|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-418 |
0e+00 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 743.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 1 MNVLVIGRGGREHALAWKFAQSEKVEKVYVAPGNEGMRDVATPVDIDENDFDALVLFAKENNVELTFVGPEIPLMNGIAD 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 81 HFKEEGLRVFGPNKAAAVIEGSKAFTKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVAMTLE 160
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 161 EALQAVKEMLQDVKFGAASKKVVIEEFLDGQEFSLMAFVNGTTVHPMVIAQDHKRAFDGDKGPNTGGMGAYSPVPQIPES 240
Cdd:COG0151 161 EALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 241 AVQEAIKTVLHPTAKAMIAENRSFTGILYAGLILTKDGPKVIEFNARFGDPETEVVLPRLENDLVDVCNAVLDE--SELT 318
Cdd:COG0151 241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGrlDEVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 319 LQWSEEAVIGVVLASKGYPEAYKKGDMINKLDALQ--DVIVFHSGTAMKHGDFVTNGGRVLFVACKANTLQEAKDKVYKE 396
Cdd:COG0151 321 LEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEaeGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERAYEA 400
|
410 420
....*....|....*....|..
gi 983471343 397 IGKIESDGLFYRRDIGYRAIGH 418
Cdd:COG0151 401 VEKIRFEGMFYRRDIGWRALKR 422
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-416 |
0e+00 |
|
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273315 [Multi-domain] Cd Length: 422 Bit Score: 574.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 1 MNVLVIGRGGREHALAWKFAQSEKVEKVYVAPGNEGMRDVATP--VDIDENDFDALVLFAKENNVELTFVGPEIPLMNGI 78
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNknVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 79 ADHFKEEGLRVFGPNKAAAVIEGSKAFTKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVAMT 158
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 159 LEEALQAVKEMLQDvKFGAASKKVVIEEFLDGQEFSLMAFVNGTTVHPMVIAQDHKRAFDGDKGPNTGGMGAYSPVPQIP 238
Cdd:TIGR00877 161 NEEAIKAVEDILEQ-KFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 239 ESAVQEAIKTVLHPTAKAMIAENRSFTGILYAGLILTKDGPKVIEFNARFGDPETEVVLPRLENDLVDVCNAVLDES--E 316
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKldE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 317 LTLQWSEEAVIGVVLASKGYPEAYKKGDMINKLDALQ--DVIVFHSGTAMKHGDFVTNGGRVLFVACKANTLQEAKDKVY 394
Cdd:TIGR00877 320 VELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEaeGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERAY 399
|
410 420
....*....|....*....|..
gi 983471343 395 KEIGKIESDGLFYRRDIGYRAI 416
Cdd:TIGR00877 400 EAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-422 |
3.40e-175 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 496.57 E-value: 3.40e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 4 LVIGRGGREHALAWKFAQSEKVEKVYVAPGNEGM---RDVATPVDIDENDFDALVLFAKENNVELTFVGPEIPLMNGIAD 80
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIatsGDATCVPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 81 HFKEEGLRVFGPNKAAAVIEGSKAFTKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVAMTLE 160
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 161 EALQAVKEMLQDVKFGAASKKVVIEEFLDGQEFSLMAFVNGTTVHPMVIAQDHKRAFDGDKGPNTGGMGAYSPVPQIPES 240
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 241 AVQEAIKTVLHPTAKAMIAENRSFTGILYAGLILTKDG--PKVIEFNARFGDPETEVVLPRLENDLVDV----CNAVLDE 314
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVllaaCKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 315 SELTlqWSEEAVIGVVLASKGYPEAYKKGDMINKLDALQDVI----VFHSGTAMKH-GDFVTNGGRVLFVACKANTLQEA 389
Cdd:PLN02257 321 VSLT--WSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVApgvkVFHAGTALDSdGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|...
gi 983471343 390 KDKVYKEIGKIESDGLFYRRDIGYRAIGHEMMK 422
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQVA 431
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
101-293 |
2.74e-108 |
|
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: 317.30 E-value: 2.74e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 101 GSKAFTKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPI-VIKADGLAAGKGVTVAMTLEEALQAVKEMLQDVKFGAAS 179
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 180 KKVVIEEFLDGQEFSLMAFVNGTTVHPMVIAQDHKRAFDGDKGPNTGGMGAYSPVPQIPESAVQEAIKTVLHPTAKAMIA 259
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 983471343 260 ENRSFTGILYAGLILTKDGPKVIEFNARFGDPET 293
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-100 |
1.37e-53 |
|
Phosphoribosylglycinamide synthetase, N 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 N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam00289). This domain is structurally related to the PreATP-grasp domain.
