|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-422 |
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: 753.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 1 MKVMVVGSGGREHALAWKLARSPKVQVVYVAPGNGGTALDKRLQNVPITDPEVLAAFVEREGVHFTVVGPEAPLAAGIVD 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 81 LFRAKGLRIFGPTRAAAQLESSKDFAKAFMQRHGIPTAKYQTFGNAAEAHAYVDRGGAPIVIKADGLAAGKGVVVAMSLE 160
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 161 EAHGAIDMMLADNRLGDAGARVVIEEFLAGEEASFIVVCDGKDVVAMATSQDHKRLLDGDAGPNTGGMGAYSPAPVVTPT 240
Cdd:COG0151 161 EALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 241 LHARVLREIILPTIRGMEKDGIPYTGFLYAGLMIDAGGnPKTLEFNCRMGDPETQPIMSRMKTDLFDVLDRAIDGKLDGM 320
Cdd:COG0151 241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 321 ELEWDRRTALGVVMAAHGYPDTPRKGDVITGIPR-ETEDSVTFHAGTTLKDGVLTTNGGRVLCVVGLADTVKAAQRAAYG 399
Cdd:COG0151 320 ELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEaEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERAYE 399
|
410 420
....*....|....*....|...
gi 489355132 400 AAEQIQFDGAQYRKDIGHRAIRR 422
Cdd:COG0151 400 AVEKIRFEGMFYRRDIGWRALKR 422
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-420 |
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: 571.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 1 MKVMVVGSGGREHALAWKLARSPKVQVVYVAPGNGGTALDKRLQNVPI--TDPEVLAAFVEREGVHFTVVGPEAPLAAGI 78
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIeiTDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 79 VDLFRAKGLRIFGPTRAAAQLESSKDFAKAFMQRHGIPTAKYQTFGNAAEAHAYVDRGGAPIVIKADGLAAGKGVVVAMS 158
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 159 LEEAHGAIDMMLADNrLGDAGARVVIEEFLAGEEASFIVVCDGKDVVAMATSQDHKRLLDGDAGPNTGGMGAYSPAPVVT 238
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 239 PTLHARVLREIILPTIRGMEKDGIPYTGFLYAGLMIDAGGnPKTLEFNCRMGDPETQPIMSRMKTDLFDVLDRAIDGKLD 318
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 319 GMELEWDRRTALGVVMAAHGYPDTPRKGDVITGIPR-ETEDSVTFHAGTTLKDGVLTTNGGRVLCVVGLADTVKAAQRAA 397
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLaEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 489355132 398 YGAAEQIQFDGAQYRKDIGHRAI 420
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-422 |
1.83e-172 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 489.64 E-value: 1.83e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 4 MVVGSGGREHALAWKLARSPKVQVVYVAPGNGGTALDKRLQNVP---ITDPEVLAAFVEREGVHFTVVGPEAPLAAGIVD 80
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdldISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 81 LFRAKGLRIFGPTRAAAQLESSKDFAKAFMQRHGIPTAKYQTFGNAAEAHAYVDRGGAPIVIKADGLAAGKGVVVAMSLE 160
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 161 EAHGAIDMMLADNRLGDAGARVVIEEFLAGEEASFIVVCDGKDVVAMATSQDHKRLLDGDAGPNTGGMGAYSPAPVVTPT 240
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 241 LHARVLREIILPTIRGMEKDGIPYTGFLYAGLMIDA-GGNPKTLEFNCRMGDPETQPIMSRMKTDLFDVLDRAIDGKLDG 319
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKkSGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 320 MELEWDRRTALGVVMAAHGYPDTPRKGDVITGIPRETEDSVT---FHAGTTLK-DGVLTTNGGRVLCVVGLADTVKAAQR 395
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVAPGvkvFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEARA 400
|
410 420
....*....|....*....|....*..
gi 489355132 396 AAYGAAEQIQFDGAQYRKDIGHRAIRR 422
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVAR 427
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
101-294 |
2.07e-95 |
|
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: 284.56 E-value: 2.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 101 SSKDFAKAFMQRHGIPTAKYQTFGNAAEAHAYVDRGGAPI-VIKADGLAAGKGVVVAMSLEEAHGAIDMMLADNRLGDAG 179
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 180 ARVVIEEFLAGEEASFIVVCDGKDVVAMATSQDHKRLLDGDAGPNTGGMGAYSPAPVVTPTLHARVLREIILPTIRGMEK 259
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 489355132 260 DGIPYTGFLYAGLMIDAGGnPKTLEFNCRMGDPET 294
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-100 |
3.63e-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: 172.54 E-value: 3.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 1 MKVMVVGSGGREHALAWKLARSPKVQVVYVAPGNGGTALDKRLQNVPITDPEVLAAFVEREGVHFTVVGPEAPLAAGIVD 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80
|
90 100
....*....|....*....|..
