|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
403-1455 |
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: 1637.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 403 PRKVLILGSGGLSIGQAGEFDYSGSQAIKAMRESNIQTVLINPNIATVQTSKGMADKCYFLPLTPHYVEQVIKSERPNGV 482
Cdd:TIGR01369 6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 483 LLTFGGQTALNCGVQLERAGVFSKYNVRILGTPIQSIIETEDRKLFAERVNEIGEQVAPSEAVYSVAQALDAASRLGYPV 562
Cdd:TIGR01369 86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 563 MARAAFSLGGLGSGFANNEEELQSLAQQALAHS--SQLIVDKSLKGWKEVEYEVVRDAYNNCITVCNMENFDPLGIHTGE 640
Cdd:TIGR01369 166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 641 SIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYALCPHSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLA 720
Cdd:TIGR01369 246 SIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 721 LGLPLPDIKNSVTGNTTACFEPSLDYCVVKIPRWDLAKFVRVSKHIGSSMKSVGEVMAIGRNFEEAFQKALRMVDSDVLG 800
Cdd:TIGR01369 326 VGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 801 FD-PDVVPLNKEQLAEQLSEPTDRRPFVIAAALQLGMSLRELHQLTNIDYWFLEKLERII-LLQSLLTRNGSRTDAALLL 878
Cdd:TIGR01369 406 FDlPDREVEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVdLEEELEEVKLTDLDPELLR 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 879 KAKRFGFSDKQIAKYIKSTELAVRHQRQEFGIRPHVKQIDTVAGEWPASTNYLYHTYNGSEHDVDFPGGHTIVV-GSGVY 957
Cdd:TIGR01369 486 RAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSGPN 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 958 RIGSSVEFDWCAVGCLRELRKLQRPTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYEMENSEGIILSMGGQLPNNI 1037
Cdd:TIGR01369 566 RIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLNL 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1038 AMDLHRQQAKVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYS 1117
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYN 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1118 NQDLETYLNAASEVSREHPVVISKFLTEAKEIDVDAVASDGRILCMAVSEHVENAGVHSGDATLVTPPQDLNAETLEAIK 1197
Cdd:TIGR01369 726 EEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIK 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1198 RITCDLASVLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLDHDFVATATRAIVGLDVEPLDVL--HGVGKVGV 1275
Cdd:TIGR01369 806 DIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEPKYVAV 885
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1276 KVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKNAVLLSIGSFKHKMELLPSIRDLAKMGYK 1355
Cdd:TIGR01369 886 KEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKGYK 965
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1356 LYASMGTGDFYAEHGVNVESVQWTFDKTtpddingelRHLAEFLANKQFDLVINLPMSGGGARRVssfmthGYRTRRLAV 1435
Cdd:TIGR01369 966 LYATEGTAKFLGEAGIKPELVLKVSEGR---------PNILDLIKNGEIELVINTTSKGAGTATD------GYKIRREAL 1030
|
1050 1060
....*....|....*....|
gi 665391904 1436 DYSIPLVTDVKCTKLLVESM 1455
Cdd:TIGR01369 1031 DYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
402-1456 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1425.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 402 MPR-----KVLILGSGGLSIGQAGEFDYSGSQAIKAMRESNIQTVLINPNIATVQTSKGMADKCYFLPLTPHYVEQVIKS 476
Cdd:PRK05294 1 MPKrtdikKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 477 ERPNGVLLTFGGQTALNCGVQLERAGVFSKYNVRILGTPIQSIIETEDRKLFAERVNEIGEQVAPSEAVYSVAQALDAAS 556
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 557 RLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQALAHS--SQLIVDKSLKGWKEVEYEVVRDAYNNCITVCNMENFDPL 634
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 635 GIHTGESIVVAPSQTLSDREYQMLRSTALKVIRHFGVV-GECNIQYALCPHSEQYYIIEVNARLSRSSALASKATGYPLA 713
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 714 YVAAKLALGLPLPDIKNSVTGNTTACFEPSLDYCVVKIPRWDLAKFVRVSKHIGSSMKSVGEVMAIGRNFEEAFQKALRM 793
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 794 VDSDVLGFDPDVV-PLNKEQLAEQLSEPTDRRPFVIAAALQLGMSLRELHQLTNIDYWFLEKLERIILLQSLLTRNGSRT 872
Cdd:PRK05294 401 LEIGVTGLDEDLFeEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 873 DAALLLKAKRFGFSDKQIAKYIKSTELAVRHQRQEFGIRPHVKQIDTVAGEWPASTNYLYHTYNGsEHDVDfPGGHT--I 950
Cdd:PRK05294 481 DAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEE-ECESN-PSDRKkvL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 951 VVGSGVYRIGSSVEFDWCAVGCLRELRKLQRPTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYEMENSEGIILSMG 1030
Cdd:PRK05294 559 VLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1031 GQLPNNIAMDLHRQQAKVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGA 1110
Cdd:PRK05294 639 GQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGR 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1111 AMNVAYSNQDLETYLNAASEVSREHPVVISKFLTEAKEIDVDAVaSDG-RILCMAVSEHVENAGVHSGDATLVTPPQDLN 1189
Cdd:PRK05294 719 AMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGeDVLIGGIMEHIEEAGVHSGDSACSLPPQTLS 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1190 AETLEAIKRITCDLASVLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLDHDFVATATRAIVGLDVEPLDVLHG 1269
Cdd:PRK05294 798 EEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKG 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1270 V--GKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKN-AVLLSIGSfKHKMELLPSI 1346
Cdd:PRK05294 878 LipPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSVRD-RDKEEVVELA 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1347 RDLAKMGYKLYASMGTGDFYAEHGVNVESVqwtfdkttpDDINGELRHLAEFLANKQFDLVINLPmSGGGARRvssfmtH 1426
Cdd:PRK05294 957 KRLLELGFKILATSGTAKFLREAGIPVELV---------NKVHEGRPHIVDLIKNGEIDLVINTP-TGRQAIR------D 1020
|
1050 1060 1070
....*....|....*....|....*....|
gi 665391904 1427 GYRTRRLAVDYSIPLVTDVKCTKLLVESMR 1456
Cdd:PRK05294 1021 GFSIRRAALEYKVPYITTLAGARAAVKAIE 1050
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
402-1455 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1083.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 402 MPR-----KVLILGSGGLSIGQAGEFDYSGSQAIKAMRESNIQTVLINPNIATVQTSKGMADKCYFLPLTPHYVEQVIKS 476
Cdd:PRK12815 1 MPKdtdiqKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 477 ERPNGVLLTFGGQTALNCGVQLERAGVFSKYNVRILGTPIQSIIETEDRKLFAERVNEIGEQVAPSEAVYSVAQALDAAS 556
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 557 RLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQALAHS--SQLIVDKSLKGWKEVEYEVVRDAYNNCITVCNMENFDPL 634
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASpiHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 635 GIHTGESIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYALCPHSEQYYIIEVNARLSRSSALASKATGYPLAY 714
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 715 VAAKLALGLPLPDIKNSVTGNTTACFEPSLDYCVVKIPRWDLAKFVRVSKHIGSSMKSVGEVMAIGRNFEEAFQKALRMV 794
Cdd:PRK12815 321 IAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 795 DSDVLGFDPDVV--PLNKEQLAEQLSEPTDRRPFVIAAALQLGMSLRELHQLTNIDYWFLEKLERIILLQSLLTRNGSRT 872
Cdd:PRK12815 401 EIKRNGLSLPIElsGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 873 DAALLLKAKRFGFSDKQIAKYIKSTELAVRHQRQEFGIRPHVKQIDTVAGEWPASTNYLYHTYNGsEHDVDFPGGH--TI 950
