|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-428 |
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: 741.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 1 MKILVIGGGGREHALAWKLAQSPKATKVFVAPGNGGTGLAGgKLQNLPITDVVKLREWAQVEGVALTVVGPEAPLAAGVV 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLA-ECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 81 DEFRAHGLKVFGPTKAAAQLESSKAFSKAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPIVIKADGLAAGKGVVVAMTL 160
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 161 QEAHDAVDFMLVDNKYGvqhnEGGARVVIEEFLAGEEASFIVLCDGKNVVAMATSQDHKRLKDNDEGPNTGGMGAYSPAP 240
Cdd:COG0151 160 EEALAAVDDMLADGKFG----DAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 241 VVTADVHARAMREIILPTIRGMEKDGIPFTGFLYAGLMIDGNGhPKTLEFNTRMGDPETQPIMMRLKSDLVDVMQAAVDG 320
Cdd:COG0151 236 VVTEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 321 KLDQVELEWDRRTALGVVMAAAGYPEDPRKGDAITGLP-AEVDDAVVFHAGTQLNEAGVpVTSGGRVLCVTVLADSVRQA 399
Cdd:COG0151 315 RLDEVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEeAEAEGVKVFHAGTALEDGKL-VTNGGRVLGVTALGDTLEEA 393
|
410 420
....*....|....*....|....*....
gi 759660256 400 QTRVYDVTRGIHFDGMQYRRDIGFRAIKG 428
Cdd:COG0151 394 RERAYEAVEKIRFEGMFYRRDIGWRALKR 422
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-427 |
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: 566.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 1 MKILVIGGGGREHALAWKLAQSPKATKVFVAPG-NGGTGLAGGKLQNLPITDVVKLREWAQVEGVALTVVGPEAPLAAGV 79
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGnAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 80 VDEFRAHGLKVFGPTKAAAQLESSKAFSKAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPIVIKADGLAAGKGVVVAMT 159
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 160 LQEAHDAVDFMLVDNkygvqHNEGGARVVIEEFLAGEEASFIVLCDGKNVVAMATSQDHKRLKDNDEGPNTGGMGAYSPA 239
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-----FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 240 PVVTADVHARAMREIILPTIRGMEKDGIPFTGFLYAGLMIDGNGhPKTLEFNTRMGDPETQPIMMRLKSDLVDVMQAAVD 319
Cdd:TIGR00877 236 PVFTEEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 320 GKLDQVELEWDRRTALGVVMAAAGYPEDPRKGDAITGLP-AEVDDAVVFHAGTQLnEAGVPVTSGGRVLCVTVLADSVRQ 398
Cdd:TIGR00877 315 GKLDEVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPlAEAEGVKVFHAGTKA-DNGKLVTNGGRVLAVTALGKTLEE 393
|
410 420
....*....|....*....|....*....
