|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
98-531 |
0e+00 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 922.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 98 LVIGGGGREHALCHALKRSPSCDSVLCAPGNAGISSSGDATCVPDLDISDSLAVISFCQKWNVGLVVVGPEVPLVAGLAN 177
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 178 DLVKAGILTFGPSSQAAALEGSKNFMKNLCHKYNIPTAKYKTFSDASAAKEYIQEQGAPIVIKADGLAAGKGVTVAMELE 257
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 258 EAFEAVDSMLVKGVFGSAGCQVVVEEFLEGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTKE 337
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 338 LQDFVMESIIHPTVKGMAEEGCKFVGVLFAGLMIEKKSGLPKLIEFNVRFGDPECQVLMMRLESDLAKVLLAACKGELSG 417
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 418 VSLDWSKDSAMVVVMASNGYPGSYEKGSIIKNLEEAERVAPGVKVFHAGTGLDSEGNVVATGGRVLGVTAKGKDLEEARE 497
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVAPGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEARA 400
|
410 420 430
....*....|....*....|....*....|....
gi 15218286 498 RAYSAVQQINWPGGFFRHDIGWRALRQKQVATKE 531
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARLQVANKR 434
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
96-523 |
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: 763.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 96 NVLVIGGGGREHALCHALKRSPSCDSVLCAPGNAGISssGDATCVpDLDISDSLAVISFCQKWNVGLVVVGPEVPLVAGL 175
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTA--QLAECV-DIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 176 ANDLVKAGILTFGPSSQAAALEGSKNFMKNLCHKYNIPTAKYKTFSDASAAKEYIQEQGAPIVIKADGLAAGKGVTVAME 255
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 256 LEEAFEAVDSMLVKGVFGSAGCQVVVEEFLEGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLT 335
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 336 KELQDFVMESIIHPTVKGMAEEGCKFVGVLFAGLMIEKKsGlPKLIEFNVRFGDPECQVLMMRLESDLAKVLLAACKGEL 415
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITAD-G-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 416 SGVSLDWSKDSAMVVVMASNGYPGSYEKGSIIKNLEEAErvAPGVKVFHAGTGLDsEGNVVATGGRVLGVTAKGKDLEEA 495
Cdd:COG0151 317 DEVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAE--AEGVKVFHAGTALE-DGKLVTNGGRVLGVTALGDTLEEA 393
|
410 420
....*....|....*....|....*...
gi 15218286 496 RERAYSAVQQINWPGGFFRHDIGWRALR 523
Cdd:COG0151 394 RERAYEAVEKIRFEGMFYRRDIGWRALK 421
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
96-522 |
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: 581.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 96 NVLVIGGGGREHALCHALKRSPSCDSVLCAPGNAGISSSGDATCVpDLDISDSLAVISFCQKWNVGLVVVGPEVPLVAGL 175
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNV-AIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 176 ANDLVKAGILTFGPSSQAAALEGSKNFMKNLCHKYNIPTAKYKTFSDASAAKEYIQEQGAPIVIKADGLAAGKGVTVAME 255
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 256 LEEAFEAVDSMLVKGvFGSAGCQVVVEEFLEGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLT 335
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 336 KELQDFVMESIIHPTVKGMAEEGCKFVGVLFAGLMIEKKSglPKLIEFNVRFGDPECQVLMMRLESDLAKVLLAACKGEL 415
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG--PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 416 SGVSLDWSKDSAMVVVMASNGYPGSYEKGSIIKNLEEAErvAPGVKVFHAGTGLDsEGNVVATGGRVLGVTAKGKDLEEA 495
Cdd:TIGR00877 318 DEVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAE--AEGVKVFHAGTKAD-NGKLVTNGGRVLAVTALGKTLEEA 394
|
410 420
....*....|....*....|....*..
