|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-419 |
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: 733.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 1 MKVLVVGRGGREHALAWKFAQSPNVEKVYVAPGNDGMTDVAELVAIDENDHNGLIAFAKEAEVSLTFVGPEAPLSEGIVN 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 81 RFEEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTLE 160
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 161 DALAAIDEMMNQAKFGEASSKVVVEEFLEGEEFSFMAFVKGEKVYPMVISQDHKRAYDGDQGPNTGGMGAYSPVPQIPEE 240
Cdd:COG0151 161 EALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 241 ALDTAFKTILQSTANAMIAENRYFTGILYAGLILTATGPKVIEFNARFGDPETQVILPRLENDLAELINDILDDK--PVE 318
Cdd:COG0151 241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRldEVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 319 LRWSNEAVIGVVLAATGYPNEYEKGHVIHGL-HAMSDDIFVFHAGTKKRDDSFVTNGGRVLLAATKGNDLAEAQNQLYKQ 397
Cdd:COG0151 321 LEWDDRAAVCVVLASGGYPGSYEKGDVITGLeEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERAYEA 400
|
410 420
....*....|....*....|..
gi 489425903 398 LEKVHCDGLFYRKDIGYRTIAY 419
Cdd:COG0151 401 VEKIRFEGMFYRRDIGWRALKR 422
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-417 |
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: 591.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 1 MKVLVVGRGGREHALAWKFAQSPNVEKVYVAPGNDGMTDVAE--LVAIDENDHNGLIAFAKEAEVSLTFVGPEAPLSEGI 78
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKnkNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 79 VNRFEEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALT 158
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 159 LEDALAAIDEMMNQaKFGEASSKVVVEEFLEGEEFSFMAFVKGEKVYPMVISQDHKRAYDGDQGPNTGGMGAYSPVPQIP 238
Cdd:TIGR00877 161 NEEAIKAVEDILEQ-KFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 239 EEALDTAFKTILQSTANAMIAENRYFTGILYAGLILTATGPKVIEFNARFGDPETQVILPRLENDLAELINDILDDK--P 316
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKldE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 317 VELRWSNEAVIGVVLAATGYPNEYEKGHVIHGLHAMSD-DIFVFHAGTKKRDDSFVTNGGRVLLAATKGNDLAEAQNQLY 395
Cdd:TIGR00877 320 VELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAeGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERAY 399
|
410 420
....*....|....*....|..
gi 489425903 396 KQLEKVHCDGLFYRKDIGYRTI 417
Cdd:TIGR00877 400 EAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-422 |
7.59e-180 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 508.12 E-value: 7.59e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 4 LVVGRGGREHALAWKFAQSPNVEKVYVAPGNDGMT---DVAELVAIDENDHNGLIAFAKEAEVSLTFVGPEAPLSEGIVN 80
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIAtsgDATCVPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 81 RFEEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTLE 160
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 161 DALAAIDEMMNQAKFGEASSKVVVEEFLEGEEFSFMAFVKGEKVYPMVISQDHKRAYDGDQGPNTGGMGAYSPVPQIPEE 240
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 241 ALDTAFKTILQSTANAMIAENRYFTGILYAGLILTATG--PKVIEFNARFGDPETQVILPRLENDLAELI----NDILDD 314
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLlaacKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 315 kpVELRWSNEAVIGVVLAATGYPNEYEKGHVIHGL---HAMSDDIFVFHAGT-KKRDDSFVTNGGRVLLAATKGNDLAEA 390
Cdd:PLN02257 321 --VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLdeaEAVAPGVKVFHAGTaLDSDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|..