Pssm-ID: 460723 [Multi-domain] Cd Length: 102 Bit Score: 173.70 E-value: 1.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 1 MNVLVIGRGGREHALAWKFAQSEKVEKVYVAPGNEGMRDVATPVDIDENDFDALVLFAKENNVELTFVGPEIPLMNGIAD 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80
|
90 100
....*....|....*....|..
gi 983471343 81 HFKEE--GLRVFGPNKAAAVIE 100
Cdd:pfam02844 81 ALRERaaGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
327-414 |
7.13e-37 |
|
Phosphoribosylglycinamide synthetase, C 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 C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02787).
Pssm-ID: 460722 [Multi-domain] Cd Length: 88 Bit Score: 129.49 E-value: 7.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 327 IGVVLASKGYPEAYKKGDMINKLDALqDVIVFHSGTAMKHGDFVTNGGRVLFVACKANTLQEAKDKVYKEIGKIESDGLF 406
Cdd:pfam02843 2 VCVVLASGGYPGSYEKGDVITGLDEA-GVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFEGMF 80
|
....*...
gi 983471343 407 YRRDIGYR 414
Cdd:pfam02843 81 YRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
52-289 |
2.53e-24 |
|
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: 101.10 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 52 DALVLFAKENNVE--LTFVGPEIPLMNGIADHFkeeGLRvfGPNKAAAVIEGSKAFTKELMKKYNIPTAAYETFTDYEEA 129
Cdd:COG0439 7 AAAAELARETGIDavLSESEFAVETAAELAEEL---GLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 130 VQYIEKVGAPIVIKADGLAAGKGVTVAMTLEEALQAVKEMLQDVKFGAASKKVVIEEFLDGQEFSLMAFVNGTTVHPMVI 209
Cdd:COG0439 82 LAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 210 AQDHKrafdgdKGPNTGGMGAYSPVPqIPESAVQEAIKTVlhptAKAMIAENRSFtGILYAGLILTKDG-PKVIEFNARF 288
Cdd:COG0439 162 TRKHQ------KPPYFVELGHEAPSP-LPEELRAEIGELV----ARALRALGYRR-GAFHTEFLLTPDGePYLIEINARL 229
|
.
gi 983471343 289 G 289
Cdd:COG0439 230 G 230
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
77-294 |
8.46e-14 |
|
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: 71.51 E-value: 8.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 77 GIADHFKEEGLRVFgpNKAAAV-IEGSKAFTKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIK-ADGlAAGKGVT 154
Cdd:COG0189 72 ALLRQLEAAGVPVV--NDPEAIrRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKpLDG-SGGRGVF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 155 VAMTLEEALQAVKEMLQDvkfgaASKKVVIEEFL---DGQEFSLMaFVNGTTVHPM--VIAQDHKRAfdgdkgpNTGGMG 229
Cdd:COG0189 149 LVEDEDALESILEALTEL-----GSEPVLVQEFIpeeDGRDIRVL-VVGGEPVAAIrrIPAEGEFRT-------NLARGG 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983471343 230 AYSPVPqIPESAVQEAIKTvlhptAKAMiaenrsftGILYAG--LILTKDGPKVIEFNARFGDPETE 294
Cdd:COG0189 216 RAEPVE-LTDEERELALRA-----APAL--------GLDFAGvdLIEDDDGPLVLEVNVTPGFRGLE 268
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-289 |
5.34e-13 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 69.53 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 1 MNVLVIGrGGREHALAWKFAQSEKVEKVYVA---PGNEGMRDVATPVDI----DENDFDALVLFAKENNVELTFVG--PE 71
Cdd:PRK12767 2 MNILVTS-AGRRVQLVKALKKSLLKGRVIGAdisELAPALYFADKFYVVpkvtDPNYIDRLLDICKKEKIDLLIPLidPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 72 IPLMNGIADHFKEEGLRVFGPNKAAAVIEGSKAFTKELMKKYNIPTAAYETFTDYE--EAVQYIEKVGAPIVIKADGLAA 149
Cdd:PRK12767 81 LPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEdfKAALAKGELQFPLFVKPRDGSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 150 GKGVTVAMTLEEALQAVKEMlqdvkfgaasKKVVIEEFLDGQEFSLMAFV--NGTTVHPMVIAQDHKRAFDGDKGpntgg 227
