|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-426 |
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: 805.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 1 MKVLVIGNGGREHALAWKAAQSPQVETVFVAPGNAGTALEPalQNVAIGVTDIPALLSFARNENIDLTIVGPEAPLVIGV 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLA--ECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 81 VDAFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMT 160
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 161 LEEAEAAVQDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGNADTGPNTGGMGAYSPAPVVT 240
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 241 DEVHQRTMDRIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPETQPIMLRMKSDLVDLCLAACEGKLN 320
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 321 EKTSEWDERASLGVVIAAGGYPGSYNTGDEIHGLPLEEIDGAKVFHAGTKLsDDDRVLTNGGRVLCATALGHTVAEAQKR 400
Cdd:COG0151 318 EVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTAL-EDGKLVTNGGRVLGVTALGDTLEEARER 396
|
410 420
....*....|....*....|....*.
gi 550713825 401 AYALMADIHWNGSFSRQDIGYRAIAR 426
Cdd:COG0151 397 AYEAVEKIRFEGMFYRRDIGWRALKR 422
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-424 |
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: 682.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 1 MKVLVIGNGGREHALAWKAAQSPQVETVFVAPGNAGTALEPALQNVAIGVTDIPALLSFARNENIDLTIVGPEAPLVIGV 80
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 81 VDAFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMT 160
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 161 LEEAEAAVQDMLAGNaFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGNADTGPNTGGMGAYSPAPVVT 240
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 241 DEVHQRTMDRIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPETQPIMLRMKSDLVDLCLAACEGKLN 320
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 321 EKTSEWDERASLGVVIAAGGYPGSYNTGDEIHGLPLEEIDGAKVFHAGTKlSDDDRVLTNGGRVLCATALGHTVAEAQKR 400
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTK-ADNGKLVTNGGRVLAVTALGKTLEEARER 397
|
410 420
....*....|....*....|....
gi 550713825 401 AYALMADIHWNGSFSRQDIGYRAI 424
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: 582.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 4 LVIGNGGREHALAWKAAQSPQVETVFVAPGNAGTALEPALQNVA-IGVTDIPALLSFARNENIDLTIVGPEAPLVIGVVD 82
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 83 AFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLE 162
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 163 EAEAAVQDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGNADTGPNTGGMGAYSPAPVVTDE 242
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 243 VHQRTMDRIIWPTVKGMAAEGNTYTGFLYAGLMIDKQ-GNPKVIEFNCRFGDPETQPIMLRMKSDLVDLCLAACEGKLNE 321
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKsGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 322 KTSEWDERASLGVVIAAGGYPGSYNTGDEIHGLPLEE--IDGAKVFHAGTKLSDDDRVLTNGGRVLCATALGHTVAEAQK 399
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEavAPGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEARA 400
|
410 420
....*....|....*....|....*....
gi 550713825 400 RAYALMADIHWNGSFSRQDIGYRAIAREQ 428
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARLQ 429
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
103-296 |
9.92e-110 |
|
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: 321.15 E-value: 9.92e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 103 GSKAFTKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPI-VIKADGLAAGKGVIVAMTLEEAEAAVQDMLAGNAFGDAG 181
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 182 HRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGNADTGPNTGGMGAYSPAPVVTDEVHQRTMDRIIWPTVKGMAA 261
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 550713825 262 EGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPET 296
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-102 |
3.56e-55 |
|
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: 177.93 E-value: 3.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 1 MKVLVIGNGGREHALAWKAAQSPQVETVFVAPGNAGTALEPalQNVAIGVTDIPALLSFARNENIDLTIVGPEAPLVIGV 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLA--ECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGI 78
|
90 100
....*....|....*....|....
gi 550713825 81 VDAF--RAAGLKIFGPTEGAAQLE 102
Cdd:pfam02844 79 VDALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
331-422 |
1.42e-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: 134.11 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 331 SLGVVIAAGGYPGSYNTGDEIHGLpleEIDGAKVFHAGTKLsDDDRVLTNGGRVLCATALGHTVAEAQKRAYALMADIHW 410
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGL---DEAGVKVFHAGTKL-KDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDF 76
|
90
....*....|..
