|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-420 |
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: 650.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 1 MKLLVVGSGGREHAIAKKLLESKDVEQVFVAPGNDGMTLDGlDLINIGISEHSKLIDFAKANDIAWTFIGPDDALAAGIV 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLA-ECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 81 DDFNAAGLKAFGPTKAAAELEWSKDFAKEIMVKYDVPTAAYGTFSDFEEAKAYIEEKGAPIVVKADGLALGKGVVVAETV 160
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 161 EQAVEAAHEMLLDNKFGDSGARVVIEEFLDGEEFSLFAFVNGDKFYIMPTAQDHKRAYDGDKGPNTGGMGAYAPVPHLPQ 240
Cdd:COG0151 160 EEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 241 SVVDTAVDTIVKPVLEGMIKEGRPYTGVLYAGLILTADGPKVIEFNSRFGDPETQIILPRLTSDFAQNITDILEGK--EP 318
Cdd:COG0151 240 ELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRldEV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 319 AITWtDKGVTLGVVVASNGYPLAYEKGVK---LPAKTEGDIITYYAGAKFaENGQdLLSNGGRVYMLVTTADTVKDGQNI 395
Cdd:COG0151 320 ELEW-DDRAAVCVVLASGGYPGSYEKGDVitgLEEAEAEGVKVFHAGTAL-EDGK-LVTNGGRVLGVTALGDTLEEARER 396
|
410 420
....*....|....*....|....*
gi 548304838 396 IYNELNKQNTEGLFYRNDIGSKANK 420
Cdd:COG0151 397 AYEAVEKIRFEGMFYRRDIGWRALK 421
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-418 |
9.82e-179 |
|
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: 504.92 E-value: 9.82e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 1 MKLLVVGSGGREHAIAKKLLESKDVEQVFVAPGNDG-MTLDGLDLINIGISEHSKLIDFAKANDIAWTFIGPDDALAAGI 79
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGtARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 80 VDDFNAAGLKAFGPTKAAAELEWSKDFAKEIMVKYDVPTAAYGTFSDFEEAKAYIEEKGAPIVVKADGLALGKGVVVAET 159
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 160 VEQAVEAAHEMLlDNKFGDSGARVVIEEFLDGEEFSLFAFVNGDKFYIMPTAQDHKRAYDGDKGPNTGGMGAYAPVPHLP 239
Cdd:TIGR00877 161 NEEAIKAVEDIL-EQKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 240 QSVVDTAVDTIVKPVLEGMIKEGRPYTGVLYAGLILTADGPKVIEFNSRFGDPETQIILPRLTSDFAQNITDILEGK-EP 318
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKlDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 319 AITWTDKGVTLGVVVASNGYPLAYEKGVK---LPAKTEGDIITYYAGAKfAENGQdLLSNGGRVYMLVTTADTVKDGQNI 395
Cdd:TIGR00877 320 VELRFDNRAAVTVVLASEGYPEDYRKGDPitgEPLAEAEGVKVFHAGTK-ADNGK-LVTNGGRVLAVTALGKTLEEARER 397
|
410 420
....*....|....*....|...