Cdd:PRK12815 481 SADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFG-ESEAEPSSEKkkVL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 951 VVGSGVYRIGSSVEFDWCAVGCLRELRKLQRPTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYEMENSEGIILSMG 1030
Cdd:PRK12815 560 ILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFG 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1031 GQLPNNIAMDLHRQQAKVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGA 1110
Cdd:PRK12815 640 GQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQ 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1111 AMNVAYSNQDLETYLnaASEVSREHPVVISKFLtEAKEIDVDAVaSDGR-ILCMAVSEHVENAGVHSGDATLVTPPQDLN 1189
Cdd:PRK12815 720 GMAVVYDEPALEAYL--AENASQLYPILIDQFI-DGKEYEVDAI-SDGEdVTIPGIIEHIEQAGVHSGDSIAVLPPQSLS 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1190 AETLEAIKRITCDLASVLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLDHDFVATATRAIVGL----DVEPLD 1265
Cdd:PRK12815 796 EEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKslaeLGYPNG 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1266 VLHGVGKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKNAVLLSIGSFKHKMELLPS 1345
Cdd:PRK12815 876 LWPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKL 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1346 IRDLAKMGYKLYASMGTGDFYAEHGVNVESVQwtfdkttpdDINGELRHLAEFLANKQFDLVINLPMSGGGARrvssfmt 1425
Cdd:PRK12815 956 ARRFAQLGFKLLATEGTANWLAEEGITTGVVE---------KVQEGSPSLLERIKQHRIVLVVNTSLSDSASE------- 1019
|
1050 1060 1070
....*....|....*....|....*....|
gi 665391904 1426 HGYRTRRLAVDYSIPLVTDVKCTKLLVESM 1455
Cdd:PRK12815 1020 DAIKIRDEALSTHIPVFTELETAQAFLQVL 1049
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
404-1456 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 887.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 404 RKVLILGSGGLSIGQAGEFDYSGSQAIKAMRESNIQTVLINPNIATVQTSKGMADKCYFLPLTPHYVEQVIKSERPNGVL 483
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 484 LTFGGQTALNCGVQLERAGVFSKYNVRILGTPIQSIIETEDRKLFAERVNEIGEQVAPSEAVYSVAQALDAASRLG-YPV 562
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 563 MARAAFSLGGLGSGFANNEEELQSLAQQALAHS--SQLIVDKSLKGWKEVEYEVVRDAYNNCITVCNMENFDPLGIHTGE 640
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAASitSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 641 SIVVAPSQTLSDREYQMLRSTALKVIRHFGVvgEC---NIQYALCPHSEQYYIIEVNARLSRSSALASKATGYPLAYVAA 717
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 718 KLALGLPLPDIKNSVTGNTTACFEPSLDYCVVKIPRWDLAKFVRVSKHIGSSMKSVGEVMAIGRNFEEAFQKALRMVDSD 797
Cdd:PLN02735 342 KLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 798 VLGFDPDVV---PLNKEQLAEQLSEPTDRRPFVIAAALQLGMSLRELHQLTNIDYWFLEKLERII-LLQSLLTRNGSRTD 873
Cdd:PLN02735 422 FSGWGCAKVkelDWDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVdVEQFLKSRSLSELS 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 874 AALLLKAKRFGFSDKQIAKYIKSTELAVRHQRQEFGIRPHVKQIDTVAGEWPASTNYLYHTYNGSEHDVDFPGGHTIVVG 953
Cdd:PLN02735 502 KDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLILG 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 954 SGVYRIGSSVEFDWCAVGCLRELRKLQRPTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYEMENSEGIILSMGGQL 1033
Cdd:PLN02735 582 GGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGGQT 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1034 PNNIAMDLHRQ-------------QAKVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCL 1100
Cdd:PLN02735 662 PLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYPVV 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1101 VRPSYVLSGAAMNVAYSNQDLETYLNAASEVSREHPVVISKFLTEAKEIDVDAVA-SDGRILCMAVSEHVENAGVHSGDA 1179
Cdd:PLN02735 742 VRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSGDS 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1180 TLVTPPQDLNAETLEAIKRITCDLASVLDVTGPFNMQL-IAKNNELKVIECNVRVSRSFPFVSKTLDHDFVATATRAIVG 1258
Cdd:PLN02735 822 ACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSG 901
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1259 LDVEPLDVLHGV--GKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKNA-VLLSIGS 1335
Cdd:PLN02735 902 KSLKDLGFTEEVipAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGtVFISLND 981
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1336 fKHKMELLPSIRDLAKMGYKLYASMGTGDFYAEHGVNVESVQwtfdkttpdDINGELRHLAEFLANKQFDLVInLPMSGG 1415
Cdd:PLN02735 982 -LTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVL---------KLHEGRPHAGDMLANGQIQLMV-ITSSGD 1050
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 665391904 1416 GARrvssfMTHGYRTRRLAVDYSIPLVTDVKCTKLLVESMR 1456
Cdd:PLN02735 1051 ALD-----QKDGRQLRRMALAYKVPIITTVAGALATAQAVK 1086
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
409-954 |
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: 658.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 409 LGSGGLSIGQAGEFDYSGSQAIKAMRESNIQTVLINPNIATVQTSKGMADKCYFLPLTPHYVEQVIKSERPNGVLLTFGG 488
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 489 QTALNCGVQLERAGVFSkyNVRILGTPIQSIIETEDRKLFAERVNEIGEQVAPSEAVYSVAQALDAASRLGYPVMARAAF 568
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 569 SLGGLGSGFANNEEELQSLAQQALAHS--SQLIVDKSLKGWKEVEYEVVRDAYNNCITVCNMENFDPLGIHTGESIVVAP 646
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 647 SQTLSDREYQMLRSTALKVIRHFGVVGECNIQYALcpHSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGLPLP 726
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAV--DDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 727 DIKNSvTGnttacFEPSLDYCVVKIPRWDLAKFVRVSKHIGSSMKSVGEVMAIGRNFEEAFQKALRMVDSDVLG--FDPD 804
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 805 VvpLNKEQLAEQLSEPTDRRPFVIAAALQLGMSLRELHQLTNIDYWFLEKLERIILLqsLLTRNGSRTDAALLLKAKRFG 884
Cdd:COG0458 391 V--ADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVD--EIELEEIILVINTLLGAKSLG 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 885 FSDKQIAKYIKSTELAVRHQRQEFGIRPHVKQIDTVAGEWPASTNYLYHTYNGSEHDVDFPGGHTIVVGS 954
Cdd:COG0458 467 DSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
1475-1821 |
0e+00 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 644.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1475 RIVKLPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASD 1554
Cdd:cd01316 1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1555 DNWAQVNELASHACGLKMYLNDTFGTLKLSDMTSWQRHLSHWPKRSPIVCHAERQSTAAVIMLAHLLDRSVHICHVARKE 1634
Cdd:cd01316 81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1635 EIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERlghGMSEVRPLLCSPEDQEALWENIDYIDVFATDHAPHTLAEKRSER 1714
Cdd:cd01316 161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR---GQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1715 PPPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNLPDQAQTYVEVDLDEEWTITGNEMKSKSGWTPFEGTKV 1794
Cdd:cd01316 238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317
|
330 340
....*....|....*....|....*..
