNGILRTSIaPARISAELQAQAEEIASRI 236
|
170 180
....*....|....*....|....*.
gi 504288768 287 FKAIDGSGLVRADFFLTADGEVLINE 312
Cdd:PRK06019 237 AEELDYVGVLAVEFFVTGDGELLVNE 262
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
163-315 |
1.99e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 49.33 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 163 RSPKESCEQVEqELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQY------DRKVVVEEGI-NGREIEIGVLGND 235
Cdd:PRK05586 139 ENEEEALEIAK-EIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEakaafgDDSMYIEKFIeNPKHIEFQILGDN 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 236 --------DPKCSV------VGEIAPKTdfydykakyedgdtdlmipaIVTDEEYATISDMAIKAFKAIDGSGLVRADFF 301
Cdd:PRK05586 218 ygnvvhlgERDCSLqrrnqkVLEEAPSP--------------------VMTEELRKKMGEIAVKAAKAVNYKNAGTIEFL 277
|
170
....*....|....
gi 504288768 302 LTADGEVLINEVNT 315
Cdd:PRK05586 278 LDKDGNFYFMEMNT 291
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
161-315 |
2.65e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 49.21 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 161 WTRSPKESCEQ---VEQELGYPCFVKPANLGSSVGISKCRNREELQKAFE----LAFQY--DRKVVVEEGI-NGREIEIG 230
Cdd:PRK08654 133 GTEEGIEDIEEakeIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIEstqsIAQSAfgDSTVFIEKYLeKPRHIEIQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 231 VLGND--------DPKCSV------VGEIAPKtdfydykakyedgdtdlmipAIVTDEEYATISDMAIKAFKAID--GSG 294
Cdd:PRK08654 213 ILADKhgnvihlgDRECSIqrrhqkLIEEAPS--------------------PIMTPELRERMGEAAVKAAKAINyeNAG 272
|
170 180
....*....|....*....|.
gi 504288768 295 LVRadfFLTADGEVLINEVNT 315
Cdd:PRK08654 273 TVE---FLYSNGNFYFLEMNT 290
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
175-324 |
4.06e-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: 47.73 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 175 ELGYPCFVKPANLGSSVGISKCRNREELQKAFEL--AFQYDRKV-VVEEGIN---GREIEIGVLGNDdpkcsVVGEIAPK 248
Cdd:TIGR00768 121 EIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHfeQLNGPQNLfLVQEYIKkpgGRDIRVFVVGDE-----VVAAIYRI 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504288768 249 TDfYDYKAKYEDGDTDLMIPaiVTDEeyatISDMAIKAFKAIDGsGLVRADFFLTADGeVLINEVNTMPGFTPFSM 324
Cdd:TIGR00768 196 TS-GHWRSNLARGGKAEPCS--LTEE----IEELAIKAAKALGL-DVAGVDLLESEDG-LLVNEVNANPEFKNSVK 262
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
135-314 |
5.59e-06 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 46.51 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 135 DKVVMKHLFAQAGLAQAKYAAFlkkdwtRSPKESCEQVeQELGYPCFV-KPANLGSSVGISKCRNREELQKAFELAFQ-- 211
Cdd:pfam01071 2 SKSFAKDFMKRYGIPTAEYETF------TDPEEAKSYI-QEAGFPAIVvKADGLAAGKGVIVASSNEEAIKAVDEILEqk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 212 ----YDRKVVVEEGINGreIEIGVLgnddpkCSVVGE-IAPKTDFYDYKAKYEdGDTDL----M---IPA-IVTDEEYAT 278
Cdd:pfam01071 75 kfgeAGETVVIEEFLEG--EEVSVL------AFVDGKtVKPLPPAQDHKRAGE-GDTGPntggMgaySPApVITPELLER 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504288768 279 ISDMAIKafKAIDG--------SGLVRADFFLTADGEVLInEVN 314
Cdd:pfam01071 146 IKETIVE--PTVDGlrkegipfKGVLYAGLMLTKDGPKVL-EFN 186
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
174-234 |
1.75e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 46.69 E-value: 1.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504288768 174 QELGYPCFVKPAN----LGSSVGISkcrNREELQKAFELAFQYDRKVVVEEGINGREIEIGVLGN 234
Cdd:PRK14016 246 EEIGYPVVVKPLDgnhgRGVTVNIT---TREEIEAAYAVASKESSDVIVERYIPGKDHRLLVVGG 307
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
136-235 |
1.80e-05 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 46.46 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 136 KVVMKHLFAQAGLAQAKYAAFlkkdwtRSPKESCEQVEQELGYPCFVKPANLGSSVGISKCR---NREELQKAFELAFQY 212
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEF------TSLEEALADYSLFADKAIVVKPKSTNFGLGISIFKepaSLEDYEKALEIAFRE 562
|
90 100
....*....|....*....|...