gi 489425903 391 QNQLYKQLEKVHCDGLFYRKDIGYRTIAYAKA 422
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQV 430
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
101-293 |
3.33e-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: 316.92 E-value: 3.33e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 101 GSKSFAKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPI-VIKADGLAAGKGVVVALTLEDALAAIDEMMNQAKFGEAS 179
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 180 SKVVVEEFLEGEEFSFMAFVKGEKVYPMVISQDHKRAYDGDQGPNTGGMGAYSPVPQIPEEALDTAFKTILQSTANAMIA 259
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 489425903 260 ENRYFTGILYAGLILTATGPKVIEFNARFGDPET 293
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-100 |
2.22e-52 |
|
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: 170.61 E-value: 2.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 1 MKVLVVGRGGREHALAWKFAQSPNVEKVYVAPGNDGMTDVAELVAIDENDHNGLIAFAKEAEVSLTFVGPEAPLSEGIVN 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80
|
90 100
....*....|....*....|..
gi 489425903 81 RF--EEAGLRAFGPRKEAAIIE 100
Cdd:pfam02844 81 ALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
327-415 |
1.26e-36 |
|
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: 128.72 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 327 IGVVLAATGYPNEYEKGHVIHGLHAMsdDIFVFHAGTKKRDDSFVTNGGRVLLAATKGNDLAEAQNQLYKQLEKVHCDGL 406
Cdd:pfam02843 2 VCVVLASGGYPGSYEKGDVITGLDEA--GVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFEGM 79
|
....*....
gi 489425903 407 FYRKDIGYR 415
Cdd:pfam02843 80 FYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
83-289 |
1.66e-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: 101.49 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 83 EEAGLRafGPRKEAAIIEGSKSFAKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTLEDA 162
Cdd:COG0439 37 EELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 163 LAAIDEMMNQAKFGEASSKVVVEEFLEGEEFSFMAFVKGEKVYPMVISQDHKRaydgdqGPNTGGMGAYSPVPqIPEEAL 242
Cdd:COG0439 115 EAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKHQK------PPYFVELGHEAPSP-LPEELR 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489425903 243 DtafkTILQSTANAMIAENrYFTGILYAGLILTATG-PKVIEFNARFG 289
Cdd:COG0439 188 A----EIGELVARALRALG-YRRGAFHTEFLLTPDGePYLIEINARLG 230
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
77-289 |
9.09e-11 |
|
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: 62.27 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 77 GIVNRFEEAGLRAFGPRkEAAIIEGSKSFAKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIK-ADGlAAGKGVVV 155
Cdd:COG0189 72 ALLRQLEAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKpLDG-SGGRGVFL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 156 ALTLEDALAAIDEMmnqakFGEASSKVVVEEFLEGEEFSFM-AFVKGEKVYPM---VISQDHKRAYDgDQGpntggmGAY 231
Cdd:COG0189 150 VEDEDALESILEAL-----TELGSEPVLVQEFIPEEDGRDIrVLVVGGEPVAAirrIPAEGEFRTNL-ARG------GRA 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 232 SPVPqIPEEALDTAFKtilqsTANAMiaenryftGILYAG--LILTATGPKVIEFNARFG 289
Cdd:COG0189 218 EPVE-LTDEERELALR-----AAPAL--------GLDFAGvdLIEDDDGPLVLEVNVTPG 263
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
103-194 |
4.12e-09 |
|
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: 57.42 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 103 KSFAKDLMKKYNIPTAKYETFTSYE--EARAYIEEQGAPIVIKADGLAAGKGVVVALTLEDALAAIDEMmnqAKFGEass 180
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGElaDLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEA---FKYDD--- 169
|
90
....*....|....
gi 489425903 181 KVVVEEFLEGEEFS 194
Cdd:COG1181 170 KVLVEEFIDGREVT 183
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
107-208 |
5.33e-09 |
|
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: 57.39 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 107 KDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKA-----DglaaGKGVVVALTLEDALAAIDEMMNQAkfgeassk 181
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAALGGGP-------- 161
|
90 100 110
....*....|....*....|....*....|.