gi 665391904 1795 KGRVHRVVLRGEVAFVDGQVLVQPGFG 1821
Cdd:cd01316 318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
952-1457 |
7.54e-165 |
|
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: 517.89 E-value: 7.54e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 952 VGSGVYRIGSSVEFDWCAVGCLRELRKLQRPTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYEMENSEGIILSMGG 1031
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1032 QLPNNIAMDLHRQQA----KVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVL 1107
Cdd:COG0458 81 QTALNLAVELEEAGIlegvKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1108 SGAAMNVAYSNQDLETYLNAASEVSREHPVVISKFLTEAKEIDVDAVA-SDGRILCMAVSEHVENAGVHSGDATLVTPPQ 1186
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRdGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1187 DLNAETLEAIKRITCDLASVLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKtldhdfvAT-------ATRAIVGL 1259
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASK-------ATgypiakiAAKLALGY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1260 DVEPLDVLHGV----GKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPkNAVLLSIGS 1335
Cdd:COG0458 314 TLDELGNDTGFeptlDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP-GTVLLSLVA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1336 FKHKMELLPSIRDLAKMGYKLYASMGTGDFYAEHGVnvesvqwtfDKTTPDDINGELRHLAEFLANKQFDLVINLPMSGG 1415
Cdd:COG0458 393 DDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGI---------TVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAK 463
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 665391904 1416 GARRvssfmthGYRTRRLAVDYSIPLVTDVKCTKLLVESMRM 1457
Cdd:COG0458 464 SLGD-------SDGIIRRALAAKVPYVTTLAAAAAAALAIKA 498
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
7-376 |
1.75e-157 |
|
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: 489.83 E-value: 1.75e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 7 YLALEDGTVLPGYSFGYvpsenesKVGFGGEVVFQTGMVGYTEALTDRSYSGQILVLTYPLIGNYGVPAPDedehglplh 86
Cdd:TIGR01368 2 YLVLEDGTVFRGYSFGA-------EGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDED--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 87 FEWMKgvVQATALVVGEVAEEAFHWRKWKTLPDWLKQHKVPGIQDIDTRALTKKLREQGSMLGKIVYEKPPVEGLPKSSF 166
Cdd:TIGR01368 66 AESKG--IHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 167 VDPNVR--NLAKECSVKERQVYGNPNGKGPRIAILDCGLKLNQLRCLLQRGASVTLLPWSARLED---EQFDALFLSNGP 241
Cdd:TIGR01368 144 VSPDITgiNLVAEVSTKEPYTWGQRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEikkYNPDGIFLSNGP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 242 GNPESCDQIVQQVRKVIEegQKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPCLHRATGRCLMTSQNHGYAVDLEQL 321
Cdd:TIGR01368 224 GDPAAVEPAIETIRKLLE--KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 665391904 322 P-DGWSELFVNANDGTNEGIVHASKPYFSVQFHPEHHAGPQDTEFLFDVFMESIQQ 376
Cdd:TIGR01368 302 PaGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
7-374 |
6.72e-156 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 485.73 E-value: 6.72e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 7 YLALEDGTVLPGYSFGYvpsENESkvgfGGEVVFQTGMVGYTEALTDRSYSGQILVLTYPLIGNYGVPapDEDehglplh 86
Cdd:PRK12564 6 YLVLEDGTVFEGKAFGA---EGET----VGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVN--RED------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 87 FEWMKgvVQATALVVGEVAEEAFHWRKWKTLPDWLKQHKVPGIQDIDTRALTKKLREQGSMLGKIVYEKPPVEGLPK--S 164
Cdd:PRK12564 70 FESDR--PHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEkaR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 165 SFVDPNVRNLAKECSVKER-QVYGNPNGKGPRIAILDCGLKLNQLRCLLQRGASVTLLPWSARLED---EQFDALFLSNG 240
Cdd:PRK12564 148 AFPGLLGLDLVKEVSTKEPyPWPGPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEilaLNPDGVFLSNG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 241 PGNPESCDQIVQQVRKVIEEGqKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPCLHRATGRCLMTSQNHGYAVDLEQ 320
Cdd:PRK12564 228 PGDPAALDYAIEMIRELLEKK-IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDS 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 665391904 321 LPDGWSELFVNANDGTNEGIVHASKPYFSVQFHPEHHAGPQDTEFLFDVFMESI 374
Cdd:PRK12564 307 LPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
7-375 |
1.80e-152 |
|
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: 476.05 E-value: 1.80e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 7 YLALEDGTVLPGYSFGYvpsENESkvgfGGEVVFQTGMVGYTEALTDRSYSGQILVLTYPLIGNYGVPapDEDehglplh 86
Cdd:COG0505 6 LLVLEDGTVFEGKSFGA---EGET----VGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVN--DED------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 87 FEWMKgvVQATALVVGEVAEEAFHWRKWKTLPDWLKQHKVPGIQDIDTRALTKKLREQGSMLGKIVYEKPPVEGLPK--S 164
Cdd:COG0505 70 FESDR--PWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEkaR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 165 SFVDPNVRNLAKECSVKERQVYGNPNGKGPRIAILDCGLKLNQLRCLLQRGASVTLLPWSARLED---EQFDALFLSNGP 241
Cdd:COG0505 148 AAPGMEGLDLVKEVSTKEPYEWTEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEilaLNPDGVFLSNGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 242 GNPESCDQIVQQVRKVIEEGqKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPCLHRATGRCLMTSQNHGYAVDLEQL 321
Cdd:COG0505 228 GDPAALDYAIETIRELLGKG-IPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSL 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 665391904 322 PD-GWSELFVNANDGTNEGIVHASKPYFSVQFHPEHHAGPQDTEFLFDVFMESIQ 375
Cdd:COG0505 307 PAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| PyrB |
COG0540 |
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ... |
1913-2221 |
1.18e-129 |
|
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440306 [Multi-domain] Cd Length: 306 Bit Score: 409.44 E-value: 1.18e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1913 HSLMGKHILAVDMFNKDHLNDIFNLAQLLK--LRGTKDRPvdeLLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMD 1990