gi 504288768 213 DRKVVVEEGINGREIEIGVLGND 235
Cdd:PRK02471 563 DSSVLVEEFIVGTEYRFFVLDGK 585
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
112-314 |
2.16e-04 |
|
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: 43.45 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 112 QGMLELLNIPYVGNGVLASSAGMDKVVMKHLFAQAGLAQAKYAAflkkdwTRSPKEsCEQVEQELGYPCFVKPA-NLGSS 190
Cdd:TIGR01369 104 SGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEI------AHSVEE-ALAAAKEIGYPVIVRPAfTLGGT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 191 vGISKCRNREELQKAFE--LAFQYDRKVVVEEGING-REIEIGVLGNDDPKCSVVGEIapktdfydykakyED------- 260
Cdd:TIGR01369 177 -GGGIAYNREELKEIAEraLSASPINQVLVEKSLAGwKEIEYEVMRDSNDNCITVCNM-------------ENfdpmgvh 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504288768 261 -GDTDLMIPA-IVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTAD-GEVLINEVN 314
Cdd:TIGR01369 243 tGDSIVVAPSqTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsGRYYVIEVN 299
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
164-315 |
2.19e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 43.09 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 164 SPKESCEqVEQELGYPCFVKPANLGSSVGISKCRNREELQKAFEL------AFQYDRKVVVEEGI-NGREIEIGVL---- 232
Cdd:PRK06111 140 DAEEAIA-IARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESnkkraaNFFGNGEMYIEKYIeDPRHIEIQLLadth 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 233 GND----DPKCSV------VGEIAPkTDFYDykakyedgdtdlmipaivtDEEYATISDMAIKAFKAIDGSGLVRADFFL 302
Cdd:PRK06111 219 GNTvylwERECSVqrrhqkVIEEAP-SPFLD-------------------EETRKAMGERAVQAAKAIGYTNAGTIEFLV 278
|
170
....*....|...
gi 504288768 303 TADGEVLINEVNT 315
Cdd:PRK06111 279 DEQKNFYFLEMNT 291
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
167-315 |
8.40e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 41.28 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 167 ESCEQVEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELA-------FQYDRkVVVEEGI-NGREIEIGVLGN---- 234
Cdd:PRK12999 146 EEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAkreakaaFGNDE-VYLEKYVeNPRHIEVQILGDkhgn 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 235 ----DDPKCSV------VGEIAPKtdfydykakyedgdtdlmiPAIvTDEEYATISDMAIKAFKAIDGSGLVRADFFLTA 304
Cdd:PRK12999 225 vvhlYERDCSVqrrhqkVVEIAPA-------------------PGL-SEELRERICEAAVKLARAVGYVNAGTVEFLVDA 284
|
170
....*....|..
gi 504288768 305 DGE-VLInEVNT 315
Cdd:PRK12999 285 DGNfYFI-EVNP 295
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
116-314 |
1.17e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 40.78 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 116 ELLNIPYvGNGVLASSAGMDKVVMKHLFAQAGLAQAKYAAflkkdwTRSPKESCEQVEQE--LGYPCFVKPANLGSSVGI 193
Cdd:PRK07206 90 EILTPQY-SNDPALSSARRNKAEMINALAEAGLPAARQIN------TADWEEAEAWLRENglIDRPVVIKPLESAGSDGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 194 SKCRNREELQKAFEL----AFQYD---RKVVVEEGINGREIEIG---VLGNddpkcSVVGEIAP--KTDFYDYKAKYedg 261
Cdd:PRK07206 163 FICPAKGDWKHAFNAilgkANKLGlvnETVLVQEYLIGTEYVVNfvsLDGN-----HLVTEIVRyhKTSLNSGSTVY--- 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504288768 262 DTDLMIPAivTDEEYATISDMAIKAFKAID-GSGLVRADFFLTADGEVLInEVN 314
Cdd:PRK07206 235 DYDEFLDY--SEPEYQELVDYTKQALDALGiKNGPAHAEVMLTADGPRLI-EIG 285
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
135-324 |
1.18e-03 |
|
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: 39.41 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 135 DKVVMKHLFAQAGLAQAKYAAflkkdwTRSPKESCEQVEQ-ELGYPCFVKPANLGSSVGISKCRNREELQKAFElafQYD 213
