|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
346-1282 |
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: 1549.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 346 PKKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTVLINPNIATVQTSKGLADKVYFLPLTPEYVEQVIRSERPSGV 425
Cdd:TIGR01369 6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 426 LLTFGGQTALNCGVELQKNGVFQKYNIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAPSEAAYSVHEALYAAKKLGYPV 505
Cdd:TIGR01369 86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 506 MARAAFSLGGLGSGFANNEEELRILAQQALAHS--SQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGE 583
Cdd:TIGR01369 166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 584 SIVVAPSQTLSNKEYNMLRTTALKVIRHFGVIGECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 663
Cdd:TIGR01369 246 SIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 664 LSIPLPEIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFLRVSKNIGSSMKSVGEVMSIGRNFEEAFQKALRMVDENVNG 743
Cdd:TIGR01369 326 VGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 744 FDPYIKEVNENE-----LIQATDKRMFVLAAALKANYSIEKLHDLTKIDPWFLNKMKNIINHLNTLESHGNN-LSHEILL 817
Cdd:TIGR01369 406 FDLPDREVEPDEdlwraLKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTdLDPELLR 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 818 DAKKLGFSDRQIALAIKSTDLVIRHEREELGIVPFVKQIDTVAGEWPASTNYLYLTYNADSNDIEFPGGYTIVV-GSGVY 896
Cdd:TIGR01369 486 RAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSGPN 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 897 RIGSSVEFDWCAVGCLRELRNLGRKTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIEKPDGIILSMGGQLPNNI 976
Cdd:TIGR01369 566 RIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLNL 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 977 AMDLHRQQARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYS 1056
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYN 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1057 NEDLEQYLNAASLVSKEYPVVISKFLQEAKEIDVDAVAAEGEILCLAVSEHVENAGVHSGDATLVTPPQDINSETLLKIK 1136
Cdd:TIGR01369 726 EEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIK 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1137 EITQDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIGLPVEPVEVL--HGCGKVGV 1214
Cdd:TIGR01369 806 DIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEPKYVAV 885
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450087 1215 KVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMISTGFQIPRKAILLSIGRYKHRVELL 1282
Cdd:TIGR01369 886 KEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELL 953
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
345-1272 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1336.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 345 MPK-----KILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTVLINPNIATVQTSKGLADKVYFLPLTPEYVEQVIRS 419
Cdd:PRK05294 1 MPKrtdikKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 420 ERPSGVLLTFGGQTALNCGVELQKNGVFQKYNIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAPSEAAYSVHEALYAAK 499
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 500 KLGYPVMARAAFSLGGLGSGFANNEEELRILAQQALAHS--SQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENLDPL 577
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 578 GIHTGESIVVAPSQTLSNKEYNMLRTTALKVIRHFGVI-GECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLA 656
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 657 YVAAKLSLSIPLPEIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFLRVSKNIGSSMKSVGEVMSIGRNFEEAFQKALRM 736
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 737 VDENVNGFDPYI-KEVNENELIQ----ATDKRMFVLAAALKANYSIEKLHDLTKIDPWFLNKMKNIINHLNTLESHGNNL 811
Cdd:PRK05294 401 LEIGVTGLDEDLfEEESLEELREelkePTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 812 SHEILLDAKKLGFSDRQIALAIKSTDLVIRHEREELGIVPFVKQIDTVAGEWPASTNYLYLTYNADSNDIEFPGGYTIVV 891
Cdd:PRK05294 481 DAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 892 GSGVYRIGSSVEFDWCAVGCLRELRNLGRKTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIEKPDGIILSMGGQ 971
Cdd:PRK05294 561 GSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 972 LPNNIAMDLHRQQARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAM 1051
Cdd:PRK05294 641 TPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1052 NVAYSNEDLEQYLNAASLVSKEYPVVISKFLQEAKEIDVDAVAAEGEILCLAVSEHVENAGVHSGDATLVTPPQDINSET 1131
Cdd:PRK05294 721 EIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1132 LLKIKEITQDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIG-----LPVEPVEVL 1206
Cdd:PRK05294 801 IEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGkklaeLGYTKGLIP 880
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86450087 1207 HGcgkVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMISTGFQIPRK-AILLSI 1272
Cdd:PRK05294 881 PY---VAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV 944
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
352-893 |
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: 649.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 352 LGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTVLINPNIATVQTSKGLADKVYFLPLTPEYVEQVIRSERPSGVLLTFGG 431
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 432 QTALNCGVELQKNGVFQkyNIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAPSEAAYSVHEALYAAKKLGYPVMARAAF 511
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 512 SLGGLGSGFANNEEELRILAQQALAHS--SQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGESIVVAP 589
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 590 SQTLSNKEYNMLRTTALKVIRHFGVIGECNIQYALNpeSEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLSIPLP 669
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 670 EIKNSvTGvttacFEPSLDYCVVKIPRWDLSKFLRVSKNIGSSMKSVGEVMSIGRNFEEAFQKALRMVDENVNG--FDPY 747
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 748 I--KEVNENELIQATDKRMFVLAAALKANYSIEKLHDLTKIDPWFLNKMKNIINHLNTLESHGNNLshEILLDAKKLGFS 825
Cdd:COG0458 391 VadDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVI--NTLLGAKSLGDS 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450087 826 DRQIALAIKSTDLVIRHEREELGIVPFVKQIDTVAGEWPASTNYLYLTYNADSNDIEFPGGYTIVVGS 893
Cdd:COG0458 469 DGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-312 |
8.21e-131 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 405.61 E-value: 8.21e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDevddfglpkyFEwTTGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:PRK12564 51 QIVTFTYPLIGNYGVNRED----------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 81 KKIRDNGTILGRITHKLPDKNENL----NFIDPNLRNLVAECSVAEPKIY---NPNGYPRICAIDCGLKLNQIRCFIARG 153
Cdd:PRK12564 120 RKLREKGAMKGVIATEDFDAEELLekarAFPGLLGLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAERG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 154 ARVELVPW----DKIL--NPeefDGLFISNGPGDPKVCKNTVHQIQNILNnSDKPIFGICLGHQLLATAIGCKTYKMKYG 227
Cdd:PRK12564 200 CRVTVVPAtttaEEILalNP---DGVFLSNGPGDPAALDYAIEMIRELLE-KKIPIFGICLGHQLLALALGAKTYKMKFG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 228 NRGHNLPCIHHGTGRCFMTSQNHGFAVNADTLPKNWEPLFTNANDFTNEGIIHNTKPYFSVQFHPEHTAGPEDLEVLFNV 307
Cdd:PRK12564 276 HRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDE 355
|
....*
gi 86450087 308 FLEAV 312
Cdd:PRK12564 356 FVELM 360
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-313 |
1.76e-125 |
|
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: 391.69 E-value: 1.76e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDevddfglpkyFEwTTGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:COG0505 51 QIVTFTYPHIGNYGVNDED----------FE-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 81 KKIRDNGTILGRITHKLPDKNENL----NFIDPNLRNLVAECSVAEPKIYNPNGYP--RICAIDCGLKLNQIRCFIARGA 154
Cdd:COG0505 120 RHLREKGAMKGVISTGDLDIEELLekarAAPGMEGLDLVKEVSTKEPYEWTEAPGAgfHVVALDFGVKRNILRELAERGC 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 155 RVELVPWD----KIL--NPeefDGLFISNGPGDPKVCKNTVHQIQNILNnSDKPIFGICLGHQLLATAIGCKTYKMKYGN 228
Cdd:COG0505 200 RVTVVPATtsaeEILalNP---DGVFLSNGPGDPAALDYAIETIRELLG-KGIPIFGICLGHQLLALALGAKTYKLKFGH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 229 RGHNLPCIHHGTGRCFMTSQNHGFAVNADTLPK-NWEPLFTNANDFTNEGIIHNTKPYFSVQFHPEHTAGPEDLEVLFNV 307
Cdd:COG0505 276 RGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDR 355
|
....*.
gi 86450087 308 FLEAVK 313
Cdd:COG0505 356 FIELME 361
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-314 |
2.71e-124 |
|
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: 388.14 E-value: 2.71e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDEVDDfglpkyfewttGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:TIGR01368 47 QIVVFTYPLIGNYGVNDEDAESK-----------GIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 81 KKIRDNGTILGRITHKLPDKNENLNFI--DPNLR--NLVAECSVAEPKIYNP--NGYPRICAIDCGLKLNQIRCFIARGA 154
Cdd:TIGR01368 116 KKIREKGTMKGVISTEDSNDEELVEKArvSPDITgiNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 155 RVELVPWD------KILNPeefDGLFISNGPGDPKVCKNTVHQIQNILNnsDKPIFGICLGHQLLATAIGCKTYKMKYGN 228
Cdd:TIGR01368 196 EVTVVPYDtdaeeiKKYNP---DGIFLSNGPGDPAAVEPAIETIRKLLE--KIPIFGICLGHQLLALAFGAKTYKMKFGH 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 229 RGHNLPCIHHGTGRCFMTSQNHGFAVNADTLPKN-WEPLFTNANDFTNEGIIHNTKPYFSVQFHPEHTAGPEDLEVLFNV 307
Cdd:TIGR01368 271 RGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGdLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDE 350
|
....*..