Cdd:COG0540 1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKevLRPIKKVP---LLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1991 NITSSVKKGESLEDSIKVVSSY-ADVVVLRHPSPGAVARAATFSRKPLINAGDGVGEHPTQALLDIFTIREEFGTVNGLT 2069
Cdd:COG0540 78 ASTSSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2070 ITMVGDLKNGRTVHSLARLLTLYNVNLQYVAPNSLqMPDEvvqfVHQRGVKQlfARDLKNVLPDTDVLYMTRIQRERFDN 2149
Cdd:COG0540 158 VAIVGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEE----IEELGVEV--TTDLDEALPDADVVYMLRIQKERFTD 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665391904 2150 --VEDYEKCCGHLVLTPEHMMRAKKRSIVLHPLPRL--NEISREIDSDPRAAYFRQAEYGMYIRMALLAMVVGGRN 2221
Cdd:COG0540 231 glFPSYREYKRSYGLTAERLALAKPDAIVMHPGPRNrgVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGGEE 306
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
7-377 |
3.31e-124 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 395.80 E-value: 3.31e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 7 YLALEDGTVLPGYSFGyvpseneSKVGFGGEVVFQTGMVGYTEALTDRSYSGQILVLTYPLIGNYGVPAPDeDEHGLPlh 86
Cdd:PRK12838 4 YLILEDGTVFEGELIG-------APIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADD-YESKQP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 87 feWMKGVVqatalvVGEVAEEAFHWRKWKTLPDWLKQHKVPGIQDIDTRALTKKLREQGSMLGKIVyekpPVEGLPKSSF 166
Cdd:PRK12838 74 --QVKGVI------VYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASIT----TTDDAHAFDQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 167 VDPNV--RNLAKECSVKERQVYGNpngKGPRIAILDCGLKLNQLRCLLQRGASVTLLPWSARLED---EQFDALFLSNGP 241
Cdd:PRK12838 142 IKALVlpKNVVAQVSTKEPYTYGN---GGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEiknLNPDGIVLSNGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 242 GNPESCDQIVQQVRKVIEegQKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPCLHRATGRCLMTSQNHGYAVDLEQL 321
Cdd:PRK12838 219 GDPKELQPYLPEIKKLIS--SYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSL 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 665391904 322 -PDGWSELFVNANDGTNEGIVHASKPYFSVQFHPEHHAGPQDTEFLFDVFMESIQQK 377
Cdd:PRK12838 297 dGTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKA 353
|
|
| PLN02527 |
PLN02527 |
aspartate carbamoyltransferase |
1918-2220 |
7.26e-120 |
|
aspartate carbamoyltransferase
Pssm-ID: 178142 [Multi-domain] Cd Length: 306 Bit Score: 381.40 E-value: 7.26e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1918 KHILAVDMFNKDHLNDIFNLAQLLKlRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNI--TSS 1995
Cdd:PLN02527 1 SDVIEAQQFDREMLELLFEVAREME-KVERGSPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENAgeFSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1996 VKKGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINAGDGVGEHPTQALLDIFTIREEFGTVNGLTITMVGD 2075
Cdd:PLN02527 80 AAKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2076 LKNGRTVHSLARLLTLY-NVNLQYVAPNSLQMPDEVVQFVHQRGVKQLFARDLKNVLPDTDVLYMTRIQRERF-DNVEDY 2153
Cdd:PLN02527 160 LANGRTVRSLAYLLAKYeDVKIYFVAPDVVKMKDDIKDYLTSKGVEWEESSDLMEVASKCDVLYQTRIQRERFgERIDLY 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665391904 2154 EKCCGHLVLTPEHMMRAKKRSIVLHPLPRLNEISREIDSDPRAAYFRQAEYGMYIRMALLAMVVGGR 2220
Cdd:PLN02527 240 EAARGKYIVDKKVMDVLPKHAVVMHPLPRLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLLGGW 306
|
|
| pyrB |
PRK00856 |
aspartate carbamoyltransferase catalytic subunit; |
1914-2221 |
1.86e-118 |
|
aspartate carbamoyltransferase catalytic subunit;
Pssm-ID: 234849 [Multi-domain] Cd Length: 305 Bit Score: 377.11 E-value: 1.86e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1914 SLMGKHILAVDMFNKDHLNDIFNLAQLLK---LRGTKDRPvdeLLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMD 1990
Cdd:PRK00856 2 PLKMKHLLSIEDLSREEIELLLDTAEEFKevlRREVKKVP---LLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1991 NITSSVKKGESLEDSIKVVSSY-ADVVVLRHPSPGAVARAATFSRKPLINAGDGVGEHPTQALLDIFTIREEFGTVNGLT 2069
Cdd:PRK00856 79 ASTSSVSKGETLADTIRTLSAMgADAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2070 ITMVGDLKNGRTVHSLARLLTLYNVNLQYVAPNSLQMPDEVVQFVHqrgvkqlfaRDLKNVLPDTDVLYMTRIQRERFDN 2149
Cdd:PRK00856 159 VAIVGDIKHSRVARSNIQALTRLGAEVRLIAPPTLLPEGMPEYGVH---------TDLDEVIEDADVVMMLRVQKERMDG 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665391904 2150 --VEDYEKCCGHLVLTPEHMMRAKKRSIVLHPLP--RLNEISREIDSDPRAAYFRQAEYGMYIRMALLAMVVGGRN 2221
Cdd:PRK00856 230 glLPSYEEYKRSYGLTAERLALAKPDAIVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGGRL 305
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
1479-1826 |
1.61e-111 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 362.87 E-value: 1.61e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDNWA 1558
Cdd:COG0044 49 LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1559 QVNELA----SHACGLKMYLNDTFGTLKLSD-----------------------------------MTSWQRHLSHWPKr 1599
Cdd:COG0044 129 NLAELGalaeAGAVAFKVFMGSDDGNPVLDDgllrraleyaaefgalvavhaedpdlirggvmnegKTSPRLGLKGRPA- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1600 spivcHAERQSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLGHG--MSevrP 1677
Cdd:COG0044 208 -----EAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNfkVN---P 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1678 LLCSPEDQEALWENI--DYIDVFATDHAPHTLAEKRSERP--PPGFPGVETILPLLLQ-AVHEGRLTMEDIKRKFHRNPK 1752
Cdd:COG0044 280 PLRTEEDREALWEGLadGTIDVIATDHAPHTLEEKELPFAeaPNGIPGLETALPLLLTeLVHKGRLSLERLVELLSTNPA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1753 IIFNLPDQAqtYVE---------VDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDGQVLVQPgFGQN 1823
Cdd:COG0044 360 RIFGLPRKG--RIAvgadadlvlFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEP-RGRF 436
|
...