gi 489425903 182 VVVEEFLEGE-EFSFMA--FVKGE-KVYPMV 208
Cdd:COG0026 162 CILEEFVPFErELSVIVarSPDGEvATYPVV 192
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
74-205 |
4.53e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 54.99 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 74 LSE--GIVNRFEEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNIPT--AKYETFTSYEEARAYIEEQGAPIVIKADGLAA 149
Cdd:PRK08654 85 LAEnpEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVlpGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGG 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489425903 150 GKGVVVALTLEDALAAIDEMMNQAK--FGEASskVVVEEFLEGE---EFSFMAFVKGEKVY 205
Cdd:PRK08654 165 GIGMRVVYSEEELEDAIESTQSIAQsaFGDST--VFIEKYLEKPrhiEIQILADKHGNVIH 223
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
103-206 |
6.69e-08 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 53.58 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 103 KSFAKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKAdgLAAGK--GVVVALTLEDALAAIDEmmnQAKFGEass 180
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALEL---AFKYDD--- 170
|
90 100
....*....|....*....|....*.
gi 489425903 181 KVVVEEFLEGEEFSfmAFVKGEKVYP 206
Cdd:PRK01372 171 EVLVEKYIKGRELT--VAVLGGKALP 194
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
103-193 |
2.12e-07 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 53.24 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 103 KSFAKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKA-DGlAAGKGVVVAL-TLEDALAAIDEMMnqakfgEASS 180
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPlDG-NHGRGVTVNItTREEIEAAYAVAS------KESS 287
|
90
....*....|...
gi 489425903 181 KVVVEEFLEGEEF 193
Cdd:PRK14016 288 DVIVERYIPGKDH 300
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
50-189 |
2.31e-07 |
|
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: 53.16 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 50 DHNGLIAFAKEAEVsltfvgpEA--P----LSEGI--VNRFEEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNIPT--AK 119
Cdd:COG1038 65 DIEEIIRVAKEKGV-------DAihPgygfLSENPefARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVipGT 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489425903 120 YETFTSYEEARAYIEEQGAPIVIKAdglAA---GKGVVVALTLEDALAAIDEMMNQAK--FGeaSSKVVVEEFLE 189
Cdd:COG1038 138 EGPVDDLEEALAFAEEIGYPVMLKA---AAgggGRGMRVVRSEEELEEAFESARREAKaaFG--DDEVFLEKYIE 207
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
114-287 |
3.35e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 51.95 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 114 NIPTAKYETFTSYEEARAYIEEQ---GAPIVIKADGLAAGKGVVVALTLEDALAAIDEMMNQA-KFGEASSKVVVEEFLE 189
Cdd:PRK07206 120 GLPAARQINTADWEEAEAWLRENgliDRPVVIKPLESAGSDGVFICPAKGDWKHAFNAILGKAnKLGLVNETVLVQEYLI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 190 GEEFSFMAFVKGEKVYPMVISQDHKRaydgdqgPNTGGMGAYSPVPQIPEEALDtaFKTILQSTANAMIAenryfTGILY 269
Cdd:PRK07206 200 GTEYVVNFVSLDGNHLVTEIVRYHKT-------SLNSGSTVYDYDEFLDYSEPE--YQELVDYTKQALDA-----LGIKN 265
|
170 180
....*....|....*....|..
gi 489425903 270 ----AGLILTATGPKVIEFNAR 287
Cdd:PRK07206 266 gpahAEVMLTADGPRLIEIGAR 287
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
40-208 |
3.54e-07 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 51.69 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 40 VAELVAIDENDHNGLIAFAKEAEVsLTF----VgPEAPLSEgivnrfeEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNI 115
Cdd:PRK06019 43 ADEVIVADYDDVAALRELAEQCDV-ITYefenV-PAEALDA-------LAARVPVPPGPDALAIAQDRLTEKQFLDKLGI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 116 PTAKYETFTSYEEARAYIEEQGAPIVIKA-----DglaaGKGVVVALTLEDALAAIDEMMNQAkfgeasskVVVEEFLEG 190
Cdd:PRK06019 114 PVAPFAVVDSAEDLEAALADLGLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWALLGSVP--------CILEEFVPF 181
|
170 180
....*....|....*....|..