gi 489355132 81 LF--RAKGLRIFGPTRAAAQLE 100
Cdd:pfam02844 81 ALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
329-418 |
5.59e-34 |
|
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: 121.79 E-value: 5.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 329 ALGVVMAAHGYPDTPRKGDVITGIprETEDSVTFHAGTTLKDGVLTTNGGRVLCVVGLADTVKAAQRAAYGAAEQIQFDG 408
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGL--DEAGVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFEG 78
|
90
....*....|
gi 489355132 409 AQYRKDIGHR 418
Cdd:pfam02843 79 MFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
84-290 |
8.73e-20 |
|
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: 88.39 E-value: 8.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 84 AKGLRIFGPTRAAAQLESSKDFAKAFMQRHGIPTAKYQTFGNAAEAHAYVDRGGAPIVIKADGLAAGKGVVVAMSLEEAH 163
Cdd:COG0439 36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 164 GAIDMMLADNRLGDAGARVVIEEFLAGEEASF-IVVCDGKdVVAMATSQDHKrlldgdAGPNTGGMGAYSPAPvVTPTLH 242
Cdd:COG0439 116 AALAEARAEAKAGSPNGEVLVEEFLEGREYSVeGLVRDGE-VVVCSITRKHQ------KPPYFVELGHEAPSP-LPEELR 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489355132 243 ARVLREiilpTIRGMEKDGIPYtGFLYAGLMIDAGGNPKTLEFNCRMG 290
Cdd:COG0439 188 AEIGEL----VARALRALGYRR-GAFHTEFLLTPDGEPYLIEINARLG 230
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
75-208 |
1.05e-09 |
|
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: 59.18 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 75 AAGIVDLFRAKGLRIFGPTRAAAQLeSSKDFAKAFMQRHGIPTAKYQTFGNAAEAHAYVDRGGAPIVIK-ADGlAAGKGV 153
Cdd:COG0189 70 GLALLRQLEAAGVPVVNDPEAIRRA-RDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKpLDG-SGGRGV 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489355132 154 VVAMSLEEAHGAIDMMLADNRlgdagARVVIEEFLAGEEASF--IVVCDGKDVVAMA 208
Cdd:COG0189 148 FLVEDEDALESILEALTELGS-----EPVLVQEFIPEEDGRDirVLVVGGEPVAAIR 199
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
107-198 |
3.03e-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: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 107 KAFMQRHGIPTAKYQTFGNAAEAHAYVDRGGAPIVIKA-----DglaaGKGVVVAMSLEEAHGAIDMMladnrlgdAGAR 181
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGP 161
|
90
....*....|....*...
gi 489355132 182 VVIEEFLAGE-EASFIVV 198
Cdd:COG0026 162 CILEEFVPFErELSVIVA 179
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
103-192 |
5.57e-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: 53.96 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 103 KDFAKAFMQRHGIPTAKYQTF--GNAAEAHAYVDRGGAPIVIKADGLAAGKGVVVAMSLEEAHGAIDMMLAdnrlgdAGA 180
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLrrGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFK------YDD 169
|
90
....*....|..
gi 489355132 181 RVVIEEFLAGEE 192
Cdd:COG1181 170 KVLVEEFIDGRE 181
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
47-205 |
5.75e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 51.89 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 47 PITDPEVLAaFVEREGVHFTVVGPEAPLAAGIVDLFRAKGLRIFGPTRAAAQLESSKDFAKAFMQRHGIPTAKYQTFGNA 126
Cdd:PRK12815 616 PLTLEDVLN-VAEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 127 AEAHAYVDRGGAPIVIKADGLAAGKGVVVAMS-------LEEAHGAIDMMLadnrlgdagarvvIEEFLAGEEASFIVVC 199
Cdd:PRK12815 695 EEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDepaleayLAENASQLYPIL-------------IDQFIDGKEYEVDAIS 761
|
....*.
gi 489355132 200 DGKDVV 205
Cdd:PRK12815 762 DGEDVT 767
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
47-290 |
1.50e-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: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 47 PITDPEVLAAFVEREG--VHFTVVGPEAPLAAGIVDLFRA---KGLRIFGPTRAAAQLESSKDFAKAFMQRHGIPTAKYQ 121
Cdd:COG3919 57 PGDDPEAFVDALLELAerHGPDVLIPTGDEYVELLSRHRDeleEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 122 TFGNAAEAHAYVDRGGAPIVIK-ADGLAA-------GKGVVVAMSLEEAHGAIDmmladnRLGDAGARVVIEEFL---AG 190
Cdd:COG3919 137 VLDSADDLDALAEDLGFPVVVKpADSVGYdelsfpgKKKVFYVDDREELLALLR------RIAAAGYELIVQEYIpgdDG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 191 EEASFIVVCDGK-DVVAMATsqdHKRLLdgdAGPNTGGmgayspAPVVTPTLHARVLREIILPTIRGMEkdgipYTGFLY 269
Cdd:COG3919 211 EMRGLTAYVDRDgEVVATFT---GRKLR---HYPPAGG------NSAARESVDDPELEEAARRLLEALG-----YHGFAN 273
|
250 260
....*....|....*....|..