gi 759660256 399 AQTRVYDVTRGIHFDGMQYRRDIGFRAIK 427
Cdd:TIGR00877 394 ARERAYEAVEYIKFEGMFYRKDIGFRALE 422
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-427 |
1.06e-176 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 500.42 E-value: 1.06e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 4 LVIGGGGREHALAWKLAQSPKATKVFVAP--GNGGTGLAGGKLQNLPITDVVKLREWAQVEGVALTVVGPEAPLAAGVVD 81
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPgnAGIATSGDATCVPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 82 EFRAHGLKVFGPTKAAAQLESSKAFSKAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPIVIKADGLAAGKGVVVAMTLQ 161
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 162 EAHDAVDFMLVDNKYGvqhnEGGARVVIEEFLAGEEASFIVLCDGKNVVAMATSQDHKRLKDNDEGPNTGGMGAYSPAPV 241
Cdd:PLN02257 161 EAYEAVDSMLVKGAFG----SAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 242 VTADVHARAMREIILPTIRGMEKDGIPFTGFLYAGLMIDG-NGHPKTLEFNTRMGDPETQPIMMRLKSDLVDVMQAAVDG 320
Cdd:PLN02257 237 LTPELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKkSGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 321 KLDQVELEWDRRTALGVVMAAAGYPEDPRKGDAITGLPA--EVDDAV-VFHAGTQLNEAGVPVTSGGRVLCVTVLADSVR 397
Cdd:PLN02257 317 ELSGVSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEaeAVAPGVkVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIA 396
|
410 420 430
....*....|....*....|....*....|
gi 759660256 398 QAQTRVYDVTRGIHFDGMQYRRDIGFRAIK 427
Cdd:PLN02257 397 EARARAYDAVDQIDWPGGFFRRDIGWRAVA 426
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
102-299 |
3.12e-94 |
|
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: 281.48 E-value: 3.12e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 102 SSKAFSKAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPI-VIKADGLAAGKGVVVAMTLQEAHDAVDFMLVDNKYGvqh 180
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 181 nEGGARVVIEEFLAGEEASFIVLCDGKNVVAMATSQDHKRLKDNDEGPNTGGMGAYSPAPVVTADVHARAMREIILPTIR 260
Cdd:pfam01071 78 -EAGETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVD 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 759660256 261 GMEKDGIPFTGFLYAGLMIDGNGhPKTLEFNTRMGDPET 299
Cdd:pfam01071 157 GLRKEGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-101 |
2.15e-43 |
|
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: 147.12 E-value: 2.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 1 MKILVIGGGGREHALAWKLAQSPKATKVFVAPgNGGTGLAGGKLQNLPITDVVKLREWAQVEGVALTVVGPEAPLAAGVV 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAP-GNGGTAQLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIV 79
|
90 100
....*....|....*....|...
gi 759660256 81 DEF--RAHGLKVFGPTKAAAQLE 101
Cdd:pfam02844 80 DALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
334-424 |
4.08e-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: 132.96 E-value: 4.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 334 ALGVVMAAAGYPEDPRKGDAITGLPAEvdDAVVFHAGTQLNEAGVpVTSGGRVLCVTVLADSVRQAQTRVYDVTRGIHFD 413
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA--GVKVFHAGTKLKDGKL-VTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFE 77
|
90
....*....|.
gi 759660256 414 GMQYRRDIGFR 424
Cdd:pfam02843 78 GMFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
55-295 |
3.14e-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: 86.85 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 55 LREWAQVEGVA--LTVVGPEAPLAAGVVDEFRahglkVFGPTKAAAQLESSKAFSKAFMRRHGIPTADYDTFTDPVAAHA 132
Cdd:COG0439 9 AAELARETGIDavLSESEFAVETAAELAEELG-----LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 133 FVERLGAPIVIKADGLAAGKGVVVAMTLQEAHDAVDFMLVDNKYGvqhnEGGARVVIEEFLAGEEASFIVLCDGKNVVAM 212
Cdd:COG0439 84 FAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAG----SPNGEVLVEEFLEGREYSVEGLVRDGEVVVC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 213 ATSQDHKrlkdndEGPNTGGMGAYSPAPvVTADVHARaMREIilpTIRGMEKDGIPFtGFLYAGLMIDGNGHPKTLEFNT 292
Cdd:COG0439 160 SITRKHQ------KPPYFVELGHEAPSP-LPEELRAE-IGEL---VARALRALGYRR-GAFHTEFLLTPDGEPYLIEINA 227
|
...