gi 15218286 496 RERAYSAVQQINWPGGFFRHDIGWRAL 522
Cdd:TIGR00877 395 RERAYEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
198-392 |
8.28e-115 |
|
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: 337.72 E-value: 8.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 198 GSKNFMKNLCHKYNIPTAKYKTFSDASAAKEYIQEQGAPI-VIKADGLAAGKGVTVAMELEEAFEAVDSMLVKGVFGSAG 276
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 277 CQVVVEEFLEGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTKELQDFVMESIIHPTVKGMAE 356
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 15218286 357 EGCKFVGVLFAGLMIEKKSglPKLIEFNVRFGDPEC 392
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDG--PKVLEFNCRFGDPET 194
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
427-520 |
1.20e-44 |
|
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: 152.22 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 427 AMVVVMASNGYPGSYEKGSIIKNLEEAervapGVKVFHAGTGLDsEGNVVATGGRVLGVTAKGKDLEEARERAYSAVQQI 506
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA-----GVKVFHAGTKLK-DGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKI 74
|
90
....*....|....
gi 15218286 507 NWPGGFFRHDIGWR 520
Cdd:pfam02843 75 DFEGMFYRKDIGTR 88
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
96-197 |
4.31e-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: 148.66 E-value: 4.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 96 NVLVIGGGGREHALCHALKRSPSCDSVLCAPGNAGISSsgDATCVPdLDISDSLAVISFCQKWNVGLVVVGPEVPLVAGL 175
Cdd:pfam02844 2 KVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQ--LAECVD-IDATDFEALVAFAKENNIDLVVVGPEAPLVAGI 78
|
90 100
....*....|....*....|....
gi 15218286 176 ANDLV--KAGILTFGPSSQAAALE 197
Cdd:pfam02844 79 VDALRerAAGIPVFGPSKAAAQLE 102
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
150-414 |
1.08e-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: 91.86 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 150 AVISFCQKWnvglvvvgpeVPLVAGLANDLvkaGIltFGPSSQAAALEGSKNFMKNLCHKYNIPTAKYKTFSDASAAKEY 229
Cdd:COG0439 20 AVLSESEFA----------VETAAELAEEL---GL--PGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 230 IQEQGAPIVIKADGLAAGKGVTVAMELEEAFEAVDSMLVKGVFGSAGCQVVVEEFLEGEEASFFALVDGENAIPLESAQD 309
Cdd:COG0439 85 AEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 310 HKrvgdgdTGPNTGGMGAYSPAPvLTKELQDFVMEsiihptvkgMAEEGCKFVGVLFAGLMIE---KKSGLPKLIEFNVR 386
Cdd:COG0439 165 HQ------KPPYFVELGHEAPSP-LPEELRAEIGE---------LVARALRALGYRRGAFHTEfllTPDGEPYLIEINAR 228
|
250 260
....*....|....*....|....*....
gi 15218286 387 F-GDPECQVLMMRLESDLAKVLLAACKGE 414
Cdd:COG0439 229 LgGEHIPPLTELATGVDLVREQIRLALGE 257
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
179-388 |
7.06e-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: 63.04 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 179 LVKAGILTFgPSSQAAALEGSKNFMKNLCHKYNIPTAKYKTFSDASAAKEYIQEQGAPIVIK-ADGlAAGKGVTVAMELE 257
Cdd:COG0189 77 LEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKpLDG-SGGRGVFLVEDED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 258 EAFEAVDSMlvkgvFGSAGCQVVVEEFLEGEEASFF--ALVDGEN--AIPLESAQDHKRVgdgdtgpNTGGMGAYSPAPv 333
Cdd:COG0189 155 ALESILEAL-----TELGSEPVLVQEFIPEEDGRDIrvLVVGGEPvaAIRRIPAEGEFRT-------NLARGGRAEPVE- 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15218286 334 LTKELQDfvmesiihptvkgMAEEGCKFVGVLFAGL-MIEKKSGlPKLIEFNVRFG 388
Cdd:COG0189 222 LTDEERE-------------LALRAAPALGLDFAGVdLIEDDDG-PLVLEVNVTPG 263
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
96-297 |
5.19e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 57.97 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 96 NVLVIGGGGReHALCHALKRSPSCDSVLCA---PGNAGISSSGDATCVPDLDISDSL-AVISFCQKWNVGLVVVG--PEV 169
