|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
335-955 |
0e+00 |
|
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: 1073.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 335 ERPKKVLILGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERPT 414
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 415 GVLLTFGGQTALNCGVQLKRTGVFDKYNVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSAAVASVDGAISAAKEIGY 494
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 495 PVMARAAFSLGGLGSGFANTEEELRALAHQALSHS--DQLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLGIHT 572
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 573 GESIVVAPSQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALNPYSEDFYIIEVNARLSRSSALASKATGYPLAYVAAK 652
Cdd:TIGR01369 244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 653 LALQVPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQKAFRMVDENV 732
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 733 NGFDPNIKKVDENE-----LKEPTDKRMFVLAAALKEGYSVEKLYQMTKIDRWFLEKLKNITDYYSILEGV----ISAEM 803
Cdd:TIGR01369 404 TGFDLPDREVEPDEdlwraLKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVkltdLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 804 LRNAKQIGFSDKQIAAAIKSTEIAVRKQRQENNITPFVKQIDTVAAEWPASTNYLYLTYNGTTHDVEFVTGY-VMVLGSG 882
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKkVLVLGSG 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1095161062 883 VYRIGSSVEFDWCAVSCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNMEQPEGVVLS 955
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
338-954 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 965.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 338 KKVLILGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERPTGVL 417
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 418 LTFGGQTALNCGVQLKRTGVFDKYNVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSAAVASVDGAISAAKEIGYPVM 497
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 498 ARAAFSLGGLGSGFANTEEELRALAHQALSHS--DQLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLGIHTGES 575
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 576 IVVAPSQTLSNREYYMLRNTAIKVIRHFGIV-GECNIQYALNPYSEDFYIIEVNARLSRSSALASKATGYPLAYVAAKLA 654
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 655 LQVPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQKAFRMVDENVNG 734
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 735 FDP-NIKKVDENE----LKEPTDKRMFVLAAALKEGYSVEKLYQMTKIDRWFLEKLKNITDYYSILEG---VISAEMLRN 806
Cdd:PRK05294 408 LDEdLFEEESLEElreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEnglPLDAELLRE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 807 AKQIGFSDKQIAAAIKSTEIAVRKQRQENNITPFVKQIDTVAAEWPASTNYLYLTYNGTTHDVefVTGY--VMVLGSGVY 884
Cdd:PRK05294 488 AKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESN--PSDRkkVLVLGSGPN 565
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 885 RIGSSVEFDWCAVSCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNMEQPEGVVL 954
Cdd:PRK05294 566 RIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIV 635
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
343-881 |
0e+00 |
|
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: 621.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 343 LGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERPTGVLLTFGG 422
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 423 QTALNCGVQLKRTGVFDkyNVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSAAVASVDGAISAAKEIGYPVMARAAF 502
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 503 SLGGLGSGFANTEEELRALAHQALSHSD--QLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLGIHTGESIVVAP 580
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPdhPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 581 SQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALNpySEDFYIIEVNARLSRSSALASKATGYPLAYVAAKLALQVPLP 660
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 661 IIKNSvTGvttacFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQKAFRMVDENVNG--FDPN 738
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 739 IKKVDENELKE--PTDKRMFVLAAALKEGYSVEKLYQMTKIDRWFLEKLKNITDYYSILEGVISAEM-LRNAKQIGFSDK 815
Cdd:COG0458 391 VADDDKEEALLlaRRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINtLLGAKSLGDSDG 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1095161062 816 QIAAAIKSTEIAVRKQRQENNITPFVKQIDTVAAEWPASTNYLYLTYNGTTHDVEFVTGYVMVLGS 881
Cdd:COG0458 471 IIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-308 |
4.36e-141 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 424.87 E-value: 4.36e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVPDEsdfdehglprWFESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:PRK12564 38 GYQEILTDPSYAGQIVTFTYPLIGNYGVNRE----------DFESDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 81 SGICGIDTRALTRRLRD-GVTLGRIIQGT------------IADPNTRNLVAEVSIKGPKIYNAKGD---FTIVAIDCGL 144
Cdd:PRK12564 108 PGISGIDTRALTRKLREkGAMKGVIATEDfdaeellekaraFPGLLGLDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 145 KYNQLRCFIKRNAKVILVPWDHPIDPT---QYDGLFISNGPGDPEMCRKTVENLKNVI---KPIFGICLGHQLLSTAVGC 218
Cdd:PRK12564 188 KRNILRELAERGCRVTVVPATTTAEEIlalNPDGVFLSNGPGDPAALDYAIEMIRELLekkIPIFGICLGHQLLALALGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 219 KTYKMSYGNRGHNLPCTHTDTGRCFMTSQNHGFAVDVKSLPENWKELFINENDKTNEGIIHESLPYLSVQFHPEHTAGPT 298
Cdd:PRK12564 268 KTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPH 347
|
330
....*....|
gi 1095161062 299 DLECLFDIFV 308
Cdd:PRK12564 348 DSAYLFDEFV 357
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-313 |
6.23e-138 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 416.64 E-value: 6.23e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVPDEsdfdehglprWFESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:TIGR01368 34 GYQEILTDPSYKGQIVVFTYPLIGNYGVNDE----------DAESKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 81 SGICGIDTRALTRRLRD-GVTLGRIIQGTI----------ADPNTR--NLVAEVSIKGPKIYNAKGD--FTIVAIDCGLK 145
Cdd:TIGR01368 104 PGIYGVDTRALVKKIREkGTMKGVISTEDSndeelvekarVSPDITgiNLVAEVSTKEPYTWGQRGGkgKRVVVIDFGVK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 146 YNQLRCFIKRNAKVILVPWDHP---IDPTQYDGLFISNGPGDPEMCRKTVENLKNVI--KPIFGICLGHQLLSTAVGCKT 220
Cdd:TIGR01368 184 RNILRRLVKRGCEVTVVPYDTDaeeIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLekIPIFGICLGHQLLALAFGAKT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 221 YKMSYGNRGHNLPCTHTDTGRCFMTSQNHGFAVDVKSLPEN-WKELFINENDKTNEGIIHESLPYLSVQFHPEHTAGPTD 299
Cdd:TIGR01368 264 YKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGdLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHD 343
|
330
....*....|....
gi 1095161062 300 LECLFDIFVSSVKA 313
Cdd:TIGR01368 344 TEYLFDEFIDLMKK 357
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-312 |
1.46e-136 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 413.26 E-value: 1.46e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVPDEsdfdehglprWFESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:COG0505 38 GYQEILTDPSYAGQIVTFTYPHIGNYGVNDE----------DFESDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 81 SGICGIDTRALTRRLRD-GVTLGRIIQGTI------------ADPNTRNLVAEVSIKGPKIYNAKGD--FTIVAIDCGLK 145
Cdd:COG0505 108 PGISGIDTRALTRHLREkGAMKGVISTGDLdieellekaraaPGMEGLDLVKEVSTKEPYEWTEAPGagFHVVALDFGVK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 146 YNQLRCFIKRNAKVILVPWDHPID------PtqyDGLFISNGPGDPEMCRKTVENLKNVI---KPIFGICLGHQLLSTAV 216
Cdd:COG0505 188 RNILRELAERGCRVTVVPATTSAEeilalnP---DGVFLSNGPGDPAALDYAIETIRELLgkgIPIFGICLGHQLLALAL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 217 GCKTYKMSYGNRGHNLPCTHTDTGRCFMTSQNHGFAVDVKSLPE-NWKELFINENDKTNEGIIHESLPYLSVQFHPEHTA 295
Cdd:COG0505 265 GAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASP 344
|
330
....*....|....*..
gi 1095161062 296 GPTDLECLFDIFVSSVK 312
Cdd:COG0505 345 GPHDSAYLFDRFIELME 361
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
458-660 |
1.85e-99 |
|
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: 310.39 E-value: 1.85e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 458 DRKIFAEKINAIGEKVAPSAAVA--SVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEELRALAHQALSHS------ 529
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 530 DQLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLgiHTGESIVVAPSQTLSNREYYMLRNTAIKVIRHFGIVGEC 609
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1095161062 610 NIQYALNPYSEDFYIIEVNARLSRSSALASKATGYPLAYVAAKLALQVPLP 660
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
137-308 |
2.48e-98 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 305.96 E-value: 2.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 137 IVAIDCGLKYNQLRCFIKRNAKVILVPWDHPIDPT---QYDGLFISNGPGDPEMCRKTVENLKNVI---KPIFGICLGHQ 210
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlklDPDGIFLSNGPGDPALLDEAIKTVRKLLgkkIPIFGICLGHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 211 LLSTAVGCKTYKMSYGNRGHNLPCTHTDTGRCFMTSQNHGFAVDVKSLPENWKELFINENDKTNEGIIHESLPYLSVQFH 290
Cdd:cd01744 81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160
|
170
....*....|....*...