gi 550713825 411 NGSFSRQDIGYR 422
Cdd:pfam02843 77 EGMFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
52-292 |
1.07e-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: 96.48 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 52 DIPALLS----FARNENIDlTIVGPEAPLVIGVvdAFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHNIPTAEYQNFTE 127
Cdd:COG0439 1 DIDAIIAaaaeLARETGID-AVLSESEFAVETA--AELAEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 128 VEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVQDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVL 207
Cdd:COG0439 78 PEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 208 PMATSQDHKrvgnadTGPNTGGMGAYSPAPvVTDEVHQRTMDRiiwpTVKGMAAEGNTYtGFLYAGLMIDKQGNPKVIEF 287
Cdd:COG0439 158 VCSITRKHQ------KPPYFVELGHEAPSP-LPEELRAEIGEL----VARALRALGYRR-GAFHTEFLLTPDGEPYLIEI 225
|
....*
gi 550713825 288 NCRFG 292
Cdd:COG0439 226 NARLG 230
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
1-206 |
4.24e-10 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 60.94 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 1 MKVLVIGNG--GREHALAwkaAQSPQVETVFVAPGNAGTALEPALQNVAIGVTDIPALLSFAR--------NENID---L 67
Cdd:PRK06019 3 KTIGIIGGGqlGRMLALA---AAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEqcdvityeFENVPaeaL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 68 TIVGPEAPLVIGVvDAFRAAGLKIfgpTEgaaqlegskaftKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKA- 146
Cdd:PRK06019 80 DALAARVPVPPGP-DALAIAQDRL---TE------------KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTr 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550713825 147 ----DglaaGKGVIVAMTLEEAEAAVQDMLAGNAfgdaghriVIEEFLDGE-EASFIVM--VDGEHV 206
Cdd:PRK06019 144 rggyD----GKGQWVIRSAEDLEAAWALLGSVPC--------ILEEFVPFErEVSVIVArgRDGEVV 198
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
79-288 |
1.17e-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: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 79 GVVDAFRAAGLKIFGPTEgAAQLEGSKAFTKDFLARHNIPTAEyqnfTEV----EPALAYLREKGAPIVIK-ADGlAAGK 153
Cdd:COG0189 72 ALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPP----TLVtrdpDDLRAFLEELGGPVVLKpLDG-SGGR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 154 GVIVAMTLEEAEAAVQDMlagnaFGDAGHRIVIEEFLDGEEASF--IVMVDGEHVLPMA-TSQDHKRVGNADTGpntggm 230
Cdd:COG0189 146 GVFLVEDEDALESILEAL-----TELGSEPVLVQEFIPEEDGRDirVLVVGGEPVAAIRrIPAEGEFRTNLARG------ 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 550713825 231 GAYSPAPvVTDEVHQrtmdriiwptvkgMAAEGNTYTGFLYAGL-MIDKQGNPKVIEFN 288
Cdd:COG0189 215 GRAEPVE-LTDEERE-------------LALRAAPALGLDFAGVdLIEDDDGPLVLEVN 259
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
105-209 |
5.55e-09 |
|
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: 57.04 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 105 KAFTKDFLARHNIPTAEYQNFTEVEPALAYLREK--GAPIVIKADGLAAGKGVIVAMTLEEAEAAVQDMLAGnafgdaGH 182
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEelGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90 100
....*....|....*....|....*...
gi 550713825 183 RIVIEEFLDGEEASFIVMVDGE-HVLPM 209
Cdd:COG1181 170 KVLVEEFIDGREVTVGVLGNGGpRALPP 197
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
109-206 |
6.04e-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: 57.39 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 109 KDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKA-----DglaaGKGVIVAMTLEEAEAAVQDMlagnafgdAGHR 183
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGP 161
|
90 100
....*....|....*....|....*.
