|
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: 783.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 1 MNVLIIGAGGREHALGWKAAQNPNVETVFIAPGNAGTALEPklENVNIGVEDIAGLVAFAQDKKIELTIVGPEAPLVIGV 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLA--ECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 81 VDAFREVGLPIFGPTQAAAQLEGSKAFTKDFLARHDIPTGYYSNFTEIEPAIAYVREQGAPIVVKADGLAAGKGVIVAMT 160
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 161 LEEAEDAIKDMLAGNAFGEAGSRVVIEEFLEGEEASFIVMVDGSSVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVT 240
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 241 PEIHNRILEEVIYPTVRGMDAEGAPYTGFLYAGLMIDADGtPKVIEYNCRFGDPETQPIMMRMESDLVELCLMAIDEKLD 320
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 321 EAESKWDPRASIGVVLAAGGYPADYAKGDVIS-LPTSEVEGQKVFHAGTTnNEAGDVVTNGGRVLCATALGNTVSEAQER 399
Cdd:COG0151 318 EVELEWDDRAAVCVVLASGGYPGSYEKGDVITgLEEAEAEGVKVFHAGTA-LEDGKLVTNGGRVLGVTALGDTLEEARER 396
|
410 420
....*....|....*....|....*.
gi 515630102 400 AYALTKQVSWNGMFHRNDIGYRAIAR 425
Cdd:COG0151 397 AYEAVEKIRFEGMFYRRDIGWRALKR 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: 638.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 1 MNVLIIGAGGREHALGWKAAQNPNVETVFIAPGNAGTALEPKLENVNIGVEDIAGLVAFAQDKKIELTIVGPEAPLVIGV 80
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 81 VDAFREVGLPIFGPTQAAAQLEGSKAFTKDFLARHDIPTGYYSNFTEIEPAIAYVREQGAPIVVKADGLAAGKGVIVAMT 160
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 161 LEEAEDAIKDMLAGNaFGEAGSRVVIEEFLEGEEASFIVMVDGSSVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVT 240
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 241 PEIHNRILEEVIYPTVRGMDAEGAPYTGFLYAGLMIDADGtPKVIEYNCRFGDPETQPIMMRMESDLVELCLMAIDEKLD 320
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 321 EAESKWDPRASIGVVLAAGGYPADYAKGDVIS-LPTSEVEGQKVFHAGtTNNEAGDVVTNGGRVLCATALGNTVSEAQER 399
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITgEPLAEAEGVKVFHAG-TKADNGKLVTNGGRVLAVTALGKTLEEARER 397
|
410 420
....*....|....*....|....
gi 515630102 400 AYALTKQVSWNGMFHRNDIGYRAI 423
Cdd:TIGR00877 398 AYEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-428 |
0e+00 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 576.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 4 LIIGAGGREHALGWKAAQNPNVETVFIAPGNAGTALEPKLENV-NIGVEDIAGLVAFAQDKKIELTIVGPEAPLVIGVVD 82
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVpDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 83 AFREVGLPIFGPTQAAAQLEGSKAFTKDFLARHDIPTGYYSNFTEIEPAIAYVREQGAPIVVKADGLAAGKGVIVAMTLE 162
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 163 EAEDAIKDMLAGNAFGEAGSRVVIEEFLEGEEASFIVMVDGSSVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTPE 242
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 243 IHNRILEEVIYPTVRGMDAEGAPYTGFLYAGLMIDA-DGTPKVIEYNCRFGDPETQPIMMRMESDLVELCLMAIDEKLDE 321
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKkSGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 322 AESKWDPRASIGVVLAAGGYPADYAKGDVIS-LPTSE--VEGQKVFHAGTTNNEAGDVVTNGGRVLCATALGNTVSEAQE 398
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKnLDEAEavAPGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEARA 400
|
410 420 430
....*....|....*....|....*....|
gi 515630102 399 RAYALTKQVSWNGMFHRNDIGYRAIAREQE 428
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARLQV 430
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
103-296 |
2.45e-105 |
|
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: 309.98 E-value: 2.45e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 103 GSKAFTKDFLARHDIPTGYYSNFTEIEPAIAYVREQGAPI-VVKADGLAAGKGVIVAMTLEEAEDAIKDMLAGNAFGEAG 181
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 182 SRVVIEEFLEGEEASFIVMVDGSSVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTPEIHNRILEEVIYPTVRGMDA 261
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 515630102 262 EGAPYTGFLYAGLMIDADGtPKVIEYNCRFGDPET 296
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-102 |
6.71e-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: 172.16 E-value: 6.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 1 MNVLIIGAGGREHALGWKAAQNPNVETVFIAPGNAGTALEPKleNVNIGVEDIAGLVAFAQDKKIELTIVGPEAPLVIGV 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAE--CVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGI 78
|
90 100
....*....|....*....|....