gi 489425903 191 E-EFSFMA--FVKGE-KVYPMV 208
Cdd:PRK06019 182 ErEVSVIVarGRDGEvVFYPLV 203
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
46-189 |
4.96e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 52.06 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 46 IDEndhngLIAFAKEAEVsltfvgpEA--P----LSEGI--VNRFEEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNIPT 117
Cdd:PRK12999 67 IDE-----IIRVAKQAGV-------DAihPgygfLSENPefARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPV 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489425903 118 --AKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTLEDALAAIDEMMNQAK--FGeaSSKVVVEEFLE 189
Cdd:PRK12999 135 ipGSEGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaaFG--NDEVYLEKYVE 208
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
83-189 |
6.42e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 51.34 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 83 EEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNIPTAKYET--FTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTLE 160
Cdd:PRK08591 96 EDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDgpVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEA 175
|
90 100 110
....*....|....*....|....*....|.
gi 489425903 161 DALAAIDEMMNQAK--FGEASskVVVEEFLE 189
Cdd:PRK08591 176 ELEKAFSMARAEAKaaFGNPG--VYMEKYLE 204
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
106-189 |
1.20e-06 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 48.80 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 106 AKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAP-IVIKADGLAAGK----GVVVALTLEDALAAIDEMMNQ-------A 173
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKvYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEMLGKnlvtkqtG 86
|
90
....*....|....*.
gi 489425903 174 KFGEASSKVVVEEFLE 189
Cdd:pfam08442 87 PDGQPVNKVLVEEALD 102
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
103-190 |
1.67e-06 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 48.45 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 103 KSFAKDLMKKYNIPTAKYE--TFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTLEDALAAIDEMMNQAKFGEASS 180
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTagPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90
....*....|
gi 489425903 181 KVVVEEFLEG 190
Cdd:pfam02786 82 QVLVEKSLKG 91
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
106-169 |
1.90e-06 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 49.70 E-value: 1.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489425903 106 AKDLMKKYNIPTAKYETFTSYEEARAYIEE-QGAPIVIKADGLAAGK----GVVVALTLEDALAAIDEM 169
Cdd:PRK00696 8 AKELFAKYGVPVPRGIVATTPEEAVEAAEElGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQI 76
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
74-189 |
2.49e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 49.64 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 74 LSE--GIVNRFEEAGLRAFGPrkEAAIIE--GSKSFAKDLMKKYNIPT--AKYETFTSYEEARAYIEEQGAPIVIKADGL 147
Cdd:PRK06111 85 LSEnaSFAERCKEEGIVFIGP--SADIIAkmGSKIEARRAMQAAGVPVvpGITTNLEDAEEAIAIARQIGYPVMLKASAG 162
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489425903 148 AAGKGVVVALTLEDALAAIDemMNQAK----FGEASskVVVEEFLE 189
Cdd:PRK06111 163 GGGIGMQLVETEQELTKAFE--SNKKRaanfFGNGE--MYIEKYIE 204
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
119-291 |
3.00e-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: 46.99 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 119 KYETFTSYEEAR---------AYIEEQGAPIVIK-ADGlAAGKGVVVAltledalaaidemMNQAKFGEASSKVVVEEFL 188
Cdd:pfam02655 4 KLKTYKALKNAGvptpetlqaEELLREEKKYVVKpRDG-CGGEGVRKV-------------ENGREDEAFIENVLVQEFI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 189 EGEEFSFMAFVKGEKVYPMVISQDHKrAYDGDQGPNTGGMGAYSPVPQipEEALDTAFKTILQstanamiaenryFTGIL 268
Cdd:pfam02655 70 EGEPLSVSLLSDGEKALPLSVNRQYI-DNGGSGFVYAGNVTPSRTELK--EEIIELAEEVVEC------------LPGLR 134
|
170 180
....*....|....*....|....*.
gi 489425903 269 -YAG--LILTATGPKVIEFNARFGDP 291
Cdd:pfam02655 135 gYVGvdLVLKDNEPYVIEVNPRITTS 160
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
83-189 |
3.66e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 48.94 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 83 EEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNIPTAK-YE-TFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTLE 160
Cdd:PRK05586 96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPgSEgEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175
|
90 100 110
....*....|....*....|....*....|.