gi 665391904 1824 VRP 1826
Cdd:COG0044 437 LRR 439
|
|
| asp_carb_tr |
TIGR00670 |
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ... |
1918-2218 |
1.19e-105 |
|
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273209 [Multi-domain] Cd Length: 301 Bit Score: 340.49 E-value: 1.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1918 KHILAVDMFNKDHLNDIFNLAQLLKlRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISM-DNITSSV 1996
Cdd:TIGR00670 1 RHLISISDLSREEIELLLETARELE-QVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFsDSETSSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1997 KKGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINAGDGVGEHPTQALLDIFTIREEFGTVNGLTITMVGDL 2076
Cdd:TIGR00670 80 AKGETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2077 KNGRTVHSLARLLTLYNVNLQYVAPNSLQMPDEVVQFVHQRGVKQLFARDLKNVLPDTDVLYMTRIQRERFDNVEDYEKC 2156
Cdd:TIGR00670 160 KYGRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665391904 2157 CGHLVLTPEHMMRAKKRSIVLHPLPRLNEISREIDSDPRAAYFRQAEYGMYIRMALLAMVVG 2218
Cdd:TIGR00670 240 KGSYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
196-371 |
1.44e-99 |
|
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: 317.52 E-value: 1.44e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 196 IAILDCGLKLNQLRCLLQRGASVTLLPWSARLED---EQFDALFLSNGPGNPESCDQIVQQVRKVIEEGqKPVFGICLGH 272
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEilkLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK-IPIFGICLGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 273 QLLAKAIGCSTYKMKYGNRGHNLPCLHRATGRCLMTSQNHGYAVDLEQLPDGWSELFVNANDGTNEGIVHASKPYFSVQF 352
Cdd:cd01744 80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159
|
170
....*....|....*....
gi 665391904 353 HPEHHAGPQDTEFLFDVFM 371
Cdd:cd01744 160 HPEASPGPHDTEYLFDEFL 178
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
1479-1805 |
1.77e-99 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 325.06 E-value: 1.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDNwa 1558
Cdd:cd01318 5 LPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTGSE-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1559 QVNEL-ASHACGLKMYLNDTFGTLkLSDMTSWQRHLSHwpKRSPIVCHAERQ---------------------------S 1610
Cdd:cd01318 83 DLEELdKAPPAGYKIFMGDSTGDL-LDDEETLERIFAE--GSVLVTFHAEDEdrlrenrkelkgesahprirdaeaaavA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1611 TAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEkgvKVTCEVCPHHLFLSTKDVERLGHgMSEVRPLLCSPEDQEALWE 1690
Cdd:cd01318 160 TARALKLARRHGARLHICHVSTPEELKLIKKAKP---GVTVEVTPHHLFLDVEDYDRLGT-LGKVNPPLRSREDRKALLQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1691 NIDY--IDVFATDHAPHTLAEKRS--ERPPPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNLPDQAQ---- 1762
Cdd:cd01318 236 ALADgrIDVIASDHAPHTLEEKRKgyPAAPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIKNKGRiaeg 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 665391904 1763 ---TYVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRG 1805
Cdd:cd01318 316 ydaDLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
524-726 |
6.00e-98 |
|
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: 314.24 E-value: 6.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 524 DRKLFAERVNEIGEQVAPSEAVY--SVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQALAHS------ 595
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 596 SQLIVDKSLKGWKEVEYEVVRDAYNNCITVCNMENFDPLgiHTGESIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGEC 675
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 665391904 676 NIQYALCPHSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGLPLP 726
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
1479-1801 |
1.75e-97 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 318.57 E-value: 1.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGAT-HKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASD-DN 1556
Cdd:cd01302 4 LPGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGPgDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1557 WAQVNELASH-ACGLKMYLNDTFGTLKLSDMTSWQRHLSHWPKR-SPIVCHAERqstaaVIMLAHLLDRSVHICHVARKE 1634
Cdd:cd01302 84 TDELKKLFDAgINSLKVFMNYYFGELFDVDDGTLMRTFLEIASRgGPVMVHAER-----AAQLAEEAGANVHIAHVSSGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1635 EIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLGHGMsEVRPLLCSPEDQEALWENI--DYIDVFATDHAPHTLAEKRS 1712
Cdd:cd01302 159 ALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWG-KVNPPLRSKEDREALWEGVknGKIDTIASDHAPHSKEEKES 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1713 ----ERPPPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNLPDQA-------QTYVEVDLDEEWTITGNEMK 1781
Cdd:cd01302 238 gkdiWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPARIFGLYPKGtiavgydADLVIVDPKKEWKVTAEEIE 317
|
330 340
....*....|....*....|
gi 665391904 1782 SKSGWTPFEGTKVKGRVHRV 1801
Cdd:cd01302 318 SKADWTPFEGMEVTGKPVST 337
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
1479-1811 |
1.61e-94 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 312.84 E-value: 1.61e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDN-- 1556
Cdd:TIGR00857 38 LPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNqg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1557 --WAQVNELASHACGLKMYLNDTFGTLKLSDMT---------------------------------SWQRHLSHWPkrsp 1601
Cdd:TIGR00857 118 keLTEAYELKEAGAVGRMFTDDGSEVQDILSMRraleyaaiagvpialhaedpdliyggvmhegpsAAQLGLPARP---- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1602 ivCHAERQSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLgHGMSEVRPLLCS 1681
Cdd:TIGR00857 194 --PEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARL-DGNGKVNPPLRE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1682 PEDQEALWENI--DYIDVFATDHAPHTLAEKRS--ERPPPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNL 1757
Cdd:TIGR00857 271 KEDRLALIEGLkdGIIDIIATDHAPHTLEEKTKefAAAPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGL 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665391904 1758 PDQ-------AQTYVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVD 1811
Cdd:TIGR00857 351 PDKgtleegnPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| PRK08192 |
PRK08192 |
aspartate carbamoyltransferase; Provisional |
1917-2218 |
3.86e-87 |
|
aspartate carbamoyltransferase; Provisional
Pssm-ID: 169269 [Multi-domain] Cd Length: 338 Bit Score: 288.55 E-value: 3.86e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1917 GKHILAVDMFNKDHLNDIFNLAQLLKLRGTKDRpVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRV---ISMDNit 1993
Cdd:PRK08192 5 GSHILSVNQLDRDAIQRIFNVADRMEPYALREK-RTRVLEGAILGNLFFEPSTRTRVSFGCAFNLLGGHVretTGMAS-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1994 SSVKKGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINAGDGVGEHPTQALLDIFTIREEF----GTVNGLT 2069
Cdd:PRK08192 82 SSLSKGESLYDTARVLSTYSDVIAMRHPDAGSVKEFAEGSRVPVINGGDGSNEHPTQALLDLFTIQKELahagRGIDGMH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2070 ITMVGDLKNGRTVHSLARLLTLY-NVNLQYVAPNSLQMPDEVVQFVHQRGVKQLFARDLKNVLPDTDVLYMTRIQRERFD 2148
Cdd:PRK08192 162 IAMVGDLKFGRTVHSLSRLLCMYkNVSFTLVSPKELAMPDYVISDIENAGHKITITDQLEGNLDKADILYLTRIQEERFP 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665391904 2149 NVEDYEKCCGHLVLTPE-HMMRAKKRSIVLHPLPR-----LNEISREIDSDPRAAYFRQAEYGMYIRMALLAMVVG 2218
Cdd:PRK08192 242 SQEEANKYRGKFRLNQSiYTQHCKSNTVIMHPLPRdsraqANELDNDLNSHPNLAIFRQADNGLLIRMALFALTLG 317
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
397-792 |
2.66e-84 |
|
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: 301.53 E-value: 2.66e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 397 DSAPVMPRKVLILGSGGLSIGQAGEFDYSGSQAIKAMRESNIQTVLINPNIATVQTSKGMADKCYFLPLTPHYVEQVIKS 476
Cdd:TIGR01369 548 DVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIEL 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 477 ERPNGVLLTFGGQTALNCGVQLERAGvfskynVRILGTPIQSIIETEDRKLFAERVNEIGEQVAPSEAVYSVAQALDAAS 556
Cdd:TIGR01369 628 EKPEGVIVQFGGQTPLNLAKALEEAG------VPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFAS 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 557 RLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQALAHSSQ--LIVDKSLKGWKEVEYEVVrdAYNNCITVCN-MENFDP 633
Cdd:TIGR01369 702 EIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAV--SDGEEVLIPGiMEHIEE 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 634 LGIHTGESIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYALcpHSEQYYIIEVNARLSRSSALASKATGYPLA 713
Cdd:TIGR01369 780 AGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGEVYVIEVNPRASRTVPFVSKATGVPLA 857
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665391904 714 YVAAKLALGLplpDIKNSVTGNttacfEPSLDYCVVKIPRWDLAKFVRVSKHIGSSMKSVGEVMAIGRNFEEAFQKALR 792
Cdd:TIGR01369 858 KLAVRVMLGK---KLEELGVGK-----EKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQL 928
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1479-1829 |
2.10e-81 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 276.15 E-value: 2.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASDdNWA 1558
Cdd:PRK02382 53 LPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTG-NWD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1559 QVNELAShaCGL----KMYLNDTFGTLKLsDMTSWQRHLSHWPKRSPIVC-HAERQS----------------------- 1610
Cdd:PRK02382 132 PLESLWE--RGVfalgEIFMADSTGGMGI-DEELFEEALAEAARLGVLATvHAEDEDlfdelakllkgdadadawsayrp 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1611 ----TAAV---IMLAHLLDRSVHICHVARKEEIQLIRSAKekgvkVTCEVCPHHLFLSTKDVERLG-HGmsEVRPLLCSP 1682
Cdd:PRK02382 209 aaaeAAAVeraLEVASETGARIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGtFG--KMNPPLRSE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1683 EDQEALWENID--YIDVFATDHAPHTLAEKRSE--RPPPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNLP 1758
Cdd:PRK02382 282 KRREALWERLNdgTIDVVASDHAPHTREEKDADiwDAPSGVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGLD 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1759 DQ---AQTY----VEVDLDEEWTITGNEMKSKSGWTPFEGTKVkgrV--HRVVLRGEVAFVDGQVLVQPGFGQNVRPKQS 1829
Cdd:PRK02382 362 GKgriAEGYdadlVLVDPDAAREIRGDDLHSKAGWTPFEGMEG---VfpELTMVRGTVVWDGDDINAKRGRGEFLRGRGY 438
|
|
| PRK11891 |
PRK11891 |
aspartate carbamoyltransferase; Provisional |
1887-2218 |
2.07e-80 |
|
aspartate carbamoyltransferase; Provisional
Pssm-ID: 183362 [Multi-domain] Cd Length: 429 Bit Score: 272.89 E-value: 2.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1887 RIRLDSASNTTLREYLQRTTNSNPVAHSLM--GK-HILAVDMFNKDHLNDIFNLAQLLKLRGTKdRPVDELLPGKIMASV 1963
Cdd:PRK11891 54 RFVSEIVERAAPGEKYTQSVDEQPLADQFAfeGKpQLLSVDQFSRDSVEALFRVADVMQPIARR-QKISRVLEGAVLGNL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1964 FYEVSTRTQCSFAAAMLRLGGRVISMDNIT-SSVKKGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINAGD 2042
Cdd:PRK11891 133 FFEASTRTRVSFGAAFCRLGGSVCDTTGFTfSSMAKGESIYDTSRVMSGYVDALVIRHPEQGSVAEFARATNLPVINGGD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2043 GVGEHPTQALLDIFTIREEFG----TVNGLTITMVGDLKNGRTVHSLARLLTLYN-VNLQYVAPNSLQMPDEVVQFVHQR 2117
Cdd:PRK11891 213 GPGEHPSQALLDLYTIQREFSrlgkIVDGAHIALVGDLKYGRTVHSLVKLLALYRgLKFTLVSPPTLEMPAYIVEQISRN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2118 GVKQLFARDLKNVLPDTDVLYMTRIQRERFDNvEDYEKCCGHLVLTPEHMMRA-KKRSIVLHPLPR-----LNEISREID 2191
Cdd:PRK11891 293 GHVIEQTDDLAAGLRGADVVYATRIQKERFAD-ESFEGYTPDFQINQALVDAVcKPDTLIMHPLPRdsrpgANDLSTDLN 371
|
330 340
....*....|....*....|....*..