gi 515630102 81 VDAF--REVGLPIFGPTQAAAQLE 102
Cdd:pfam02844 79 VDALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
331-421 |
5.07e-38 |
|
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: 132.57 E-value: 5.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 331 SIGVVLAAGGYPADYAKGDVISLptSEVEGQKVFHAGTTNNEaGDVVTNGGRVLCATALGNTVSEAQERAYALTKQVSWN 410
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITG--LDEAGVKVFHAGTKLKD-GKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFE 77
|
90
....*....|.
gi 515630102 411 GMFHRNDIGYR 421
Cdd:pfam02843 78 GMFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
85-292 |
9.77e-22 |
|
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: 93.78 E-value: 9.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 85 REVGLPifGPTQAAAQLEGSKAFTKDFLARHDIPTGYYSNFTEIEPAIAYVREQGAPIVVKADGLAAGKGVIVAMTLEEA 164
Cdd:COG0439 37 EELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 165 EDAIKDMLAGNAFGEAGSRVVIEEFLEGEEASFIVMVDGSSVLPMATSQDHKrvgdkdTGPNTGGMGAYSPAPvVTPEIH 244
Cdd:COG0439 115 EAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKHQ------KPPYFVELGHEAPSP-LPEELR 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515630102 245 NRILEEViyptVRGMDAEGAPYtGFLYAGLMIDADGTPKVIEYNCRFG 292
Cdd:COG0439 188 AEIGELV----ARALRALGYRR-GAFHTEFLLTPDGEPYLIEINARLG 230
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
79-288 |
3.77e-08 |
|
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: 54.56 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 79 GVVDAFREVGLPIFGPTQAAAQLeGSKAFTKDFLARHDIP---TGYYSNFTEIEPAIAyvrEQGAPIVVK-ADGlAAGKG 154
Cdd:COG0189 72 ALLRQLEAAGVPVVNDPEAIRRA-RDKLFTLQLLARAGIPvppTLVTRDPDDLRAFLE---ELGGPVVLKpLDG-SGGRG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 155 VIVAMTLEEAEDAIKDMlagnaFGEAGSRVVIEEFLEGEEASF--IVMVDGSSVLPMA--TSQDHKRVgdkdtgpNTGGM 230
Cdd:COG0189 147 VFLVEDEDALESILEAL-----TELGSEPVLVQEFIPEEDGRDirVLVVGGEPVAAIRriPAEGEFRT-------NLARG 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515630102 231 GAYSPAPvVTPEIHnRILEEViyptvrgmdaegAPYTGFLYAGL-MIDADGTPKVIEYN 288
Cdd:COG0189 215 GRAEPVE-LTDEER-ELALRA------------APALGLDFAGVdLIEDDDGPLVLEVN 259
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
105-200 |
1.69e-06 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 50.31 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 105 KAFTKDFLARHDIPTGYYSNFTEIEPAIAYVRE-QGAPIVVKADGLAAGKGVIV---AMTLEEAEDAIKdmlagNAFGEa 180
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISIfkePASLEDYEKALE-----IAFRE- 562
|
90 100
....*....|....*....|
gi 515630102 181 GSRVVIEEFLEGEEASFIVM 200
Cdd:PRK02471 563 DSSVLVEEFIVGTEYRFFVL 582
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
105-292 |
2.81e-06 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 49.16 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 105 KAFTKDFLARHDIP---TGYYSNFTEIEPAIAyvrEQGAPIVVK-ADGLAA-------GKGVIVAMTLEEAEDAIKDMLA 173