Cdd:PRK12767 161 SIGVFKVNDKEELEFLLEYV----------PNLIIQEFIEGQEYTVDVLCdlNGEVISIVPRKRIEVRAGETSKG----- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983471343 228 mgaYSpvpqIPESAVQEAIKTvlhptakamIAENRSFTGILYAGLILTKDGPKVIEFNARFG 289
Cdd:PRK12767 226 ---VT----VKDPELFKLAER---------LAEALGARGPLNIQCFVTDGEPYLFEINPRFG 271
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
103-194 |
6.45e-11 |
|
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: 62.82 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 103 KAFTKELMKKYNIPTAAYETFTDYEEAV--QYIEKVGAPIVIKADGLAAGKGVTVAMTLEEALQAVKEMLqdvKFGaasK 180
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADleAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAF---KYD---D 169
|
90
....*....|....
gi 983471343 181 KVVIEEFLDGQEFS 194
Cdd:COG1181 170 KVLVEEFIDGREVT 183
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
79-205 |
3.99e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 61.54 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 79 ADHFKEEGLRVFGPNKAAAVIEGSKAFTKELMKKYNIPT--AAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVA 156
Cdd:PRK08654 92 AKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVlpGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVV 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 983471343 157 MT---LEEALQAVKEMLQDVkFGAASkkVVIEEFLDGQ---EFSLMAFVNGTTVH 205
Cdd:PRK08654 172 YSeeeLEDAIESTQSIAQSA-FGDST--VFIEKYLEKPrhiEIQILADKHGNVIH 223
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
107-210 |
1.64e-09 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 57.27 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 107 KELMKKYNIPTAAYETFTDYEEAVQYIEKVGAP-IVIKADGLAAGK----GVTVAMTLEEALQAVKEML-------QDVK 174
Cdd:pfam08442 8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKvYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEMLgknlvtkQTGP 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 983471343 175 FGAASKKVVIEEFLD-GQEFSLMAFVNGTTVHPMVIA 210
Cdd:pfam08442 88 DGQPVNKVLVEEALDiKKEYYLSIVLDRASKGPVIIA 124
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
49-208 |
1.00e-08 |
|
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: 56.62 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 49 NDFDALVLFAKENNVeLTFvgpEIPLMNGIADHFKEEGLRVFgPNKAAAVIEGSKAFTKELMKKYNIPTAAYETFTDYEE 128
Cdd:COG0026 41 DDEEALREFAERCDV-VTF---EFENVPAEALEALEAEVPVR-PGPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLED 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 129 AVQYIEKVGAPIVIKA-----DglaaGKGVTVAMTLEEALQAVKEMlqdvkfgaASKKVVIEEFLD-GQEFSLMA--FVN 200
Cdd:COG0026 116 LEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGPCILEEFVPfERELSVIVarSPD 183
|
....*....
gi 983471343 201 GTTVH-PMV 208
Cdd:COG0026 184 GEVATyPVV 192
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
94-204 |
1.02e-08 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 57.47 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 94 KAAAV-IEGSKAFTKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKA-DGlAAGKGVTVAMTLEEALQAVKEMLQ 171
Cdd:PRK14016 205 SAIAVdIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPlDG-NHGRGVTVNITTREEIEAAYAVAS 283
|
90 100 110
....*....|....*....|....*....|...
