|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-425 |
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: 770.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 1 MNVLVIGSGGREHALAFKAAQNTKVNTVFVAPGNAGTALEPklENVAINVDDLEGLLSFAQQNKVELTIVGPEIPLVLGV 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLA--ECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 81 VDKFREHNMAIFGPTAGAAQLEGSKSFTKDFLARHNIPSGDYQTFEQIDPALAYLKEKGAPIVVKADGLAAGKGVIVAMT 160
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 161 EADAEDAIRDMLAGNAFGDAGSRVVIEEFLEGEEASFIVMVDGKNVLPFATSQDHKRAYNGDAGPNTGGMGAYSPAPVVT 240
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 241 DEIHQRIMNEVIYPTVEGMASEGHPYTGFLYAGLMIDETGtPKVIEYNCRFGDPETQPMMLRLQSDLVELIEAANRVELD 320
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 321 KTTIKFDPRAAVGVVLAAKGYPGDYPKGDAISGLKVDYPAGEKVFHAGTKQSGNDVVTAGGRVLCATALGNTVTQAQQRA 400
Cdd:COG0151 318 EVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERA 397
|
410 420
....*....|....*....|....*
gi 1942031941 401 YELVKHISWDGMEYRTDIAYRAIAR 425
Cdd:COG0151 398 YEAVEKIRFEGMFYRRDIGWRALKR 422
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-423 |
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: 610.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 1 MNVLVIGSGGREHALAFKAAQNTKVNTVFVAPGNAGTALEPKLENVAINVDDLEGLLSFAQQNKVELTIVGPEIPLVLGV 80
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 81 VDKFREHNMAIFGPTAGAAQLEGSKSFTKDFLARHNIPSGDYQTFEQIDPALAYLKEKGAPIVVKADGLAAGKGVIVAMT 160
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 161 EADAEDAIRDMLAGNaFGDAGSRVVIEEFLEGEEASFIVMVDGKNVLPFATSQDHKRAYNGDAGPNTGGMGAYSPAPVVT 240
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 241 DEIHQRIMNEVIYPTVEGMASEGHPYTGFLYAGLMIDETGtPKVIEYNCRFGDPETQPMMLRLQSDLVELIEAANRVELD 320
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 321 KTTIKFDPRAAVGVVLAAKGYPGDYPKGDAISGLKVDYPAGEKVFHAGTKQSGNDVVTAGGRVLCATALGNTVTQAQQRA 400
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 1942031941 401 YELVKHISWDGMEYRTDIAYRAI 423
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-427 |
0e+00 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 542.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 4 LVIGSGGREHALAFKAAQNTKVNTVFVAPGNAGTALEPKLENVA-INVDDLEGLLSFAQQNKVELTIVGPEIPLVLGVVD 82
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 83 KFREHNMAIFGPTAGAAQLEGSKSFTKDFLARHNIPSGDYQTFEQIDPALAYLKEKGAPIVVKADGLAAGKGVIVAMTEA 162
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 163 DAEDAIRDMLAGNAFGDAGSRVVIEEFLEGEEASFIVMVDGKNVLPFATSQDHKRAYNGDAGPNTGGMGAYSPAPVVTDE 242
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 243 IHQRIMNEVIYPTVEGMASEGHPYTGFLYAGLMID-ETGTPKVIEYNCRFGDPETQPMMLRLQSDLVELIEAANRVELDK 321
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEkKSGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 322 TTIKFDPRAAVGVVLAAKGYPGDYPKGDAISGLKV--DYPAGEKVFHAGT-KQSGNDVVTAGGRVLCATALGNTVTQAQQ 398
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEaeAVAPGVKVFHAGTaLDSDGNVVAAGGRVLGVTAKGKDIAEARA 400
|
410 420
....*....|....*....|....*....
gi 1942031941 399 RAYELVKHISWDGMEYRTDIAYRAIAREQ 427
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARLQ 429
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
103-296 |
1.76e-104 |
|
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: 307.67 E-value: 1.76e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 103 GSKSFTKDFLARHNIPSGDYQTFEQIDPALAYLKEKGAPI-VVKADGLAAGKGVIVAMTEADAEDAIRDMLAGNAFGDAG 181
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 182 SRVVIEEFLEGEEASFIVMVDGKNVLPFATSQDHKRAYNGDAGPNTGGMGAYSPAPVVTDEIHQRIMNEVIYPTVEGMAS 261
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1942031941 262 EGHPYTGFLYAGLMIDETGtPKVIEYNCRFGDPET 296
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-102 |
3.70e-48 |
|
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: 159.83 E-value: 3.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 1 MNVLVIGSGGREHALAFKAAQNTKVNTVFVAPGNAGTALEPKleNVAINVDDLEGLLSFAQQNKVELTIVGPEIPLVLGV 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAE--CVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGI 78
|
90 100
....*....|....*....|....