gi 665391904 2192 SDPRAAYFRQAEYGMYIRMALLAMVVG 2218
Cdd:PRK11891 372 RDPRLAIFRQTDNGIPVRMAIFAVLLG 398
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
8-376 |
3.19e-80 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 270.51 E-value: 3.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 8 LALEDGTVLPGYSFgyvpseNESKVGFGgEVVFQTGMVGYTEALTDRSYSGQILVLTYPLIGNYGVPAPDEDEHGlplhf 87
Cdd:CHL00197 9 LVLEDGTYYRGWSF------SNPITTIG-EVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVK----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 88 ewmkgvVQATALVVGEVAEEAFHWRKWKTLPDWLKQHKVPGIQDIDTRALTKKLREQGSMLGKI---VYEKPPVEGLPKS 164
Cdd:CHL00197 77 ------IQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCIsnqNLNLSYLRAKIKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 165 SFVDPNVrNLAKECSVK---ERQVYGNPN-----------GKGPRIAILDCGLKLNQLRCLLQRGASVTLLPWSARLED- 229
Cdd:CHL00197 151 SPHMPSS-DLIPRVTTSsyyEWDEKSHPSfyladnkrphsSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDi 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 230 --EQFDALFLSNGPGNPESCDQIVQQVRKVIEEgQKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPC-LHRatgRCL 306
Cdd:CHL00197 230 lsYQPDGILLSNGPGDPSAIHYGIKTVKKLLKY-NIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSgLNQ---QVE 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665391904 307 MTSQNHGYAVDLEQL-PDGWSELFVNANDGTNEGIVHASKPYFSVQFHPEHHAGPQDTEFLFDVFMESIQQ 376
Cdd:CHL00197 306 ITSQNHGFAVNLESLaKNKFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKH 376
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
397-790 |
8.35e-80 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 288.15 E-value: 8.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 397 DSAPVMPRKVLILGSGGLSIGQAGEFDYSGSQAIKAMRESNIQTVLINPNIATVQTSKGMADKCYFLPLTPHYVEQVIKS 476
Cdd:PRK05294 548 ESNPSDRKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEK 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 477 ERPNGVLLTFGGQTALNCGVQLERAGvfskynVRILGTPIQSIIETEDRKLFAERVNEIGEQVAPSEAVYSVAQALDAAS 556
Cdd:PRK05294 628 EKPKGVIVQFGGQTPLKLAKALEAAG------VPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAE 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 557 RLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQALAHSSQ--LIVDKSLKGWKEVeyEVvrDAynncitVCN------- 627
Cdd:PRK05294 702 EIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDhpVLIDKFLEGAIEV--DV--DA------ICDgedvlig 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 628 --MENFDPLGIHTGESIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYALcpHSEQYYIIEVNARLSRSSALAS 705
Cdd:PRK05294 772 giMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAV--KDDEVYVIEVNPRASRTVPFVS 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 706 KATGYPLAYVAAKLALGLPLPDIknsvtGNTTacfEPSLDYCVVKIPRWDLAKFVRVSKHIGSSMKSVGEVMAIGRNFEE 785
Cdd:PRK05294 850 KATGVPLAKIAARVMLGKKLAEL-----GYTK---GLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGE 921
|
....*
gi 665391904 786 AFQKA 790
Cdd:PRK05294 922 AFAKA 926
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1479-1811 |
7.95e-79 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 267.83 E-value: 7.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDY----ALYVGASD 1554
Cdd:PRK09357 52 APGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVlpvgAITKGLAG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1555 DNWAQVNELASHacGLKMYLNDTFGtlkLSDMTSWQRHL----SHWpkrSPIVCHAE----------------------- 1607
Cdd:PRK09357 132 EELTEFGALKEA--GVVAFSDDGIP---VQDARLMRRALeyakALD---LLIAQHCEdpslteggvmnegevsarlglpg 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1608 RQSTAAVIMLAH--LLDRS----VHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLGhGMSEVRPLLCS 1681
Cdd:PRK09357 204 IPAVAEEVMIARdvLLAEAtgarVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYD-PNYKVNPPLRT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1682 PEDQEALWENI--DYIDVFATDHAPHTLAEKRSE--RPPPGFPGVETILPLLLQA-VHEGRLTMEDIKRKFHRNPKIIFN 1756
Cdd:PRK09357 283 EEDREALIEGLkdGTIDAIATDHAPHAREEKECEfeAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTINPARILG 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665391904 1757 LPD------QAQTYVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVD 1811
Cdd:PRK09357 363 LPAgplaegEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1479-1825 |
2.26e-78 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 267.56 E-value: 2.26e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDNWA 1558
Cdd:PRK09060 55 LPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNAD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1559 QVNEL--ASHACGLKMYLNDTFGTLKLSDMTSWQRHLSHWPKRSPIvcHAE-----------------------RQSTAA 1613
Cdd:PRK09060 135 ELAELerLPGCAGIKVFMGSSTGDLLVEDDEGLRRILRNGRRRAAF--HSEdeyrlrerkglrvegdpsshpvwRDEEAA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1614 V------IMLAHLLDRSVHICHVARKEEIQLIRSAKEkgvKVTCEVCPHHLFLSTKDV-ERLGhGMSEVRPLLCSPEDQE 1686
Cdd:PRK09060 213 LlatrrlVRLARETGRRIHVLHVSTAEEIDFLADHKD---VATVEVTPHHLTLAAPECyERLG-TLAQMNPPIRDARHRD 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1687 ALWENID--YIDVFATDHAPHTLAEKRSERP--PPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNLPDQ-- 1760
Cdd:PRK09060 289 GLWRGVRqgVVDVLGSDHAPHTLEEKAKPYPasPSGMTGVQTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIAGKgr 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665391904 1761 -AQTY----VEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGR-VHRVVlRGEVAFVDGQvLVQPGFGQNVR 1825
Cdd:PRK09060 369 iAVGYdadfTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWpVGTIV-RGQRVMWDGE-LVGPPTGEPVR 437
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1479-1814 |
3.67e-78 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 266.54 E-value: 3.67e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTqfQELAKAGARC--DYALYVGASDDN 1556
Cdd:PRK07575 55 LPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQAALD--DKLARAAEKCvvNYGFFIGATPDN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1557 WAQVNeLASHACGLKMYLNDTFGTLKLSDMTSWQRHLSHWPKrsPIVCHAERQST------------------------A 1612
Cdd:PRK07575 133 LPELL-TANPTCGIKIFMGSSHGPLLVDEEAALERIFAEGTR--LIAVHAEDQARirarraefagisdpadhsqiqdeeA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1613 AVIMLAHLLD------RSVHICHVARKEEIQLIRsaKEKGVKVTCEVCPHHLFLSTKDVERLGhGMSEVRPLLCSPEDQE 1686
Cdd:PRK07575 210 ALLATRLALKlskkyqRRLHILHLSTAIEAELLR--QDKPSWVTAEVTPQHLLLNTDAYERIG-TLAQMNPPLRSPEDNE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1687 ALWENI--DYIDVFATDHAPHTLAEKRSERP--PPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNLPDQ-- 1760
Cdd:PRK07575 287 ALWQALrdGVIDFIATDHAPHTLEEKAQPYPnsPSGMPGVETSLPLMLTAAMRGKCTVAQVVRWMSTAVARAYGIPNKgr 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 665391904 1761 -AQTY----VEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDGQV 1814
Cdd:PRK07575 367 iAPGYdadlVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
1479-1818 |
2.49e-76 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 260.09 E-value: 2.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYAL------YVGA 1552
Cdd:PRK04250 46 LPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALnfliagNCEK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1553 SDDNWAQVNELASHACGLKMYLND-TFGTLKLSDMTSWQ----RHLSHWPKRSPIvchAERQSTAAVIMLAHLLDRSVHI 1627
Cdd:PRK04250 126 AEEIKADFYKIFMGASTGGIFSENfEVDYACAPGIVSVHaedpELIREFPERPPE---AEVVAIERALEAGKKLKKPLHI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1628 CHVARKEEIQLIrsaKEKGVK-VTCEVCPHHLFLSTKDVERlgHGMSEVRPLLCSPEDQEALWENIDYIDVFATDHAPHT 1706
Cdd:PRK04250 203 CHISTKDGLKLI---LKSNLPwVSFEVTPHHLFLTRKDYER--NPLLKVYPPLRSEEDRKALWENFSKIPIIASDHAPHT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1707 LAEKrsERPPPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNLPDQA------QTYVEVDLDEEWTITGNEM 1780
Cdd:PRK04250 278 LEDK--EAGAAGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKNYGieegnyANFAVFDMKKEWTIKAEEL 355
|
330 340 350
....*....|....*....|....*....|....*...