gi 983471343 172 DVkfgaaSKKVVIEEFLDGQEFSLMAfVNGTTV 204
Cdd:PRK14016 284 KE-----SSDVIVERYIPGKDHRLLV-VGGKLV 310
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
103-194 |
3.63e-08 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 54.73 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 103 KAFTKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKadglAAGKGVTVAMTLEEALQAVKEMLQDV-KFGaasKK 181
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK----PAREGSSVGVSKVKEEDELQAALELAfKYD---DE 171
|
90
....*....|...
gi 983471343 182 VVIEEFLDGQEFS 194
Cdd:PRK01372 172 VLVEKYIKGRELT 184
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
111-220 |
4.88e-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: 52.26 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 111 KKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKADGLA-AGKGVTVAMTLEEALQAVKEmlqdvkfgAASKKVVIEEFLD 189
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEE--------LGDGPVIVEEFVP 72
|
90 100 110
....*....|....*....|....*....|....
gi 983471343 190 -GQEFSLMA--FVNGTTVHPMVIAQDHKrafDGD 220
Cdd:pfam02222 73 fDRELSVLVvrSVDGETAFYPVVETIQE---DGI 103
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
107-205 |
6.45e-08 |
|
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: 52.69 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 107 KELMKKYNIPTAAYE--TFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVAMTLEEALQAVKEMLQDVKFGAASKKVVI 184
Cdd:pfam02786 6 KAAMKEAGVPTVPGTagPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNPQVLV 85
|
90 100
....*....|....*....|....
gi 983471343 185 EEFLDGQ---EFSLMAFVNGTTVH 205
Cdd:pfam02786 86 EKSLKGPkhiEYQVLRDAHGNCIT 109
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
125-287 |
3.33e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 51.95 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 125 DYEEAVQYIEK---VGAPIVIKADGLAAGKGVTVAMTLEEALQAVKEMLQDV-KFGAASKKVVIEEFLDGQEFSlmafVN 200
Cdd:PRK07206 131 DWEEAEAWLREnglIDRPVVIKPLESAGSDGVFICPAKGDWKHAFNAILGKAnKLGLVNETVLVQEYLIGTEYV----VN 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 201 GTTVH--PMV--IAQDHKRAFDGdkgpntgGMGAYSPVPQIPESA-VQEAIKTVLHPTAKAM-IAEnrsftGILYAGLIL 274
Cdd:PRK07206 207 FVSLDgnHLVteIVRYHKTSLNS-------GSTVYDYDEFLDYSEpEYQELVDYTKQALDALgIKN-----GPAHAEVML 274
|
170
....*....|...
gi 983471343 275 TKDGPKVIEFNAR 287
Cdd:PRK07206 275 TADGPRLIEIGAR 287
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
66-287 |
4.02e-07 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 52.31 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 66 TFVGPEIPlmNGIADHFKEEGLRVFGPN-KAAAVIEGSKAFTkELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKA 144
Cdd:TIGR01369 635 VQFGGQTP--LNLAKALEEAGVPILGTSpESIDRAEDREKFS-ELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRP 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 145 DGLAAGKGVTVAMTLEEALQAVKEMLqdvkfgAASKK--VVIEEFL-DGQEFSLMAFVNGTTVHPMVIAQDHKRAfdgdk 221
Cdd:TIGR01369 712 SYVLGGRAMEIVYNEEELRRYLEEAV------AVSPEhpVLIDKYLeDAVEVDVDAVSDGEEVLIPGIMEHIEEA----- 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983471343 222 GPNTGGMGAYSPvPQIPESAVQEAIKTVLHPTAKAMiaenrSFTGILYAGLILTKDGPKVIEFNAR 287
Cdd:TIGR01369 781 GVHSGDSTCVLP-PQTLSAEIVDRIKDIVRKIAKEL-----NVKGLMNIQFAVKDGEVYVIEVNPR 840
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
79-205 |
1.04e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 50.48 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 79 ADHFKEEGLRVFGPNKAAAVIEGSKAFTKELMKKYNIPTA-AYE-TFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVA 156
Cdd:PRK05586 92 AKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVpGSEgEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIV 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 983471343 157 MTLEEALQAVKEMLQDVKFGAASKKVVIEEFLDGQ---EFSLMAFVNGTTVH 205
Cdd:PRK05586 172 RSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPkhiEFQILGDNYGNVVH 223
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
107-210 |
1.05e-06 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 50.44 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 107 KELMKKYNIPTAAYETFTDYEEAVQYIEKVG-APIVIKADGLAAGK----GVTVAMTLEEALQAVKEML-------QDVK 174
Cdd:COG0045 9 KELLAKYGVPVPRGIVATTPEEAVAAAEELGgPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAAEEILgmtlvthQTGP 88
|
90 100 110
....*....|....*....|....*....|....*..