gi 1942031941 81 VDKF--REHNMAIFGPTAGAAQLE 102
Cdd:pfam02844 79 VDALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
331-421 |
3.16e-42 |
|
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: 143.74 E-value: 3.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 331 AVGVVLAAKGYPGDYPKGDAISGLKvdyPAGEKVFHAGTKQSGNDVVTAGGRVLCATALGNTVTQAQQRAYELVKHISWD 410
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLD---EAGVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFE 77
|
90
....*....|.
gi 1942031941 411 GMEYRTDIAYR 421
Cdd:pfam02843 78 GMFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
93-292 |
7.43e-21 |
|
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: 91.47 E-value: 7.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 93 GPTAGAAQLEGSKSFTKDFLARHNIPSGDYQTFEQIDPALAYLKEKGAPIVVKADGLAAGKGVIVAMTEADAEDAIRDML 172
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 173 AGNAFGDAGSRVVIEEFLEGEEASFIVMVDGKNVLPFATSQDHKrayngdAGPNTGGMGAYSPAPvVTDEIHQRIMNEVi 252
Cdd:COG0439 123 AEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKHQ------KPPYFVELGHEAPSP-LPEELRAEIGELV- 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1942031941 253 yptVEGMASEGHPYtGFLYAGLMIDETGTPKVIEYNCRFG 292
Cdd:COG0439 195 ---ARALRALGYRR-GAFHTEFLLTPDGEPYLIEINARLG 230
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
109-199 |
2.15e-07 |
|
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: 52.38 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 109 KDFLARHNIPSGDYQTFEQIDPALAYLKEKGAPIVVKA-----DglaaGKGVIVAMTEADAEDAIRDMlagnafgdAGSR 183
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGP 161
|
90
....*....|....*..
gi 1942031941 184 VVIEEFLEGE-EASFIV 199
Cdd:COG0026 162 CILEEFVPFErELSVIV 178
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
105-194 |
2.20e-07 |
|
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: 52.03 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 105 KSFTKDFLARHNIPSGDYQTFEQIDPALAYLKEK--GAPIVVKADGLAAGKGVIVAMTEADAEDAIRDMLagnAFGDags 182
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEelGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAF---KYDD--- 169
|
90
....*....|..
gi 1942031941 183 RVVIEEFLEGEE 194
Cdd:COG1181 170 KVLVEEFIDGRE 181
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
9.83e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 50.57 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 85 REHNMAIFGPTAGAAQLEGSKSFTKDFLARHNIPS--GDYQTFEQIDPALAYLKEKGAPIVVKADGLAAGKGVIVAMTEA 162
Cdd:PRK08591 96 EDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVvpGSDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEA 175
|
90 100 110
....*....|....*....|....*....|..
gi 1942031941 163 DAEDAIRdML---AGNAFGDAGsrVVIEEFLE 191
Cdd:PRK08591 176 ELEKAFS-MAraeAKAAFGNPG--VYMEKYLE 204
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
78-316 |
2.34e-06 |
|
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: 48.78 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 78 LGVVDKFREHNMAIFGPTAgAAQLEGSKSFTKDFLARHNIPSGDYQTFEQIDPALAYLKEKGAPIVVK-ADGlAAGKGVI 156
Cdd:COG0189 71 LALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKpLDG-SGGRGVF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 157 VAMTEADAEDAIRDMlagnaFGDAGSRVVIEEFLEGEEASF--IVMVDGKnvlPFA-----TSQDHKRAyNGDAGpntgg 229
Cdd:COG0189 149 LVEDEDALESILEAL-----TELGSEPVLVQEFIPEEDGRDirVLVVGGE---PVAairriPAEGEFRT-NLARG----- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 230 mGAYSPAPvVTDEIHQ---RIMneviyptvegmaseghPYTGFLYAGL-MIDETGTPKVIEYNCRFGDPE-TQPMMLRLQ 304
Cdd:COG0189 215 -GRAEPVE-LTDEERElalRAA----------------PALGLDFAGVdLIEDDDGPLVLEVNVTPGFRGlERATGVDIA 276
|
250
....*....|..