gi 1095161062 291 PEHTAGPTDLECLFDIFV 308
Cdd:cd01744 161 PEASPGPHDTEYLFDEFL 178
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
138-308 |
5.50e-59 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 200.16 E-value: 5.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 138 VAIDCGL--KYNQLRCFIKRNAKVILVPWDHP---IDPTQYDGLFISNGPGDPEMCRKTVENLKNVI---KPIFGICLGH 209
Cdd:pfam00117 1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPaeeILEENPDGIILSGGPGSPGAAGGAIEAIREARelkIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 210 QLLSTAVGCKTYKMS-YGNRGHNLPCTHT------DTGRCFMTSQNHGFAVDVKSLPENWKELFINENDKTNEGIIHESL 282
Cdd:pfam00117 81 QLLALAFGGKVVKAKkFGHHGKNSPVGDDgcglfyGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKL 160
|
170 180
....*....|....*....|....*.
gi 1095161062 283 PYLSVQFHPEHTAGPTDLECLFDIFV 308
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFI 186
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
744-862 |
2.29e-52 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 178.80 E-value: 2.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 744 ENELKEPTDKRMFVLAAALKEGYSVEKLYQMTKIDRWFLEKLKNITDYYSILE----GVISAEMLRNAKQIGFSDKQIAA 819
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKkgglDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1095161062 820 AIKSTEIAVRKQRQENNITPFVKQIDTVAAEWPASTNYLYLTY 862
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-104 |
2.11e-45 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses 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 synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 159.46 E-value: 2.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVPDEsdfdehglprWFESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:smart01097 36 GYQEILTDPSYAGQIVVFTYPLIGNYGVNDE----------DFESDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGI 105
|
90 100
....*....|....*....|....*
gi 1095161062 81 SGICGIDTRALTRRLRD-GVTLGRI 104
Cdd:smart01097 106 PGISGIDTRALTRKLREkGAMKGVI 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
335-955 |
0e+00 |
|
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: 1073.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 335 ERPKKVLILGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERPT 414
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 415 GVLLTFGGQTALNCGVQLKRTGVFDKYNVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSAAVASVDGAISAAKEIGY 494
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 495 PVMARAAFSLGGLGSGFANTEEELRALAHQALSHS--DQLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLGIHT 572
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 573 GESIVVAPSQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALNPYSEDFYIIEVNARLSRSSALASKATGYPLAYVAAK 652
Cdd:TIGR01369 244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 653 LALQVPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQKAFRMVDENV 732
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 733 NGFDPNIKKVDENE-----LKEPTDKRMFVLAAALKEGYSVEKLYQMTKIDRWFLEKLKNITDYYSILEGV----ISAEM 803
Cdd:TIGR01369 404 TGFDLPDREVEPDEdlwraLKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVkltdLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 804 LRNAKQIGFSDKQIAAAIKSTEIAVRKQRQENNITPFVKQIDTVAAEWPASTNYLYLTYNGTTHDVEFVTGY-VMVLGSG 882
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKkVLVLGSG 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1095161062 883 VYRIGSSVEFDWCAVSCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNMEQPEGVVLS 955
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
338-954 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 965.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 338 KKVLILGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERPTGVL 417
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 418 LTFGGQTALNCGVQLKRTGVFDKYNVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSAAVASVDGAISAAKEIGYPVM 497
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 498 ARAAFSLGGLGSGFANTEEELRALAHQALSHS--DQLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLGIHTGES 575
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 576 IVVAPSQTLSNREYYMLRNTAIKVIRHFGIV-GECNIQYALNPYSEDFYIIEVNARLSRSSALASKATGYPLAYVAAKLA 654
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 655 LQVPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQKAFRMVDENVNG 734
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 735 FDP-NIKKVDENE----LKEPTDKRMFVLAAALKEGYSVEKLYQMTKIDRWFLEKLKNITDYYSILEG---VISAEMLRN 806
Cdd:PRK05294 408 LDEdLFEEESLEElreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEnglPLDAELLRE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 807 AKQIGFSDKQIAAAIKSTEIAVRKQRQENNITPFVKQIDTVAAEWPASTNYLYLTYNGTTHDVefVTGY--VMVLGSGVY 884
Cdd:PRK05294 488 AKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESN--PSDRkkVLVLGSGPN 565
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 885 RIGSSVEFDWCAVSCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNMEQPEGVVL 954
Cdd:PRK05294 566 RIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIV 635
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
338-954 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 742.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 338 KKVLILGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERPTGVL 417
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 418 LTFGGQTALNCGVQLKRTGVFDKYNVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSAAVASVDGAISAAKEIGYPVM 497
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 498 ARAAFSLGGLGSGFANTEEELRALAHQAL--SHSDQLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLGIHTGES 575
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLqaSPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 576 IVVAPSQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALNPYSEDFYIIEVNARLSRSSALASKATGYPLAYVAAKLAL 655
Cdd:PRK12815 248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 656 QVPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQKAFRMVDENVNGF 735
Cdd:PRK12815 328 GYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 736 D--PNIKKVDENELKE----PTDKRMFVLAAALKEGYSVEKLYQMTKIDRWFLEKLKNITDYYSIL---EGVISAEMLRN 806
Cdd:PRK12815 408 SlpIELSGKSDEELLQdlrhPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLaedGLDLSADLLRK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 807 AKQIGFSDKQIAAAIKSTEIAVRKQRQENNITPFVKQIDTVAAEWPASTNYLYLTYNGTThDVEFVTG--YVMVLGSGVY 884
Cdd:PRK12815 488 VKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGES-EAEPSSEkkKVLILGSGPI 566
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 885 RIGSSVEFDWCAVSCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNMEQPEGVVL 954
Cdd:PRK12815 567 RIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIV 636
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
338-954 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 622.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 338 KKVLILGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERPTGVL 417
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 418 LTFGGQTALNCGVQLKRTGVFDKYNVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSAAVASVDGAISAAKEIG-YPV 496
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 497 MARAAFSLGGLGSGFANTEEELRALAHQAL--SHSDQLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLGIHTGE 574
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLaaSITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 575 SIVVAPSQTLSNREYYMLRNTAIKVIRHFGIvgEC---NIQYALNPYSEDFYIIEVNARLSRSSALASKATGYPLAYVAA 651
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 652 KLALQVPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQKAFRMVDEN 731
Cdd:PLN02735 342 KLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 732 VNGFD-PNIKKVD------ENELKEPTDKRMFVLAAALKEGYSVEKLYQMTKIDRWFLEKLKNITDYYSILEGVISAEML 804