gi 759660256 293 RMG 295
Cdd:COG0439 228 RLG 230
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
76-295 |
3.21e-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: 63.81 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 76 AAGVVDEFRAHGLKVFGPTkAAAQLESSKAFSKAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPIVIK-ADGlAAGKGV 154
Cdd:COG0189 70 GLALLRQLEAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKpLDG-SGGRGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 155 VVAMTLQEAHDAVDFMLvdnkygvqhNEGGARVVIEEFLAGEEASF--IVLCDGKNVVAMatsqdhKRLKDNDEGP-NTG 231
Cdd:COG0189 148 FLVEDEDALESILEALT---------ELGSEPVLVQEFIPEEDGRDirVLVVGGEPVAAI------RRIPAEGEFRtNLA 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759660256 232 GMGAYSPAPvVTADVHARAMReiILPTIrgmekdgipftGFLYAGL-MIDGNGHPKTLEFNTRMG 295
Cdd:COG0189 213 RGGRAEPVE-LTDEERELALR--AAPAL-----------GLDFAGVdLIEDDDGPLVLEVNVTPG 263
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
93-202 |
3.08e-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: 58.16 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 93 PTKAAAQLESSKAFS---------------KAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPIVIKA-----DglaaGK 152
Cdd:COG0026 64 PAEALEALEAEVPVRpgpealeiaqdrlleKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GK 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 759660256 153 GVVVAMTLQEAHDAVDFMlvdnkygvqhneGGARVVIEEFLAGE-EASFIV 202
Cdd:COG0026 140 GQVVIKSAADLEAAWAAL------------GGGPCILEEFVPFErELSVIV 178
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
104-212 |
1.73e-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: 55.50 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 104 KAFSKAFMRRHGIPTADYDTFT--DPVAAHAFVERLGAPIVIKADGLAAGKGVVVAMTLQEAHDAVDFMLvdnKYgvqhn 181
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAF---KY----- 167
|
90 100 110
....*....|....*....|....*....|.
gi 759660256 182 egGARVVIEEFLAGEEASFIVLcDGKNVVAM 212
Cdd:COG1181 168 --DDKVLVEEFIDGREVTVGVL-GNGGPRAL 195
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
48-210 |
4.12e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 49.20 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 48 PIT--DVVKLREWAQVEGVaLTVVGPEAPLAagVVDEFRAHGLKVFGPT-KAAAQLESSKAFsKAFMRRHGIPTADYDTF 124
Cdd:PRK12815 616 PLTleDVLNVAEAENIKGV-IVQFGGQTAIN--LAKGLEEAGLTILGTSpDTIDRLEDRDRF-YQLLDELGLPHVPGLTA 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 125 TDPVAAHAFVERLGAPIVIKADGLAAGKGVVV-----AMT--LQEAHDAVDFMLVDnkygvqhneggarvvieEFLAGEE 197
Cdd:PRK12815 692 TDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVvydepALEayLAENASQLYPILID-----------------QFIDGKE 754
|
170
....*....|...
gi 759660256 198 ASFIVLCDGKNVV 210
Cdd:PRK12815 755 YEVDAISDGEDVT 767
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
108-202 |
7.80e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 47.84 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 108 KAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPIVIKA-----DglaaGKGVVVAMTLQEAHDAVDFMlvdnkygvqhne 182
Cdd:PRK06019 105 KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWALL------------ 168
|
90 100
....*....|....*....|.
gi 759660256 183 GGARVVIEEFLAGE-EASFIV 202
Cdd:PRK06019 169 GSVPCILEEFVPFErEVSVIV 189
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
81-295 |
3.09e-05 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 45.69 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 81 DEFRAHgLKVFGPTKAAAQLESSKAFSKAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPIVIK-ADGLAA-------GK 152
Cdd:COG3919 96 DELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKpADSVGYdelsfpgKK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 153 GVVVAMTLQEAHDAVDFMLvdnkygvqhnEGGARVVIEEFL---AGEEASFIVLCDGK-NVVAMATsqdHKRLKdndEGP 228
Cdd:COG3919 175 KVFYVDDREELLALLRRIA----------AAGYELIVQEYIpgdDGEMRGLTAYVDRDgEVVATFT---GRKLR---HYP 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759660256 229 NTGGmgayspAPVVTADVHARAMREIILPTIRGMEkdgipFTGFLYAGLMIDG-NGHPKTLEFNTRMG 295