gi 548304838 396 IYNELNKQNTEGLFYRNDIGSKA 418
Cdd:TIGR00877 398 AYEAVEYIKFEGMFYRKDIGFRA 420
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-418 |
3.98e-141 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 409.90 E-value: 3.98e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 4 LVVGSGGREHAIAKKLLESKDVEQVFVAPGNDGMTLDGlDLINIG---ISEHSKLIDFAKANDIAWTFIGPDDALAAGIV 80
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSG-DATCVPdldISDSAAVISFCRKWGVGLVVVGPEAPLVAGLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 81 DDFNAAGLKAFGPTKAAAELEWSKDFAKEIMVKYDVPTAAYGTFSDFEEAKAYIEEKGAPIVVKADGLALGKGVVVAETV 160
Cdd:PLN02257 80 DDLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 161 EQAVEAAHEMLLDNKFGDSGARVVIEEFLDGEEFSLFAFVNGDKFYIMPTAQDHKRAYDGDKGPNTGGMGAYAPVPHLPQ 240
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 241 SVVDTAVDTIVKPVLEGMIKEGRPYTGVLYAGLILTADG--PKVIEFNSRFGDPETQIILPRLTSDFAQNITDILEGK-- 316
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGEls 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 317 EPAITWTDkGVTLGVVVASNGYPLAYEKGVKLPAKTEGDIIT-----YYAGAKFAENGqDLLSNGGRVYMLVTTADTVKD 391
Cdd:PLN02257 320 GVSLTWSP-DSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVApgvkvFHAGTALDSDG-NVVAAGGRVLGVTAKGKDIAE 397
|
410 420
....*....|....*....|....*..
gi 548304838 392 GQNIIYNELNKQNTEGLFYRNDIGSKA 418
Cdd:PLN02257 398 ARARAYDAVDQIDWPGGFFRRDIGWRA 424
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
103-294 |
1.03e-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: 308.06 E-value: 1.03e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 103 SKDFAKEIMVKYDVPTAAYGTFSDFEEAKAYIEEKGAPI-VVKADGLALGKGVVVAETVEQAVEAAHEMLLDNKFGDSGA 181
Cdd:pfam01071 2 SKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 182 RVVIEEFLDGEEFSLFAFVNGDKFYIMPTAQDHKRAYDGDKGPNTGGMGAYAPVPHLPQSVVDTAVDTIVKPVLEGMIKE 261
Cdd:pfam01071 82 TVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRKE 161
|
170 180 190
....*....|....*....|....*....|...
gi 548304838 262 GRPYTGVLYAGLILTADGPKVIEFNSRFGDPET 294
Cdd:pfam01071 162 GIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-101 |
2.06e-44 |
|
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: 149.81 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 1 MKLLVVGSGGREHAIAKKLLESKDVEQVFVAPGNDGMTLDGlDLINIGISEHSKLIDFAKANDIAWTFIGPDDALAAGIV 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLA-ECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIV 79
|
90 100
....*....|....*....|...
gi 548304838 81 DDF--NAAGLKAFGPTKAAAELE 101
Cdd:pfam02844 80 DALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
328-417 |
2.05e-22 |
|
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: 90.58 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 328 TLGVVVASNGYPLAYEKGVKLPAKTEGDIITYYAGAKFaeNGQDLLSNGGRVYMLVTTADTVKDGQNIIYNELNKQNTEG 407
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEAGVKVFHAGTKL--KDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFEG 78
|
90
....*....|
gi 548304838 408 LFYRNDIGSK 417
Cdd:pfam02843 79 MFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
75-290 |
1.32e-19 |
|
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: 87.62 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 75 LAAGIVDDFNAAGLKAfgptkAAAELEWSKDFAKEIMVKYDVPTAAYGTFSDFEEAKAYIEEKGAPIVVKADGLALGKGV 154
Cdd:COG0439 31 TAAELAEELGLPGPSP-----EAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 155 VVAETVEQAVEAAHEMLLDNKFGDSGARVVIEEFLDGEEFSLFAFVNGDKFYIMPTAQDHKraydgdKGPNTGGMGAYAP 234
Cdd:COG0439 106 RVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKHQ------KPPYFVELGHEAP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 548304838 235 VPhLPQSVVDTAVDTIVKpVLEGM-IKEgrpytGVLYAGLILTADG-PKVIEFNSRFG 290
Cdd:COG0439 180 SP-LPEELRAEIGELVAR-ALRALgYRR-----GAFHTEFLLTPDGePYLIEINARLG 230
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
104-319 |
7.51e-10 |
|
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: 59.57 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 104 KDFAKEIMVKYDVPTAAYGTFSDFEEAKAYIEEKGAPIVVK-ADGlALGKGVVVAETVEQAveaahEMLLDNKFGDSGAR 182