gi 489425903 161 DALAAIDEMMNQAK--FGEASskVVVEEFLE 189
Cdd:PRK05586 176 ELIKAFNTAKSEAKaaFGDDS--MYIEKFIE 204
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
103-204 |
3.68e-06 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 49.15 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 103 KSFAKDLMKKYNIPTAKYETFTSYEEARAYIEE-QGAPIVIKADGLAAGKGVVVALTLEDaLAAIDEMMNQAkFGEASSk 181
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISIFKEPAS-LEDYEKALEIA-FREDSS- 565
|
90 100
....*....|....*....|...
gi 489425903 182 VVVEEFLEGEEFSFmaFVKGEKV 204
Cdd:PRK02471 566 VLVEEFIVGTEYRF--FVLDGKV 586
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
137-290 |
4.08e-06 |
|
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: 46.51 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 137 GAPIVIKADGLAAGKGVVVALTLED---ALAAIDEMMNQAK-----FGEASSKVVVEEFLEGEEFSFMAFVKgEKVYPMV 208
Cdd:pfam13535 2 PYPCVIKPSVGFFSVGVYKINNREEwkaAFAAIREEIEQWKemypeAVVDGGSFLVEEYIEGEEFAVDAYFD-ENGEPVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 209 ISQDHKRAYDGDQGPNTGgmgaYSPVPQIPEEALDtAFKTILQSTANAMIAENryftGILYAGLILTATGPKV-IEFNA- 286
Cdd:pfam13535 81 LNILKHDFASSEDVSDRI----YVTSASIIRETQA-AFTEFLKRINALLGLKN----FPVHIELRVDEDGQIIpIEVNPl 151
|
....
gi 489425903 287 RFGD 290
Cdd:pfam13535 152 RFAG 155
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
106-189 |
8.02e-06 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 47.82 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 106 AKDLmkkyNIPTAKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTLEDALAAIDEMMNQAKFGeaSSKVVVE 185
Cdd:PRK09288 122 AEEL----GLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPEDIEKAWEYAQEGGRGG--AGRVIVE 195
|
....
gi 489425903 186 EFLE 189
Cdd:PRK09288 196 EFID 199
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
106-170 |
1.61e-05 |
|
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: 46.58 E-value: 1.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 106 AKDLMKKYNIPTAKYETFTSYEEARAYIEE-QGAPIVIKADGLAAGK----GVVVALTLEDALAAIDEMM 170
Cdd:COG0045 8 AKELLAKYGVPVPRGIVATTPEEAVAAAEElGGPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAAEEIL 77
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
111-208 |
1.72e-05 |
|
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: 44.94 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 111 KKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKADGLA-AGKGVVVALTLEDALAAIDEMmnqakfgeASSKVVVEEFLE 189
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEEL--------GDGPVIVEEFVP 72
|
90 100
....*....|....*....|...
gi 489425903 190 GE-EFSFMA--FVKGEKV-YPMV 208
Cdd:pfam02222 73 FDrELSVLVvrSVDGETAfYPVV 95
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
83-189 |
2.55e-05 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 46.34 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 83 EEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNIP----TAKYETfTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALT 158
Cdd:PRK08463 95 EDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPivpgTEKLNS-ESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHK 173
|
90 100 110
....*....|....*....|....*....|.