Cdd:COG3919 239 PAGG------NSAARESVDDPELEEAARRLLEALG-----YHGFANVEFKRDPrDGEYKLIEINPRFW 295
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
62-211 |
3.10e-05 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 45.65 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 62 EGVALTVVG--PEAPLAAGVVDEFRAHGLKVFGPTKAAAQLESSKAFSKAFMRRHGIPTAdyDTFT----DPVAAHAFVE 135
Cdd:PRK12767 68 EKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTP--KSYLpeslEDFKAALAKG 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759660256 136 RLGAPIVIKADGLAAGKGVVVAMTLQEAHDAVDFMlvdnkygvqhneggARVVIEEFLAGEEASFIVLCD-GKNVVA 211
Cdd:PRK12767 146 ELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYV--------------PNLIIQEFIEGQEYTVDVLCDlNGEVIS 208
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
75-210 |
4.37e-05 |
|
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: 45.64 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 75 LAAGVVDEFRAHGLKVFGpTKAAA--QLESSKAFsKAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPIVIKADGLAAGK 152
Cdd:COG0458 86 LAVELEEAGILEGVKILG-TSPDAidLAEDRELF-KELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVLGGR 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 153 GVVVAMTLQEAHDAVdfmlvdnKYGVQHNeGGARVVIEEFLAG-EEASFIVLCDGK-NVV 210
Cdd:COG0458 164 GMGIVYNEEELEEYL-------ERALKVS-PDHPVLIDESLLGaKEIEVDVVRDGEdNVI 215
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
83-163 |
1.01e-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: 43.87 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 83 FRAHGLKVFGPTKAAAqLESSKAFSKAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPIVIKADGLAAGKGVVVAMTLQE 162
Cdd:TIGR00768 69 LESLGVPVINSSDAIL-NAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQA 147
|
.
gi 759660256 163 A 163
Cdd:TIGR00768 148 A 148
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
48-293 |
1.02e-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: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 48 PIT--DVVKLREWAQVEGVALTVVGPeapLAAGVVDEFRAHGLKVFG-PTKAAAQLESSKAFSKaFMRRHGIPTADYDTF 124
Cdd:TIGR01369 615 PLTfeDVMNIIELEKPEGVIVQFGGQ---TPLNLAKALEEAGVPILGtSPESIDRAEDREKFSE-LLDELGIPQPKWKTA 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 125 TDPVAAHAFVERLGAPIVIKADGLAAGKGVVVAMTLQEAHDAVDFMLVDNKygvqhnegGARVVIEEFL-AGEEASFIVL 203
Cdd:TIGR01369 691 TSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSP--------EHPVLIDKYLeDAVEVDVDAV 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 204 CDGKNVVAMATSQDHKRlkdndEGPNTGGMGAYSPAPVVTADVHARaMREIILPTIRGMEkdgipftgflYAGLM----I 279
Cdd:TIGR01369 763 SDGEEVLIPGIMEHIEE-----AGVHSGDSTCVLPPQTLSAEIVDR-IKDIVRKIAKELN----------VKGLMniqfA 826
|
250
....*....|....
gi 759660256 280 DGNGHPKTLEFNTR 293
Cdd:TIGR01369 827 VKDGEVYVIEVNPR 840
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
86-294 |
1.25e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 44.20 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 86 HGLKVFGPTKAAAQLESSKAFSKAFMRRHGIPT--ADYDTFTDPVAAHAFVERLGAPIVIKADGLAAGKGVVVAMTLQEA 163
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVlpGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEEL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 164 HDAVDfmlvDNKYGVQHNEGGARVVIEEFLagEEASFI---VLCDGK-NVVAMA-----TSQDHKRLKDNdegpntggmg 234
Cdd:PRK08654 178 EDAIE----STQSIAQSAFGDSTVFIEKYL--EKPRHIeiqILADKHgNVIHLGdrecsIQRRHQKLIEE---------- 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759660256 235 aySPAPVVTADVHARaMREIilpTIRGMEKDGIPFTG---FLYAglmidgNGHPKTLEFNTRM 294
Cdd:PRK08654 242 --APSPIMTPELRER-MGEA---AVKAAKAINYENAGtveFLYS------NGNFYFLEMNTRL 292
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
112-192 |
1.73e-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: 41.86 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 112 RRHGIPTADYDTFTDPVAAHAFVERLGAPIVIKADGLA-AGKGVVVAMTLQEAHDAVDFMlvdnkygvqhneGGARVVIE 190
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEEL------------GDGPVIVE 68
|
..