Cdd:PLN02735 422 FSGWGcAKVKELDwdweqlKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLSELS 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 805 RN----AKQIGFSDKQIAAAIKSTEIAVRKQRQENNITPFVKQIDTVAAEWPASTNYLYLTYNGTTHDVEFVTGYVMVLG 880
Cdd:PLN02735 502 KDdfyeVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLILG 581
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1095161062 881 SGVYRIGSSVEFDWCAVSCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNMEQPEGVVL 954
Cdd:PLN02735 582 GGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIV 655
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
343-881 |
0e+00 |
|
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: 621.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 343 LGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERPTGVLLTFGG 422
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 423 QTALNCGVQLKRTGVFDkyNVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSAAVASVDGAISAAKEIGYPVMARAAF 502
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 503 SLGGLGSGFANTEEELRALAHQALSHSD--QLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLGIHTGESIVVAP 580
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPdhPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 581 SQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALNpySEDFYIIEVNARLSRSSALASKATGYPLAYVAAKLALQVPLP 660
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 661 IIKNSvTGvttacFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQKAFRMVDENVNG--FDPN 738
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 739 IKKVDENELKE--PTDKRMFVLAAALKEGYSVEKLYQMTKIDRWFLEKLKNITDYYSILEGVISAEM-LRNAKQIGFSDK 815
Cdd:COG0458 391 VADDDKEEALLlaRRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINtLLGAKSLGDSDG 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1095161062 816 QIAAAIKSTEIAVRKQRQENNITPFVKQIDTVAAEWPASTNYLYLTYNGTTHDVEFVTGYVMVLGS 881
Cdd:COG0458 471 IIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-308 |
4.36e-141 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 424.87 E-value: 4.36e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVPDEsdfdehglprWFESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:PRK12564 38 GYQEILTDPSYAGQIVTFTYPLIGNYGVNRE----------DFESDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 81 SGICGIDTRALTRRLRD-GVTLGRIIQGT------------IADPNTRNLVAEVSIKGPKIYNAKGD---FTIVAIDCGL 144
Cdd:PRK12564 108 PGISGIDTRALTRKLREkGAMKGVIATEDfdaeellekaraFPGLLGLDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 145 KYNQLRCFIKRNAKVILVPWDHPIDPT---QYDGLFISNGPGDPEMCRKTVENLKNVI---KPIFGICLGHQLLSTAVGC 218
Cdd:PRK12564 188 KRNILRELAERGCRVTVVPATTTAEEIlalNPDGVFLSNGPGDPAALDYAIEMIRELLekkIPIFGICLGHQLLALALGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 219 KTYKMSYGNRGHNLPCTHTDTGRCFMTSQNHGFAVDVKSLPENWKELFINENDKTNEGIIHESLPYLSVQFHPEHTAGPT 298
Cdd:PRK12564 268 KTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPH 347
|
330
....*....|
gi 1095161062 299 DLECLFDIFV 308
Cdd:PRK12564 348 DSAYLFDEFV 357
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-313 |
6.23e-138 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 416.64 E-value: 6.23e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVPDEsdfdehglprWFESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:TIGR01368 34 GYQEILTDPSYKGQIVVFTYPLIGNYGVNDE----------DAESKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 81 SGICGIDTRALTRRLRD-GVTLGRIIQGTI----------ADPNTR--NLVAEVSIKGPKIYNAKGD--FTIVAIDCGLK 145
Cdd:TIGR01368 104 PGIYGVDTRALVKKIREkGTMKGVISTEDSndeelvekarVSPDITgiNLVAEVSTKEPYTWGQRGGkgKRVVVIDFGVK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 146 YNQLRCFIKRNAKVILVPWDHP---IDPTQYDGLFISNGPGDPEMCRKTVENLKNVI--KPIFGICLGHQLLSTAVGCKT 220
Cdd:TIGR01368 184 RNILRRLVKRGCEVTVVPYDTDaeeIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLekIPIFGICLGHQLLALAFGAKT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 221 YKMSYGNRGHNLPCTHTDTGRCFMTSQNHGFAVDVKSLPEN-WKELFINENDKTNEGIIHESLPYLSVQFHPEHTAGPTD 299
Cdd:TIGR01368 264 YKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGdLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHD 343
|
330
....*....|....
gi 1095161062 300 LECLFDIFVSSVKA 313
Cdd:TIGR01368 344 TEYLFDEFIDLMKK 357
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-312 |
1.46e-136 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 413.26 E-value: 1.46e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVPDEsdfdehglprWFESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:COG0505 38 GYQEILTDPSYAGQIVTFTYPHIGNYGVNDE----------DFESDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 81 SGICGIDTRALTRRLRD-GVTLGRIIQGTI------------ADPNTRNLVAEVSIKGPKIYNAKGD--FTIVAIDCGLK 145
Cdd:COG0505 108 PGISGIDTRALTRHLREkGAMKGVISTGDLdieellekaraaPGMEGLDLVKEVSTKEPYEWTEAPGagFHVVALDFGVK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 146 YNQLRCFIKRNAKVILVPWDHPID------PtqyDGLFISNGPGDPEMCRKTVENLKNVI---KPIFGICLGHQLLSTAV 216
Cdd:COG0505 188 RNILRELAERGCRVTVVPATTSAEeilalnP---DGVFLSNGPGDPAALDYAIETIRELLgkgIPIFGICLGHQLLALAL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 217 GCKTYKMSYGNRGHNLPCTHTDTGRCFMTSQNHGFAVDVKSLPE-NWKELFINENDKTNEGIIHESLPYLSVQFHPEHTA 295
Cdd:COG0505 265 GAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASP 344
|
330
....*....|....*..
gi 1095161062 296 GPTDLECLFDIFVSSVK 312
Cdd:COG0505 345 GPHDSAYLFDRFIELME 361
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
1-315 |
1.62e-103 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 326.46 E-value: 1.62e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVPDESdfdehglprwFESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:PRK12838 36 GYQEVLTDPSYKGQIVVFTYPLIGNYGINADD----------YESKQPQVKGVIVYELSREGSHYRAKQSLDDFLKEWNI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 81 SGICGIDTRALTRRLRDGVTLGRII----QGTIADPN-----TRNLVAEVSIKGPKIYNAkGDFTIVAIDCGLKYNQLRC 151
Cdd:PRK12838 106 PGISGVDTRALVKHIREKGTMKASItttdDAHAFDQIkalvlPKNVVAQVSTKEPYTYGN-GGKHVALIDFGYKKSILRS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 152 FIKRNAKVILVPWDHP---IDPTQYDGLFISNGPGDPEMCRKTVENLKNVIK--PIFGICLGHQLLSTAVGCKTYKMSYG 226
Cdd:PRK12838 185 LSKRGCKVTVLPYDTSleeIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISsyPILGICLGHQLIALALGADTEKLPFG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 227 NRGHNLPCTHTDTGRCFMTSQNHGFAVDVKSLPEN-WKELFINENDKTNEGIIHESLPYLSVQFHPEHTAGPTDLECLFD 305
Cdd:PRK12838 265 HRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGTpLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFD 344
|
330
....*....|
gi 1095161062 306 IFVSSVKAYR 315
Cdd:PRK12838 345 EFLEMMEKAR 354
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
458-660 |
1.85e-99 |
|
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: 310.39 E-value: 1.85e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 458 DRKIFAEKINAIGEKVAPSAAVA--SVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEELRALAHQALSHS------ 529
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 530 DQLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLgiHTGESIVVAPSQTLSNREYYMLRNTAIKVIRHFGIVGEC 609
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1095161062 610 NIQYALNPYSEDFYIIEVNARLSRSSALASKATGYPLAYVAAKLALQVPLP 660
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
137-308 |
2.48e-98 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 305.96 E-value: 2.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 137 IVAIDCGLKYNQLRCFIKRNAKVILVPWDHPIDPT---QYDGLFISNGPGDPEMCRKTVENLKNVI---KPIFGICLGHQ 210
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlklDPDGIFLSNGPGDPALLDEAIKTVRKLLgkkIPIFGICLGHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 211 LLSTAVGCKTYKMSYGNRGHNLPCTHTDTGRCFMTSQNHGFAVDVKSLPENWKELFINENDKTNEGIIHESLPYLSVQFH 290
Cdd:cd01744 81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160
|
170
....*....|....*...