gi 1942031941 305 SDLVELIEAANR 316
Cdd:COG0189 277 EAIADYLEARAA 288
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-194 |
2.48e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 49.11 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 1 MNVLVIGSGGReHAL--AFKaaQNTKVNTVFVA-PGNAGTALE--------PKlenvainVDD---LEGLLSFAQQNKVE 66
Cdd:PRK12767 2 MNILVTSAGRR-VQLvkALK--KSLLKGRVIGAdISELAPALYfadkfyvvPK-------VTDpnyIDRLLDICKKEKID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 67 LTIVG--PEIPLVLGVVDKFREHNMAIFGPTAGAAQLEGSKSFTKDFLARHNIP---SGDYQTFEQIDPALAyLKEKGAP 141
Cdd:PRK12767 72 LLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPtpkSYLPESLEDFKAALA-KGELQFP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1942031941 142 IVVKADGLAAGKGVIVAMTEADAEDAIRDMLAgnafgdagsrVVIEEFLEGEE 194
Cdd:PRK12767 151 LFVKPRDGSASIGVFKVNDKEELEFLLEYVPN----------LIIQEFIEGQE 193
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
105-204 |
4.14e-06 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 49.15 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 105 KSFTKDFLARHNIPSGDYQTFEQIDPALAYLKE-KGAPIVVKADGLAAGKGVIVAMTEADAED---AIRdmlagNAFGDa 180
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISIFKEPASLEDyekALE-----IAFRE- 562
|
90 100
....*....|....*....|....
gi 1942031941 181 GSRVVIEEFLEGEEASFIVMvDGK 204
Cdd:PRK02471 563 DSSVLVEEFIVGTEYRFFVL-DGK 585
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
85-191 |
2.40e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 46.24 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 85 REHNMAIFGPTAGAAQLEGSKSFTKDFLARHNIP--SGDYQTFEQIDPALAYLKEKGAPIVVKADGLAAGKGVIVAMTEA 162
Cdd:PRK05586 96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVPvvPGSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175
|
90 100 110
....*....|....*....|....*....|.
gi 1942031941 163 DAEDAIRDML--AGNAFGDagSRVVIEEFLE 191
Cdd:PRK05586 176 ELIKAFNTAKseAKAAFGD--DSMYIEKFIE 204
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
103-294 |
6.27e-05 |
|
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: 43.14 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 103 GSKSFTKDFLARHNIPSGDYQTFEQIDPAlaylkekGAPIVVK-ADGlAAGKGVIVAMteadaedairdmlAGNAFGDAG 181
Cdd:pfam02655 2 SDKLKTYKALKNAGVPTPETLQAEELLRE-------EKKYVVKpRDG-CGGEGVRKVE-------------NGREDEAFI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 182 SRVVIEEFLEGEEASFIVMVDGKNVLPFATSqdhkRAYNGDAGPNTGGMGAYSPAPVVTDEIHQRIMNEVIyPTVEGMAS 261
Cdd:pfam02655 61 ENVLVQEFIEGEPLSVSLLSDGEKALPLSVN----RQYIDNGGSGFVYAGNVTPSRTELKEEIIELAEEVV-ECLPGLRG 135
|
170 180 190
....*....|....*....|....*....|....*
gi 1942031941 262 eghpytgflYAG--LMIDETGtPKVIEYNCRFGDP 294
Cdd:pfam02655 136 ---------YVGvdLVLKDNE-PYVIEVNPRITTS 160
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
109-199 |
8.43e-05 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 44.37 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 109 KDFLARHNIPSGDYQTFEQIDPALAYLKEKGAPIVVKA-----DglaaGKGVIVAMTEADAEDAIRDMLAGNAfgdagsr 183
Cdd:PRK06019 105 KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWALLGSVPC------- 173
|
90
....*....|....*..
gi 1942031941 184 vVIEEFLEGE-EASFIV 199
Cdd:PRK06019 174 -ILEEFVPFErEVSVIV 189
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
86-207 |
9.77e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 44.36 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 86 EHNMAIF-GPTAGAAQLEGSKSFTKDFLARHNIPS--GDYQTFEQIDPALAYLKEKGAPIVVKADGLAAGKGVIVAMTEA 162
Cdd:PRK12833 99 EAAGLIFvGPDAQTIRTMGDKARARRTARRAGVPTvpGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAA 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1942031941 163 D--AEDAIRDMLAGNAFGDAGsrVVIEEFLegEEASFI---VMVDGKNVL 207
Cdd:PRK12833 179 QlaAELPLAQREAQAAFGDGG--VYLERFI--ARARHIevqILGDGERVV 224
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
1.93e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 43.48 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 85 REHNMAIFGPTAGAAQLEGSKSFTKDFLARHNIP--SGDYQTFEQIDPALAYLKEKGAPIVVKAdglAAGKGVIvAMTEA 162
Cdd:PRK06111 96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPvvPGITTNLEDAEEAIAIARQIGYPVMLKA---SAGGGGI-GMQLV 171
|
90 100 110
....*....|....*....|....*....|....*
gi 1942031941 163 DAEDAIRDMLAGN------AFGDAgsRVVIEEFLE 191
Cdd:PRK06111 172 ETEQELTKAFESNkkraanFFGNG--EMYIEKYIE 204
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
113-204 |
3.06e-04 |
|
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: 41.09 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 113 ARHNIPSGDYQTFEQIDPALAYLKEKGAPIVVKADGLA-AGKGVIVAMTEADAEDAIRDMLAGnafgdagsRVVIEEFLE 191
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEELGDG--------PVIVEEFVP 72
|
90
....*....|....*.