Cdd:PRK12767 3 NILVTSAGRR-VQLVKALKKSLLKGRVIGAdisELAPALYFADKFYVVPKVTDPNYIdRLLDICKKEKIDLLIPLidPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 170 PLVAGLANDLVKAGILTFGPSSQAAALEGSKNFMKNLCHKYNIPTAKYKTFSDASAAKEYIQ--EQGAPIVIKADGLAAG 247
Cdd:PRK12767 82 PLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAkgELQFPLFVKPRDGSAS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15218286 248 KGVTVAM---ELEEAFEAVDsmlvkgvfgsagcQVVVEEFLEGEEASFFALVD 297
Cdd:PRK12767 162 IGVFKVNdkeELEFLLEYVP-------------NLIIQEFIEGQEYTVDVLCD 201
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
200-388 |
3.47e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 55.70 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 200 KNFMKNLCHKYNIPTAKYKTFSDASAAKEYIQEQGAPIVIK-ADGLAA-------GKGVTVAMELEEAFEAVDSMLvkgv 271
Cdd:COG3919 118 KERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKpADSVGYdelsfpgKKKVFYVDDREELLALLRRIA---- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 272 fgSAGCQVVVEEFLEG---EEASFFALVDGENAIPLESAQdHKRVGDgdtgPNTGGMGAYspapvltkelqdfvMESIIH 348
Cdd:COG3919 194 --AAGYELIVQEYIPGddgEMRGLTAYVDRDGEVVATFTG-RKLRHY----PPAGGNSAA--------------RESVDD 252
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15218286 349 PTVKGMAE---EGCKFVGVLFAGLMIEKKSGLPKLIEFNVRFG 388
Cdd:COG3919 253 PELEEAARrllEALGYHGFANVEFKRDPRDGEYKLIEINPRFW 295
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
173-286 |
8.60e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 54.60 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 173 AGLANDLVKAGILTFGPSSQAAALEGSKNFMKNLCHKYNIPT--AKYKTFSDASAAKEYIQEQGAPIVIKADGLAAGKGV 250
Cdd:PRK08654 89 PEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVlpGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGM 168
|
90 100 110
....*....|....*....|....*....|....*....
gi 15218286 251 TVAM---ELEEAFEAVDSMlVKGVFGSAgcQVVVEEFLE 286
Cdd:PRK08654 169 RVVYseeELEDAIESTQSI-AQSAFGDS--TVFIEKYLE 204
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
176-262 |
4.67e-06 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 49.04 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 176 ANDLVKAGILTFGPSSQAAALEGSKNFMKNLCHKYNIP----TAKYKTFSdASAAKEYIQEQGAPIVIKADGLAAGKGVT 251
Cdd:PRK08463 91 AKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPivpgTEKLNSES-MEEIKIFARKIGYPVILKASGGGGGRGIR 169
|
90
....*....|....
gi 15218286 252 VAM---ELEEAFEA 262
Cdd:PRK08463 170 VVHkeeDLENAFES 183
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
200-289 |
5.63e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 49.00 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 200 KNFMKNLCHKYNIPTAKYKTFSDASAAKEYIQEQGAPIVIKA-DGlAAGKGVTVAM----ELEEAFEAVDSmlvkgvFGS 274
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPlDG-NHGRGVTVNIttreEIEAAYAVASK------ESS 287
|
90
....*....|....*
gi 15218286 275 AgcqVVVEEFLEGEE 289
Cdd:PRK14016 288 D---VIVERYIPGKD 299
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
142-386 |
1.55e-05 |
|
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: 47.69 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 142 DLDISDSL--------AVISFCQKWNVGLVVV--GPEVPLvaGLANDLVKAGILTFGPSSQAA-ALEGSKNFMKnLCHKY 210
Cdd:TIGR01369 604 DYDTSDRLyfepltfeDVMNIIELEKPEGVIVqfGGQTPL--NLAKALEEAGVPILGTSPESIdRAEDREKFSE-LLDEL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 211 NIPTAKYKTFSDASAAKEYIQEQGAPIVIKADGLAAGKgvtvAMELEEAFEAVDSMLVKGVFGSAGCQVVVEEFLE-GEE 289
Cdd:TIGR01369 681 GIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGR----AMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEdAVE 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 290 ASFFALVDGENA-IP-----LESAQDHKrvgdGDTgpntggmGAYSPAPVLTKELQDfVMESIIHPTVKGMaeegcKFVG 363
Cdd:TIGR01369 757 VDVDAVSDGEEVlIPgimehIEEAGVHS----GDS-------TCVLPPQTLSAEIVD-RIKDIVRKIAKEL-----NVKG 819
|
250 260
....*....|....*....|...