gi 983471343 175 FGAASKKVVIEEFLD-GQEFSLMAFVNGTTVHPMVIA 210
Cdd:COG0045 89 KGKPVNKVLVEEGVDiAKELYLSILLDRATRRPVIMA 125
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
103-289 |
1.10e-06 |
|
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: 48.65 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 103 KAFTKELMKKYNIPTAAYETFTDYEEAVQYIEKVG--APIVIKADGLAAGKGVTVAMTLEEALQAVKemlqdvkfgAASK 180
Cdd:pfam08443 4 KAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrqFPVIVKSIYGSQGIGVFLAEDEQKLRQTLS---------ATNE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 181 KVVIEEFLDgqeFSLMAFVNGTTVHPMVIAQDHKRAFDGDKGPNTGGMGAYSPVpQIPESAVQEAIKtvlhpTAKAMiae 260
Cdd:pfam08443 75 QILVQEFIA---EANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKY-QLSQEETELAIK-----AAQAM--- 142
|
170 180 190
....*....|....*....|....*....|.
gi 983471343 261 nrsftGILYAG--LILTKDGPKVIEFNARFG 289
Cdd:pfam08443 143 -----QLDVAGvdLLRQKRGLLVCEVNSSPG 168
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
101-291 |
1.26e-06 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 48.15 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 101 GSKAFTKELMKKYNIPTAayETFTDYEeavqyIEKVGAPIVIK-ADGlAAGKGVTVAMTLEEALQAVKEMLqdvkfgaas 179
Cdd:pfam02655 2 SDKLKTYKALKNAGVPTP--ETLQAEE-----LLREEKKYVVKpRDG-CGGEGVRKVENGREDEAFIENVL--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 180 kkvvIEEFLDGQEFSLMAFVNGTTVHPMVIAQDHKrAFDGDKGPNTGGMGAYSPVPQipESAVQEAIKTVlhptakamia 259
Cdd:pfam02655 65 ----VQEFIEGEPLSVSLLSDGEKALPLSVNRQYI-DNGGSGFVYAGNVTPSRTELK--EEIIELAEEVV---------- 127
|
170 180 190
....*....|....*....|....*....|....*
gi 983471343 260 enRSFTGIL-YAG--LILTKDGPKVIEFNARFGDP 291
Cdd:pfam02655 128 --ECLPGLRgYVGvdLVLKDNEPYVIEVNPRITTS 160
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
107-210 |
1.36e-06 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 50.09 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 107 KELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPI-VIKADGLAAGK----GVTVAMTLEEALQAVKEML-------QDVK 174
Cdd:PRK00696 9 KELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVwVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQILgmtlvthQTGP 88
|
90 100 110
....*....|....*....|....*....|....*..