Cdd:COG3919 118 KERFYELAEELGVPvpkTVVLDSADDLDALAE---DLGFPVVVKpADSVGYdelsfpgKKKVFYVDDREELLALLRRIAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 174 gnafgeAGSRVVIEEFLEG---EEASFIVMVDGSSVLPMATSQdHKRVGDkdtgPNTGGMGAYspapVVT---PEIHN-- 245
Cdd:COG3919 195 ------AGYELIVQEYIPGddgEMRGLTAYVDRDGEVVATFTG-RKLRHY----PPAGGNSAA----RESvddPELEEaa 259
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515630102 246 -RILEEViyptvrgmdaegaPYTGFLYAGLMIDA-DGTPKVIEYNCRFG 292
Cdd:COG3919 260 rRLLEAL-------------GYHGFANVEFKRDPrDGEYKLIEINPRFW 295
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
105-194 |
7.69e-06 |
|
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: 47.41 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 105 KAFTKDFLARHDIPTGYYSNFTEIEPA-IAYVREQ-GAPIVVKADGLAAGKGVIVAMTLEEAEDAIKDmlagnAFGEaGS 182
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELAdLEAIEEElGLPLFVKPAREGSSVGVSKVKNAEELAAALEE-----AFKY-DD 169
|
90
....*....|..
gi 515630102 183 RVVIEEFLEGEE 194
Cdd:COG1181 170 KVLVEEFIDGRE 181
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
109-199 |
2.75e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 45.84 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 109 KDFLARHDIPTGYYSNFTEIEPAIAYVREQGAPIVVKA-----DglaaGKGVIVAMTLEEAEDAIKDMlagnafgeAGSR 183
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGP 161
|
90
....*....|....*..
gi 515630102 184 VVIEEFLEGE-EASFIV 199
Cdd:COG0026 162 CILEEFVPFErELSVIV 178
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
103-294 |
7.07e-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: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 103 GSKAFTKDFLARHDIPTGYYSNFTEIEPAiayvreqGAPIVVK-ADGlAAGKGVIVAMTLEEAEDAIKDMLagnafgeag 181
Cdd:pfam02655 2 SDKLKTYKALKNAGVPTPETLQAEELLRE-------EKKYVVKpRDG-CGGEGVRKVENGREDEAFIENVL--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 182 srvvIEEFLEGEEASFIVMVDGSSVLPMATSqdhKRVGDKDTGPN--TGGMgaySPAPVVTPEIHNRILEEVI--YPTVR 257
Cdd:pfam02655 65 ----VQEFIEGEPLSVSLLSDGEKALPLSVN---RQYIDNGGSGFvyAGNV---TPSRTELKEEIIELAEEVVecLPGLR 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 515630102 258 GmdaegapytgflYAG--LMIdADGTPKVIEYNCRFGDP 294
Cdd:pfam02655 135 G------------YVGvdLVL-KDNEPYVIEVNPRITTS 160
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
1.20e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 44.25 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 85 REVGLPIFGPTQAAAQLEGSKAFTKDFLARHDIPT--GYYSNFTEIEPAIAYVREQGAPIVVKAdglAAGKGVIvAMTLE 162
Cdd:PRK06111 96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVvpGITTNLEDAEEAIAIARQIGYPVMLKA---SAGGGGI-GMQLV 171
|
90 100 110
....*....|....*....|....*....|....*
gi 515630102 163 EAEDAIKDMLAGN------AFGEAgsRVVIEEFLE 191
Cdd:PRK06111 172 ETEQELTKAFESNkkraanFFGNG--EMYIEKYIE 204
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
3-252 |
2.71e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 43.42 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 3 VLIIGAG------GRE------HALgwKAAQNPNVETVFIA--PGNAGTA--------LEPklenvnIGVEDIaglVAFA 60