gi 1095161062 291 PEHTAGPTDLECLFDIFV 308
Cdd:cd01744 161 PEASPGPHDTEYLFDEFL 178
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
338-730 |
9.54e-81 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 283.78 E-value: 9.54e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 338 KKVLILGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERPTGVL 417
Cdd:PRK12815 556 KKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVI 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 418 LTFGGQTALNCGVQLKRTGvfdkynVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSAAVASVDGAISAAKEIGYPVM 497
Cdd:PRK12815 636 VQFGGQTAINLAKGLEEAG------LTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVL 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 498 ARAAFSLGGLGSGFANTEEELRALAHQALSHSDQLIIDKSLKGwKEVEYEVVRDAFDncITVCN-MENVDPLGIHTGESI 576
Cdd:PRK12815 710 IRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPILIDQFIDG-KEYEVDAISDGED--VTIPGiIEHIEQAGVHSGDSI 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 577 VVAPSQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALnpYSEDFYIIEVNARLSRSSALASKATGYPLAYVAAKLALQ 656
Cdd:PRK12815 787 AVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL--ANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLG 864
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1095161062 657 vplpiiKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQKAFRMVDE 730
Cdd:PRK12815 865 ------KSLAELGYPNGLWPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDL 932
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
336-726 |
1.34e-80 |
|
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: 283.04 E-value: 1.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 336 RPKKVLILGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERPTG 415
Cdd:TIGR01369 553 DKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEG 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 416 VLLTFGGQTALNCGVQLKRTGvfdkynVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSAAVASVDGAISAAKEIGYP 495
Cdd:TIGR01369 633 VIVQFGGQTPLNLAKALEEAG------VPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYP 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 496 VMARAAFSLGGLGSGFANTEEELRALAHQALSHSDQ--LIIDKSLKGWKEVEYEVVRDafDNCITVCN-MENVDPLGIHT 572
Cdd:TIGR01369 707 VLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAVSD--GEEVLIPGiMEHIEEAGVHS 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 573 GESIVVAPSQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALnpYSEDFYIIEVNARLSRSSALASKATGYPLAYVAAK 652
Cdd:TIGR01369 785 GDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVR 862
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1095161062 653 LALQ---VPLPIIKnsvtgvttacfEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQKAFR 726
Cdd:TIGR01369 863 VMLGkklEELGVGK-----------EKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQL 928
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
338-725 |
8.38e-75 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 266.58 E-value: 8.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 338 KKVLILGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERPTGVL 417
Cdd:PRK05294 555 KKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVI 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 418 LTFGGQTALNCGVQLKrtgvfdKYNVSVLGTPIQSiIDT-EDRKIFAEKINAIGEKVAPSAAVASVDGAISAAKEIGYPV 496
Cdd:PRK05294 635 VQFGGQTPLKLAKALE------AAGVPILGTSPDA-IDLaEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPV 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 497 MARAAFSLGGLGSGFANTEEELRALAHQALSHSDQ--LIIDKSLKGWKEVeyEVvrDAfdncitVCN---------MENV 565
Cdd:PRK05294 708 LVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDhpVLIDKFLEGAIEV--DV--DA------ICDgedvliggiMEHI 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 566 DPLGIHTGESIVVAPSQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALnpYSEDFYIIEVNARLSRSSALASKATGYP 645
Cdd:PRK05294 778 EEAGVHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAV--KDDEVYVIEVNPRASRTVPFVSKATGVP 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 646 LAYVAAKLALQVPLPIIknsvtGVTTacfEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQKAF 725
Cdd:PRK05294 856 LAKIAARVMLGKKLAEL-----GYTK---GLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQ 927
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-319 |
9.70e-65 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 223.14 E-value: 9.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVPDESdfdehglprwFESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:CHL00197 40 GYQEIITDPSYFEQIVTFTYPEIGNTGINLED----------IESVKIQVKGIIAKNICKSSSNWRQQESLVSYLQRHKI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 81 SGICGIDTRALTRRLRDGVTLGRIIQGTIADPN-------------TRNLVAEVSIKG---------PKIYNAKGD---- 134
Cdd:CHL00197 110 PFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSylrakikesphmpSSDLIPRVTTSSyyewdekshPSFYLADNKrphs 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 135 ---FTIVAIDCGLKYNQLRCFIKRNAKVILVPWDHP---IDPTQYDGLFISNGPGDPEMCRKTVENLKNVIK---PIFGI 205
Cdd:CHL00197 190 syqLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPyqdILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKyniPIFGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 206 CLGHQLLSTAVGCKTYKMSYGNRGHNLPcthtdTG---RCFMTSQNHGFAVDVKSLPENWKEL-FINENDKTNEGIIHES 281
Cdd:CHL00197 270 CMGHQILSLALEAKTFKLKFGHRGLNHP-----SGlnqQVEITSQNHGFAVNLESLAKNKFYItHFNLNDGTVAGISHSP 344
|
330 340 350
....*....|....*....|....*....|....*...
gi 1095161062 282 LPYLSVQFHPEHTAGPTDLECLFDIFVSSVKAYRDKKS 319
Cdd:CHL00197 345 KPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSSKN 382
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
1-304 |
2.55e-60 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 211.76 E-value: 2.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVpdesDFDEHglprwfESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:PLN02771 90 GYQEILTDPSYAGQFVLMTNPHIGNTGV----NFDDE------ESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 81 SGICGIDTRALTRRLR-DGVTLGRIiqgTIADPNTR---------------NLVAEVSIKGPKIY----NAKGDFT---- 136
Cdd:PLN02771 160 MGIYDVDTRAITRRLReDGSLIGVL---STEDSKTDeellkmsrswdivgiDLISGVSCKSPYEWvdktNPEWDFNtnsr 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 137 ------IVAIDCGLKYNQLRCFIKRNAKVILVPWDHPIDPT---QYDGLFISNGPGDPEMCRKTVENLKNVIK--PIFGI 205
Cdd:PLN02771 237 dgesyhVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEAlkmKPDGVLFSNGPGDPSAVPYAVETVKELLGkvPVFGI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 206 CLGHQLLSTAVGCKTYKMSYGNRGHNLPCTHTDTGRCFMTSQNHGFAVDVKSLPENWKELFINENDKTNEGIIHESLPYL 285
Cdd:PLN02771 317 CMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVM 396
|
330
....*....|....*....
gi 1095161062 286 SVQFHPEHTAGPTDLECLF 304
Cdd:PLN02771 397 SLQYHPEASPGPHDSDNAF 415
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
334-724 |
9.51e-60 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 222.35 E-value: 9.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 334 PERPKKVLILGSGGLSIGQAGEFDYSGSQAVKAMQEEKILTVLINPNIATVQTSKGLADKVYFLPITPHYVEQVIKAERP 413
Cdd:PLN02735 571 PTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERP 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 414 TGVLLTFGGQTALNCGVQLKRtgVFDKY---------NVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSAAVASVDG 484
Cdd:PLN02735 651 DGIIVQFGGQTPLKLALPIQK--YLDKNpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEAD 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 485 AISAAKEIGYPVMARAAFSLGGLGSGFANTEEELRALAHQALSHSDQ--LIIDKSLKGWKEVEYEVVRDAFDNCITVCNM 562
Cdd:PLN02735 729 ALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPErpVLVDKYLSDATEIDVDALADSEGNVVIGGIM 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 563 ENVDPLGIHTGESIVVAPSQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALNPySEDFYIIEVNARLSRSSALASKAT 642
Cdd:PLN02735 809 EHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITP-SGEVYIIEANPRASRTVPFVSKAI 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 643 GYPLAYVAAKLALQVPLPIIknsvtGVTTacfEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRNFEEAIQ 722
Cdd:PLN02735 888 GHPLAKYASLVMSGKSLKDL-----GFTE---EVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFA 959
|
..
gi 1095161062 723 KA 724
Cdd:PLN02735 960 KA 961
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
138-308 |
5.50e-59 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 200.16 E-value: 5.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 138 VAIDCGL--KYNQLRCFIKRNAKVILVPWDHP---IDPTQYDGLFISNGPGDPEMCRKTVENLKNVI---KPIFGICLGH 209
Cdd:pfam00117 1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPaeeILEENPDGIILSGGPGSPGAAGGAIEAIREARelkIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 210 QLLSTAVGCKTYKMS-YGNRGHNLPCTHT------DTGRCFMTSQNHGFAVDVKSLPENWKELFINENDKTNEGIIHESL 282
Cdd:pfam00117 81 QLLALAFGGKVVKAKkFGHHGKNSPVGDDgcglfyGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKL 160
|
170 180
....*....|....*....|....*.