gi 489425903 159 LEDALAAIDEMMNQAKFGEASSKVVVEEFLE 189
Cdd:PRK08463 174 EEDLENAFESCKREALAYFNNDEVFMEKYVV 204
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
77-287 |
3.44e-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: 46.15 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 77 GIVNRFEEAGLRAFGPRKEAA-IIEGSKSFAKdLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVV 155
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIdRAEDREKFSE-LLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEI 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 156 ALTLEDalaaIDEMMNQAKFGEASSKVVVEEFLE-GEEFSFMAFVKGEKVYPMVISQDHKRAydgdqGPNTGGMGAYSPV 234
Cdd:TIGR01369 723 VYNEEE----LRRYLEEAVAVSPEHPVLIDKYLEdAVEVDVDAVSDGEEVLIPGIMEHIEEA-----GVHSGDSTCVLPP 793
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489425903 235 PQIPEEALDtafkTILQSTANamIAENRYFTGILYAGLILTATGPKVIEFNAR 287
Cdd:TIGR01369 794 QTLSAEIVD----RIKDIVRK--IAKELNVKGLMNIQFAVKDGEVYVIEVNPR 840
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
106-174 |
9.38e-05 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 44.73 E-value: 9.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489425903 106 AKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKAD--GLA----AGkGVVVALTLEDAL-AAIDEMMNQAK 174
Cdd:COG1042 493 AKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVspDILhksdVG-GVRLNLRDAEAVrAAFEEILARVR 567
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
107-190 |
1.05e-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: 44.60 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 107 KDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTLEDALAAIDEMMNQAKFGEasskVVVEE 186
Cdd:TIGR01369 132 REAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQ----VLVEK 207
|
....
gi 489425903 187 FLEG 190
Cdd:TIGR01369 208 SLAG 211
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
108-289 |
1.14e-04 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 44.15 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 108 DLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIK-ADGLAA-------GKGVVVALTLEDALAAIDEMmnqakfGEAS 179
Cdd:COG3919 123 ELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKpADSVGYdelsfpgKKKVFYVDDREELLALLRRI------AAAG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 180 SKVVVEEFLEG---EEFSFMAFVKGE-KVYPMVISQDHkRAYdgdqgPNTGGMGAYspVPQIPEEALDTAFKTILQSTAn 255
Cdd:COG3919 197 YELIVQEYIPGddgEMRGLTAYVDRDgEVVATFTGRKL-RHY-----PPAGGNSAA--RESVDDPELEEAARRLLEALG- 267
|
170 180 190
....*....|....*....|....*....|....*.
gi 489425903 256 amiaenryFTGILYAGLILTA-TG-PKVIEFNARFG 289
Cdd:COG3919 268 --------YHGFANVEFKRDPrDGeYKLIEINPRFW 295
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
82-310 |
1.26e-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: 43.49 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 82 FEEAGLRAFGPrkEAAIIE-GSKSFAKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTlE 160
Cdd:TIGR00768 69 LESLGVPVINS--SDAILNaGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARD-R 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 161 DALAAIDEMMNQakFGEASSKVVVEEFL-EGEEFSFMAFVKGEKvypmVISQDHkRAYDGDQGPNTGGMGAYSPVPQIPE 239
Cdd:TIGR00768 146 QAAESLLEHFEQ--LNGPQNLFLVQEYIkKPGGRDIRVFVVGDE----VVAAIY-RITSGHWRSNLARGGKAEPCSLTEE 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489425903 240 EaldtafKTILQSTANAMiaenryftGILYAG--LILTATGPKVIEFNArfgDPETQVILPRLENDLAELIND 310
Cdd:TIGR00768 219 I------EELAIKAAKAL--------GLDVAGvdLLESEDGLLVNEVNA---NPEFKNSVKTTGVNIAGKLLD 274
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
82-192 |
1.29e-04 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 43.57 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 82 FEEAGLRAFGPRkeaaiIEGSK-SFAKDLMKKY----NIPTAKYETFTSYEEARAYIEEQ----GAPIVIKADGLAAGKG 152
Cdd:PRK01966 103 LELLGIPYVGCG-----VLASAlSMDKILTKRLlaaaGIPVAPYVVLTRGDWEEASLAEIeaklGLPVFVKPANLGSSVG 177
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489425903 153 VVVALTLEDALAAIDEmmnqAkFGEaSSKVVVEEFLEGEE 192
Cdd:PRK01966 178 ISKVKNEEELAAALDL----A-FEY-DRKVLVEQGIKGRE 211
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
77-205 |
2.75e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 43.42 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 77 GIVNRFEEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVA 156
Cdd:PRK12815 645 NLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVV 724
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489425903 157 ltleDALAAIDEMMNQAKFGEasSKVVVEEFLEGEEFSFMAFVKGEKVY 205
Cdd:PRK12815 725 ----YDEPALEAYLAENASQL--YPILIDQFIDGKEYEVDAISDGEDVT 767
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
107-190 |
3.87e-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: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 107 KDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTLEDalaaIDEMMNQAKfgEASSK--VVV 184
Cdd:COG0458 119 KELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEE----LEEYLERAL--KVSPDhpVLI 192
|
....*.