gi 86450087 308 FLEAVKD 314
Cdd:TIGR01368 351 FIDLMKK 357
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
467-669 |
3.05e-97 |
|
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: 309.23 E-value: 3.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 467 DRKIFAERVAEIGEKVAPSEAAY--SVHEALYAAKKLGYPVMARAAFSLGGLGSGFANNEEELRILAQQALAHS------ 538
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 539 SQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENLDPLgiHTGESIVVAPSQTLSNKEYNMLRTTALKVIRHFGVIGEC 618
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 86450087 619 NIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLSIPLP 669
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
134-309 |
2.74e-95 |
|
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: 302.49 E-value: 2.74e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 134 ICAIDCGLKLNQIRCFIARGARVELVPWD----KILNpEEFDGLFISNGPGDPKVCKNTVHQIQNILNnSDKPIFGICLG 209
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNtdaeEILK-LDPDGIFLSNGPGDPALLDEAIKTVRKLLG-KKIPIFGICLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 210 HQLLATAIGCKTYKMKYGNRGHNLPCIHHGTGRCFMTSQNHGFAVNADTLPKNWEPLFTNANDFTNEGIIHNTKPYFSVQ 289
Cdd:cd01744 79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158
|
170 180
....*....|....*....|
gi 86450087 290 FHPEHTAGPEDLEVLFNVFL 309
Cdd:cd01744 159 FHPEASPGPHDTEYLFDEFL 178
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
137-311 |
9.22e-62 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 209.02 E-value: 9.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 137 IDCGL--KLNQIRCFIARGARVELVPWDKILN---PEEFDGLFISNGPGDPKVCKNTVHQIQNILNNsDKPIFGICLGHQ 211
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTPAEeilEENPDGIILSGGPGSPGAAGGAIEAIREAREL-KIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 212 LLATAIGCKTYKMK-YGNRGHNLPCIH------HGTGRCFMTSQNHGFAVNADTLPKNWEPLFTNANDFTNEGIIHNTKP 284
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*..
gi 86450087 285 YFSVQFHPEHTAGPEDLEVLFNVFLEA 311
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
753-874 |
8.44e-53 |
|
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: 180.72 E-value: 8.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 753 ENELIQATDKRMFVLAAALKANYSIEKLHDLTKIDPWFLNKMKNIINHLNTLESHG-NNLSHEILLDAKKLGFSDRQIAL 831
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGlDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 86450087 832 AIKSTDLVIRHEREELGIVPFVKQIDTVAGEWPASTNYLYLTY 874
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
5.75e-36 |
|
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: 132.88 E-value: 5.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDevddfglpkyFEwTTGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:smart01097 49 QIVVFTYPLIGNYGVNDED----------FE-SDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALT 117
|
90
....*....|...
gi 86450087 81 KKIRDNGTILGRI 93
Cdd:smart01097 118 RKLREKGAMKGVI 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
346-1282 |
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: 1549.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 346 PKKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTVLINPNIATVQTSKGLADKVYFLPLTPEYVEQVIRSERPSGV 425
Cdd:TIGR01369 6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 426 LLTFGGQTALNCGVELQKNGVFQKYNIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAPSEAAYSVHEALYAAKKLGYPV 505
Cdd:TIGR01369 86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 506 MARAAFSLGGLGSGFANNEEELRILAQQALAHS--SQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGE 583
Cdd:TIGR01369 166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 584 SIVVAPSQTLSNKEYNMLRTTALKVIRHFGVIGECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 663
Cdd:TIGR01369 246 SIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 664 LSIPLPEIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFLRVSKNIGSSMKSVGEVMSIGRNFEEAFQKALRMVDENVNG 743
Cdd:TIGR01369 326 VGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 744 FDPYIKEVNENE-----LIQATDKRMFVLAAALKANYSIEKLHDLTKIDPWFLNKMKNIINHLNTLESHGNN-LSHEILL 817
Cdd:TIGR01369 406 FDLPDREVEPDEdlwraLKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTdLDPELLR 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 818 DAKKLGFSDRQIALAIKSTDLVIRHEREELGIVPFVKQIDTVAGEWPASTNYLYLTYNADSNDIEFPGGYTIVV-GSGVY 896
Cdd:TIGR01369 486 RAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSGPN 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 897 RIGSSVEFDWCAVGCLRELRNLGRKTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIEKPDGIILSMGGQLPNNI 976
Cdd:TIGR01369 566 RIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLNL 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 977 AMDLHRQQARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYS 1056
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYN 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1057 NEDLEQYLNAASLVSKEYPVVISKFLQEAKEIDVDAVAAEGEILCLAVSEHVENAGVHSGDATLVTPPQDINSETLLKIK 1136
Cdd:TIGR01369 726 EEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIK 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1137 EITQDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIGLPVEPVEVL--HGCGKVGV 1214
Cdd:TIGR01369 806 DIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEPKYVAV 885
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450087 1215 KVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMISTGFQIPRKAILLSIGRYKHRVELL 1282
Cdd:TIGR01369 886 KEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELL 953
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
345-1272 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1336.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 345 MPK-----KILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTVLINPNIATVQTSKGLADKVYFLPLTPEYVEQVIRS 419
Cdd:PRK05294 1 MPKrtdikKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 420 ERPSGVLLTFGGQTALNCGVELQKNGVFQKYNIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAPSEAAYSVHEALYAAK 499
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 500 KLGYPVMARAAFSLGGLGSGFANNEEELRILAQQALAHS--SQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENLDPL 577
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 578 GIHTGESIVVAPSQTLSNKEYNMLRTTALKVIRHFGVI-GECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLA 656
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 657 YVAAKLSLSIPLPEIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFLRVSKNIGSSMKSVGEVMSIGRNFEEAFQKALRM 736
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 737 VDENVNGFDPYI-KEVNENELIQ----ATDKRMFVLAAALKANYSIEKLHDLTKIDPWFLNKMKNIINHLNTLESHGNNL 811
Cdd:PRK05294 401 LEIGVTGLDEDLfEEESLEELREelkePTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 812 SHEILLDAKKLGFSDRQIALAIKSTDLVIRHEREELGIVPFVKQIDTVAGEWPASTNYLYLTYNADSNDIEFPGGYTIVV 891
Cdd:PRK05294 481 DAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 892 GSGVYRIGSSVEFDWCAVGCLRELRNLGRKTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIEKPDGIILSMGGQ 971
Cdd:PRK05294 561 GSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 972 LPNNIAMDLHRQQARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAM 1051
Cdd:PRK05294 641 TPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1052 NVAYSNEDLEQYLNAASLVSKEYPVVISKFLQEAKEIDVDAVAAEGEILCLAVSEHVENAGVHSGDATLVTPPQDINSET 1131
Cdd:PRK05294 721 EIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1132 LLKIKEITQDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIG-----LPVEPVEVL 1206
Cdd:PRK05294 801 IEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGkklaeLGYTKGLIP 880
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86450087 1207 HGcgkVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMISTGFQIPRK-AILLSI 1272
Cdd:PRK05294 881 PY---VAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV 944
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
345-1279 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1029.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 345 MPK-----KILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTVLINPNIATVQTSKGLADKVYFLPLTPEYVEQVIRS 419
Cdd:PRK12815 1 MPKdtdiqKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 420 ERPSGVLLTFGGQTALNCGVELQKNGVFQKYNIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAPSEAAYSVHEALYAAK 499
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 500 KLGYPVMARAAFSLGGLGSGFANNEEELRILAQQALAHS--SQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENLDPL 577
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASpiHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 578 GIHTGESIVVAPSQTLSNKEYNMLRTTALKVIRHFGVIGECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAY 657
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 658 VAAKLSLSIPLPEIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFLRVSKNIGSSMKSVGEVMSIGRNFEEAFQKALRMV 737
Cdd:PRK12815 321 IAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 738 DENVNGFDPYIKE--VNENELIQ----ATDKRMFVLAAALKANYSIEKLHDLTKIDPWFLNKMKNIINHLNTLESHGNNL 811
Cdd:PRK12815 401 EIKRNGLSLPIELsgKSDEELLQdlrhPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 812 SHEILLDAKKLGFSDRQIALAIKSTDLVIRHEREELGIVPFVKQIDTVAGEWPASTNYLYLTYNADsNDIEFPGG--YTI 889
Cdd:PRK12815 481 SADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGE-SEAEPSSEkkKVL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 890 VVGSGVYRIGSSVEFDWCAVGCLRELRNLGRKTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIEKPDGIILSMG 969