gi 489355132 270 AGLMIDA-GGNPKTLEFNCRMG 290
Cdd:COG3919 274 VEFKRDPrDGEYKLIEINPRFW 295
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
107-198 |
1.51e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 49.77 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 107 KAFMQRHGIPTAKYQTFGNAAEAHAYVDRGGAPIVIKA-----DglaaGKGVVVAMSLEEAHGAIDMMladnrlgdAGAR 181
Cdd:PRK06019 105 KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWALL--------GSVP 172
|
90
....*....|....*...
gi 489355132 182 VVIEEFLAGE-EASFIVV 198
Cdd:PRK06019 173 CILEEFVPFErEVSVIVA 190
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-200 |
1.20e-05 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 46.80 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 1 MKVMVVGSGGReHAL--AWKLARSPkVQVVYVAPGNGGTAL---DKRLQNVPITDPEVLAAFVE---REGVHFTVVG--P 70
Cdd:PRK12767 2 MNILVTSAGRR-VQLvkALKKSLLK-GRVIGADISELAPALyfaDKFYVVPKVTDPNYIDRLLDickKEKIDLLIPLidP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 71 EAPLAAGIVDLFRAKGLRIFGPTRAAAQLESSKDFAKAFMQRHGIPTAKYQTFGNAAEAHAYVDRG--GAPIVIKADGLA 148
Cdd:PRK12767 80 ELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGelQFPLFVKPRDGS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489355132 149 AGKGVVVAMSLEEAhgaidmmladNRLGDAGARVVIEEFLAGEEASFIVVCD 200
Cdd:PRK12767 160 ASIGVFKVNDKEEL----------EFLLEYVPNLIIQEFIEGQEYTVDVLCD 201
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
111-198 |
2.56e-05 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 44.55 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 111 QRHGIPTAKYQTFGNAAEAHAYVDRGGAPIVIKADGLA-AGKGVVVAMSLEEAHGAIDmmLADNRlgdagaRVVIEEFLA 189
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWE--ELGDG------PVIVEEFVP 72
|
90
....*....|
gi 489355132 190 GE-EASFIVV 198
Cdd:pfam02222 73 FDrELSVLVV 82
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
103-192 |
8.54e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 44.33 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 103 KDFAKAFMQRHGIPTAKYQTFGNAAEAHAYVDRGGAPIVIKadglAAGKGVVVAMSL-EEAHGAIDMMLADNRLGDagaR 181
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK----PAREGSSVGVSKvKEEDELQAALELAFKYDD---E 171
|
90
....*....|.
gi 489355132 182 VVIEEFLAGEE 192
Cdd:PRK01372 172 VLVEKYIKGRE 182
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
2-187 |
2.91e-04 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 42.82 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 2 KVMVVGSG--GREHALAWK-----------LARSPKVQVV---YVapgnggtaldkrlqnVPITDPEVLAAFVEREGVHF 65
Cdd:PRK09288 14 RVMLLGSGelGKEVAIEAQrlgveviavdrYANAPAMQVAhrsHV---------------IDMLDGDALRAVIEREKPDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 66 TVVGPEAPLAAGIVDLfRAKGLRIFgPTRAAAQLEsskdfakafMQRHGI----------PTAKYQTFGNAAEAHAYVDR 135
Cdd:PRK09288 79 IVPEIEAIATDALVEL-EKEGFNVV-PTARATRLT---------MNREGIrrlaaeelglPTSPYRFADSLEELRAAVEE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489355132 136 GGAPIVIKADGLAAGKGVVVAMSLEEAHGAIDMMLADNRlGDAGaRVVIEEF 187
Cdd:PRK09288 148 IGYPCVVKPVMSSSGKGQSVVRSPEDIEKAWEYAQEGGR-GGAG-RVIVEEF 197
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
103-203 |
3.25e-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: 41.52 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 103 KDFAKAFMQRHGIPTAKYQ--TFGNAAEAHAYVDRGGAPIVIKADGLAAGKGVVVAMSLEEAHGAIDMMLADNRLGDAGA 180
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTagPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100
....*....|....*....|....