gi 489425903 185 EEFLEG 190
Cdd:COG0458 193 DESLLG 198
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
86-189 |
5.41e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 42.04 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 86 GLRAFGPRKEAAIIEGSKSFAKDLMKKYNIPTAKYET--FTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTLEDA- 162
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDgaLKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLe 180
|
90 100 110
....*....|....*....|....*....|
gi 489425903 163 ---LAAIDEMMnqAKFGEASskVVVEEFLE 189
Cdd:PRK08462 181 nlyLAAESEAL--SAFGDGT--MYMEKFIN 206
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
83-189 |
2.11e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 40.12 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 83 EEAGLRAFGPRKEAAIIEGSKSFAKDLMKKYNIPT--AKYETFTSYEEARAYIEEQGAPIVIKADGLAAGKGVVVALTlE 160
Cdd:PRK12833 99 EAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTvpGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHD-A 177
|
90 100 110
....*....|....*....|....*....|..
gi 489425903 161 DALAA---IDEMMNQAKFGeaSSKVVVEEFLE 189
Cdd:PRK12833 178 AQLAAelpLAQREAQAAFG--DGGVYLERFIA 207
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
109-289 |
2.52e-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: 38.64 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 109 LMKKYNIPTAKYETFTSYEEARAYIEE--QGAPIVIKADGLAAGKGVVVALTlEDALAAIDEMMNQAkfgeasskVVVEE 186
Cdd:pfam08443 10 LLAKHGIGPPNTRLAWYPEDAEQFIEQikRQFPVIVKSIYGSQGIGVFLAED-EQKLRQTLSATNEQ--------ILVQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 187 FLEGEEFSFM-AFVKGEKvypmVISQDHKRAYDGDQGPNTGGMGAYSPVpQIPEEALDTAFKtilqsTANAMiaenryft 265
Cdd:pfam08443 81 FIAEANNEDIrCLVVGDQ----VVGALHRQSNEGDFRSNLHRGGVGEKY-QLSQEETELAIK-----AAQAM-------- 142
|
170 180
....*....|....*....|....*.
gi 489425903 266 GILYAG--LILTATGPKVIEFNARFG 289
Cdd:pfam08443 143 QLDVAGvdLLRQKRGLLVCEVNSSPG 168
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
106-174 |
3.08e-03 |
|
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: 39.00 E-value: 3.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489425903 106 AKDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVIKADG--LA----AGkGVVVAL-TLEDALAAIDEMMNQAK 174
Cdd:pfam13549 15 AKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSpdILhksdVG-GVRLNLrSAEAVRAAYEEILERVR 89
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
107-142 |
6.49e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 38.92 E-value: 6.49e-03
10 20 30
....*....|....*....|....*....|....*.
gi 489425903 107 KDLMKKYNIPTAKYETFTSYEEARAYIEEQGAPIVI 142
Cdd:PRK05294 133 KEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVII 168
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
109-193 |
7.56e-03 |
|
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: 37.68 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489425903 109 LMKKYNIPTAKYETFTSYE------EARAYIEEQ-GAPIVIKADGLAAGKGVVVALTLEDALAAIDEMmnqAKFGEassK 181
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTRADwklnpkEWCAQVEEAlGYPVFVKPARLGSSVGVSKVESREELQAAIEEA---FQYDE---K 74
|
90
....*....|..
gi 489425903 182 VVVEEFLEGEEF 193
Cdd:pfam07478 75 VLVEEGIEGREI 86
|
|
| |