gi 665391904 1781 KSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDGQVLVQP 1818
Cdd:PRK04250 356 YTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKP 393
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1479-1814 |
1.57e-71 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 247.48 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDNWA 1558
Cdd:PRK09236 53 LPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1559 QVNEL-ASHACGLKMYLNDTFGTLKLSDMTSWQRHLSHWPkrSPIVCHAERQST-------------AAVIMLAHLLDRS 1624
Cdd:PRK09236 133 EIKRLdPKRVCGVKVFMGASTGNMLVDNPETLERIFRDAP--TLIATHCEDTPTikanlakykekygDDIPAEMHPLIRS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1625 V---------------------HICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLGHgmsevrpLL-CSP 1682
Cdd:PRK09236 211 AeacykssslavslakkhgtrlHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGN-------LIkCNP 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1683 -----EDQEALWE--NIDYIDVFATDHAPHTLAEKRS--ERPPPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKI 1753
Cdd:PRK09236 284 aiktaSDREALRQalADDRIDVIATDHAPHTWEEKQGpyFQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAPAI 363
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665391904 1754 IFNLPDQA---QTY----VEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDGQV 1814
Cdd:PRK09236 364 LFDIKERGfirEGYwadlVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQL 431
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
1479-1801 |
3.51e-70 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 241.37 E-value: 3.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSI-----VDR------------------------- 1528
Cdd:cd01317 13 APGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIdnpavVELlknrakdvgivrvlpigaltkglkg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1529 ETFTQFQELAKAGArcdyalyVGASDDNWAQVN-ELASHAcglkMYLNDTFGTL--------KLSD--------MTSWqr 1591
Cdd:cd01317 93 EELTEIGELLEAGA-------VGFSDDGKPIQDaELLRRA----LEYAAMLDLPiivhpedpSLAGggvmnegkVASR-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1592 hlSHWPKRSPIvchAERQSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLGhG 1671
Cdd:cd01317 160 --LGLPGIPPE---AETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYD-T 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1672 MSEVRPLLCSPEDQEALWENI--DYIDVFATDHAPHTLAEKRS--ERPPPGFPGVETILPLLLQAVHEGR-LTMEDIKRK 1746
Cdd:cd01317 234 NAKVNPPLRSEEDREALIEALkdGTIDAIASDHAPHTDEEKDLpfAEAPPGIIGLETALPLLWTLLVKGGlLTLPDLIRA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665391904 1747 FHRNPKIIFNLPDQAQTYVE------VDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRV 1801
Cdd:cd01317 314 LSTNPAKILGLPPGRLEVGApadlvlFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
2-367 |
3.18e-67 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 234.10 E-value: 3.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2 ASTDCYLALEDGTVLPGYSFGyvpsENESKVGfggEVVFQTGMVGYTEALTDRSYSGQILVLTYPLIGNYGVPAPDEDEH 81
Cdd:PLN02771 53 KTSDARLVLEDGSVWKAKSFG----ARGTQVG---EVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 82 GLPLhfewmkgvvqaTALVVGEVAEEAFHWRKWKTLPDWLKQHKVPGIQDIDTRALTKKLREQGSMLGKIVYEKPPV-EG 160
Cdd:PLN02771 126 QCFL-----------AGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTdEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 161 LPKSS---------------------FVDPNVRNLAKECSVKERQVYgnpngkgpRIAILDCGLKLNQLRCLLQRGASVT 219
Cdd:PLN02771 195 LLKMSrswdivgidlisgvsckspyeWVDKTNPEWDFNTNSRDGESY--------HVIAYDFGIKHNILRRLASYGCKIT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 220 LLP--WSArLEDEQF--DALFLSNGPGNPESCDQIVQQVRKVIeeGQKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNL 295
Cdd:PLN02771 267 VVPstWPA-SEALKMkpDGVLFSNGPGDPSAVPYAVETVKELL--GKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNH 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665391904 296 PCLHRATGRCLMTSQNHGYAVDLEQLPDGWSELFVNANDGTNEGIVHASKPYFSVQFHPEHHAGPQDTEFLF 367
Cdd:PLN02771 344 PVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
397-790 |
6.02e-66 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 245.84 E-value: 6.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 397 DSAPVMPRKVLILGSGGLSIGQAGEFDYSGSQAIKAMRESNIQTVLINPNIATVQTSKGMADKCYFLPLTPHYVEQVIKS 476
Cdd:PLN02735 568 ESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDL 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 477 ERPNGVLLTFGGQTALNCGVQLERA-------GVFSKYNVRILGTPIQSIIETEDRKLFAERVNEIGEQVAPSEAVYSVA 549
Cdd:PLN02735 648 ERPDGIIVQFGGQTPLKLALPIQKYldknpppSASGNGNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEA 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 550 QALDAASRLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQALAHSSQ--LIVDKSLKGWKEVEYEVVRDAYNNCITVCN 627
Cdd:PLN02735 728 DALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPErpVLVDKYLSDATEIDVDALADSEGNVVIGGI 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 628 MENFDPLGIHTGESIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYALCPHSEqYYIIEVNARLSRSSALASKA 707
Cdd:PLN02735 808 MEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGE-VYIIEANPRASRTVPFVSKA 886
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 708 TGYPLAYVAAKLALGLPLPDIknsvtgnttaCF--EPSLDYCVVKIPRWDLAKFVRVSKHIGSSMKSVGEVMAIGRNFEE 785
Cdd:PLN02735 887 IGHPLAKYASLVMSGKSLKDL----------GFteEVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSK 956
|
....*
gi 665391904 786 AFQKA 790
Cdd:PLN02735 957 AFAKA 961
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
8-151 |
1.90e-64 |
|
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: 214.88 E-value: 1.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 8 LALEDGTVLPGYSFGYVPSEneskvgfGGEVVFQTGMVGYTEALTDRSYSGQILVLTYPLIGNYGVPAPDEDEHGlplhf 87
Cdd:pfam00988 1 LVLEDGTVFEGKSFGAAGST-------VGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDK----- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391904 88 ewmkgvVQATALVVGEVAEEAFHWRKWKTLPDWLKQHKVPGIQDIDTRALTKKLREQGSMLGKI 151
Cdd:pfam00988 69 ------IHVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
7-151 |
1.97e-62 |
|
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: 209.15 E-value: 1.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 7 YLALEDGTVLPGYSFGYvpsENESkvgfGGEVVFQTGMVGYTEALTDRSYSGQILVLTYPLIGNYGVPapDEDehglplh 86
Cdd:smart01097 4 YLVLEDGTVFEGESFGA---EGET----VGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVN--DED------- 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665391904 87 FEWMKgvVQATALVVGEVAEEAFHWRKWKTLPDWLKQHKVPGIQDIDTRALTKKLREQGSMLGKI 151
Cdd:smart01097 68 FESDK--IQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
1479-1825 |
5.12e-62 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 220.24 E-value: 5.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMP-NTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDNW 1557
Cdd:cd01315 51 MPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1558 AQVNELASHAC-GLKMYLNDTfGTLKLSDMTSWQ-----RHLSHWPKrsPIVCHAE-------RQSTAA----------- 1613
Cdd:cd01315 131 DQLRPLDEAGVvGFKCFLCPS-GVDEFPAVDDEQleeamKELAKTGS--VLAVHAEnpeiteaLQEQAKakgkrdyrdyl 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1614 --------------VIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLGhgmSEVRpll 1679
Cdd:cd01315 208 asrpvfteveaiqrILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGG---TEFK--- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1680 CSP-----EDQEALWENI--DYIDVFATDHAPHTLAEKRSERPP-----PGFPGVETILPLLL-QAVHEGRLTMEDIKRK 1746
Cdd:cd01315 282 CAPpirdaANQEQLWEALenGDIDMVVSDHSPCTPELKLLGKGDffkawGGISGLQLGLPVMLtEAVNKRGLSLEDIARL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1747 FHRNPKIIFNLPDQAQT--------YVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDGQVLVQP 1818
Cdd:cd01315 362 MCENPAKLFGLSHQKGRiavgydadFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGEP 441
|
....*..
gi 665391904 1819 gFGQNVR 1825
Cdd:cd01315 442 -LGQLLL 447
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1479-1826 |
2.19e-57 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 206.86 E-value: 2.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMP-NTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDNW 1557
Cdd:PRK06189 53 FPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1558 AQVNELA-SHACGLKMYLN----DTF-----GTLkLSDMTSWQRHlshwpkRSPIVCHAER---------------QSTA 1612
Cdd:PRK06189 133 EHLRELAeAGVIGFKAFMSnsgtDEFrssddLTL-YEGMKEIAAL------GKILALHAESdaltrhlttqarqqgKTDV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1613 --------------AV---IMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLGhGMSEV 1675
Cdd:PRK06189 206 rdylesrpvvaeleAVqraLLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIG-AVAKC 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1676 RPLLCSPEDQEALWENI--DYIDVFATDHAPHTLAEKRSE---RPPPGFPGVETILPLLLQ-AVHEGRLTMEDIKRKFHR 1749
Cdd:PRK06189 285 APPLRSRSQKEELWRGLlaGEIDMISSDHSPCPPELKEGDdffLVWGGISGGQSTLLVMLTeGYIERGIPLETIARLLAT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1750 NPKIIFNLPDQAQ-------TYVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDGQVlVQPGFGQ 1822
Cdd:PRK06189 365 NPAKRFGLPQKGRlevgadaDFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV-FPPPRGQ 443
|
....
gi 665391904 1823 NVRP 1826
Cdd:PRK06189 444 LLRP 447
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
197-372 |
4.58e-56 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 193.22 E-value: 4.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 197 AILDCGL--KLNQLRCLLQRGASVTLLPWSA---RLEDEQFDALFLSNGPGNPESCDQIVQQVRKVIEEGqKPVFGICLG 271
Cdd:pfam00117 1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREARELK-IPILGICLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 272 HQLLAKAIGCSTYKMK-YGNRGHNLPCLHR------ATGRCLMTSQNHGYAVDLEQLPDGWSELFVNANDGTNEGIVHAS 344
Cdd:pfam00117 80 HQLLALAFGGKVVKAKkFGHHGKNSPVGDDgcglfyGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKK 159
|
170 180
....*....|....*....|....*...