Cdd:COG0189 97 KLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKpLDG-SGGRGVFLVEDEDAL-----ESILEALTELGSEP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 183 VVIEEFL---DGEEFSLFaFVNGDKFYIMptaqdhkrAYDGDKGP---NTGGMGAYAPVPhLPQSVVDTAVDtiVKPVLe 256
Cdd:COG0189 171 VLVQEFIpeeDGRDIRVL-VVGGEPVAAI--------RRIPAEGEfrtNLARGGRAEPVE-LTDEERELALR--AAPAL- 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548304838 257 gmikegrpytGVLYAG--LILTADGPKVIEFNSRFGDPEtqiiLPRLT-SDFAQNITDILEGKEPA 319
Cdd:COG0189 238 ----------GLDFAGvdLIEDDDGPLVLEVNVTPGFRG----LERATgVDIAEAIADYLEARAAR 289
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
102-209 |
9.60e-08 |
|
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: 53.19 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 102 WSKDFAKEIMVKYDVPTAAYGTFS--DFEEAKAYIEEKGAPIVVKAdgLALG--KGVVVAETVEQAVEAAHEMLldnKFG 177
Cdd:COG1181 94 MDKALTKRVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKP--AREGssVGVSKVKNAEELAAALEEAF---KYD 168
|
90 100 110
....*....|....*....|....*....|..
gi 548304838 178 DsgaRVVIEEFLDGEEFSLfAFVNGDKFYIMP 209
Cdd:COG1181 169 D---KVLVEEFIDGREVTV-GVLGNGGPRALP 196
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
109-290 |
1.39e-06 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 49.93 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 109 EIMVKYDVPTAAYGTFSDFEEAKAYIEEKGAPIVVK-ADGLA-------LGKGVVVAETVEQAVEAAHEMLldnkfgDSG 180
Cdd:COG3919 123 ELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKpADSVGydelsfpGKKKVFYVDDREELLALLRRIA------AAG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 181 ARVVIEEFL---DGEEFSLFAFVNGDKFYIMPTAQDHKRAYdgdkgPNTGGMGAYApvphlpQSVVDTAVDTIVKPVLEG 257
Cdd:COG3919 197 YELIVQEYIpgdDGEMRGLTAYVDRDGEVVATFTGRKLRHY-----PPAGGNSAAR------ESVDDPELEEAARRLLEA 265
|
170 180 190
....*....|....*....|....*....|....*
gi 548304838 258 MikegrPYTGVLYAGLILTA-DG-PKVIEFNSRFG 290
Cdd:COG3919 266 L-----GYHGFANVEFKRDPrDGeYKLIEINPRFW 295
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
86-189 |
1.43e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 50.37 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 86 AGLKAFGPTKAAAELEWSKDFAKEIMVKYDVPTAAyGT---FSDFEEAKAYIEEKGAPIVVKADGLALGKGVVVA---ET 159
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLP-GTeegIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVyseEE 176
|
90 100 110
....*....|....*....|....*....|
gi 548304838 160 VEQAVEAAHEMlLDNKFGDSgaRVVIEEFL 189
Cdd:PRK08654 177 LEDAIESTQSI-AQSAFGDS--TVFIEKYL 203
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
107-171 |
3.47e-06 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 48.93 E-value: 3.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 107 AKEIMVKYDVPTAAYGTFSDFEEAKAYIEE-KGAPIVVKADGLALGK----GVVVAETVEQAVEAAHEML 171
Cdd:PRK00696 8 AKELFAKYGVPVPRGIVATTPEEAVEAAEElGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQIL 77
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
107-171 |
3.78e-06 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 47.26 E-value: 3.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 107 AKEIMVKYDVPTAAYGTFSDFEEAKAYIEEKGAP-IVVKADGLALGK----GVVVAETVEQAVEAAHEML 171
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKvYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEML 76
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
104-191 |
7.81e-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: 46.53 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 104 KDFAKEIMVKYDVPTA--AYGTFSDFEEAKAYIEEKGAPIVVKADGLALGKGVVVAETVEQAVEAAHEMLLDNKFGDSGA 181
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVpgTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90
....*....|
gi 548304838 182 RVVIEEFLDG 191
Cdd:pfam02786 82 QVLVEKSLKG 91
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
104-190 |
8.16e-06 |
|
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: 47.38 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 104 KDFAKEImvkyDVPTAAYGTFSDFEEAKAYIEEKGAPIVVKA-----DglalGKGVVVAETVEQAVEAAHEMlldnkfgd 178
Cdd:COG0026 94 KAFLAEL----GIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL-------- 157
|
90
....*....|..