gi 983471343 175 FGAASKKVVIEEFLD-GQEFSLMAFVNGTTVHPMVIA 210
Cdd:PRK00696 89 KGQPVNKVLVEEGADiAKEYYLSIVLDRATRRVVFMA 125
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
47-204 |
3.16e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 49.00 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 47 DENDFDALVLFAKENNVeLTF----VgPEIPLMNGIADHfkeeglRVFgPNKAAAVIEGSKAFTKELMKKYNIPTAAYET 122
Cdd:PRK06019 50 DYDDVAALRELAEQCDV-ITYefenV-PAEALDALAARV------PVP-PGPDALAIAQDRLTEKQFLDKLGIPVAPFAV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 123 FTDYEEAVQYIEKVGAPIVIKA-----DglaaGKGVTVAMTLEEALQAVKEMlqdvkfgaASKKVVIEEFLD-GQEFSLM 196
Cdd:PRK06019 121 VDSAEDLEAALADLGLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWALL--------GSVPCILEEFVPfEREVSVI 188
|
170
....*....|
gi 983471343 197 A--FVNGTTV 204
Cdd:PRK06019 189 VarGRDGEVV 198
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
77-205 |
5.75e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 48.49 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 77 GIADHFKEEGLRVFGPnkAAAVIE--GSKAFTKELMKKYNIPT--AAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKG 152
Cdd:PRK06111 90 SFAERCKEEGIVFIGP--SADIIAkmGSKIEARRAMQAAGVPVvpGITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIG 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 983471343 153 VTVAMTLEEALQAV---KEMLQDVkFGAASkkVVIEEFLDGQ---EFSLMAFVNGTTVH 205
Cdd:PRK06111 168 MQLVETEQELTKAFesnKKRAANF-FGNGE--MYIEKYIEDPrhiEIQLLADTHGNTVY 223
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
83-190 |
2.83e-05 |
|
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: 46.53 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 83 KEEGLRVFG-PNKAAAVIEGSKAFtKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVAMTLEE 161
Cdd:TIGR01369 108 EKYGVEVLGtPVEAIKKAEDRELF-REAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREE 186
|
90 100
....*....|....*....|....*....
gi 983471343 162 ALQAVKEMLQDvkfgAASKKVVIEEFLDG 190
Cdd:TIGR01369 187 LKEIAERALSA----SPINQVLVEKSLAG 211
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
99-195 |
4.71e-05 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 45.11 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 99 IEGS-----KAFTKELMKKYNIPTAAYETFT--DYEEAV--QYIEKVGAPIVIKADGLAAGKGVTVAMTLEEALQAVKEm 169
Cdd:PRK01966 115 VLASalsmdKILTKRLLAAAGIPVAPYVVLTrgDWEEASlaEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDL- 193
|
90 100
....*....|....*....|....*...
gi 983471343 170 lqdvkfgAA--SKKVVIEEFLDGQEFSL 195
Cdd:PRK01966 194 -------AFeyDRKVLVEQGIKGREIEC 214
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
105-204 |
5.31e-05 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 45.73 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 105 FTKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVAMTLEEALQAVKEMLQDVKFgaasKKVVI 184
Cdd:PRK12815 131 RFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPI----HQCLL 206
|
90 100
....*....|....*....|...
gi 983471343 185 EEFLDG---QEFSLMAFVNGTTV 204
Cdd:PRK12815 207 EESIAGwkeIEYEVMRDRNGNCI 229
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
86-189 |
1.67e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 43.64 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 86 GLRVFGPNKAAAVIEGSKAFTKELMKKYNIPT--AAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVAMTLEEAL 163
Cdd:PRK08591 99 GFTFIGPSAETIRLMGDKVTAKATMKKAGVPVvpGSDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELE 178
|
90 100
....*....|....*....|....*...
gi 983471343 164 QAVKEMLQDVK--FGAASkkVVIEEFLD 189
Cdd:PRK08591 179 KAFSMARAEAKaaFGNPG--VYMEKYLE 204
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
136-204 |
1.89e-04 |
|
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: 41.89 E-value: 1.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983471343 136 VGAPIVIKADGLAAGKGVTVAMTLEE---ALQAVKEMLQDVKFGAASKKV-----VIEEFLDGQEFSLMAFV--NGTTV 204
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEwkaAFAAIREEIEQWKEMYPEAVVdggsfLVEEYIEGEEFAVDAYFdeNGEPV 79
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
109-193 |
3.12e-04 |
|
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: 41.53 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 109 LMKKYNIPTAAYETFT-------DYEEAVQYIEKVGAPIVIKADGLAAGKGVTVAMTLEEALQAVKEMLQdvkfgaASKK 181
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTradwklnPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQ------YDEK 74
|
90
....*....|..