gi 1095161062 283 PYLSVQFHPEHTAGPTDLECLFDIFV 308
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFI 186
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
744-862 |
2.29e-52 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 178.80 E-value: 2.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 744 ENELKEPTDKRMFVLAAALKEGYSVEKLYQMTKIDRWFLEKLKNITDYYSILE----GVISAEMLRNAKQIGFSDKQIAA 819
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKkgglDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1095161062 820 AIKSTEIAVRKQRQENNITPFVKQIDTVAAEWPASTNYLYLTY 862
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-104 |
2.01e-48 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. 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 pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 167.89 E-value: 2.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVPDEsdfdehglprWFESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:pfam00988 32 GYQEILTDPSYAGQIVVFTYPLIGNYGVNPE----------DFESDKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGI 101
|
90 100
....*....|....*....|....*
gi 1095161062 81 SGICGIDTRALTRRLRD-GVTLGRI 104
Cdd:pfam00988 102 PGISGVDTRALTRKIREkGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-104 |
2.11e-45 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses 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 synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 159.46 E-value: 2.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 1 GYPESLTDPSYHSQLLVLTYPLIGNYGVPDEsdfdehglprWFESSRIWAAALIVGEISKKACHWRAKKSLGRWMAAQGI 80
Cdd:smart01097 36 GYQEILTDPSYAGQIVVFTYPLIGNYGVNDE----------DFESDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGI 105
|
90 100
....*....|....*....|....*
gi 1095161062 81 SGICGIDTRALTRRLRD-GVTLGRI 104
Cdd:smart01097 106 PGISGIDTRALTRKLREkGAMKGVI 130
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
879-955 |
3.93e-33 |
|
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: 135.39 E-value: 3.93e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1095161062 879 LGSGVYRIGSSVEFDWCAVSCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNMEQPEGVVLS 955
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQ 77
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
746-819 |
7.41e-32 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 118.63 E-value: 7.41e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1095161062 746 ELKEPTDKRMFVLAAALKEGYSVEKLYQMTKIDRWFLEKLKNITDYYSILE---GVISAEMLRNAKQIGFSDKQIAA 819
Cdd:pfam02787 2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKeagLDLDAELLREAKRLGFSDRQIAK 78
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
146-292 |
5.94e-21 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 91.44 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 146 YNQLRCFIKRNAKVILVPWDHP----IDPTQYDGLFISNGPGDPE---MCRKTVENLKNVIkPIFGICLGHQLLSTAVGC 218
Cdd:cd01743 12 YNLVQYLRELGAEVVVVRNDEItleeLELLNPDAIVISPGPGHPEdagISLEIIRALAGKV-PILGVCLGHQAIAEAFGG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 219 KTYKMSYGNRGHNLPCTHTDTGRCFMTSQN------HGFAVDVKSLPENWKELfinenDKTNEGII----HESLPYLSVQ 288
Cdd:cd01743 91 KVVRAPEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLEVT-----ASTEDGVImalrHRDLPIYGVQ 165
|
....
gi 1095161062 289 FHPE 292
Cdd:cd01743 166 FHPE 169
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
459-655 |
2.77e-18 |
|
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: 85.69 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 459 RKIFAEKinaiGEKVAPSAAVASVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEELRALAHQALSH------SDQL 532
Cdd:COG0439 59 REALAAA----GVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEakagspNGEV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 533 IIDKSLKGwKEVEYEVVrdAFDNCITVCNM---ENVDPLGIHTGEsivVAPSQtLSNREYYMLRNTAIKVIRHFGIV-GE 608
Cdd:COG0439 135 LVEEFLEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGA 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1095161062 609 CNIQYALNPySEDFYIIEVNARLS--RSSALASKATGYPLAYVAAKLAL 655
Cdd:COG0439 208 FHTEFLLTP-DGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLAL 255
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
161-305 |
1.09e-14 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 74.21 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 161 LVPWDHPIDptQYDGLFISNGPGDPEMCRKTVENLKNVI-------KPIFGICLGHQLLSTAVGCKTYKMSYGNRG---- 229
Cdd:COG0518 39 ILPYDPDLE--DPDGLILSGGPMSVYDEDPWLEDEPALIreafelgKPVLGICYGAQLLAHALGGKVEPGPGREIGwapv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 230 ---------HNLPcthtDTGRCFMTsqnHGFAVDvkSLPENWKELFINENDKtNEGIIHESlPYLSVQFHPEHTagPTDL 300
Cdd:COG0518 117 elteadplfAGLP----DEFTVWMS---HGDTVT--ELPEGAEVLASSDNCP-NQAFRYGR-RVYGVQFHPEVT--HTMM 183
|
....*
gi 1095161062 301 ECLFD 305
Cdd:COG0518 184 EAWLE 188
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
137-294 |
1.33e-13 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 70.04 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 137 IVAIDCGLKYNQLrcfIKRNAKVI-----LVPWDHPID------PTqydGLFISNGP-----GDPEMCRKTVENLKnviK 200
Cdd:TIGR00888 1 ILVLDFGSQYTQL---IARRLRELgvyseLVPNTTPLEeireknPK---GIILSGGPssvyaENAPRADEKIFELG---V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 201 PIFGICLGHQLLSTAVGCKTYKMSYGNRGH------NLPCTHTDTGRCFMTSQNHGFAvdVKSLPENWKELFINENDKtN 274
Cdd:TIGR00888 72 PVLGICYGMQLMAKQLGGEVGRAEKREYGKaeleilDEDDLFRGLPDESTVWMSHGDK--VKELPEGFKVLATSDNCP-V 148
|
170 180
....*....|....*....|..
gi 1095161062 275 EGIIHESLPYLSVQFHPE--HT 294
Cdd:TIGR00888 149 AAMAHEEKPIYGVQFHPEvtHT 170
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
153-292 |
2.34e-13 |
|
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 69.30 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 153 IKRNAKVilvPWDHpIDPTQYDGLFISNGPGDPE---MCRKTVENLKNVIkPIFGICLGHQLLSTAVGCKTYKMSYGNRG 229
Cdd:COG0512 27 VVRNDEI---TLEE-IEALAPDGIVLSPGPGTPEeagISLEVIRAFAGKI-PILGVCLGHQAIGEAFGGKVVRAPEPMHG 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1095161062 230 HNLPCTHTDTGrCFmtsQN----------HGFAVDVKSLPEnwkELFINENDKTNE--GIIHESLPYLSVQFHPE 292
Cdd:COG0512 102 KTSPITHDGSG-LF---AGlpnpftatryHSLVVDRETLPD---ELEVTAWTEDGEimGIRHRELPIEGVQFHPE 169
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
165-293 |
4.75e-13 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 68.43 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 165 DHPIDPTQYDGLFISNGPGDPEMCR-----KTVENLKNVI---KPIFGICLGHQLLSTAVGCKTYKMSYGNRGHNLPCTH 236
Cdd:cd01741 39 ELLPDLDDYDGLVILGGPMSVDEDDypwlkKLKELIRQALaagKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTL 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1095161062 237 TDTGRCFMTSQNHGFAVD--------VKSLPENWKELFINENDKtNEGIIHESLpYLSVQFHPEH 293
Cdd:cd01741 119 TEAGKADPLFAGLPDEFPvfhwhgdtVVELPPGAVLLASSEACP-NQAFRYGDR-ALGLQFHPEE 181
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
463-739 |
3.17e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 69.67 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 463 AEKINAIGEKVA---------------PSAAVASVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEELRAL------ 521
Cdd:PRK06111 107 ADIIAKMGSKIEarramqaagvpvvpgITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAfesnkk 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 522 -AHQALSHSdQLIIDKSLKGWKEVEYEVVRDAFDNCitvcnmenvdplgIHTGE---SI------VV--APSQTLSNREY 589
Cdd:PRK06111 187 rAANFFGNG-EMYIEKYIEDPRHIEIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPFLDEETR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 590 YMLRNTAIKVIRHFGIVGECNIQYALNPySEDFYIIEVNARLSRSSALASKATGYPLAYVAAKLALQVPLPIIKNSVTGV 669
Cdd:PRK06111 253 KAMGERAVQAAKAIGYTNAGTIEFLVDE-QKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQDDIKRS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 670 TTA-----------CFEPSLDycvvKIPRWDLAK--FNRVSTKIGSSMK-------SVGEVMSIGRNFEEAIQKAFRMVD 729
Cdd:PRK06111 332 GHAievriyaedpkTFFPSPG----KITDLTLPGgeGVRHDHAVENGVTvtpfydpMIAKLIAHGETREEAISRLHDALE 407
|
330
....*....|.