gi 15218286 364 VLfaGLMIEKKSGLPKLIEFNVR 386
Cdd:TIGR01369 820 LM--NIQFAVKDGEVYVIEVNPR 840
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
200-285 |
2.12e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 46.61 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 200 KNFMKNLchkyNIPTAKYKTFSDASAAKEYIQEQGAPIVIKA-----DglaaGKGVTVAMELEEAFEAVDSMlvkgvfgs 274
Cdd:COG0026 94 KAFLAEL----GIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL-------- 157
|
90
....*....|.
gi 15218286 275 AGCQVVVEEFL 285
Cdd:COG0026 158 GGGPCILEEFV 168
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
173-304 |
5.19e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 45.90 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 173 AGLANDLVKAGILTFGPSSQAAALEGSKNFMKNLCHKYNIPT--AKYKTFSDASAAKEYIQEQGAPIVIKADGLAAGKGV 250
Cdd:PRK12833 92 AAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTvpGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGI 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15218286 251 TV---AMELEEAFEAVDSMlVKGVFGSAGcqVVVEEFLE-GEEASFFALVDGENAIPL 304
Cdd:PRK12833 172 RVahdAAQLAAELPLAQRE-AQAAFGDGG--VYLERFIArARHIEVQILGDGERVVHL 226
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
173-261 |
5.85e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 42.32 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 173 AGLANDLVKAGILTFGPSSQAAALEGSKNFMKNLCHKYNIPTAKYKTFS--DASAAKEYIQEQGAPIVIKADGLAAGKGV 250
Cdd:PRK06111 89 ASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNleDAEEAIAIARQIGYPVMLKASAGGGGIGM 168
|
90
....*....|....
gi 15218286 251 TVAM---ELEEAFE 261
Cdd:PRK06111 169 QLVEteqELTKAFE 182
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
211-299 |
7.85e-04 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 42.22 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 211 NIPTAKYKTFSDASAAKEYIQE-QGAPIVIKADGLAAGKGVTVAME----------LEEAFEAvDSmlvkgvfgsagcQV 279
Cdd:PRK02471 500 GFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISIFKEpasledyekaLEIAFRE-DS------------SV 566
|
90 100
....*....|....*....|
gi 15218286 280 VVEEFLEGEEASFFALvDGE 299
Cdd:PRK02471 567 LVEEFIVGTEYRFFVL-DGK 585
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
182-286 |
8.93e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 42.05 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 182 AGIlTF-GPSSQAAALEGSKNFMKNLCHKYNIPT--AKYKTFSDASAAKEYIQEQGAPIVIKADGLAAGKG---VTVAME 255
Cdd:PRK12999 102 AGI-TFiGPTAEVLRLLGDKVAARNAAIKAGVPVipGSEGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGmriVRSEEE 180
|
90 100 110
....*....|....*....|....*....|.