gi 983471343 182 VVIEEFLDGQEF 193
Cdd:pfam07478 75 VLVEEGIEGREI 86
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
79-286 |
3.21e-04 |
|
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: 42.33 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 79 ADHFKEEGLRVFGPNKAaavIE--GSKAFTKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVA 156
Cdd:TIGR00768 66 LRYLESLGVPVINSSDA---ILnaGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 157 MTlEEALQAVKEMLQdvKFGAASKKVVIEEFLDGQEF-SLMAFVNGTTvhpmVIAQDHkRAFDGDKGPNTGGMGAYSPVP 235
Cdd:TIGR00768 143 RD-RQAAESLLEHFE--QLNGPQNLFLVQEYIKKPGGrDIRVFVVGDE----VVAAIY-RITSGHWRSNLARGGKAEPCS 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 983471343 236 QIPESAvQEAIKtvlhpTAKAMiaenrsftGILYAG--LILTKDGPKVIEFNA 286
Cdd:TIGR00768 215 LTEEIE-ELAIK-----AAKAL--------GLDVAGvdLLESEDGLLVNEVNA 253
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
107-190 |
3.82e-04 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 42.56 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 107 KELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVAMTLEEALQAVKEMLQdvkfgaASKK--VVI 184
Cdd:COG0458 119 KELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLERALK------VSPDhpVLI 192
|
....*.
gi 983471343 185 EEFLDG 190
Cdd:COG0458 193 DESLLG 198
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
79-167 |
4.31e-04 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 42.49 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 79 ADHFKEEGLRVFGPNKAAAVIEGSKAFTKELMKKYNIPTA-AYETFTDY--EEAVQYIEKVGAPIVIKADGLAAGKGVTV 155
Cdd:PRK08463 91 AKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVpGTEKLNSEsmEEIKIFARKIGYPVILKASGGGGGRGIRV 170
|
90
....*....|....*
gi 983471343 156 AMT---LEEALQAVK 167
Cdd:PRK08463 171 VHKeedLENAFESCK 185
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
65-169 |
5.09e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 42.43 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 65 LTFVGPeiplmngiadhfKEEGLRVFGpNKAAAviegskaftKELMKKYNIPT--AAYETFTDYEEAVQYIEKVGAPIVI 142
Cdd:PRK12999 104 ITFIGP------------TAEVLRLLG-DKVAA---------RNAAIKAGVPVipGSEGPIDDIEEALEFAEEIGYPIML 161
|
90 100 110
....*....|....*....|....*....|
gi 983471343 143 KADGLAAGKGVTVAMT---LEEALQAVKEM 169
Cdd:PRK12999 162 KASAGGGGRGMRIVRSeeeLEEAFERAKRE 191
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
103-193 |
5.81e-04 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 42.22 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 103 KAFTKELMKKYNIPTAAYETFTDYEEAVQYIEKVGA-PIVIKADGLAAGKGVTVAMT------LEEAL-QAVKEmlqdvk 174
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLFADkAIVVKPKSTNFGLGISIFKEpasledYEKALeIAFRE------ 562
|
90
....*....|....*....