gi 1095161062 730 E-NVNGFDPNI 739
Cdd:PRK06111 408 ElKVEGIKTNI 418
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
339-662 |
9.84e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 67.22 E-value: 9.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 339 KVLILGSGGlsigqagefdysGSQAVKAMQEE----KILTVLINPNIATVQtskgLADKVYFLP-IT-PHYVEQVI---K 409
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSllkgRVIGADISELAPALY----FADKFYVVPkVTdPNYIDRLLdicK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 410 AERPTGVLLTFGGQTALNCgvqlKRTGVFDKYNVSVLGTPiQSIIDT-EDRKIFAEKINAIGEKVAPSAAVASVD--GAI 486
Cdd:PRK12767 67 KEKIDLLIPLIDPELPLLA----QNRDRFEEIGVKVLVSS-KEVIEIcNDKWLTYEFLKENGIPTPKSYLPESLEdfKAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 487 SAAKEIGYPVMARAAFSLGGLGSGFANTEEELRalahQALSHSDQLIIDKSLKGwKEVEYEVVRDAFDNCITVCNMENVD 566
Cdd:PRK12767 142 LAKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 567 PLGihtGESivvapSQTLSnREYYMLRNTAIKVIRHFGIVGECNIQYALNPysEDFYIIEVNARLSrssalaskaTGYPL 646
Cdd:PRK12767 217 VRA---GET-----SKGVT-VKDPELFKLAERLAEALGARGPLNIQCFVTD--GEPYLFEINPRFG---------GGYPL 276
|
330 340
....*....|....*....|....*
gi 1095161062 647 AYVA---------AKLALQVPLPII 662
Cdd:PRK12767 277 SYMAganepdwiiRNLLGGENEPII 301
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
148-292 |
2.25e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 64.30 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 148 QL--RCFIKRNAKVILVpwDHPIDPTQYDGLFISNGPGDPE---MCRKTVENLKNVIKPIFGICLGHQLLSTAVGCKTYK 222
Cdd:PRK07765 22 QLgvEAEVWRNDDPRLA--DEAAVAAQFDGVLLSPGPGTPEragASIDMVRACAAAGTPLLGVCLGHQAIGVAFGATVDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 223 MSYGNRGHNLPCTHTDTG------RCFMTSQNHGFAVDVKSLPEnwkELFINEndKTNEGII----HESLPYLSVQFHPE 292
Cdd:PRK07765 100 APELLHGKTSSVHHTGVGvlaglpDPFTATRYHSLTILPETLPA---ELEVTA--RTDSGVImavrHRELPIHGVQFHPE 174
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
137-294 |
4.86e-11 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 62.55 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 137 IVAIDCGLKYNQLrcfIKRNAKVI-----LVPWDHPIDP---TQYDGLFISNGPG--DPEMCRKTVENLKNVIKPIFGIC 206
Cdd:cd01742 1 ILILDFGSQYTHL---IARRVRELgvyseILPNTTPLEEiklKNPKGIILSGGPSsvYEEDAPRVDPEIFELGVPVLGIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 207 LGHQLLSTAVGCKTYKMSYGNRGHNLpCTHTDTGRCF----------MtsqNHGfavD-VKSLPENWKELFINENDKtNE 275
Cdd:cd01742 78 YGMQLIAKALGGKVERGDKREYGKAE-IEIDDSSPLFeglpdeqtvwM---SHG---DeVVKLPEGFKVIASSDNCP-VA 149
|
170 180
....*....|....*....|.
gi 1095161062 276 GIIHESLPYLSVQFHPE--HT 294
Cdd:cd01742 150 AIANEEKKIYGVQFHPEvtHT 170
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
137-294 |
5.07e-11 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 62.56 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 137 IVAIDCGLKYNQLrcfIKRNAKVI-----LVPWDHPIDP--TQYDGLFISNGPgdpEM-----CRKTVENLKnviKPIFG 204
Cdd:PRK00758 2 IVVVDNGGQYNHL---IHRTLRYLgvdakIIPNTTPVEEikAFEDGLILSGGP---DIeragnCPEYLKELD---VPILG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 205 ICLGHQLLSTAVGCKTYKMSYGNRGH-NLPCTHTDT-----GRCFMTSQNHgfAVDVKSLPENWKELFINENDKTnEGII 278
Cdd:PRK00758 73 ICLGHQLIAKAFGGEVGRGEYGEYALvEVEILDEDDilkglPPEIRVWASH--ADEVKELPDGFEILARSDICEV-EAMK 149
|
170
....*....|....*...
gi 1095161062 279 HESLPYLSVQFHPE--HT 294
Cdd:PRK00758 150 HKEKPIYGVQFHPEvaHT 167
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
146-292 |
1.70e-10 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 61.30 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 146 YN---QLRCF-----IKRNAKVILVPwdhpIDPTQYDGLFISNGPGDPE---MCRKTVENLKNVIkPIFGICLGHQLLST 214
Cdd:PRK05670 13 YNlvqYLGELgaevvVYRNDEITLEE----IEALNPDAIVLSPGPGTPAeagISLELIREFAGKV-PILGVCLGHQAIGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 215 AVGC-----------KTYKMSYGNRG--HNLPcTHTDTGRcfmtsqNHGFAVDVKSLPEnwkELFIN--ENDKTNEGIIH 279
Cdd:PRK05670 88 AFGGkvvrakeimhgKTSPIEHDGSGifAGLP-NPFTVTR------YHSLVVDRESLPD---CLEVTawTDDGEIMGVRH 157
|
170
....*....|...
gi 1095161062 280 ESLPYLSVQFHPE 292
Cdd:PRK05670 158 KELPIYGVQFHPE 170
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
146-292 |
2.21e-10 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 60.96 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 146 YNQLRCFIKRNAKVIlVPWDHPIDPTQYDGLF-----ISNGPGDPEMCRKTVENLKNVIK--PIFGICLGHQLLSTAVGC 218
Cdd:TIGR00566 13 YNLVQYFCELGAEVV-VKRNDSLTLQEIEALLpllivISPGPCTPNEAGISLEAIRHFAGklPILGVCLGHQAMGQAFGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 219 KTYKMSYGNRGHNLPCTHTDTGRC------FMTSQNHGFAVDVKSLPENWKELFINENDKTNEGIIHESLPYLSVQFHPE 292
Cdd:TIGR00566 92 DVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPE 171
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
153-292 |
3.51e-10 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 60.26 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 153 IKRNAKVILVPWDHpIDPTQydgLFISNGPGDPEMCRKTVENLKNVIK--PIFGICLGHQLLSTAVGCKTYKMSYGNRGH 230
Cdd:PRK06774 28 VKRNDELQLTDIEQ-LAPSH---LVISPGPCTPNEAGISLAVIRHFADklPILGVCLGHQALGQAFGARVVRARQVMHGK 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1095161062 231 NLPCTHTDTG------RCFMTSQNHGFAVDVKSLPENWKELFINEND-KTNE--GIIHESLPYLSVQFHPE 292
Cdd:PRK06774 104 TSAICHSGQGvfrglnQPLTVTRYHSLVIAADSLPGCFELTAWSERGgEMDEimGIRHRTLPLEGVQFHPE 174
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
149-212 |
6.98e-10 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 57.61 E-value: 6.98e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1095161062 149 LRCFIKRNAKVILVPWDHP-----IDPTQYDGLFISNGPGDPEMCRKTVENLKNVI------KPIFGICLGHQLL 212
Cdd:cd01653 18 LDALREAGAEVDVVSPDGGpvesdVDLDDYDGLILPGGPGTPDDLARDEALLALLReaaaagKPILGICLGAQLL 92
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
440-631 |
7.77e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 62.07 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 440 KYNVSVLGTPIQSIIDTEDRKIFAEKINAIGEKVAPSA--AVASVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEE 517
Cdd:PRK08462 99 HHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 518 LR----ALAHQALSH--SDQLIIDKSLKGWKEVEYEVVRDAFDNCITV----CNMENvdplgiHTGESIVVAPSQTLSNR 587
Cdd:PRK08462 179 LEnlylAAESEALSAfgDGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVLDEK 252
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1095161062 588 EYYMLRNTAIKVIRHFGIVGECNIQYALNPySEDFYIIEVNARL 631
Cdd:PRK08462 253 TRERLHETAIKAAKAIGYEGAGTFEFLLDS-NLDFYFMEMNTRL 295
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
146-292 |
7.83e-10 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 59.51 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 146 YNQLRCFIKRNAKVILVPWDH-------PIDPTQydgLFISNGPGDPEMCRKTVENLKNVIK--PIFGICLGHQLLSTAV 216
Cdd:PRK08857 13 YNLYQYFCELGAQVKVVRNDEididgieALNPTH---LVISPGPCTPNEAGISLQAIEHFAGklPILGVCLGHQAIAQVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 217 GCKTYKMSYGNRGHNLPCTHTDTGrCFMTSQN-------HGFAVDVKSLPE-----NWKELFINENDKTnEGIIHESLPY 284
Cdd:PRK08857 90 GGQVVRARQVMHGKTSPIRHTGRS-VFKGLNNpltvtryHSLVVKNDTLPEcfeltAWTELEDGSMDEI-MGFQHKTLPI 167
|
....*...