Cdd:PRK12815 560 ILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFG 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 970 GQLPNNIAMDLHRQQARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGA 1049
Cdd:PRK12815 640 GQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQ 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1050 AMNVAYSNEDLEQYLNAAslVSKEYPVVISKFLqEAKEIDVDAVAAEGEILCLAVSEHVENAGVHSGDATLVTPPQDINS 1129
Cdd:PRK12815 720 GMAVVYDEPALEAYLAEN--ASQLYPILIDQFI-DGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQSLSE 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1130 ETLLKIKEITQDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIGLPVE----PVEV 1205
Cdd:PRK12815 797 EQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAelgyPNGL 876
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450087 1206 LHGCGKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMISTGFQIPRKA-ILLSI-GRYKHRV 1279
Cdd:PRK12815 877 WPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGtIFISVrDEDKPEV 952
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
347-1264 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 865.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 347 KKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTVLINPNIATVQTSKGLADKVYFLPLTPEYVEQVIRSERPSGVL 426
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 427 LTFGGQTALNCGVELQKNGVFQKYNIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAPSEAAYSVHEALYAAKKLG-YPV 505
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 506 MARAAFSLGGLGSGFANNEEELRILAQQALAHS--SQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGE 583
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAASitSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 584 SIVVAPSQTLSNKEYNMLRTTALKVIRHFGVigEC---NIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAA 660
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 661 KLSLSIPLPEIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFLRVSKNIGSSMKSVGEVMSIGRNFEEAFQKALRMVDEN 740
Cdd:PLN02735 342 KLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 741 VNGFD-PYIKEVN------ENELIQATDKRMFVLAAALKANYSIEKLHDLTKIDPWFLNKMKNIINHLNTLESHG-NNLS 812
Cdd:PLN02735 422 FSGWGcAKVKELDwdweqlKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSlSELS 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 813 HEILLDAKKLGFSDRQIALAIKSTDLVIRHEREELGIVPFVKQIDTVAGEWPASTNYLYLTYNADSNDIEFPGGYTIVVG 892
Cdd:PLN02735 502 KDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLILG 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 893 SGVYRIGSSVEFDWCAVGCLRELRNLGRKTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIEKPDGIILSMGGQL 972
Cdd:PLN02735 582 GGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGGQT 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 973 PNNIAMDLHRQ-------------QARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCL 1039
Cdd:PLN02735 662 PLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYPVV 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1040 VRPSYVLSGAAMNVAYSNEDLEQYLNAASLVSKEYPVVISKFLQEAKEIDVDAVA-AEGEILCLAVSEHVENAGVHSGDA 1118
Cdd:PLN02735 742 VRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSGDS 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1119 TLVTPPQDINSETLLKIKEITQDLAALLDVTGPFNMQL-IAKNNELKVIECNVRVSRSFPFVSKTLNHDF-------VAT 1190
Cdd:PLN02735 822 ACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLakyaslvMSG 901
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450087 1191 ATRAVIGLPVEPVEvlhgcGKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMISTGFQIP 1264
Cdd:PLN02735 902 KSLKDLGFTEEVIP-----AHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLP 970
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
352-893 |
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: 649.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 352 LGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTVLINPNIATVQTSKGLADKVYFLPLTPEYVEQVIRSERPSGVLLTFGG 431
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 432 QTALNCGVELQKNGVFQkyNIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAPSEAAYSVHEALYAAKKLGYPVMARAAF 511
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 512 SLGGLGSGFANNEEELRILAQQALAHS--SQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGESIVVAP 589
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 590 SQTLSNKEYNMLRTTALKVIRHFGVIGECNIQYALNpeSEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLSIPLP 669
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 670 EIKNSvTGvttacFEPSLDYCVVKIPRWDLSKFLRVSKNIGSSMKSVGEVMSIGRNFEEAFQKALRMVDENVNG--FDPY 747
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 748 I--KEVNENELIQATDKRMFVLAAALKANYSIEKLHDLTKIDPWFLNKMKNIINHLNTLESHGNNLshEILLDAKKLGFS 825
Cdd:COG0458 391 VadDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVI--NTLLGAKSLGDS 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450087 826 DRQIALAIKSTDLVIRHEREELGIVPFVKQIDTVAGEWPASTNYLYLTYNADSNDIEFPGGYTIVVGS 893
Cdd:COG0458 469 DGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
891-1282 |
3.28e-157 |
|
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: 482.07 E-value: 3.28e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 891 VGSGVYRIGSSVEFDWCAVGCLRELRNLGRKTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIEKPDGIILSMGG 970
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 971 QLPNNIAMDLHRQQA----RVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVL 1046
Cdd:COG0458 81 QTALNLAVELEEAGIlegvKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1047 SGAAMNVAYSNEDLEQYLNAASLVSKEYPVVISKFLQEAKEIDVDAVA-AEGEILCLAVSEHVENAGVHSGDATLVTPPQ 1125
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRdGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1126 DINSETLLKIKEITQDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIGLPVEPVEV 1205
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1206 LHGC----GKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMISTGFQIPRKaILLSIGRYKHRVEL 1281
Cdd:COG0458 321 DTGFeptlDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDKEEA 399
|
.
gi 86450087 1282 L 1282
Cdd:COG0458 400 L 400
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-312 |
8.21e-131 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 405.61 E-value: 8.21e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDevddfglpkyFEwTTGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:PRK12564 51 QIVTFTYPLIGNYGVNRED----------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 81 KKIRDNGTILGRITHKLPDKNENL----NFIDPNLRNLVAECSVAEPKIY---NPNGYPRICAIDCGLKLNQIRCFIARG 153
Cdd:PRK12564 120 RKLREKGAMKGVIATEDFDAEELLekarAFPGLLGLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAERG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 154 ARVELVPW----DKIL--NPeefDGLFISNGPGDPKVCKNTVHQIQNILNnSDKPIFGICLGHQLLATAIGCKTYKMKYG 227
Cdd:PRK12564 200 CRVTVVPAtttaEEILalNP---DGVFLSNGPGDPAALDYAIEMIRELLE-KKIPIFGICLGHQLLALALGAKTYKMKFG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 228 NRGHNLPCIHHGTGRCFMTSQNHGFAVNADTLPKNWEPLFTNANDFTNEGIIHNTKPYFSVQFHPEHTAGPEDLEVLFNV 307
Cdd:PRK12564 276 HRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDE 355
|
....*
gi 86450087 308 FLEAV 312
Cdd:PRK12564 356 FVELM 360
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-313 |
1.76e-125 |
|
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: 391.69 E-value: 1.76e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDevddfglpkyFEwTTGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:COG0505 51 QIVTFTYPHIGNYGVNDED----------FE-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 81 KKIRDNGTILGRITHKLPDKNENL----NFIDPNLRNLVAECSVAEPKIYNPNGYP--RICAIDCGLKLNQIRCFIARGA 154
Cdd:COG0505 120 RHLREKGAMKGVISTGDLDIEELLekarAAPGMEGLDLVKEVSTKEPYEWTEAPGAgfHVVALDFGVKRNILRELAERGC 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 155 RVELVPWD----KIL--NPeefDGLFISNGPGDPKVCKNTVHQIQNILNnSDKPIFGICLGHQLLATAIGCKTYKMKYGN 228
Cdd:COG0505 200 RVTVVPATtsaeEILalNP---DGVFLSNGPGDPAALDYAIETIRELLG-KGIPIFGICLGHQLLALALGAKTYKLKFGH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 229 RGHNLPCIHHGTGRCFMTSQNHGFAVNADTLPK-NWEPLFTNANDFTNEGIIHNTKPYFSVQFHPEHTAGPEDLEVLFNV 307
Cdd:COG0505 276 RGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDR 355
|
....*.
gi 86450087 308 FLEAVK 313
Cdd:COG0505 356 FIELME 361
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-314 |
2.71e-124 |
|
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: 388.14 E-value: 2.71e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDEVDDfglpkyfewttGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:TIGR01368 47 QIVVFTYPLIGNYGVNDEDAESK-----------GIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 81 KKIRDNGTILGRITHKLPDKNENLNFI--DPNLR--NLVAECSVAEPKIYNP--NGYPRICAIDCGLKLNQIRCFIARGA 154
Cdd:TIGR01368 116 KKIREKGTMKGVISTEDSNDEELVEKArvSPDITgiNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 155 RVELVPWD------KILNPeefDGLFISNGPGDPKVCKNTVHQIQNILNnsDKPIFGICLGHQLLATAIGCKTYKMKYGN 228
Cdd:TIGR01368 196 EVTVVPYDtdaeeiKKYNP---DGIFLSNGPGDPAAVEPAIETIRKLLE--KIPIFGICLGHQLLALAFGAKTYKMKFGH 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 229 RGHNLPCIHHGTGRCFMTSQNHGFAVNADTLPKN-WEPLFTNANDFTNEGIIHNTKPYFSVQFHPEHTAGPEDLEVLFNV 307
Cdd:TIGR01368 271 RGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGdLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDE 350
|
....*..