gi 983471343 175 fgaaSKKVVIEEFLDGQEF 193
Cdd:PRK02471 563 ----DSSVLVEEFIVGTEY 577
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
38-313 |
6.44e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 42.14 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 38 RDVATPVDIDENDFDALVLFAKEnnveltfvgpeIPLMNGIA---DHFKEEGLRVF-------GPNKAAAVIEGSKAFTK 107
Cdd:PRK02186 45 AIRVVTISADTSDPDRIHRFVSS-----------LDGVAGIMsssEYFIEVASEVArrlglpaANTEAIRTCRDKKRLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 108 ELmKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVAMTLEEALQAVKEMLQdvkfgAASKKVVIEEF 187
Cdd:PRK02186 114 TL-RDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRR-----AGTRAALVQAY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 188 LDGQEFSLMAFVNGTTVHPMVIAQDHKrafdgDKGPNTGGMGAYSPVPqIPESAVQEAIKTVLhptaKAMIAENRSFtGI 267
Cdd:PRK02186 188 VEGDEYSVETLTVARGHQVLGITRKHL-----GPPPHFVEIGHDFPAP-LSAPQRERIVRTVL----RALDAVGYAF-GP 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 983471343 268 LYAGLILTKDGPKVIEFNARFGDPETEVVLPRLENdlVDVCNAVLD 313
Cdd:PRK02186 257 AHTELRVRGDTVVIIEINPRLAGGMIPVLLEEAFG--VDLLDHVID 300
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
106-195 |
8.25e-04 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 40.54 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 106 TKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKADG--LA----AGkGVTVA-MTLEEALQAVKEMLQDVKfgAA 178
Cdd:pfam13549 15 AKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSpdILhksdVG-GVRLNlRSAEAVRAAYEEILERVR--RY 91
|
90 100
....*....|....*....|...
gi 983471343 179 SKKVVIEEFL------DGQEFSL 195
Cdd:pfam13549 92 RPDARIEGVLvqpmapGGRELIV 114
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
106-195 |
9.22e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 41.65 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 106 TKELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKAD--GLA----AGkGVTVA-MTLEEALQAVKEMLQDVKfgAA 178
Cdd:COG1042 493 AKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVspDILhksdVG-GVRLNlRDAEAVRAAFEEILARVR--AA 569
|
90 100
....*....|....*....|...
gi 983471343 179 SKKVVIEEFL------DGQEFSL 195
Cdd:COG1042 570 RPDARIDGVLvqpmvpGGVELIV 592
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
65-168 |
9.94e-04 |
|
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: 41.60 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 65 LTFVGPEiplmngiADHfkeegLRVFGpNKAAAviegskaftKELMKKYNIPT--AAYETFTDYEEAVQYIEKVGAPIVI 142
Cdd:COG1038 103 ITFIGPS-------PEV-----LEMLG-DKVAA---------RAAAIEAGVPVipGTEGPVDDLEEALAFAEEIGYPVML 160
|
90 100
....*....|....*....|....*....
gi 983471343 143 KAdglAA---GKGVTVAMTLEEALQAVKE 168
Cdd:COG1038 161 KA---AAgggGRGMRVVRSEEELEEAFES 186
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
76-204 |
2.15e-03 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 40.34 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 76 NGIADHFKEEGLRVFGPN-KAAAVIEGSKAFTkELMKKYNIPTAAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVT 154
Cdd:PRK12815 644 INLAKGLEEAGLTILGTSpDTIDRLEDRDRFY-QLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMA 722
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 983471343 155 VAMTlEEALQAVKEMLQDVKFgaaskKVVIEEFLDGQEFSLMAFVNGTTV 204
Cdd:PRK12815 723 VVYD-EPALEAYLAENASQLY-----PILIDQFIDGKEYEVDAISDGEDV 766
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
46-189 |
2.72e-03 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 39.74 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983471343 46 IDENDFDAL-VLFAKENNvelTFVGPEIplmNGIA-DHFKE---EGLRVFgPNKAAAVI----EGSKAF-TKELmkkyNI 115
Cdd:PRK09288 59 IDMLDGDALrAVIEREKP---DYIVPEI---EAIAtDALVElekEGFNVV-PTARATRLtmnrEGIRRLaAEEL----GL 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983471343 116 PTAAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTVAMTLEEALQAVKEMLQdvkfGA--ASKKVVIEEFLD 189
Cdd:PRK09288 128 PTSPYRFADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPEDIEKAWEYAQE----GGrgGAGRVIVEEFID 199
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
83-155 |
4.58e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 38.96 E-value: 4.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983471343 83 KEEGLRVFGPNKAAAVIEGSKAFTKELMKKYNIPT--AAYETFTDYEEAVQYIEKVGAPIVIKADGLAAGKGVTV 155
Cdd:PRK08462 98 SHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVipGSDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRV 172
|
|
| |