gi 489355132 181 RVVIEEFLAG-EEASFIVVCDGKD 203
Cdd:pfam02786 82 QVLVEKSLKGpKHIEYQVLRDAHG 105
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
47-318 |
4.10e-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: 42.68 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 47 PITdPEVLAAFVEREGVHFTVVGPEAPLAAGIVDLFRAKGLRIFG-PTRAAAQLESSKDFAKaFMQRHGIPTAKYQTFGN 125
Cdd:TIGR01369 615 PLT-FEDVMNIIELEKPEGVIVQFGGQTPLNLAKALEEAGVPILGtSPESIDRAEDREKFSE-LLDELGIPQPKWKTATS 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 126 AAEAHAYVDRGGAPIVIKADGLAAGKGVVVAMSLEEAHGAIDMMLADNRlgdaGARVVIEEFL-AGEEASFIVVCDGKDV 204
Cdd:TIGR01369 693 VEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSP----EHPVLIDKYLeDAVEVDVDAVSDGEEV 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 205 VAMATSQDHKRlldgdAGPNTGGMGAYSPApvvtPTLHARVLREIILPTIRGMEKDGIpytgflyAGLM----IDAGGNP 280
Cdd:TIGR01369 769 LIPGIMEHIEE-----AGVHSGDSTCVLPP----QTLSAEIVDRIKDIVRKIAKELNV-------KGLMniqfAVKDGEV 832
|
250 260 270
....*....|....*....|....*....|....*....
gi 489355132 281 KTLEFNCRMGdpETQPIMSR-MKTDLFDVLDRAIDGKLD 318
Cdd:TIGR01369 833 YVIEVNPRAS--RTVPFVSKaTGVPLAKLAVRVMLGKKL 869
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
106-206 |
6.65e-04 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 41.84 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 106 AKAFMQRHGIPTAKYQTFGNAAEAHAYVDR-GGAPIVIKADGLAAGKGVVV---AMSLEEAHGAIDMMLADNrlgdagAR 181
Cdd:PRK02471 492 TKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISIfkePASLEDYEKALEIAFRED------SS 565
|
90 100
....*....|....*....|....*
gi 489355132 182 VVIEEFLAGEEASFIVVcDGKdVVA 206
Cdd:PRK02471 566 VLVEEFIVGTEYRFFVL-DGK-VEA 588
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
103-208 |
2.28e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 40.14 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 103 KDFAKAFMQRHGIPTAKYQTFGNAAEAHAYVDRGGAPIVIKA-DGlAAGKGVVVAMSLEEahgaiDMMLADNRLGDAGAR 181
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPlDG-NHGRGVTVNITTRE-----EIEAAYAVASKESSD 288
|
90 100
....*....|....*....|....*..
gi 489355132 182 VVIEEFLAGEEASFIVVcDGKdVVAMA 208
Cdd:PRK14016 289 VIVERYIPGKDHRLLVV-GGK-LVAAA 313
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
79-155 |
2.50e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 40.11 E-value: 2.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489355132 79 VDLFRAKGLRIFGPTRAAAQLESSKDFAKAFMQRHGIPTAKYQT--FGNAAEAHAYVDRGGAPIVIKADGLAAGKGVVV 155
Cdd:PRK08462 94 VEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDgaLKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRV 172
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
85-244 |
3.52e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 39.58 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 85 KGLRIFGPTRAAAQLESSKDFAKAFMQRHGIPT--AKYQTFGNAAEAHAYVDRGGAPIVIKADGLAAGKGVVVAMSLEEA 162
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVlpGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEEL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 163 HGAID--MMLADNRLGDagARVVIEEFLagEEASFI---VVCDGK-DVVAMA-----TSQDHKRLLDgdagpntggmgaY 231
Cdd:PRK08654 178 EDAIEstQSIAQSAFGD--STVFIEKYL--EKPRHIeiqILADKHgNVIHLGdrecsIQRRHQKLIE------------E 241
|
170
....*....|...
gi 489355132 232 SPAPVVTPTLHAR 244
Cdd:PRK08654 242 APSPIMTPELRER 254
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
106-186 |
3.73e-03 |
|
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: 39.26 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489355132 106 AKAFMQRHGIPTAKYQTFGNAAEAHAYVDR-GGAPIVIKADGLAAGK----GVVVAMSLEEAHGA----IDMMLADNRLG 176
Cdd:COG0045 8 AKELLAKYGVPVPRGIVATTPEEAVAAAEElGGPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAaeeiLGMTLVTHQTG 87
|
90
....*....|...
gi 489355132 177 DAG---ARVVIEE 186
Cdd:COG0045 88 PKGkpvNKVLVEE 100
|
|
| |