Cdd:PRK12815 558 VLILGSGpirigqGIEfdyssvHAA--FALKKEGYETIMINnnPETVSTDydtadrlyFEP------LTLEDV---LNVA 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 61 QDKKIELTIVGPEAPLVIGVVDAFREVGLPIFGPTQAAA-QLEGSKAFTKdFLARHDIPTGYYSNFTEIEPAIAYVREQG 139
Cdd:PRK12815 627 EAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIdRLEDRDRFYQ-LLDELGLPHVPGLTATDEEEAFAFAKRIG 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 140 APIVVKADGLAAGKGVIVAmtleEAEDAIKDMLAGNAfgEAGSRVVIEEFLEGEEASFIVMVDGSSVLpMATSQDHKrvg 219
Cdd:PRK12815 706 YPVLIRPSYVIGGQGMAVV----YDEPALEAYLAENA--SQLYPILIDQFIDGKEYEVDAISDGEDVT-IPGIIEHI--- 775
|
250 260 270
....*....|....*....|....*....|...
gi 515630102 220 dKDTGPNTGGMGAYSPAPVVTPEIHNRILEEVI 252
Cdd:PRK12815 776 -EQAGVHSGDSIAVLPPQSLSEEQQEKIRDYAI 807
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
105-300 |
8.57e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 41.25 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 105 KAFTKDFLARHDIPTGYYSNFTEIEPAIAYVREQGAPIVVKadglAAGKGVIVAMTLEEAEDAIKDMLAgNAFgEAGSRV 184
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK----PAREGSSVGVSKVKEEDELQAALE-LAF-KYDDEV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 185 VIEEFLEGEEasFIVMVDGSSVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPvVTPEIHNRILEEViyptVRGMDAEGA 264
Cdd:PRK01372 173 LVEKYIKGRE--LTVAVLGGKALPVIEIVPAGEFYDYEAKYLAGGTQYICPAG-LPAEIEAELQELA----LKAYRALGC 245
|
170 180 190
....*....|....*....|....*....|....*.
gi 515630102 265 pyTGFLYAGLMIDADGTPKVIEYNcrfgdpeTQPIM 300
Cdd:PRK01372 246 --RGWGRVDFMLDEDGKPYLLEVN-------TQPGM 272
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
1.22e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 40.94 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 85 REVGLPIFGPTQAAAQLEGSKAFTKDFLARHDIPT--GYYSNFTEIEPAIAYVREQGAPIVVKADGLAAGKGVIVAMTLE 162
Cdd:PRK08591 96 EDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVvpGSDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEA 175
|
90 100 110
....*....|....*....|....*....|..
gi 515630102 163 EAEDAIKdML---AGNAFGEAGsrVVIEEFLE 191
Cdd:PRK08591 176 ELEKAFS-MAraeAKAAFGNPG--VYMEKYLE 204
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-203 |
1.69e-03 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 39.60 E-value: 1.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515630102 128 IEPAIAYVREQGAPIVVKADGLAAGKGVIVAMTLEEAEDAIKDML--AGNAFGEagSRVVIEEFLEG-EEASFIVMVDG 203
Cdd:pfam02786 27 EEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALaeAPAAFGN--PQVLVEKSLKGpKHIEYQVLRDA 103
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
85-191 |
3.69e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 39.31 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 85 REVGLPIFGPTQAAAQLEGSKAFTKDFLARHDIPT--GYYSNFTEIEPAIAYVREQGAPIVVKADGLAAGKGVIVAMTLE 162
Cdd:PRK05586 96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVvpGSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175
|
90 100 110
....*....|....*....|....*....|.