gi 86450087 308 FLEAVKD 314
Cdd:TIGR01368 351 FIDLMKK 357
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
467-669 |
3.05e-97 |
|
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: 309.23 E-value: 3.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 467 DRKIFAERVAEIGEKVAPSEAAY--SVHEALYAAKKLGYPVMARAAFSLGGLGSGFANNEEELRILAQQALAHS------ 538
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 539 SQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENLDPLgiHTGESIVVAPSQTLSNKEYNMLRTTALKVIRHFGVIGEC 618
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 86450087 619 NIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLSIPLP 669
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
1-313 |
9.91e-97 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 313.75 E-value: 9.91e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDevddfglpkyFEwTTGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:PRK12838 49 QIVVFTYPLIGNYGINADD----------YE-SKQPQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 81 KKIRDNGTILGRIThklpdKNENLNFIDPNLR-----NLVAECSVAEPKIYnPNGYPRICAIDCGLKLNQIRCFIARGAR 155
Cdd:PRK12838 118 KHIREKGTMKASIT-----TTDDAHAFDQIKAlvlpkNVVAQVSTKEPYTY-GNGGKHVALIDFGYKKSILRSLSKRGCK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 156 VELVPWD------KILNPeefDGLFISNGPGDPKVCKNTVHQIQNILnnSDKPIFGICLGHQLLATAIGCKTYKMKYGNR 229
Cdd:PRK12838 192 VTVLPYDtsleeiKNLNP---DGIVLSNGPGDPKELQPYLPEIKKLI--SSYPILGICLGHQLIALALGADTEKLPFGHR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 230 GHNLPCIHHGTGRCFMTSQNHGFAVNADTLPKN-WEPLFTNANDFTNEGIIHNTKPYFSVQFHPEHTAGPEDLEVLFNVF 308
Cdd:PRK12838 267 GANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGTpLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEF 346
|
....*
gi 86450087 309 LEAVK 313
Cdd:PRK12838 347 LEMME 351
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
134-309 |
2.74e-95 |
|
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: 302.49 E-value: 2.74e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 134 ICAIDCGLKLNQIRCFIARGARVELVPWD----KILNpEEFDGLFISNGPGDPKVCKNTVHQIQNILNnSDKPIFGICLG 209
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNtdaeEILK-LDPDGIFLSNGPGDPALLDEAIKTVRKLLG-KKIPIFGICLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 210 HQLLATAIGCKTYKMKYGNRGHNLPCIHHGTGRCFMTSQNHGFAVNADTLPKNWEPLFTNANDFTNEGIIHNTKPYFSVQ 289
Cdd:cd01744 79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158
|
170 180
....*....|....*....|
gi 86450087 290 FHPEHTAGPEDLEVLFNVFL 309
Cdd:cd01744 159 FHPEASPGPHDTEYLFDEFL 178
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-320 |
4.62e-66 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 228.53 E-value: 4.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDEVddfglpkyfewTTGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:CHL00197 53 QIVTFTYPEIGNTGINLEDIE-----------SVKIQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 81 KKIRDNGTILGRIThklpdkNENLNF-------------IDPNLRNLVAECSV---AEPKIYNPN---------GYP-RI 134
Cdd:CHL00197 122 QHLRRFGTMNGCIS------NQNLNLsylrakikesphmPSSDLIPRVTTSSYyewDEKSHPSFYladnkrphsSYQlKI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 135 CAIDCGLKLNQIRCFIARGARVELVP-------WDKiLNPeefDGLFISNGPGDPKVCKNTVHQIQNILNNSdKPIFGIC 207
Cdd:CHL00197 196 IVIDFGVKYNILRRLKSFGCSITVVPatspyqdILS-YQP---DGILLSNGPGDPSAIHYGIKTVKKLLKYN-IPIFGIC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 208 LGHQLLATAIGCKTYKMKYGNRGhnlpcIHHGTG---RCFMTSQNHGFAVNADTLPKNwePLFT---NANDFTNEGIIHN 281
Cdd:CHL00197 271 MGHQILSLALEAKTFKLKFGHRG-----LNHPSGlnqQVEITSQNHGFAVNLESLAKN--KFYIthfNLNDGTVAGISHS 343
|
330 340 350
....*....|....*....|....*....|....*....
gi 86450087 282 TKPYFSVQFHPEHTAGPEDLEVLFNVFLEAVKDSIEKKS 320
Cdd:CHL00197 344 PKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSSKN 382
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
137-311 |
9.22e-62 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 209.02 E-value: 9.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 137 IDCGL--KLNQIRCFIARGARVELVPWDKILN---PEEFDGLFISNGPGDPKVCKNTVHQIQNILNNsDKPIFGICLGHQ 211
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTPAEeilEENPDGIILSGGPGSPGAAGGAIEAIREAREL-KIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 212 LLATAIGCKTYKMK-YGNRGHNLPCIH------HGTGRCFMTSQNHGFAVNADTLPKNWEPLFTNANDFTNEGIIHNTKP 284
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*..
gi 86450087 285 YFSVQFHPEHTAGPEDLEVLFNVFLEA 311
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
753-874 |
8.44e-53 |
|
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: 180.72 E-value: 8.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 753 ENELIQATDKRMFVLAAALKANYSIEKLHDLTKIDPWFLNKMKNIINHLNTLESHG-NNLSHEILLDAKKLGFSDRQIAL 831
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGlDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 86450087 832 AIKSTDLVIRHEREELGIVPFVKQIDTVAGEWPASTNYLYLTY 874
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
1-305 |
1.38e-48 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 179.02 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDEVddfglpkyfewTTGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:PLN02771 103 QFVLMTNPHIGNTGVNFDDEE-----------SRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAIT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 81 KKIRDNGTILGRITHKLPDKNENLNFI----DPNLRNLVAECSVAEPKI----------YNPNGYP----RICAIDCGLK 142
Cdd:PLN02771 172 RRLREDGSLIGVLSTEDSKTDEELLKMsrswDIVGIDLISGVSCKSPYEwvdktnpewdFNTNSRDgesyHVIAYDFGIK 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 143 LNQIRCFIARGARVELVP--WDKI----LNPeefDGLFISNGPGDPKVCKNTVHQIQNILNNSdkPIFGICLGHQLLATA 216
Cdd:PLN02771 252 HNILRRLASYGCKITVVPstWPASealkMKP---DGVLFSNGPGDPSAVPYAVETVKELLGKV--PVFGICMGHQLLGQA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 217 IGCKTYKMKYGNRGHNLPCIHHGTGRCFMTSQNHGFAVNADTLPKNWEPLFTNANDFTNEGIIHNTKPYFSVQFHPEHTA 296
Cdd:PLN02771 327 LGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASP 406
|
....*....
gi 86450087 297 GPEDLEVLF 305
Cdd:PLN02771 407 GPHDSDNAF 415
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
1.16e-39 |
|
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: 143.23 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDevddfglpkyFEwTTGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:pfam00988 45 QIVVFTYPLIGNYGVNPED----------FE-SDKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALT 113
|
90
....*....|...
gi 86450087 81 KKIRDNGTILGRI 93
Cdd:pfam00988 114 RKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
5.75e-36 |
|
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: 132.88 E-value: 5.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1 QILVLTYPLIGNYGVPPEDevddfglpkyFEwTTGISIAGLVVGEHCETPSHWRQSKTLSKWMEEQSVPGISGIDTRSLT 80
Cdd:smart01097 49 QIVVFTYPLIGNYGVNDED----------FE-SDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALT 117
|
90
....*....|...
gi 86450087 81 KKIRDNGTILGRI 93
Cdd:smart01097 118 RKLREKGAMKGVI 130
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
755-830 |
1.08e-34 |
|
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: 127.11 E-value: 1.08e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450087 755 ELIQATDKRMFVLAAALKANYSIEKLHDLTKIDPWFLNKMKNIINHLNTLESHGNNLSHEILLDAKKLGFSDRQIA 830
Cdd:pfam02787 2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDAELLREAKRLGFSDRQIA 77
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
153-293 |
1.13e-22 |
|
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: 96.83 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 153 GARVELVPWDKI----LNPEEFDGLFISNGPGDPKVCKNTVHQIQNILNNsdKPIFGICLGHQLLATAIGCKTYKMKYGN 228
Cdd:cd01743 22 GAEVVVVRNDEItleeLELLNPDAIVISPGPGHPEDAGISLEIIRALAGK--VPILGVCLGHQAIAEAFGGKVVRAPEPM 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450087 229 RGHNLPCIHHGTGRCFMTSQN------HGFAVNADTLPKNWEplFTNANDftnEGII----HNTKPYFSVQFHPE 293
Cdd:cd01743 100 HGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLE--VTASTE---DGVImalrHRDLPIYGVQFHPE 169
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
989-1200 |
2.87e-20 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 91.86 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 989 GTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNEDLEQYLNAAS 1068
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1069 ----LVSKEYPVVISKFLqEAKEIDVDAVAAEGEILCLAVSEHvENAGVHSGDATLVTPPqDINSETLLKIKEITQDLAA 1144
Cdd:COG0439 123 aeakAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGELVARALR 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1145 LLDV-TGPFNMQ-LIAKNNELKVIECNVRVS--RSFPFVSKTLNHDFVATATRAVIGLPV 1200
Cdd:COG0439 200 ALGYrRGAFHTEfLLTPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEPR 259
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1023-1201 |
1.02e-18 |
|
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: 86.20 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1023 NLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNEDLEQYLNAASLVSKEYP----VVISKFLQEAKEIDVDAVA-AEG 1097
Cdd:pfam02786 26 TEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLRdAHG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1098 EILCLAVSEHVENagVHSGDATLVTPPQDINSETLLKIKEITQDLAALLDVTGPFNMQLI--AKNNELKVIECNVRVSRS 1175
Cdd:pfam02786 106 NCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFAldPFSGEYYFIEMNTRLQVE 183
|
170 180
....*....|....*....|....*.
gi 86450087 1176 FPFVSKTLNHDFVATATRAVIGLPVE 1201
Cdd:pfam02786 184 HALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
133-296 |
2.47e-17 |
|
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: 82.30 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 133 RICAIDCG-------------LKLNQIRCFIARGARVELVPWDkiLNPEEFDGLFISNGPG----DPKVCKNTVHQIQNI 195
Cdd:COG0518 1 KILILDHDpfggqypgliarrLREAGIELDVLRVYAGEILPYD--PDLEDPDGLILSGGPMsvydEDPWLEDEPALIREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 196 LNnSDKPIFGICLGHQLLATAIGCKTYKMKYGNRG-------------HNLPcihhGTGRCFMTsqnHGFAVnaDTLPKN 262
Cdd:COG0518 79 FE-LGKPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelteadplfAGLP----DEFTVWMS---HGDTV--TELPEG 148
|
170 180 190
....*....|....*....|....*....|....