Cdd:pfam08443 3 DKAKSHQLLAKHGIGPPNTRL------AWYPEDAEQFIEQiKRQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLS---ATN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 214 RKVVVEEGI---NGREIEIGVLGNDdpkcsVVGEIAPKTDFYDYKAK-YEDGDTDlmiPAIVTDEEyatiSDMAIKAFKA 289
Cdd:pfam08443 74 EQILVQEFIaeaNNEDIRCLVVGDQ-----VVGALHRQSNEGDFRSNlHRGGVGE---KYQLSQEE----TELAIKAAQA 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 504288768 290 IdgsGLVRA--DFFLTADGEVLInEVNTMPGFTPFSM 324
Cdd:pfam08443 142 M---QLDVAgvDLLRQKRGLLVC-EVNSSPGLEGIEK 174
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
268-317 |
1.24e-03 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 40.81 E-value: 1.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 504288768 268 PAIVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTADGEVLINEVNTMP 317
Cdd:PLN02948 241 PANVPWKVAKLATDVAEKAVGSLEGAGVFGVELFLLKDGQILLNEVAPRP 290
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
172-314 |
1.69e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 40.53 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 172 VEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYD--RKVVVEEG-INGREIEIGVLGNDDPKCsVVGEIAPK 248
Cdd:PLN02735 732 IAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDpeRPVLVDKYlSDATEIDVDALADSEGNV-VIGGIMEH 810
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504288768 249 TDfydyKAKYEDGDTDLMIPA-IVTDEEYATISDMAIKAFKAIDGSGLVRADFFLTADGEVLINEVN 314
Cdd:PLN02735 811 IE----QAGVHSGDSACSLPTqTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEAN 873
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
152-317 |
4.08e-03 |
|
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: 39.21 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 152 KYAAFLKK------DW-TRSPKESCEQVEQELGYPCFVKPANLGSSVGISKCRNREELQKAFELAFQYDRK--VVVEEGI 222
Cdd:TIGR01369 672 KFSELLDElgipqpKWkTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYL 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 223 -NGREIEIGVLgNDDPKCSVVGeIAPKTDfydyKAKYEDGDTDLMIPAIVTDEEYA-TISDMAIKAFKAIDGSGLVRADF 300
Cdd:TIGR01369 752 eDAVEVDVDAV-SDGEEVLIPG-IMEHIE----EAGVHSGDSTCVLPPQTLSAEIVdRIKDIVRKIAKELNVKGLMNIQF 825
|
170 180
....*....|....*....|..
gi 504288768 301 FLTaDGEVLINEVN-----TMP 317
Cdd:TIGR01369 826 AVK-DGEVYVIEVNprasrTVP 846
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
167-228 |
6.19e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 38.54 E-value: 6.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504288768 167 ESCEQVEQELGYPCFVKPA-NL-GSSVGIskCRNREELQKAFELAFQYDR--KVVVEEGING-REIE 228
Cdd:PRK05294 153 EEALEVAEEIGYPVIIRPSfTLgGTGGGI--AYNEEELEEIVERGLDLSPvtEVLIEESLLGwKEYE 217
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
174-247 |
6.67e-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: 38.52 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 174 QELGYPCFVKPANLGSSVGISKCRNREELQKAFEL-------AFQYDRkVVVEEGI-NGREIEIGVL----GN------- 234
Cdd:COG1038 152 EEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESarreakaAFGDDE-VFLEKYIeRPKHIEVQILgdkhGNivhlfer 230
|
90
....*....|....*....
gi 504288768 235 DdpkCSV------VGEIAP 247
Cdd:COG1038 231 D---CSVqrrhqkVVEIAP 246
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
120-224 |
7.11e-03 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 37.99 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504288768 120 IPYVGNGVLASsaGMDKVVMKHLFAQAGLAQAKyaaflkkdwTRSPKES--CEQVEQELGYPCFVKPAN--------LGS 189
Cdd:COG3919 104 LPYPDADLLDR--LLDKERFYELAEELGVPVPK---------TVVLDSAddLDALAEDLGFPVVVKPADsvgydelsFPG 172
|
90 100 110
....*....|....*....|....*....|....*
gi 504288768 190 SVGISKCRNREELQKAFELAFQYDRKVVVEEGING 224
Cdd:COG3919 173 KKKVFYVDDREELLALLRRIAAAGYELIVQEYIPG 207
|
|
| |