gi 548304838 179 SGARVVIEEFLD 190
Cdd:COG0026 158 GGGPCILEEFVP 169
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
134-292 |
9.82e-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: 45.45 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 134 IEEKGAPIVVK-ADGLAlGKGVVVAEtveqaveaahemlLDNKFGDSGARVVIEEFLDGEEFSLFAFVNGDKFYIMPTaq 212
Cdd:pfam02655 27 LLREEKKYVVKpRDGCG-GEGVRKVE-------------NGREDEAFIENVLVQEFIEGEPLSVSLLSDGEKALPLSV-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 213 dhKRAYDGDKGPNTGGMGAYAPVPH-LPQSVVDTAVDTIVKpvLEGMikegRPYTGVlyaGLILTADGPKVIEFNSRFGD 291
Cdd:pfam02655 91 --NRQYIDNGGSGFVYAGNVTPSRTeLKEEIIELAEEVVEC--LPGL----RGYVGV---DLVLKDNEPYVIEVNPRITT 159
|
.
gi 548304838 292 P 292
Cdd:pfam02655 160 S 160
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
50-288 |
1.12e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 47.33 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 50 SEHSKLIDFAKAND----IAWTFIGPD--DALAAGIVDDFnaaglkAFGPTKAAAELEwskdfaKEIMVK----YDVPTA 119
Cdd:PRK07206 57 GDIDDLVEFLRKLGpeaiIAGAESGVElaDRLAEILTPQY------SNDPALSSARRN------KAEMINalaeAGLPAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 120 AYGTFSDFEEAKAYIEE---KGAPIVVKADGLALGKGVVVAETvEQAVEAAHEMLLD--NKFGDSGARVVIEEFLDGEEF 194
Cdd:PRK07206 125 RQINTADWEEAEAWLREnglIDRPVVIKPLESAGSDGVFICPA-KGDWKHAFNAILGkaNKLGLVNETVLVQEYLIGTEY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 195 SLFAFVNGDKFYIMPTAQDHKRaydgdkgPNTGGMGAYAPVPHLPQS--VVDTAVDtIVKPVLEGM-IKEGRPYTGVlya 271
Cdd:PRK07206 204 VVNFVSLDGNHLVTEIVRYHKT-------SLNSGSTVYDYDEFLDYSepEYQELVD-YTKQALDALgIKNGPAHAEV--- 272
|
250
....*....|....*..
gi 548304838 272 glILTADGPKVIEFNSR 288
Cdd:PRK07206 273 --MLTADGPRLIEIGAR 287
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
107-171 |
1.17e-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: 46.97 E-value: 1.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 107 AKEIMVKYDVPTAAYGTFSDFEEAKAYIEE-KGAPIVVKADGLALGK----GVVVAETVEQAVEAAHEML 171
Cdd:COG0045 8 AKELLAKYGVPVPRGIVATTPEEAVAAAEElGGPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAAEEIL 77
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
87-190 |
1.31e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 47.05 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 87 GLKAFGPTKAAAELEWSKDFAKEIMVKYDVPT--AAYGTFSDFEEAKAYIEEKGAPIVVKADGLALGKGVVVAET---VE 161
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVipGSDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDesdLE 180
|
90 100
....*....|....*....|....*....