gi 1942031941 192 GE-EASFIVM--VDGK 204
Cdd:pfam02222 73 FDrELSVLVVrsVDGE 88
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
126-205 |
8.91e-04 |
|
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: 40.37 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 126 EQIDPALAYLKEKGAPIVVKADGLAAGKGVIVAMTEADAEDAIRDML--AGNAFGDagSRVVIEEFLEG-EEASFIVMVD 202
Cdd:pfam02786 25 ETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALaeAPAAFGN--PQVLVEKSLKGpKHIEYQVLRD 102
|
...
gi 1942031941 203 GKN 205
Cdd:pfam02786 103 AHG 105
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
87-191 |
9.56e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 41.27 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 87 HNMAIFGPTAGAAQLEGSKSFTKDFLARHNIP--SGDYQTFEQIDPALAYLKEKGAPIVVKADGLAAGKGVIVAMTEADA 164
Cdd:PRK08462 100 HNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPviPGSDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDL 179
|
90 100
....*....|....*....|....*....
gi 1942031941 165 EDAI--RDMLAGNAFGDAgsRVVIEEFLE 191
Cdd:PRK08462 180 ENLYlaAESEALSAFGDG--TMYMEKFIN 206
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
105-300 |
2.00e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 40.09 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 105 KSFTKDFLARHNIPSGDYQTFEQIDPALAYLKEKGAPIVVKadglAAGKGVIVAMTEADAEDAIRDMLAgNAFGdAGSRV 184
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK----PAREGSSVGVSKVKEEDELQAALE-LAFK-YDDEV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 185 VIEEFLEGEEasFIVMVDGKNVLPFATSQDHKRAYNGDAGPNTGGMGAYSPAPvVTDEIHQRIMNEV--IYPTVEGmase 262
Cdd:PRK01372 173 LVEKYIKGRE--LTVAVLGGKALPVIEIVPAGEFYDYEAKYLAGGTQYICPAG-LPAEIEAELQELAlkAYRALGC---- 245
|
170 180 190
....*....|....*....|....*....|....*...
gi 1942031941 263 ghpyTGFLYAGLMIDETGTPKVIEYNcrfgdpeTQPMM 300
Cdd:PRK01372 246 ----RGWGRVDFMLDEDGKPYLLEVN-------TQPGM 272
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
53-252 |
2.66e-03 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 40.34 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 53 LEGLLSFAQQNKVELTIVGPEIPLVLGVVDKFREHNMAIFGPTAGAA-QLEGSKSFTKdFLARHNIPSGDYQTFEQIDPA 131
Cdd:PRK12815 619 LEDVLNVAEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIdRLEDRDRFYQ-LLDELGLPHVPGLTATDEEEA 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 132 LAYLKEKGAPIVVKADGLAAGKGVIVAmteaDAEDAIRDMLAGNAfgDAGSRVVIEEFLEGEEASFIVMVDGKNVLpFAT 211
Cdd:PRK12815 698 FAFAKRIGYPVLIRPSYVIGGQGMAVV----YDEPALEAYLAENA--SQLYPILIDQFIDGKEYEVDAISDGEDVT-IPG 770
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1942031941 212 SQDHKRayngDAGPNTGGMGAYSPAPVVTDEIHQRIMNEVI 252
Cdd:PRK12815 771 IIEHIE----QAGVHSGDSIAVLPPQSLSEEQQEKIRDYAI 807
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
103-245 |
4.48e-03 |
|
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: 38.87 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942031941 103 GSKSFTKDFLARHNIPSGDYQTFEQIDPALAYLKEKGAPIVVKADGLAAGKGVIVAMTEADAEDAIRdmlAGNAFGDAGS 182
Cdd:TIGR00768 87 GDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLE---HFEQLNGPQN 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1942031941 183 RVVIEEFLEGEEASFI-VMVDGKNVLpfATSQdhkRAYNGDAGPNTGGMGAYSPAPvVTDEIHQ 245
Cdd:TIGR00768 164 LFLVQEYIKKPGGRDIrVFVVGDEVV--AAIY---RITSGHWRSNLARGGKAEPCS-LTEEIEE 221
|
|
| |