gi 550713825 184 IVIEEFLDGE-EASFIVM--VDGEHV 206
Cdd:COG0026 162 CILEEFVPFErELSVIVArsPDGEVA 187
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-194 |
1.68e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 49.50 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 1 MKVLVIGnGGREHAL--AWKAAQSPQveTVFVA-PGNAGTALEPALQNVAI-GVTD---IPALLSFARNENIDLTIVG-- 71
Cdd:PRK12767 2 MNILVTS-AGRRVQLvkALKKSLLKG--RVIGAdISELAPALYFADKFYVVpKVTDpnyIDRLLDICKKEKIDLLIPLid 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 72 PEAPLVIGVVDAFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHNIPTAEYQNFTEVEPALAYLREK--GAPIVIKADGL 149
Cdd:PRK12767 79 PELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGelQFPLFVKPRDG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 550713825 150 AAGKGVIVAMTLEEAEAAVQDMLAgnafgdaghrIVIEEFLDGEE 194
Cdd:PRK12767 159 SASIGVFKVNDKEELEFLLEYVPN----------LIIQEFIEGQE 193
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
61-290 |
2.79e-06 |
|
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: 49.61 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 61 RNENIDLTIVGPEAPLVIGVVDAFRAAGLKIFG-PTEGAAQLEGSKAFTKdFLARHNIPTAEYQNFTEVEPALAYLREKG 139
Cdd:TIGR01369 626 ELEKPEGVIVQFGGQTPLNLAKALEEAGVPILGtSPESIDRAEDREKFSE-LLDELGIPQPKWKTATSVEEAVEFASEIG 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 140 APIVIKADGLAAGKGVIVAMTLEEAEAAVQDMLAGNafgdAGHRIVIEEFL-DGEEASFIVMVDGEHVLPMATSQdHkrV 218
Cdd:TIGR01369 705 YPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVS----PEHPVLIDKYLeDAVEVDVDAVSDGEEVLIPGIME-H--I 777
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 550713825 219 GNAdtGPNTGGMGAYSPAPVVTDEVHQRtMDRIiwptVKGMAAEGNtytgflYAGLM----IDKQGNPKVIEFNCR 290
Cdd:TIGR01369 778 EEA--GVHSGDSTCVLPPQTLSAEIVDR-IKDI----VRKIAKELN------VKGLMniqfAVKDGEVYVIEVNPR 840
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
57-207 |
6.80e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 48.43 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 57 LSFARNENIDLTIVGPEAPLVIGVVDAFRAAGLKIFGPT-EGAAQLEGSKAFTKdFLARHNIPTAEYQNFTEVEPALAYL 135
Cdd:PRK12815 623 LNVAEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSpDTIDRLEDRDRFYQ-LLDELGLPHVPGLTATDEEEAFAFA 701
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550713825 136 REKGAPIVIKADGLAAGKGVIVAmtleEAEAAVQDMLAGNAfgDAGHRIVIEEFLDGEEASFIVMVDGEHVL 207
Cdd:PRK12815 702 KRIGYPVLIRPSYVIGGQGMAVV----YDEPALEAYLAENA--SQLYPILIDQFIDGKEYEVDAISDGEDVT 767
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
82-207 |
1.75e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 46.67 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 82 DAFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHNIPTAEYQN--FTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAM 159
Cdd:PRK12833 96 EAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDgvVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAH 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 550713825 160 TLEE--AEAAVQDMLAGNAFGDAGhrIVIEEFLdgEEASFI---VMVDGEHVL 207
Cdd:PRK12833 176 DAAQlaAELPLAQREAQAAFGDGG--VYLERFI--ARARHIevqILGDGERVV 224
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
105-204 |
1.77e-05 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 47.23 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 105 KAFTKDFLARHNIPTAEYQNFTEVEPALAYLRE-KGAPIVIKADGLAAGKGVIV---AMTLEEAEAAVQdmlagNAFGDA 180
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISIfkePASLEDYEKALE-----IAFRED 563
|
90 100
....*....|....*....|....