gi 759660256 191 EF 192
Cdd:pfam02222 69 EF 70
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
102-318 |
2.36e-04 |
|
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: 41.72 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 102 SSKAFSKAFMRRHGIPTADYDTFTDPVAAHAFVER--LGAPIVIKADGLAAGKGVVVAMTLQEAHDAVDFMlvdnkygvq 179
Cdd:pfam08443 2 RDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQikRQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSAT--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 180 hnegGARVVIEEFL--AGEEASFIVLCDGKNVVAMatsqdHKRLKDNDEGPNTGGMGAYSPAPVvtadvhARAMREIILP 257
Cdd:pfam08443 73 ----NEQILVQEFIaeANNEDIRCLVVGDQVVGAL-----HRQSNEGDFRSNLHRGGVGEKYQL------SQEETELAIK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759660256 258 TIRGMEKDgipftgflYAGL-MIDGNGHPKTLEFNTrmgDPETQPIMMRLKSDLVDVMQAAV 318
Cdd:pfam08443 138 AAQAMQLD--------VAGVdLLRQKRGLLVCEVNS---SPGLEGIEKTLGINIAIKIIASI 188
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
104-197 |
2.59e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 42.79 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 104 KAFSKAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPIVIKadglAAGKGVVVAMTL-QEAHDAVDFMLVDNKYgvqhne 182
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK----PAREGSSVGVSKvKEEDELQAALELAFKY------ 168
|
90
....*....|....*
gi 759660256 183 gGARVVIEEFLAGEE 197
Cdd:PRK01372 169 -DDEVLVEKYIKGRE 182
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
84-156 |
3.80e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 42.42 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 84 RAHGLKVFGPTKAAAQLESSKAFSKAFMRRHGIPT--------ADYDtftdpvAAHAFVERLGAPIVIKADGLAAGKGVV 155
Cdd:PRK08462 98 SHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVipgsdgalKSYE------EAKKIAKEIGYPVILKAAAGGGGRGMR 171
|
.
gi 759660256 156 V 156
Cdd:PRK08462 172 V 172
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
110-211 |
4.26e-04 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 110 FMRRHGIPTADYDTFT-------DPVAAHAFVERLGAPIVIKADGLAAGKGVVVAMTLQEAHDAVDfmlvdnkYGVQHNE 182
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTradwklnPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIE-------EAFQYDE 73
|
90 100
....*....|....*....|....*....
gi 759660256 183 ggaRVVIEEFLAGEEASFIVLCDGKNVVA 211
Cdd:pfam07478 74 ---KVLVEEGIEGREIECAVLGNEDPEVS 99
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
84-162 |
4.52e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 42.48 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 84 RAHGLKVFGPTKAAAQLESSKAFSKAFMRRHGIPT---ADyDTFTDPVAAHAFVERLGAPIVIKADGLAAGKGVVVAMTL 160
Cdd:PRK08591 96 EDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVvpgSD-GPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTE 174
|
..
gi 759660256 161 QE 162
Cdd:PRK08591 175 AE 176
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
104-213 |
8.76e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 38.60 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759660256 104 KAFSKAFMRRHGIPTADYDTFTDPVAAHAFVERLGAPIVIK-ADGlAAGKGVVVAMTLQEAhdavdfmlVDNKYGVQHNE 182
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKpLDG-NHGRGVTVNITTREE--------IEAAYAVASKE 285
|
90 100 110
....*....|....*....|....*....|.
gi 759660256 183 GGArVVIEEFLAGEEasFIVLCDGKNVVAMA 213
Cdd:PRK14016 286 SSD-VIVERYIPGKD--HRLLVVGGKLVAAA 313
|
|
| |