gi 1095161062 285 LSVQFHPE 292
Cdd:PRK08857 168 EAVQFHPE 175
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
175-292 |
2.18e-09 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 58.66 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 175 GLFISNGPGDPE---MCRKTVENLKNVIkPIFGICLGHQLLSTAVGCKTYKMSYG-NRGHNLPCTHTDTG---------R 241
Cdd:PLN02335 65 GVLISPGPGTPQdsgISLQTVLELGPLV-PLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYDEKGeeglfsglpN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1095161062 242 CFMTSQNHGFAVDVKSLPENWKELFINENDKTNEGIIHESLPYLS-VQFHPE 292
Cdd:PLN02335 144 PFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPE 195
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
149-212 |
3.03e-09 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 54.90 E-value: 3.03e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1095161062 149 LRCFIKRNAKVILVPWDHP-----IDPTQYDGLFISNGPGDPEMCRKTVENLKNVI------KPIFGICLGHQLL 212
Cdd:cd03128 18 LDALREAGAEVDVVSPDGGpvesdVDLDDYDGLILPGGPGTPDDLAWDEALLALLReaaaagKPVLGICLGAQLL 92
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
176-292 |
4.52e-09 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 60.12 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 176 LFISNGPGDPEMCRKTVENLKNVIK--PIFGICLGHQLLSTAVGCKTYKMSYGNRGHNLPCTHTDTGrCFMTSQN----- 248
Cdd:PRK14607 48 IVISPGPGRPEEAGISVEVIRHFSGkvPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKG-LFRGIPNptvat 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1095161062 249 --HGFAVDVKSLPENWkELFINENDKTNEGIIHESLPYLSVQFHPE 292
Cdd:PRK14607 127 ryHSLVVEEASLPECL-EVTAKSDDGEIMGIRHKEHPIFGVQFHPE 171
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
463-631 |
6.02e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 59.43 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 463 AEKINAIGEKVAPSAA---------------VASVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEELRALAHQALS 527
Cdd:PRK08591 107 AETIRLMGDKVTAKATmkkagvpvvpgsdgpVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 528 HS------DQLIIDKSLKGWKEVEYEVVRDAFDNcitvcnmenvdplGIHTGE---SI------VV--APSQTLSNREYY 590
Cdd:PRK08591 187 EAkaafgnPGVYMEKYLENPRHIEIQVLADGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRR 253
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1095161062 591 MLRNTAIKVIRHFGIVGECNIQYaLNPYSEDFYIIEVNARL 631
Cdd:PRK08591 254 KIGEAAVKAAKAIGYRGAGTIEF-LYEKNGEFYFIEMNTRI 293
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
463-661 |
7.78e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 58.96 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 463 AEKINAIGEKVAPSAA---------------VASVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEELRALAHQALS 527
Cdd:PRK07178 106 AEVIRRMGDKTEARRAmikagvpvtpgsegnLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVIS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 528 H------SDQLIIDKSLKGWKEVEYEVVRDAFDNCITV----CNMENvdplgiHTGESIVVAPSQTLSNREYYMLRNTAI 597
Cdd:PRK07178 186 EatkafgSAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAV 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1095161062 598 KVIRHFGIVGECNIQYALNPYSEdFYIIEVNARLSRSSALASKATGYPLAYVAAKLALQVPLPI 661
Cdd:PRK07178 260 RAAKAVGYENAGTVEFLLDADGE-VYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSY 322
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
153-292 |
3.12e-08 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 54.81 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 153 IKRNAKVILvpwdHPIDPTQYDGLFISNGPGDPEMCRKTVENLKNVIK--PIFGICLGHQLLSTAVGCKTYKMSYGNRGH 230
Cdd:PRK07649 28 VKRNDEVTI----SDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGkiPIFGVCLGHQSIAQVFGGEVVRAERLMHGK 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1095161062 231 NLPCTH------TDTGRCFMTSQNHGFAVDVKSLPENWKelfinENDKTNEG----IIHESLPYLSVQFHPE 292
Cdd:PRK07649 104 TSLMHHdgktifSDIPNPFTATRYHSLIVKKETLPDCLE-----VTSWTEEGeimaIRHKTLPIEGVQFHPE 170
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
153-292 |
4.10e-08 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 54.15 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 153 IKRNAKVILVPwdhpIDPTQYDGLFISNGPGDPEMCRKTVENLKNVIK--PIFGICLGHQLLSTAVGCKTYKMSYGNRGH 230
Cdd:PRK08007 28 VKRNDALTLAD----IDALKPQKIVISPGPCTPDEAGISLDVIRHYAGrlPILGVCLGHQAMAQAFGGKVVRAAKVMHGK 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 231 NLPCTHTDTG------RCFMTSQNHGFAVDVKSLPENWKelfINENDKTNE--GIIHESLPYLSVQFHPE 292
Cdd:PRK08007 104 TSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGVQFHPE 170
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
146-292 |
7.35e-08 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 53.58 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 146 YNQLRCFIKRNAKVILVPWDH----PIDPTQYDGLFISNGPGDPE---MCRKTVENLKNVIkPIFGICLGHQLLSTAVGC 218
Cdd:CHL00101 13 YNLVQSLGELNSDVLVCRNDEidlsKIKNLNIRHIIISPGPGHPRdsgISLDVISSYAPYI-PILGVCLGHQSIGYLFGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 219 KTYKMSYGNRG------HNLPCTHTDTGRCFMTSQNHGFAVDVKSLPENWKELFInendkTNEGII----HESLPYL-SV 287
Cdd:CHL00101 92 KIIKAPKPMHGktskiyHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLEITAW-----TEDGLImacrHKKYKMLrGI 166
|
....*
gi 1095161062 288 QFHPE 292
Cdd:CHL00101 167 QFHPE 171
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
478-631 |
7.69e-08 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 55.79 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 478 AVASVDGAISAAKEIGYPVMARAAFslGGLGSGF--ANTEEELRALAHQALS------HSDQLIIDKSLKGWKEVEYEVV 549
Cdd:COG4770 137 PVQDAEEALAIAEEIGYPVLIKASA--GGGGKGMrvVRSEEELEEAFESARReakaafGDDRVYLEKYIERPRHIEVQVL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 550 RDAFDNCitvcnmenvdplgIHTGE---SI------VV--APSQTLSN--REYymLRNTAIKVIRHFGIVGECNIQYALN 616
Cdd:COG4770 215 ADKHGNV-------------VHLGErdcSIqrrhqkVIeeAPSPALTEelRER--MGEAAVRAAKAVGYVGAGTVEFLVD 279
|
170
....*....|....*
gi 1095161062 617 PySEDFYIIEVNARL 631
Cdd:COG4770 280 A-DGNFYFLEMNTRL 293
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
478-660 |
1.70e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 54.76 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 478 AVASVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEELRA---LAH---QALSHSDQLIIDKSLKGWKEVEYEVVRD 551
Cdd:PRK12833 140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpLAQreaQAAFGDGGVYLERFIARARHIEVQILGD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 552 AfdncitvcnmENVdplgIHTGES-----------IVVAPSQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALNPYSE 620
Cdd:PRK12833 220 G----------ERV----VHLFERecslqrrrqkiLEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARG 285
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1095161062 621 DFYIIEVNARLSRSSALASKATGYPLAYVAAKLALQVPLP 660
Cdd:PRK12833 286 EFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
449-631 |
2.68e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 54.22 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 449 PIQSIIDTEDRKIFAEKI-NAIGEKVAP--SAAVASVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEEL------- 518
Cdd:PRK08654 105 PSSDVIEAMGSKINAKKLmKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELedaiest 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 519 RALAHQALSHSdQLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMEnvdpLGI---HTgESIVVAPSQTLSNREYYMLRNT 595
Cdd:PRK08654 185 QSIAQSAFGDS-TVFIEKYLEKPRHIEIQILADKHGNVIHLGDRE----CSIqrrHQ-KLIEEAPSPIMTPELRERMGEA 258
|
170 180 190
....*....|....*....|....*....|....*..