gi 550713825 181 GHrIVIEEFLDGEEASFIVMvDGE 204
Cdd:PRK02471 564 SS-VLVEEFIVGTEYRFFVL-DGK 585
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
105-208 |
2.98e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 45.49 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 105 KAFTKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKadglAAGKGVIVAMTLEEAEAAVQDMLAGNA-FGDaghR 183
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK----PAREGSSVGVSKVKEEDELQAALELAFkYDD---E 171
|
90 100
....*....|....*....|....*
gi 550713825 184 IVIEEFLDGEEasFIVMVDGEHVLP 208
Cdd:PRK01372 172 VLVEKYIKGRE--LTVAVLGGKALP 194
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
109-191 |
4.54e-05 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 45.47 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 109 KDFLARHNIPTAEYQNFTEVEPALAYLRE-KGAPIVIKADGLAAGKG----VIVAMTLEEAEAAVQDML----AGNAFGD 179
Cdd:PRK00696 9 KELFAKYGVPVPRGIVATTPEEAVEAAEElGGGVWVVKAQVHAGGRGkaggVKLAKSPEEAREFAKQILgmtlVTHQTGP 88
|
90
....*....|....*
gi 550713825 180 AGH---RIVIEEFLD 191
Cdd:PRK00696 89 KGQpvnKVLVEEGAD 103
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
1-290 |
1.29e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 43.86 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 1 MKVLVIGNG---GREHALAWKAAQSPQVETVFVA--PGNAGTALEPALQNVAIGVTDIPALLSFARNENIDLTIVGPEAp 75
Cdd:PRK07206 2 MKKVVIVDPfssGKFLAPAFKKRGIEPIAVTSSCllDPYYYASFDTSDFIEVIINGDIDDLVEFLRKLGPEAIIAGAES- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 76 lviGVVDAFRAAglKIFGPTEGAAQLEGS----KAFTKDFLARHNIPTAEYQNFTEVEPALAYLRE---KGAPIVIKADG 148
Cdd:PRK07206 81 ---GVELADRLA--EILTPQYSNDPALSSarrnKAEMINALAEAGLPAARQINTADWEEAEAWLREnglIDRPVVIKPLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 149 LAAGKGVIVAMTLEEAEAAVQDMLAG-NAFGDAGHRIVIEEFLDGEE-ASFIVMVDGEHVLPMATSQDHKRVGNadtgpn 226
Cdd:PRK07206 156 SAGSDGVFICPAKGDWKHAFNAILGKaNKLGLVNETVLVQEYLIGTEyVVNFVSLDGNHLVTEIVRYHKTSLNS------ 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550713825 227 tgGMGAYSP---APVVTDEVHQrtmdriIWPTVKG-MAAEGNTYtGFLYAGLMIDKQGnPKVIEFNCR 290
Cdd:PRK07206 230 --GSTVYDYdefLDYSEPEYQE------LVDYTKQaLDALGIKN-GPAHAEVMLTADG-PRLIEIGAR 287
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
109-203 |
2.16e-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: 42.29 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 109 KDFLARHNIPTAEYQ--NFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVQDML--AGNAFGDagHRI 184
Cdd:pfam02786 6 KAAMKEAGVPTVPGTagPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALaeAPAAFGN--PQV 83
|
90 100
....*....|....*....|
gi 550713825 185 VIEEFLDG-EEASFIVMVDG 203
Cdd:pfam02786 84 LVEKSLKGpKHIEYQVLRDA 103
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
103-294 |
2.36e-04 |
|
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: 41.60 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 103 GSKAFTKDFLARHNIPTAEYQNFTEvepalayLREKGAPIVIK-ADGlAAGKGVIVAMTLEEAEAAVQDMLagnafgdag 181
Cdd:pfam02655 2 SDKLKTYKALKNAGVPTPETLQAEE-------LLREEKKYVVKpRDG-CGGEGVRKVENGREDEAFIENVL--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 182 hrivIEEFLDGEEASFIVMVDGEHVLPMATSQDHkrVGNA-DTGPNTGGMgaySPAPVVtdevhqrtMDRIIWPTVKGMA 260
Cdd:pfam02655 65 ----VQEFIEGEPLSVSLLSDGEKALPLSVNRQY--IDNGgSGFVYAGNV---TPSRTE--------LKEEIIELAEEVV 127
|
170 180 190
....*....|....*....|....*....|....
gi 550713825 261 AEGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDP 294
Cdd:pfam02655 128 ECLPGLRGYVGVDLVLKDNE-PYVIEVNPRITTS 160
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
109-191 |
3.29e-04 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 41.48 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 109 KDFLARHNIPTAEYQNFTEVEPALAYLREKGAP-IVIKADGLAAGKG----VIVAMTLEEAEAAVQDMLAGN----AFGD 179
Cdd:pfam08442 8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKvYVVKAQVLAGGRGkaggVKLAKSPEEAKEVAKEMLGKNlvtkQTGP 87
|
90
....*....|....*
gi 550713825 180 AGH---RIVIEEFLD 191
Cdd:pfam08442 88 DGQpvnKVLVEEALD 102
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
113-204 |
4.17e-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: 40.70 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 113 ARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLA-AGKGVIVAMTLEEAEAAVQDMLAGnafgdaghRIVIEEFLD 191
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEELGDG--------PVIVEEFVP 72
|
90
....*....|....*.