gi 548304838 162 QAVEAAHEMLLdNKFGDsgARVVIEEFLD 190
Cdd:PRK08462 181 NLYLAAESEAL-SAFGD--GTMYMEKFIN 206
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
104-204 |
2.15e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 46.69 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 104 KDFAKEIMVKYDVPTAAYGTFSDFEEAKAYIEEKGAPIVVK-ADGlALGKGVVVAETVEQAVEAAHEMLldNKFGDSgar 182
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKpLDG-NHGRGVTVNITTREEIEAAYAVA--SKESSD--- 288
|
90 100
....*....|....*....|..
gi 548304838 183 VVIEEFLDGEEFSLfaFVNGDK 204
Cdd:PRK14016 289 VIVERYIPGKDHRL--LVVGGK 308
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
104-195 |
3.26e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 45.49 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 104 KDFAKEIMVKYDVPTAAYGTFSDFEEAKAYIEEKGAPIVVK--ADGLALGkgvVVAETVEQAVEAAHEmlLDNKFGDsga 181
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKpaREGSSVG---VSKVKEEDELQAALE--LAFKYDD--- 170
|
90
....*....|....
gi 548304838 182 RVVIEEFLDGEEFS 195
Cdd:PRK01372 171 EVLVEKYIKGRELT 184
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
116-190 |
7.94e-05 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 44.74 E-value: 7.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548304838 116 VPTAAYGTFSDFEEAKAYIEEKGAPIVVKADGLALGKGVVVAETVEQaVEAAHEMLLDNKFGDSGaRVVIEEFLD 190
Cdd:PRK09288 127 LPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPED-IEKAWEYAQEGGRGGAG-RVIVEEFID 199
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-190 |
1.05e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 44.41 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 85 AAGLKAFGPTKAAAELEWSKDFAKEIMVKYDVPT--AAYGTFSDFEEAKAYIEEKGAPIVVKADGLALGKGVVVAETVEQ 162
Cdd:PRK08591 97 DSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVvpGSDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAE 176
|
90 100 110
....*....|....*....|....*....|
gi 548304838 163 AVEAAHEMLLDNK--FGDSGarVVIEEFLD 190
Cdd:PRK08591 177 LEKAFSMARAEAKaaFGNPG--VYMEKYLE 204
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
116-279 |
2.17e-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: 41.47 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 116 VPTAAYGTFSDFEEAKAYIEEKGAPIVVKADGLAL-GKGVVVA---ETVEQAVEAAhemlldnkfgdSGARVVIEEFLDG 191
Cdd:pfam02222 5 LPTPRFMAAESLEELIEAGQELGYPCVVKARRGGYdGKGQYVVrseADLPQAWEEL-----------GDGPVIVEEFVPF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 192 E-EFSLFA--FVNGdKFYIMPTAQDHKRayDGDKGPNtggmgaYAPVPHlPQSVVDTAVDtIVKPVLEGMikegrPYTGV 268
Cdd:pfam02222 74 DrELSVLVvrSVDG-ETAFYPVVETIQE--DGICRLS------VAPARV-PQAIQAEAQD-IAKRLVDEL-----GGVGV 137
|
170
....*....|.
gi 548304838 269 LYAGLILTADG 279
Cdd:pfam02222 138 FGVELFVTEDG 148
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
107-197 |
5.27e-04 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 42.22 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 107 AKEIMVKYDVPTAAYGTFSDFEEAKAYIEE-KGAPIVVKADGLALGKGVVVAETV------EQAVEAAHEMlldnkfgDS 179
Cdd:PRK02471 492 TKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISIFKEPasledyEKALEIAFRE-------DS 564
|
90
....*....|....*...