gi 1095161062 596 AIKVIRHFGIVGECNIQYAlnpYSE-DFYIIEVNARL 631
Cdd:PRK08654 259 AVKAAKAINYENAGTVEFL---YSNgNFYFLEMNTRL 292
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
463-631 |
2.68e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 54.76 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 463 AEKINAIGEKVA-------------PS--AAVASVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEELRALAHQALS 527
Cdd:PRK12999 111 AEVLRLLGDKVAarnaaikagvpviPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 528 H------SDQLIIDKSLKGWKEVEYEVVRDAFDNCitvcnmenvdplgIHTGE---SI------VV--APSQTLSN--RE 588
Cdd:PRK12999 191 EakaafgNDEVYLEKYVENPRHIEVQILGDKHGNV-------------VHLYErdcSVqrrhqkVVeiAPAPGLSEelRE 257
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1095161062 589 yyMLRNTAIKVIRHFGIVGECNIQYALNPySEDFYIIEVNARL 631
Cdd:PRK12999 258 --RICEAAVKLARAVGYVNAGTVEFLVDA-DGNFYFIEVNPRI 297
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
157-292 |
2.89e-07 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 54.54 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 157 AKVILVPWDHP---IDPTQYDGLFISNGPGDPE--MCRKTVENL--KNVikPIFGICLGHQLLSTAVGCKTYKMSYGNRG 229
Cdd:PRK13566 551 AEVTTVRYGFAeemLDRVNPDLVVLSPGPGRPSdfDCKATIDAAlaRNL--PIFGVCLGLQAIVEAFGGELGQLAYPMHG 628
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1095161062 230 --------------HNLPcthtdtgRCFMTSQNHGFAVDVKSLPENWKELFINEnDKTNEGIIHESLPYLSVQFHPE 292
Cdd:PRK13566 629 kpsrirvrgpgrlfSGLP-------EEFTVGRYHSLFADPETLPDELLVTAETE-DGVIMAIEHKTLPVAAVQFHPE 697
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
160-292 |
4.39e-07 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 51.87 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 160 ILVPWDHPIDPTQYDG-LFISNGPGDPEMCRKTVENLKNVI---KPIFGICLGHQLLSTAVGCKTY---KMSYGNRGHNL 232
Cdd:pfam07722 62 LLLTGGPNVDPHFYGEePSESGGPYDPARDAYELALIRAALargKPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHRE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 233 PC-------THT---DTGRCF--MTSQN-------HGFAVDVksLPENWKELFINEnDKTNEGIIHESLPY--LSVQFHP 291
Cdd:pfam07722 142 HCqvapyapSHAvnvEPGSLLasLLGSEefrvnslHHQAIDR--LAPGLRVEAVAP-DGTIEAIESPNAKGfaLGVQWHP 218
|
.
gi 1095161062 292 E 292
Cdd:pfam07722 219 E 219
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
172-292 |
6.39e-07 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 50.89 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 172 QYDGLFISNGPGDPEMCRKTVENLKNVI--KPIFGICLGHQLLSTAVGCKTYKMSYGNRGH--------------NLPCT 235
Cdd:PRK06895 43 NFSHILISPGPDVPRAYPQLFAMLERYHqhKSILGVCLGHQTLCEFFGGELYNLNNVRHGQqrplkvrsnsplfdGLPEE 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1095161062 236 htdtgrcFMTSQNHGFAVDVKSLPEnwkELFINEndKTNEGII----HESLPYLSVQFHPE 292
Cdd:PRK06895 123 -------FNIGLYHSWAVSEENFPT---PLEITA--VCDENVVmamqHKTLPIYGVQFHPE 171
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
478-630 |
8.63e-07 |
|
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: 53.16 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 478 AVASVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEELRALAHQALSH------SDQLIIDKSLKGWKEVEYEVVRD 551
Cdd:COG1038 140 PVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREakaafgDDEVFLEKYIERPKHIEVQILGD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 552 AFDNCitvcnmenvdplgIHTGE---SI------VV--APSQTLSN--REyyMLRNTAIKVIRHFGIVGECNIQYALNPy 618
Cdd:COG1038 220 KHGNI-------------VHLFErdcSVqrrhqkVVeiAPAPNLDEelRE--AICEAAVKLAKAVGYVNAGTVEFLVDD- 283
|
170
....*....|..
gi 1095161062 619 SEDFYIIEVNAR 630
Cdd:COG1038 284 DGNFYFIEVNPR 295
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
478-669 |
1.46e-06 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 51.47 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 478 AVASVDGAISAAKEIGYPVMARAA--------FSLGGLGSGFANTEEELRALAHQALSHSDQLIIDkslkgwkeveyEVV 549
Cdd:COG3919 137 VLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAGYELIVQ-----------EYI 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 550 rDAFDNCITVCNM---ENVDPLGIHTGESIVVAPSQ--------TLSNREyymLRNTAIKVIRHFGIVGECNIQYALNPY 618
Cdd:COG3919 206 -PGDDGEMRGLTAyvdRDGEVVATFTGRKLRHYPPAggnsaareSVDDPE---LEEAARRLLEALGYHGFANVEFKRDPR 281
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1095161062 619 SEDFYIIEVNARLSRSSALASKAtGYPLAYVAAKLALQVPLPIIKNSVTGV 669
Cdd:COG3919 282 DGEYKLIEINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREGV 331
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
478-739 |
2.04e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 51.25 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 478 AVASVDGAISAAKEIGYPVMARAAFSLGGLGSGFANTEEELRALAHQALSHS------DQLIIDKSLKGWKEVEYEVVRD 551
Cdd:PRK05586 137 EIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAkaafgdDSMYIEKFIENPKHIEFQILGD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 552 AFDNCITV----CNMENvdplgiHTGESIVVAPSQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALNPySEDFYIIEV 627
Cdd:PRK05586 217 NYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDK-DGNFYFMEM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 628 NARLSRSSALASKATGYPLAYVAAKLALQVPLPIIKN--SVTGVTTAC----------FEPS----------------LD 679
Cdd:PRK05586 290 NTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQEdiKINGHSIECrinaedpkngFMPCpgkieelyipgglgvrVD 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1095161062 680 ---YCVVKIPR-WDlakfnrvstkigsSMksVGEVMSIGRNFEEAIQKAFRMVDE-NVNGFDPNI 739
Cdd:PRK05586 370 savYSGYTIPPyYD-------------SM--IGKLIVYGKDREEAIQKMKRALGEfIIEGVNTNI 419
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
489-646 |
6.52e-06 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 49.81 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 489 AKEIGYPVMARAAFSLGGLGSGFANTEEEL----RALAHQALSH--SDQLIIDKSLKGWKEVEYEVVRDAFDNCITVCnm 562
Cdd:PRK08463 148 ARKIGYPVILKASGGGGGRGIRVVHKEEDLenafESCKREALAYfnNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLC-- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 563 ENVDPLGIHTGESIVVAPSQTLSNREYYMLRNTAIKVIRHFGIVGECNIQYALNPYSeDFYIIEVNARLSRSSALASKAT 642
Cdd:PRK08463 226 ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYN-RFYFMEMNTRIQVEHGVTEEIT 304
|
....
gi 1095161062 643 GYPL 646
Cdd:PRK08463 305 GIDL 308
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
173-295 |
1.25e-03 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 42.91 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 173 YDGLFISNGPGDPE------MCRKTVENLKNVikPIFGICLGHQLLSTAVGCKTYKMS------------YGNR-GHNLP 233
Cdd:PLN02889 132 FDNIVISPGPGSPTcpadigICLRLLLECRDI--PILGVCLGHQALGYVHGARIVHAPepvhgrlseiehNGCRlFDDIP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 234 C------------------------------THTDTGRCFMTSQNHGFAVDVK--------------SLPEN---WKELF 266
Cdd:PLN02889 210 SgrnsgfkvvryhslvidaeslpkelvpiawTSSSDTLSFLESQKSGLVPDAYesqigqsgssdpfsSKLKNgtsWPSSH 289
|
170 180 190
....*....|....*....|....*....|.
gi 1095161062 267 IN--ENDKTNEGIIHESLPYLSVQFHPEHTA 295
Cdd:PLN02889 290 SErmQNGKILMGIMHSTRPHYGLQFHPESIA 320
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
596-670 |
2.95e-03 |
|
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.
Pssm-ID: 434824 [Multi-domain] Cd Length: 131 Bit Score: 38.75 E-value: 2.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1095161062 596 AIKVIRHFGIVGECNIQYAlnpYSED-FYIIEVNARLsrSSALA-SKATGYPLAYVAAKLALQVPLPIIKNSVTGVT 670
Cdd:pfam15632 53 ARRLAEAFGLDGLFNVQFR---YDGDgPKLLEINPRM--SGGIGySCLAGVNLPYLALKLLLGLETPDPVEPRLGLR 124
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
143-212 |
8.87e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 38.57 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095161062 143 GLKYNQLRCFIKRNAKVILvpwdhpidptQYDGLFIsngPG----DPEMC--RKT--VENLKNVI---KPIFGICLGHQL 211
Cdd:PRK13141 18 ALERLGAEAVITSDPEEIL----------AADGVIL---PGvgafPDAMAnlRERglDEVIKEAVasgKPLLGICLGMQL 84
|
.
gi 1095161062 212 L 212
Cdd:PRK13141 85 L 85
|
|
| |