gi 550713825 192 GE-EASFIVM--VDGE 204
Cdd:pfam02222 73 FDrELSVLVVrsVDGE 88
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
1.11e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 40.94 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 85 RAAGLKIFGPTEGAAQLEGSKAFTKDFLARHNIPTAEYQN--FTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLE 162
Cdd:PRK08591 96 EDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDgpVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEA 175
|
90 100 110
....*....|....*....|....*....|..
gi 550713825 163 EAEAAVQdML---AGNAFGDAGhrIVIEEFLD 191
Cdd:PRK08591 176 ELEKAFS-MAraeAKAAFGNPG--VYMEKYLE 204
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
109-191 |
1.76e-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: 40.42 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 109 KDFLARHNIPTAEYQNFTEVEPALAYLRE-KGAPIVIKADGLAAGK----GVIVAMTLEEAEAAVQDML----AGNAFGD 179
Cdd:COG0045 9 KELLAKYGVPVPRGIVATTPEEAVAAAEElGGPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAAEEILgmtlVTHQTGP 88
|
90
....*....|....*
gi 550713825 180 AGH---RIVIEEFLD 191
Cdd:COG0045 89 KGKpvnKVLVEEGVD 103
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
4.33e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 39.24 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 85 RAAGLKIFGPTEGAAQLEGSKAFTKDFLARHNIPT--AEYQNFTEVEPALAYLREKGAPIVIKAdglAAGKGVIvAMTLE 162
Cdd:PRK06111 96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVvpGITTNLEDAEEAIAIARQIGYPVMLKA---SAGGGGI-GMQLV 171
|
90 100 110
....*....|....*....|....*....|....*
gi 550713825 163 EAEAAVQDMLAGN------AFGDAghRIVIEEFLD 191
Cdd:PRK06111 172 ETEQELTKAFESNkkraanFFGNG--EMYIEKYIE 204
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
105-194 |
5.30e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 38.98 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 105 KAFTKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKA-DGlAAGKGVIV-AMTLEEAEAAvqdMLAGNAFGDAgh 182
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPlDG-NHGRGVTVnITTREEIEAA---YAVASKESSD-- 288
|
90
....*....|..
gi 550713825 183 rIVIEEFLDGEE 194
Cdd:PRK14016 289 -VIVERYIPGKD 299
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
139-293 |
8.48e-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: 36.88 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 139 GAPIVIKADGLAAGKGVIVAMTLEEAEAAVQDMLA--------GNAFGDAGHRIVIEEFLDGEEASFIVMVD--GEHVLp 208
Cdd:pfam13535 2 PYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREeieqwkemYPEAVVDGGSFLVEEYIEGEEFAVDAYFDenGEPVI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 209 maTSQDHKRvgnadtgpntggmgaYSPAPVVTDEVHQrTMDRIIWPTVKGMA---AEGNTYTGF----LYAGLMIDKQGN 281
Cdd:pfam13535 81 --LNILKHD---------------FASSEDVSDRIYV-TSASIIRETQAAFTeflKRINALLGLknfpVHIELRVDEDGQ 142
|
170
....*....|...
gi 550713825 282 PKVIEFN-CRFGD 293
Cdd:pfam13535 143 IIPIEVNpLRFAG 155
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
79-202 |
9.09e-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: 38.44 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713825 79 GVVDAFraaGLKIFG-PTEGAAQLEGSKAFtKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIV 157
Cdd:TIGR01369 105 GVLEKY---GVEVLGtPVEAIKKAEDRELF-REAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGI 180
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 550713825 158 AMTLEEAEAavqdmLAGNAFGDAG-HRIVIEEFLDG-EEASFIVMVD 202
Cdd:TIGR01369 181 AYNREELKE-----IAERALSASPiNQVLVEKSLAGwKEIEYEVMRD 222
|
|
| |