gi 86450087 263 WEPLFTNANDfTNEGIIHNtKPYFSVQFHPEHTA 296
Cdd:COG0518 149 AEVLASSDNC-PNQAFRYG-RRVYGVQFHPEVTH 180
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
153-293 |
8.00e-16 |
|
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: 77.00 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 153 GARVELVPWDKI----LNPEEFDGLFISNGPGDPK---VCKNTVHQIqnilnNSDKPIFGICLGHQLLATAIGCKTYKMK 225
Cdd:COG0512 22 GAEVVVVRNDEItleeIEALAPDGIVLSPGPGTPEeagISLEVIRAF-----AGKIPILGVCLGHQAIGEAFGGKVVRAP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 226 YgnrghnlpcIHHGtgrcfMTSQ-------------N-------HGFAVNADTLPKNWEPlftNAndFTNEGII----HN 281
Cdd:COG0512 97 E---------PMHG-----KTSPithdgsglfaglpNpftatryHSLVVDRETLPDELEV---TA--WTEDGEImgirHR 157
|
170
....*....|..
gi 86450087 282 TKPYFSVQFHPE 293
Cdd:COG0512 158 ELPIEGVQFHPE 169
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
456-664 |
3.13e-15 |
|
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: 77.22 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 456 GTPIESIIQTEDRKIFAERVAEIGEKVAPSEAAYSVHEALYAAKKLGYPVMARAAFSLGGLGSGFANNEEELRILAQQAL 535
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 536 AH------SSQLIIDKSLKGwKEVEYEVVrdAYDNCITVCNM---ENLDPLGIHTGEsivVAPSQtLSNKEYNMLRTTAL 606
Cdd:COG0439 123 AEakagspNGEVLVEEFLEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86450087 607 KVIRHFGVI-GECNIQYALNPEsEEYYIIEVNARLS--RSSALASKATGYPLAYVAAKLSL 664
Cdd:COG0439 196 RALRALGYRrGAFHTEFLLTPD-GEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLAL 255
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
145-313 |
3.65e-15 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 75.17 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 145 QIRCFiarGARVELVPWDKI-------LNPeefDGLFISNGPGDPKVCKNTVHQIQNIlnNSDKPIFGICLGHQLLATAI 217
Cdd:PRK05670 18 YLGEL---GAEVVVYRNDEItleeieaLNP---DAIVLSPGPGTPAEAGISLELIREF--AGKVPILGVCLGHQAIGEAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 218 GC-----------KTYKMKYGNRGhnlpcIHHGTGRCFMTSQNHGFAVNADTLPKNWEPlftNANDFTNE--GIIHNTKP 284
Cdd:PRK05670 90 GGkvvrakeimhgKTSPIEHDGSG-----IFAGLPNPFTVTRYHSLVVDRESLPDCLEV---TAWTDDGEimGVRHKELP 161
|
170 180
....*....|....*....|....*....
gi 86450087 285 YFSVQFHPEHTAGPEDLEVLFNvFLEAVK 313
Cdd:PRK05670 162 IYGVQFHPESILTEHGHKLLEN-FLELAR 189
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
134-312 |
4.89e-15 |
|
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: 74.66 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 134 ICAIDCGLKLNQIrcfIARGAR-----VELVPWD-KILNPEEFD--GLFISNGPGDPKVcKNTVHQIQNILNnSDKPIFG 205
Cdd:TIGR00888 1 ILVLDFGSQYTQL---IARRLRelgvySELVPNTtPLEEIREKNpkGIILSGGPSSVYA-ENAPRADEKIFE-LGVPVLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 206 ICLGHQLLATAIGCKTYKMKYGNRGH------NLPCIHHGTGRCFMTSQNHGFAVNAdtLPKNWEPLFTNANDfTNEGII 279
Cdd:TIGR00888 76 ICYGMQLMAKQLGGEVGRAEKREYGKaeleilDEDDLFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDNC-PVAAMA 152
|
170 180 190
....*....|....*....|....*....|...
gi 86450087 280 HNTKPYFSVQFHPEHTAGPEDLEVLFNvFLEAV 312
Cdd:TIGR00888 153 HEEKPIYGVQFHPEVTHTEYGNELLEN-FVYDV 184
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
155-294 |
6.54e-14 |
|
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: 71.51 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 155 RVELVPWDKILNPEEFDGLFISNGPGDPKVCKN-----TVHQIQNILNnSDKPIFGICLGHQLLATAIGCKTYKMKYG-- 227
Cdd:cd01741 32 VVDVYAGELLPDLDDYDGLVILGGPMSVDEDDYpwlkkLKELIRQALA-AGKPVLGICLGHQLLARALGGKVGRNPKGwe 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450087 228 ---------NRGHNLPcIHHGTGRCFMTSQNHGFAVnaDTLPKNWEPLFTNAnDFTNEGIIHNTKPYfSVQFHPEH 294
Cdd:cd01741 111 igwfpvtltEAGKADP-LFAGLPDEFPVFHWHGDTV--VELPPGAVLLASSE-ACPNQAFRYGDRAL-GLQFHPEE 181
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
155-337 |
2.18e-13 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 74.37 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 155 RVELVPWDKI-------LNPEEfdgLFISNGPGDPKVCKNTVHQIQNIlnnSDK-PIFGICLGHQLLATAIGCKTYKMKY 226
Cdd:PRK14607 26 EIEVVRNDEItieeieaLNPSH---IVISPGPGRPEEAGISVEVIRHF---SGKvPILGVCLGHQAIGYAFGGKIVHAKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 227 GNRGHNLPCIHHGTGrCFMTSQN-------HGFAVNADTLPKNWEPLfTNANDFTNEGIIHNTKPYFSVQFHPEHTAGPE 299
Cdd:PRK14607 100 ILHGKTSPIDHNGKG-LFRGIPNptvatryHSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPESILTEE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 86450087 300 DLEVLFNvFLEAVKDSIEKKsngSVKEKLI--KTLSFTVA 337
Cdd:PRK14607 178 GKRILKN-FLNYQREEIDIK---SYLKKLVegEDLSFEEA 213
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
987-1178 |
8.02e-13 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 71.07 E-value: 8.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 987 VLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAIE--FCEEVGYPCLVRPSYVLSGAAMNVAYSNEDLEQYL 1064
Cdd:PRK12767 98 VLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAalAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1065 NAASlvskeyPVVISKFLQEaKEIDVDA-VAAEGEILCLAVSEHVEnagVHSGDA-TLVTPPQDinsetllKIKEITQDL 1142
Cdd:PRK12767 178 EYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETsKGVTVKDP-------ELFKLAERL 240
|
170 180 190
....*....|....*....|....*....|....*.
gi 86450087 1143 AALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPF 1178
Cdd:PRK12767 241 AEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
150-295 |
1.53e-12 |
|
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: 67.18 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 150 IAR-----GARVELVPWDKILNPEE---FDGLFISNGP------GDPKVCKNtvhqiqnILNnSDKPIFGICLGHQLLAT 215
Cdd:cd01742 14 IARrvrelGVYSEILPNTTPLEEIKlknPKGIILSGGPssvyeeDAPRVDPE-------IFE-LGVPVLGICYGMQLIAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 216 AIGCKTYKMKYGNRGHNLPCIHHGTG---------RCFMtsqNHGFAVnaDTLPKNWEPLFTNANDfTNEGIIHNTKPYF 286
Cdd:cd01742 86 ALGGKVERGDKREYGKAEIEIDDSSPlfeglpdeqTVWM---SHGDEV--VKLPEGFKVIASSDNC-PVAAIANEEKKIY 159
|
170
....*....|.
gi 86450087 287 SVQFHPE--HT 295
Cdd:cd01742 160 GVQFHPEvtHT 170
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
173-293 |
2.24e-12 |
|
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: 67.12 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 173 LFISNGPGDPKVCKNTVHQIQNIlnNSDKPIFGICLGHQLLATAIGCKTYKMKYGNRGHNLPCIHHGTGRC------FMT 246
Cdd:TIGR00566 47 IVISPGPCTPNEAGISLEAIRHF--AGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTA 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 86450087 247 SQNHGFAVNADTLPKNWEPLFTNANDFTNEGIIHNTKPYFSVQFHPE 293
Cdd:TIGR00566 125 TRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPE 171
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
153-310 |
5.02e-12 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 66.03 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 153 GARVELVPWDKilNPEE----FDGLFISNGPgdpkvcknTVHQIQN---ILNNSDKPIFGICLGHQLLATAIGCKTYKMK 225
Cdd:PRK00758 23 GVDAKIIPNTT--PVEEikafEDGLILSGGP--------DIERAGNcpeYLKELDVPILGICLGHQLIAKAFGGEVGRGE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 226 YGNRG--------HNLPCIhhGTGRCFMTSQNHgfavnAD---TLPKNWEPLFTNANdFTNEGIIHNTKPYFSVQFHPE- 293
Cdd:PRK00758 93 YGEYAlveveildEDDILK--GLPPEIRVWASH-----ADevkELPDGFEILARSDI-CEVEAMKHKEKPIYGVQFHPEv 164
|
170
....*....|....*...