gi 515630102 163 EAEDAIKDML--AGNAFGEagSRVVIEEFLE 191
Cdd:PRK05586 176 ELIKAFNTAKseAKAAFGD--DSMYIEKFIE 204
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
82-191 |
4.42e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 39.35 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 82 DAFREVGLPIFGPTQAAAQLEGSKAFTKDFLARHDIPT--GYYSNFTEIEPAIAYVREQGAPIVVKADGLAAGKGVIVAM 159
Cdd:PRK12833 96 EAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTvpGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAH 175
|
90 100 110
....*....|....*....|....*....|....
gi 515630102 160 TLEE--AEDAIKDMLAGNAFGEAGsrVVIEEFLE 191
Cdd:PRK12833 176 DAAQlaAELPLAQREAQAAFGDGG--VYLERFIA 207
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
109-199 |
7.47e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 38.21 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 109 KDFLARHDIPTGYY---SNFTEIEPAIAYVreqGAPIVVKA-----DglaaGKGVIVAMTLEEAEDAIKDMLAGNAfgea 180
Cdd:PRK06019 105 KQFLDKLGIPVAPFavvDSAEDLEAALADL---GLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWALLGSVPC---- 173
|
90 100
....*....|....*....|
gi 515630102 181 gsrvVIEEFLEGE-EASFIV 199
Cdd:PRK06019 174 ----ILEEFVPFErEVSVIV 189
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
76-290 |
7.63e-03 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 38.83 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 76 LVIGVVDAFREVGLPIFG-PTQAAAQLEGSKAFTKdFLARHDIPTGYYSNFTEIEPAIAYVREQGAPIVVKADGLAAGKG 154
Cdd:TIGR01369 641 TPLNLAKALEEAGVPILGtSPESIDRAEDREKFSE-LLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 155 VIVAMTLEEAEDAIKDMLAGNAfgeaGSRVVIEEFLE-GEEASFIVMVDGSSVLPMATSQDHKRvgdkdTGPNTGGMGAY 233
Cdd:TIGR01369 720 MEIVYNEEELRRYLEEAVAVSP----EHPVLIDKYLEdAVEVDVDAVSDGEEVLIPGIMEHIEE-----AGVHSGDSTCV 790
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515630102 234 SPAPVVTPEIHNRIlEEVIYPTVRGMDaegapytgflYAGLM----IDADGTPKVIEYNCR 290
Cdd:TIGR01369 791 LPPQTLSAEIVDRI-KDIVRKIAKELN----------VKGLMniqfAVKDGEVYVIEVNPR 840
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
113-204 |
7.84e-03 |
|
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: 37.23 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 113 ARHDIPTGYYSNFTEIEPAIAYVREQGAPIVVKADGLA-AGKGVIVAMTLEEAEDAIKDMLAGnafgeagsRVVIEEFLE 191
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEELGDG--------PVIVEEFVP 72
|
90
....*....|....*.
gi 515630102 192 GE-EASFIVM--VDGS 204
Cdd:pfam02222 73 FDrELSVLVVrsVDGE 88
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
85-290 |
9.97e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 38.29 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 85 REVGLPIfGPTQAAAQLEgSKAFTKDFLARHDIPTGYYSNFTEIEPAIAYVREQGAPIVVKAdglAAGKGVIVAMTLEEA 164
Cdd:PRK02186 90 RRLGLPA-ANTEAIRTCR-DKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKP---RMGSGSVGVRLCASV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630102 165 EDAIKdmlAGNAFGEAGSR-VVIEEFLEGEEASFIVMVDGSSVLPMATSQDHkrvgdKDTGPNTGGMGAYSPAPVVTPEi 243
Cdd:PRK02186 165 AEAAA---HCAALRRAGTRaALVQAYVEGDEYSVETLTVARGHQVLGITRKH-----LGPPPHFVEIGHDFPAPLSAPQ- 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515630102 244 hnriLEEVIYPTVRGMDAEGAPYtGFLYAGLMIDADgTPKVIEYNCR 290
Cdd:PRK02186 236 ----RERIVRTVLRALDAVGYAF-GPAHTELRVRGD-TVVIIEINPR 276
|
|
| |