gi 548304838 180 gaRVVIEEFLDGEEFSLF 197
Cdd:PRK02471 565 --SVLVEEFIVGTEYRFF 580
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
86-190 |
8.38e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 41.55 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 86 AGLKAFGPTKAAAELEWSKDFAKEIMVKYDVPTAAYGTFS--DFEEAKAYIEEKGAPIVVKADGLALGKGVVVAETvEQA 163
Cdd:PRK06111 98 EGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNleDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVET-EQE 176
|
90 100 110
....*....|....*....|....*....|...
gi 548304838 164 VEAAHEMlldNK------FGDsgARVVIEEFLD 190
Cdd:PRK06111 177 LTKAFES---NKkraanfFGN--GEMYIEKYIE 204
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
68-189 |
8.53e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 41.28 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 68 FIGPDDALAAGIvddfNAAGLKAFGPTKAAAELEWSKDFAKEIMVKYDVPT--AAYGTFSDFEEAKAYIEEKGAPIVVKA 145
Cdd:PRK12833 87 FLSENAAFAEAV----EAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTvpGSDGVVASLDAALEVAARIGYPLMIKA 162
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 548304838 146 DGLALGKGVVVAetvEQAVEAAHEMLLDNK-----FGDSGarVVIEEFL 189
Cdd:PRK12833 163 AAGGGGRGIRVA---HDAAQLAAELPLAQReaqaaFGDGG--VYLERFI 206
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
39-190 |
1.12e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 40.85 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 39 LDGLDLINIG---ISEHSKLIDFAKANDIawTFIGPDdalaagivddfnaaglkafgptKAAAELEWSKDFAKEIMVKYD 115
Cdd:PRK05586 72 LTGAQAIHPGfgfLSENSKFAKMCKECNI--VFIGPD----------------------SETIELMGNKSNAREIMIKAG 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548304838 116 VPT--AAYGTFSDFEEAKAYIEEKGAPIVVKADGLALGKGVVVAETVEQAVEAAHEMLLDNK--FGDSgaRVVIEEFLD 190
Cdd:PRK05586 128 VPVvpGSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKaaFGDD--SMYIEKFIE 204
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
104-196 |
1.81e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 40.14 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 104 KDFAKEImvkyDVPTAAYGTFSDFEEAKAYIEEKGAPIVVKA-----DglalGKGVVVAETVEQAVEAAHEMlldnkfgd 178
Cdd:PRK06019 105 KQFLDKL----GIPVAPFAVVDSAEDLEAALADLGLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWALL-------- 168
|
90
....*....|....*....
gi 548304838 179 SGARVVIEEFLDGE-EFSL 196
Cdd:PRK06019 169 GSVPCILEEFVPFErEVSV 187
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
56-190 |
4.04e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 39.68 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548304838 56 IDFAKA---NDIawTFIGPDdalaagivddfnAAGLKAFGpTKAAAelewskdfaKEIMVKYDVPT--AAYGTFSDFEEA 130
Cdd:COG1038 92 PEFARAceeAGI--TFIGPS------------PEVLEMLG-DKVAA---------RAAAIEAGVPVipGTEGPVDDLEEA 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548304838 131 KAYIEEKGAPIVVKAdglALGKG------VVVAETVEQAVEAA-HEMLldNKFGDsgARVVIEEFLD 190
Cdd:COG1038 148 LAFAEEIGYPVMLKA---AAGGGgrgmrvVRSEEELEEAFESArREAK--AAFGD--DEVFLEKYIE 207
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
138-201 |
5.05e-03 |
|
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: 37.65 E-value: 5.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548304838 138 GAPIVVKADGLALGKGVVVAETVEQAVEAAHEMLLD--------NKFGDSGARVVIEEFLDGEEFSLFAFVN 201
Cdd:pfam13535 2 PYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEieqwkemyPEAVVDGGSFLVEEYIEGEEFAVDAYFD 73
|
|
| |