gi 15218286 256 LEEAFEAVDSMlVKGVFGSAgcQVVVEEFLE 286
Cdd:PRK12999 181 LEEAFERAKRE-AKAAFGND--EVYLEKYVE 208
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
209-284 |
9.09e-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: 40.31 E-value: 9.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218286 209 KYNIPTAKYKTFSDASAAKEYIQEQGAPIVIKADGLA-AGKGVTVAMELEEAFEAVDSMlvkgvfgsAGCQVVVEEF 284
Cdd:pfam02222 2 KLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEEL--------GDGPVIVEEF 70
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
91-339 |
1.15e-03 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 41.88 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 91 SEERVNVLVIGGG------GREHALC--HALKrspscdsvlcAPGNAGIS----SSGDATCVPDLDISDSL--------A 150
Cdd:PRK12815 552 SSEKKKVLILGSGpirigqGIEFDYSsvHAAF----------ALKKEGYEtimiNNNPETVSTDYDTADRLyfepltleD 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 151 VISFCQKWNVGLVVV--GPEVPLvaGLANDLVKAGILTFGPSSQAA-ALEGSKNFmKNLCHKYNIPTAKYKTFSDASAAK 227
Cdd:PRK12815 622 VLNVAEAENIKGVIVqfGGQTAI--NLAKGLEEAGLTILGTSPDTIdRLEDRDRF-YQLLDELGLPHVPGLTATDEEEAF 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 228 EYIQEQGAPIVIKADGLAAGKGVTVAM---ELEEAFEAVDSMLVkgvfgsagcQVVVEEFLEGEEASFFALVDGENA-IP 303
Cdd:PRK12815 699 AFAKRIGYPVLIRPSYVIGGQGMAVVYdepALEAYLAENASQLY---------PILIDQFIDGKEYEVDAISDGEDVtIP 769
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15218286 304 -----LESAQDHKrvgdGDTgpntggmGAYSPAPVLTKELQ 339
Cdd:PRK12815 770 giiehIEQAGVHS----GDS-------IAVLPPQSLSEEQQ 799
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
200-288 |
1.46e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 40.91 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 200 KNFMKNLchkyNIPTAKYKTFSDASAAKEYIQEQGAPIVIKA-----DglaaGKGVTVAMELEEAFEAVDSMlvkgvfgs 274
Cdd:PRK06019 105 KQFLDKL----GIPVAPFAVVDSAEDLEAALADLGLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWALL-------- 168
|
90
....*....|....*.
gi 15218286 275 AGCQVVVEEF--LEGE 288
Cdd:PRK06019 169 GSVPCILEEFvpFERE 184
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
200-289 |
1.61e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 40.48 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 200 KNFMKNLCHKYNIPTAKYKTFSDASAAKEYIQEQGAPIVIKadglAAGKGVTVAM-------ELEEAFEAVDSMlvkgvf 272
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK----PAREGSSVGVskvkeedELQAALELAFKY------ 168
|
90
....*....|....*..
gi 15218286 273 gsaGCQVVVEEFLEGEE 289
Cdd:PRK01372 169 ---DDEVLVEKYIKGRE 182
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
204-267 |
1.69e-03 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 40.84 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218286 204 KNLCHKYNIPTAKYKTFSDASAAKEYIQE-QGAPIVIKADGLAAGK----GVTVAMELEEAFEAVDSML 267
Cdd:PRK00696 9 KELFAKYGVPVPRGIVATTPEEAVEAAEElGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQIL 77
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
181-286 |
4.98e-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: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 181 KAGIlTF-GPSSQAAALEGSKNFMKNLCHKYNIPT--AKYKTFSDASAAKEYIQEQGAPIVIKAdglAAGKG------VT 251
Cdd:COG1038 100 EAGI-TFiGPSPEVLEMLGDKVAARAAAIEAGVPVipGTEGPVDDLEEALAFAEEIGYPVMLKA---AAGGGgrgmrvVR 175
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15218286 252 VAMELEEAF-----EAvdsmlvKGVFGSAgcQVVVEEFLE 286
Cdd:COG1038 176 SEEELEEAFesarrEA------KAAFGDD--EVFLEKYIE 207
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
185-286 |
7.99e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 38.63 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218286 185 LTF-GPSSQAAALEGSKNFMKNLCHKYNIPT--AKYKTFSDASAAKEYIQEQGAPIVIKADGLAAGKGVTVAM---ELEE 258
Cdd:PRK08591 100 FTFiGPSAETIRLMGDKVTAKATMKKAGVPVvpGSDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRteaELEK 179
|
90 100 110
....*....|....*....|....*....|...
gi 15218286 259 AF-----EAvdsmlvKGVFGSAGcqVVVEEFLE 286
Cdd:PRK08591 180 AFsmaraEA------KAAFGNPG--VYMEKYLE 204
|
|
| |