gi 86450087 294 -HTagpEDLEVLFNVFLE 310
Cdd:PRK00758 165 aHT---EYGEEIFKNFLE 179
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
348-659 |
9.49e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 67.99 E-value: 9.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 348 KILILGSGGlsigqagefdysGSQAIKALKEE----KIQTVLINPNIATVQtskgLADKVYFLP--LTPEYVEQVI---R 418
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSllkgRVIGADISELAPALY----FADKFYVVPkvTDPNYIDRLLdicK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 419 SERPSGVLLTFGGQTALncgveLQKNGV-FQKYNIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAPSEAAYSV--HEAL 495
Cdd:PRK12767 67 KEKIDLLIPLIDPELPL-----LAQNRDrFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLedFKAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 496 YAAKKLGYPVMARAAFSLGGLGSGFANNEEELRilaqQALAHSSQLIIDKSLKGwKEVEYEVVRDAYDNCITVCNMENLD 575
Cdd:PRK12767 142 LAKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 576 PLGIHTGESIVVapsqtlsnkEYNMLRTTALKVIRHFGVIGECNIQYALNPesEEYYIIEVNARLSrssalaskaTGYPL 655
Cdd:PRK12767 217 VRAGETSKGVTV---------KDPELFKLAERLAEALGARGPLNIQCFVTD--GEPYLFEINPRFG---------GGYPL 276
|
....
gi 86450087 656 AYVA 659
Cdd:PRK12767 277 SYMA 280
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
458-640 |
1.30e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 68.52 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 458 PIESIIQTEDRKIFAER-VAEIGEKVAP--SEAAYSVHEALYAAKKLGYPVMARAAFSLGGLGSGFANNEEELRilaqQA 534
Cdd:PRK06111 105 PSADIIAKMGSKIEARRaMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELT----KA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 535 LAHSSQ----------LIIDKSLKGWKEVEYEVVRDAYDNCitvcnmenldplgIHTGE---SI------VV--APSQTL 593
Cdd:PRK06111 181 FESNKKraanffgngeMYIEKYIEDPRHIEIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPFL 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 86450087 594 SNKEYNMLRTTALKVIRHFGVIGECNIQYaLNPESEEYYIIEVNARL 640
Cdd:PRK06111 248 DEETRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFYFLEMNTRL 293
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
149-306 |
3.54e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 63.74 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 149 FIARGARVELVPWDKI-------LNPEEfdgLFISNGPGDPKVCKNTVHQIQNIlnnSDK-PIFGICLGHQLLATAIGCK 220
Cdd:PRK08857 19 FCELGAQVKVVRNDEIdidgieaLNPTH---LVISPGPCTPNEAGISLQAIEHF---AGKlPILGVCLGHQAIAQVFGGQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 221 TYKMKYGNRGHNLPCIHhgTGRCFMTSQN--------HGFAVNADTLPKNWE-PLFTNANDFTNE---GIIHNTKPYFSV 288
Cdd:PRK08857 93 VVRARQVMHGKTSPIRH--TGRSVFKGLNnpltvtryHSLVVKNDTLPECFElTAWTELEDGSMDeimGFQHKTLPIEAV 170
|
170
....*....|....*...
gi 86450087 289 QFHPEHTAGPEDLEVLFN 306
Cdd:PRK08857 171 QFHPESIKTEQGHQLLAN 188
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
1012-1156 |
3.92e-11 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 63.04 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1012 GILQPRWKELTNLQSAIEFCEEVGYPCLV---RPSYvlSGAAMNVAYSNEDLEQYLNAAslvsKEYPVVISKFLQEAKEI 1088
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEEL----GDGPVIVEEFVPFDREL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450087 1089 DVDAV-AAEGEILCLAVSEHVEnagvHSGDATLVTPPQDINSETLLKIKEITQDLAALLDVTGPFNMQL 1156
Cdd:pfam02222 78 SVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
146-219 |
1.76e-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: 59.53 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 146 IRCFIARGARVELVPWDK-----ILNPEEFDGLFISNGPGDPKVCKNTVHQIQNILN--NSDKPIFGICLGHQLLATAIG 218
Cdd:cd01653 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPDDLARDEALLALLREaaAAGKPILGICLGAQLLVLGVQ 97
|
.
gi 86450087 219 C 219
Cdd:cd01653 98 F 98
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
173-310 |
1.91e-10 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 61.42 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 173 LFISNGPGDPKVCKNTVHQIQNIlnnSDK-PIFGICLGHQLLATAIGCKTYKMKYGNRG------HNLPCIHHGTGRCFM 245
Cdd:PRK06774 47 LVISPGPCTPNEAGISLAVIRHF---ADKlPILGVCLGHQALGQAFGARVVRARQVMHGktsaicHSGQGVFRGLNQPLT 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450087 246 TSQNHGFAVNADTLPKNWE-PLFTNANDFTNE--GIIHNTKPYFSVQFHPEHTAGPEDLEVLFNvFLE 310
Cdd:PRK06774 124 VTRYHSLVIAADSLPGCFElTAWSERGGEMDEimGIRHRTLPLEGVQFHPESILSEQGHQLLDN-FLK 190
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
168-293 |
4.08e-10 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 61.22 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 168 EEFDGLFISNGPGDPK---VCKNTVHQIQNilnnSDKPIFGICLGHQLLATAIGC-----------KTYKMKYGNRGhnl 233
Cdd:PRK07765 45 AQFDGVLLSPGPGTPEragASIDMVRACAA----AGTPLLGVCLGHQAIGVAFGAtvdrapellhgKTSSVHHTGVG--- 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450087 234 pcIHHGTGRCFMTSQNHGFAVNADTLPKNWEplftnANDFTNEGII----HNTKPYFSVQFHPE 293
Cdd:PRK07765 118 --VLAGLPDPFTATRYHSLTILPETLPAELE-----VTARTDSGVImavrHRELPIHGVQFHPE 174
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
146-213 |
7.19e-10 |
|
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: 57.21 E-value: 7.19e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450087 146 IRCFIARGARVELVPWDK-----ILNPEEFDGLFISNGPGDPKVCKNTVHQIQNILN--NSDKPIFGICLGHQLL 213
Cdd:cd03128 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPDDLAWDEALLALLREaaAAGKPVLGICLGAQLL 92
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
165-316 |
1.22e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 59.43 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 165 LNPeefDGLFISNGPGDPKVCKNTVHQIQNILNNSdkPIFGICLGHQLLATAIGCKTYKM------KYGNRGHNLPCIHH 238
Cdd:PRK07649 42 MKP---DFLMISPGPCSPNEAGISMEVIRYFAGKI--PIFGVCLGHQSIAQVFGGEVVRAerlmhgKTSLMHHDGKTIFS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 239 GTGRCFMTSQNHGFAVNADTLPKNWEplftnANDFTNEG----IIHNTKPYFSVQFHPEHTAGPEDLEVLFNvFLEAVKD 314
Cdd:PRK07649 117 DIPNPFTATRYHSLIVKKETLPDCLE-----VTSWTEEGeimaIRHKTLPIEGVQFHPESIMTSHGKELLQN-FIRKYSP 190
|
..
gi 86450087 315 SI 316
Cdd:PRK07649 191 SV 192
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
168-293 |
3.22e-09 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 57.82 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 168 EEFDGLFISNGPGDPKVCKNTVHQIQNILNNsdKPIFGICLGHQLLATAIGCKTYkmkygnrghNLPCIHHGTGRCFMTS 247
Cdd:PRK06895 42 ENFSHILISPGPDVPRAYPQLFAMLERYHQH--KSILGVCLGHQTLCEFFGGELY---------NLNNVRHGQQRPLKVR 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450087 248 QN----------------HGFAVNADTLPknwEPLFTNANdfTNEGII----HNTKPYFSVQFHPE 293
Cdd:PRK06895 111 SNsplfdglpeefniglyHSWAVSEENFP---TPLEITAV--CDENVVmamqHKTLPIYGVQFHPE 171
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
448-640 |
5.44e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 60.14 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 448 QKYNIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAP-SEAAY-SVHEALYAAKKLGYPVMARAAFSLGGLGSGFANNEE 525
Cdd:PRK08462 98 SHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDGALkSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDES 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 526 ELR--ILAQQALAHSS----QLIIDKSLKGWKEVEYEVVRDAYDNCITV----CNMENldplgiHTGESIVVAPSQTLSN 595
Cdd:PRK08462 178 DLEnlYLAAESEALSAfgdgTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVLDE 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 86450087 596 KEYNMLRTTALKVIRHFGVIGECNIQYALNpESEEYYIIEVNARL 640
Cdd:PRK08462 252 KTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRL 295
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
458-707 |
2.55e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 57.63 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 458 PIESIIQTEDRKIFAERVAEIGEKVAPSEAAYSVHEALYAAKKLGYPVMARAA--------FSLGGLGSGFANNEEELRI 529
Cdd:COG3919 108 DADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 530 LAQQALAHSSQLIIDkslkgwkevEYEVVRDAYDNCITVCNMENLDPLGIHTGESIVVAPSQ--------TLSNKEynmL 601
Cdd:COG3919 188 LLRRIAAAGYELIVQ---------EYIPGDDGEMRGLTAYVDRDGEVVATFTGRKLRHYPPAggnsaareSVDDPE---L 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 602 RTTALKVIRHFGVIGECNIQYALNPESEEYYIIEVNARLSRSSALASKAtGYPLAYVAAKLSLSIPLPEIKNSVTGVTTA 681
Cdd:COG3919 256 EEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREGVLWR 334
|
250 260
....*....|....*....|....*...
gi 86450087 682 CFEPSLDYCVVKIPRW--DLSKFLRVSK 707
Cdd:COG3919 335 VLPGDLLLRYLRDGELrkRLRELLRRGK 362
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
458-640 |
6.78e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 56.69 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 458 PIESIIQTEDRKIFAERVA-EIGEKVAPSEAA--YSVHEALYAAKKLGYPVMARAAFSLGGLGSGFANNEEELRI---LA 531
Cdd:PRK12833 108 PDAQTIRTMGDKARARRTArRAGVPTVPGSDGvvASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpLA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 532 Q---QALAHSSQLIIDKSLKGWKEVEYEVVRDAYDnciTVCNMENLDPLGIHTGESIVVAPSQTLSNKEYNMLRTTALKV 608
Cdd:PRK12833 188 QreaQAAFGDGGVYLERFIARARHIEVQILGDGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRL 264
|
170 180 190
....*....|....*....|....*....|..
gi 86450087 609 IRHFGVIGECNIQYALNPESEEYYIIEVNARL 640
Cdd:PRK12833 265 ARQVGYRGAGTLEYLFDDARGEFYFIEMNTRI 296
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
165-306 |
9.93e-08 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 53.38 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 165 LNPEEfdgLFISNGPGDPKVCKNTVHQIQNILNNSdkPIFGICLGHQLLATAIGCKTYKMKYGNRGHNLPCIHHGTG--- 241
Cdd:PRK08007 42 LKPQK---IVISPGPCTPDEAGISLDVIRHYAGRL--PILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGvfr 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 242 ---RCFMTSQNHGFAVNADTLPKNWEplfTNANDFTNE--GIIHNTKPYFSVQFHPEHTAGPEDLEVLFN 306
Cdd:PRK08007 117 glaNPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGVQFHPESILSEQGHQLLAN 183
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
345-739 |
1.45e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 55.49 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 345 MPKKILILGSGGLSIgqagefdysgsQAIKALKEEKIQTVLINPNIATVQTSKGLADK-VYFLPLTPE--Y--VEQVIrs 419
Cdd:PRK05586 1 MFKKILIANRGEIAV-----------RIIRACREMGIETVAVYSEADKDALHVQLADEaVCIGPASSKdsYlnIQNII-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 420 erpSGVLLTfgGQTALNCGVE-LQKNGVFQKY----NIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAP-SEAAY-SVH 492
Cdd:PRK05586 68 ---SATVLT--GAQAIHPGFGfLSENSKFAKMckecNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPgSEGEIeNEE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 493 EALYAAKKLGYPVMARAAFSLGGLGSGFANNEEELRILAQQALAHSS------QLIIDKSLKGWKEVEYEVVRDAYDNCI 566
Cdd:PRK05586 143 EALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKaafgddSMYIEKFIENPKHIEFQILGDNYGNVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 567 TV----CNMENldplgiHTGESIVVAPSQTLSNKEYNMLRTTALKVIRHFGVIGECNIQYALNpESEEYYIIEVNARLSR 642
Cdd:PRK05586 223 HLgerdCSLQR------RNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTRIQV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 643 SSALASKATGYPLA----YVAAKLSLSIPLPEIKnsVTGVTTAC----------FEPS----------------LD---Y 689
Cdd:PRK05586 296 EHPITEMITGVDLVkeqiKIAYGEKLSIKQEDIK--INGHSIECrinaedpkngFMPCpgkieelyipgglgvrVDsavY 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 86450087 690 CVVKIPR-WDlskflrvsknigsSMksVGEVMSIGRNFEEAFQKALRMVDE 739
Cdd:PRK05586 374 SGYTIPPyYD-------------SM--IGKLIVYGKDREEAIQKMKRALGE 409
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
345-572 |
1.52e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 55.76 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 345 MPKKILILGSGGLSIgqagefdysgsQAIKALKEEKIQTVLINPNIATVQTSKGLADKVYFL---PLTPEY--VEQVIrs 419
Cdd:PRK08654 1 MFKKILIANRGEIAI-----------RVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIgpaPPSKSYlnIERII-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 420 erpsgvlltfggQTALNCGVE--------LQKNGVF----QKYNIQIMGtPIESIIQTEDRKIFAERV-AEIGEKVAP-- 484
Cdd:PRK08654 68 ------------DVAKKAGADaihpgygfLAENPEFakacEKAGIVFIG-PSSDVIEAMGSKINAKKLmKKAGVPVLPgt 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 485 SEAAYSVHEALYAAKKLGYPVMARAAFSLGGLGSGFANNEEELR--ILAQQALAHS----SQLIIDKSLKGWKEVEYEVV 558
Cdd:PRK08654 135 EEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEdaIESTQSIAQSafgdSTVFIEKYLEKPRHIEIQIL 214
|
250
....*....|....
gi 86450087 559 RDAYDNCITVCNME 572
Cdd:PRK08654 215 ADKHGNVIHLGDRE 228
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
490-672 |
2.02e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 55.11 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 490 SVHEALYAAKKLGYPVMARAAFSLGGLGSGFANNEEEL-----RIL--AQQALAhSSQLIIDKSLKGWKEVEYEVVRDAY 562
Cdd:PRK07178 139 DLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELeqnfpRVIseATKAFG-SAEVFLEKCIVNPKHIEVQILADSH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 563 DNCITV----CNMENldplgiHTGESIVVAPSQTLSNKEYNMLRTTALKVIRHFGVIGECNIQYALNPESeEYYIIEVNA 638
Cdd:PRK07178 218 GNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADG-EVYFMEMNT 290
|
170 180 190
....*....|....*....|....*....|....*...
gi 86450087 639 RLSRSSALASKATGYPLAY----VAAKLSLSIPLPEIK 672
Cdd:PRK07178 291 RVQVEHTITEEITGIDIVReqirIASGLPLSYKQEDIQ 328
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
163-310 |
2.75e-07 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 52.43 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 163 KILNPEefdGLFISNGPGDPKvckNTVHQIQNILNNSDK-PIFGICLGHQLLATAIGCKTYKMKYGNRGhNLPCIHHGTG 241
Cdd:CHL00101 40 KNLNIR---HIIISPGPGHPR---DSGISLDVISSYAPYiPILGVCLGHQSIGYLFGGKIIKAPKPMHG-KTSKIYHNHD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 242 RCFMTSQN-------HGFAVNADTLPknwEPLFTNAndFTNEGII----HNTKPY-FSVQFHPEHTAGPEDLEVLFNvFL 309
Cdd:CHL00101 113 DLFQGLPNpftatryHSLIIDPLNLP---SPLEITA--WTEDGLImacrHKKYKMlRGIQFHPESLLTTHGQQILRN-FL 186
|
.
gi 86450087 310 E 310
Cdd:CHL00101 187 S 187
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
170-341 |
6.47e-07 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 54.08 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 170 FDGLFISNGPGDPKVCKNTVHQIQNILNNSDKPIFGICLGHQLLATAIGC-----------KTYKMKY-GNR-GHNLPci 236
Cdd:PLN02889 132 FDNIVISPGPGSPTCPADIGICLRLLLECRDIPILGVCLGHQALGYVHGArivhapepvhgRLSEIEHnGCRlFDDIP-- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 237 hHGTGRCFMTSQNHGFAVNADTLPKNWEPL-FTNAND-----------------------------FTNE---------- 276
Cdd:PLN02889 210 -SGRNSGFKVVRYHSLVIDAESLPKELVPIaWTSSSDtlsflesqksglvpdayesqigqsgssdpFSSKlkngtswpss 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86450087 277 ------------GIIHNTKPYFSVQFHPEHTAGPEDLEvLFNVFLEAVKDSIEKKSNGSVKEKLIKTLSFTVAPNSI 341
Cdd:PLN02889 289 hsermqngkilmGIMHSTRPHYGLQFHPESIATCYGRQ-IFKNFREITQDYWLRLRSTSLRRRNSNLTANMQVPDAS 364
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
200-293 |
8.63e-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: 51.49 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 200 DKPIFGICLGHQLLATAIGCKTY---KMKYGNRGHNLPC----------IHHGTGRCF--MTSQN-------HGFAVnaD 257
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshaVNVEPGSLLasLLGSEefrvnslHHQAI--D 182
|
90 100 110
....*....|....*....|....*....|....*...
gi 86450087 258 TLPKNWEPLFTnANDFTNEGI--IHNTKPYFSVQFHPE 293
Cdd:pfam07722 183 RLAPGLRVEAV-APDGTIEAIesPNAKGFALGVQWHPE 219
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
163-321 |
1.85e-06 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 50.57 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 163 KILNPEefdGLFISNGPGDPK---VCKNTVHQIqnilnNSDKPIFGICLGHQLLATAIGCKTYKMKYG-NRGHNLPCIH- 237
Cdd:PLN02335 59 KRKNPR---GVLISPGPGTPQdsgISLQTVLEL-----GPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYd 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 238 --------HGTGRCFMTSQNHGFAVNADTLPKnwEPLFTNAndFTNEGII----HNTKPYFS-VQFHPEHTAGPEDLEVL 304
Cdd:PLN02335 131 ekgeeglfSGLPNPFTAGRYHSLVIEKDTFPS--DELEVTA--WTEDGLImaarHRKYKHIQgVQFHPESIITTEGKTIV 206
|
170
....*....|....*..
gi 86450087 305 FNvFLEAVKDSIEKKSN 321
Cdd:PLN02335 207 RN-FIKIIEKKESEKLT 222
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
469-640 |
1.92e-06 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 52.45 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 469 KIFAERVA-EIGEKVAPS--EAAYSVHEALYAAKKLGYPVMARAAFSLGGLGSGFANNEEELR--ILAQQALAHSS---- 539
Cdd:PRK12999 120 KVAARNAAiKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEeaFERAKREAKAAfgnd 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 540 QLIIDKSLKGWKEVEYEVVRDAYDNCitvcnmenldplgIHTGE---SI------VV--APSQTLSNKEYNMLRTTALKV 608
Cdd:PRK12999 200 EVYLEKYVENPRHIEVQILGDKHGNV-------------VHLYErdcSVqrrhqkVVeiAPAPGLSEELRERICEAAVKL 266
|
170 180 190
....*....|....*....|....*....|..
gi 86450087 609 IRHFGVIGECNIQYALNPESeEYYIIEVNARL 640
Cdd:PRK12999 267 ARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
150-295 |
5.47e-06 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 50.43 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 150 IARgaRV-------ELVPWD------KILNPeefDGLFISNGP------GDPKVckntvhqIQNILNnSDKPIFGICLGH 210
Cdd:PRK00074 19 IAR--RVrelgvysEIVPYDisaeeiRAFNP---KGIILSGGPasvyeeGAPRA-------DPEIFE-LGVPVLGICYGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 211 QLLATAIGCK---TYKMKYGN---RGHNLPCIHHGTGR---CFMtsqNHGFAVNAdtLPKNWEPLFTNANDfTNEGIIHN 281
Cdd:PRK00074 86 QLMAHQLGGKverAGKREYGRaelEVDNDSPLFKGLPEeqdVWM---SHGDKVTE--LPEGFKVIASTENC-PIAAIANE 159
|
170
....*....|....*.
gi 86450087 282 TKPYFSVQFHPE--HT 295
Cdd:PRK00074 160 ERKFYGVQFHPEvtHT 175
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
452-640 |
5.83e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 50.19 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 452 IQIMGTpiesiiqtedrKIFAERVA-EIGEKVAP-SEAA-YSVHEALYAAKKLGYPVMARAAFSLGGLGSGFANNEEELR 528
Cdd:PRK08591 110 IRLMGD-----------KVTAKATMkKAGVPVVPgSDGPvDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 529 ILAQQALAHS------SQLIIDKSLKGWKEVEYEVVRDAYDNcitvcnmenldplGIHTGE---SI------VV--APSQ 591
Cdd:PRK08591 179 KAFSMARAEAkaafgnPGVYMEKYLENPRHIEIQVLADGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSP 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 86450087 592 TLSNKEYNMLRTTALKVIRHFGVIGECNIQYaLNPESEEYYIIEVNARL 640
Cdd:PRK08591 246 AITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKNGEFYFIEMNTRI 293
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
988-1094 |
1.03e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 49.60 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 988 LGTSPESIDSAENRFKFSRMLDRKG--ILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNEDLEQYLN 1065
Cdd:PRK08654 103 IGPSSDVIEAMGSKINAKKLMKKAGvpVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIE 182
|
90 100 110
....*....|....*....|....*....|...
gi 86450087 1066 AASLVSKEY----PVVISKFLQEAKEIDVDAVA 1094
Cdd:PRK08654 183 STQSIAQSAfgdsTVFIEKYLEKPRHIEIQILA 215
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1011-1150 |
5.75e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 45.77 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1011 KGILQPRWKELTNLQSAiEFCEEVGYPCLVRPSYVLSGAAMNVAYSNEDLEQYLNAAslVSKEYPVVISKFLqEAKEIDV 1090
Cdd:pfam07478 13 VTFTRADWKLNPKEWCA-QVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEA--FQYDEKVLVEEGI-EGREIEC 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450087 1091 dAVAAEGEILCLAVSEHVENAGV------HSGDATLVTPPQDINSETLLKIKEITQDLAALLDVTG 1150
Cdd:pfam07478 89 -AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRG 153
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
991-1150 |
6.38e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 46.61 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 991 SPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPS---------YVLSGAamnvaysnEDLE 1061
Cdd:COG0026 80 GPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggydgkgqVVIKSA--------ADLE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1062 QYLNAASLVskeyPVVISKFLQEAKEIDVDAV-AAEGEILCLAVsehVENagVH-SGDATLVTPPQDINSETLLKIKEIT 1139
Cdd:COG0026 152 AAWAALGGG----PCILEEFVPFERELSVIVArSPDGEVATYPV---VEN--VHrNGILDESIAPARISEALAAEAEEIA 222
|
170
....*....|.
gi 86450087 1140 QDLAALLDVTG 1150
Cdd:COG0026 223 KRIAEALDYVG 233
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
432-655 |
3.20e-04 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 44.80 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 432 QTALNCGVE--------LQKNGVFQKY----NIQIMGTPIESIIQTEDRKIFAERVAEIGEKVAPSEA---AYSVHEALY 496
Cdd:PRK08463 67 EIAKACGADaihpgygfLSENYEFAKAvedaGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEklnSESMEEIKI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 497 AAKKLGYPVMARAAFSLGGLGSGFANNEEEL----RILAQQALAH--SSQLIIDKSLKGWKEVEYEVVRDAYDNCITVCn 570
Cdd:PRK08463 147 FARKIGYPVILKASGGGGGRGIRVVHKEEDLenafESCKREALAYfnNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLC- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 571 mENLDPLGIHTGESIVVAPSQTLSNKEYNMLRTTALKVIRHFGVIGECNIQYALNpESEEYYIIEVNARLSRSSALASKA 650
Cdd:PRK08463 226 -ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD-DYNRFYFMEMNTRIQVEHGVTEEI 303
|
....*
gi 86450087 651 TGYPL 655
Cdd:PRK08463 304 TGIDL 308
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1032-1137 |
4.32e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 44.05 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 1032 EEVGYPCLVRPSYVLSGAAMNVAYSNEDLEQYLNAAslVSKEYPVVISKFLqEAKEIDVDAVAAE-------GEILC--L 1102
Cdd:PRK14570 168 EVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEA--FKYDLTVVIEKFI-EAREIECSVIGNEqikiftpGEIVVqdF 244
|
90 100 110
....*....|....*....|....*....|....*
gi 86450087 1103 AVSEHVENAGVHSGDATLVTPPQDINSETLLKIKE 1137
Cdd:PRK14570 245 IFYDYDAKYSTIPGNSIVFNIPAHLDTKHLLDIKE 279
|
|
| PfpI |
TIGR01382 |
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ... |
165-216 |
4.54e-04 |
|
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273591 [Multi-domain] Cd Length: 166 Bit Score: 42.40 E-value: 4.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 86450087 165 LNPEEFDGLFISNGPGDPKVCKNT-VHQIQNILNNSDKPIFGICLGHQLLATA 216
Cdd:TIGR01382 56 VNPEEYDALVIPGGRAPEYLRLNNkAVRLVREFVEKGKPVAAICHGPQLLISA 108
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
469-639 |
6.18e-04 |
|
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: 44.30 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 469 KIFAERVA-EIGEKVAPS--EAAYSVHEALYAAKKLGYPVMARAAFSLGGLGSGFANNEEELRILAQQAL--AHSS---- 539
Cdd:COG1038 119 KVAARAAAiEAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARreAKAAfgdd 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450087 540 QLIIDKSLKGWKEVEYEVVRDAYDNCitvcnmenldplgIHTGE---SI------VV--APSQTLSNKEYNMLRTTALKV 608
Cdd:COG1038 199 EVFLEKYIERPKHIEVQILGDKHGNI-------------VHLFErdcSVqrrhqkVVeiAPAPNLDEELREAICEAAVKL 265
|
170 180 190
....*....|....*....|....*....|....*.
gi 86450087 609 IRHfgvIGECNiqyA-----LNPESEEYYIIEVNAR 639
Cdd:COG1038 266 AKA---VGYVN---AgtvefLVDDDGNFYFIEVNPR 295
|
|
| PRK08250 |
PRK08250 |
glutamine amidotransferase; Provisional |
166-220 |
6.86e-04 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181323 [Multi-domain] Cd Length: 235 Bit Score: 42.65 E-value: 6.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450087 166 NPEEFDGLFISNGPGDPKVC---------KNTVHQIQNILNnSDKPIFGICLGHQLLATAIGCK 220
Cdd:PRK08250 42 NADGFDLLIVMGGPQSPRTTreecpyfdsKAEQRLINQAIK-AGKAVIGVCLGAQLIGEALGAK 104
|
|
| GATase1_PfpI_1 |
cd03169 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
152-216 |
1.76e-03 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.
Pssm-ID: 153243 [Multi-domain] Cd Length: 180 Bit Score: 40.71 E-value: 1.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86450087 152 RGARVEL-VPWDKIlNPEEFDGLFISNGPG------DPKVCKNTVHqiqniLNNSDKPIFGICLGHQLLATA 216
Cdd:cd03169 59 PGHRFAVtADFDEV-DPDDYDALVIPGGRApeylrlDEKVLAIVRH-----FAEANKPVAAICHGPQILAAA 124
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
991-1042 |
2.83e-03 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 41.18 E-value: 2.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 86450087 991 SPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRP 1042
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKP 130
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
199-224 |
7.70e-03 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 39.54 E-value: 7.70e-03
10 20
....*....|....*....|....*.
gi 86450087 199 SDKPIFGICLGHQLLATAIGCKTYKM 224
Cdd:PRK07053 82 AGLPTLGICLGAQLIARALGARVYPG 107
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
605-679 |
9.48e-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: 37.59 E-value: 9.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450087 605 ALKVIRHFGVIGECNIQYALNpeSEEYYIIEVNARLsrSSALA-SKATGYPLAYVAAKLSLSIPLPEIKNSVTGVT 679
Cdd:pfam15632 53 ARRLAEAFGLDGLFNVQFRYD--GDGPKLLEINPRM--SGGIGySCLAGVNLPYLALKLLLGLETPDPVEPRLGLR 124
|
|
| |