gi 665391904 345 KPYFSVQFHPEHHAGPQDTEFLFDVFME 372
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
1479-1821 |
7.85e-56 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 202.06 E-value: 7.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREP--GATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDN 1556
Cdd:cd01314 50 LPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1557 WAQVNELA--------ShacgLKMY-------------LNDTFGTLKLS-----------DMTSW--QRHLS-------- 1594
Cdd:cd01314 130 DSVIEELPelvkkgisS----FKVFmaykgllmvddeeLLDVLKRAKELgalvmvhaengDVIAElqKKLLAqgktgpey 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1595 HWPKRSPIVchaERQSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLG-HGMS 1673
Cdd:cd01314 206 HALSRPPEV---EAEATARAIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWKDWfEGAK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1674 EVrpllCSP-----EDQEALWENI--DYIDVFATDHAPHTLAEKRSERP-----PPGFPGVETILPLLLQA-VHEGRLTM 1740
Cdd:cd01314 283 YV----CSPplrpkEDQEALWDGLssGTLQTVGSDHCPFNFAQKARGKDdftkiPNGVPGVETRMPLLWSEgVAKGRITL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1741 EDIKRKFHRNPKIIFNLPDQAQTYVE--------VDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDG 1812
Cdd:cd01314 359 EKFVELTSTNPAKIFGLYPRKGTIAVgsdadlviWDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDG 438
|
....*....
gi 665391904 1813 QVLVQPGFG 1821
Cdd:cd01314 439 ELVGEKGSG 447
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
813-935 |
8.61e-55 |
|
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: 187.27 E-value: 8.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 813 LAEQLSEPTDRRPFVIAAALQLGMSLRELHQLTNIDYWFLEKLERIILL-QSLLTRNGSRTDAALLLKAKRFGFSDKQIA 891
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELeKELKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 665391904 892 KYIKSTELAVRHQRQEFGIRPHVKQIDTVAGEWPASTNYLYHTY 935
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| ArgF |
COG0078 |
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine ... |
1914-2219 |
1.24e-52 |
|
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine carbamoyltransferase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439848 [Multi-domain] Cd Length: 310 Bit Score: 188.34 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1914 SLMGKHILAVDMFNKDHLNDIFNLAQLLKlRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNIT 1993
Cdd:COG0078 2 NLKGRHFLSLLDLTPEELRALLDLAAELK-AKRKAGIPHRPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIYLDPGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1994 SSVKKGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINA-GDgvGEHPTQALLDIFTIREEFGTVNGLTITM 2072
Cdd:COG0078 81 SQLGRGESIKDTARVLSRYVDGIMIRTFGHETLEELAKYAGVPVINGlTD--LFHPCQALADLLTIREHFGKLKGLKVAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2073 VGDLKNgrTVHSLARLLTLYNVNLQYVAPNSLQMPDEVV----QFVHQRGVKQLFARDLKNVLPDTDVLY------MTR- 2141
Cdd:COG0078 159 VGDGNN--VANSLLLAAAKLGMDVRIATPEGYEPDPEIVakakEIAAESGGSITITHDPAEAVKGADVVYtdvwvsMGQe 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2142 -IQRERFDNVEDYEkccghlvLTPEHMMRAKKRSIVLHPLP--RLNEISRE-IDSdPRAAYFRQAEYGMYIRMALLAMVV 2217
Cdd:COG0078 237 eEAEERIKAFKPYQ-------VNEELMALAKPDAIFMHCLPahRGEEVTDEvIDG-PQSVVFDEAENRLHAQKALLAWLL 308
|
..
gi 665391904 2218 GG 2219
Cdd:COG0078 309 GG 310
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1479-1832 |
7.19e-52 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 190.77 E-value: 7.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREP--GATHKEDFASGTAAALAGGVTLVC--AMPNTNPSIvdRETFTQFQELAKAGARCDYALYVGASD 1554
Cdd:PRK08323 48 MPGGIDPHTHMEMPfgGTVSSDDFETGTRAAACGGTTTIIdfALQPKGQSL--REALEAWHGKAAGKAVIDYGFHMIITD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1555 DNWAQVNELASH-ACG---LKMYLndTF-GTLKLSDMT---SWQR------------------------HLS-------- 1594
Cdd:PRK08323 126 WNEVVLDEMPELvEEGitsFKLFM--AYkGALMLDDDEllrALQRaaelgalpmvhaengdaiaylqakLLAegktgpey 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1595 HWPKRSPIVchaERQSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLG--HGM 1672
Cdd:PRK08323 204 HALSRPPEV---EGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDwfEGA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1673 SEVrpllCSP-----EDQEALWENI--DYIDVFATDHAPHTLAEKRSE------RPPPGFPGVETILPLL-LQAVHEGRL 1738
Cdd:PRK08323 281 KYV----MSPplrdkEHQDALWRGLqdGDLQVVATDHCPFCFEQKKQLgrgdftKIPNGTPGVEDRMPLLfSEGVMTGRI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1739 TMEdikrKFHR----NPKIIFNLPDQAQTyVEV---------DLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRG 1805
Cdd:PRK08323 357 TLN----RFVEltstNPAKIFGLYPRKGT-IAVgadadiviwDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRG 431
|
410 420
....*....|....*....|....*..
gi 665391904 1806 EVAFVDGQVLVQPGFGQNVRPKQSPLA 1832
Cdd:PRK08323 432 EVVVEDGEFRGKAGHGRFLKRKPFQAV 458
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
1479-1818 |
4.12e-51 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 188.36 E-value: 4.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMP-NTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDNW 1557
Cdd:TIGR03178 50 FPGVVDTHVHINEPGRTEWEGFETGTRAAAAGGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1558 AQVNELASH-ACGLKMYLN----DTFGTLKLSDMTSWQRHLSHWPKrsPIVCHAERQS---------------------- 1610
Cdd:TIGR03178 130 DDLRELDEAgVVGFKAFLSpsgdDEFPHVDDWQLYKGMRELARLGQ--LLLVHAENPAitsalgeeappqggvgadayla 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1611 ----------TAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLGhgmSEVR--PL 1678
Cdd:TIGR03178 208 srpvfaeveaIRRTLALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGG---TLAKcaPP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1679 LCSPEDQEALWENI--DYIDVFATDHAPHTLAEKRSE---RPPPGFPGVETILPLLL-QAVHEGRLTMEDIKRKFHRNPK 1752
Cdd:TIGR03178 285 IRDLANQEGLWEALlnGLIDCVVSDHSPCTPDLKRAGdffKAWGGIAGLQSTLDVMFdEAVQKRGLPLEDIARLMATNPA 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665391904 1753 IIFNLPDQAQT-------YVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDGQVLVQP 1818
Cdd:TIGR03178 365 KRFGLAQKGRIapgkdadFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP 437
|
|
| OTCace_N |
pfam02729 |
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain; |
1919-2060 |
1.73e-50 |
|
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
Pssm-ID: 460665 [Multi-domain] Cd Length: 140 Bit Score: 175.31 E-value: 1.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1919 HILAVDMFNKDHLNDIFNLAQLLKlRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNITSSVKK 1998
Cdd:pfam02729 1 HFLSLEDLSREEIEALLDLAAELK-EARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSS 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665391904 1999 GESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINAGdGVGEHPTQALLDIFTIRE 2060
Cdd:pfam02729 80 GESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
1479-1825 |
5.48e-48 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 179.50 E-value: 5.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREP--GATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASD-- 1554
Cdd:TIGR02033 50 LPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHwn 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1555 DNWAQVNELASHACGL---KMYL--------NDT--FGTLKL--------------SDMTSW--QRHLS--------HWP 1597
Cdd:TIGR02033 130 DSVLEEHIPEVKEEGInsfKVFMayknllmvDDEelFEILKRlkelgallqvhaenGDIIAElqARMLAqgitgpeyHAL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1598 KRsPIVCHAErqSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLG-HGMSEV- 1675
Cdd:TIGR02033 210 SR-PPELEAE--AVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDKPGfEGAKYVc 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1676 RPLLCSPEDQEALWENIDY--IDVFATDHAPHTLAEKRS------ERPPPGFPGVETILPLLL-QAVHEGRLTMEDIKRK 1746
Cdd:TIGR02033 287 SPPLREPEDQDALWSALSSgaLQTVGSDHCTFNFAQKKAigkddfTKIPNGGPGVEERMSLLFdEGVAKGRITLEKFVEV 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1747 FHRNPKIIFNLPDQAQTYVE--------VDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDGQVLVQP 1818
Cdd:TIGR02033 367 TSTNPAKIFNLYPRKGTIAVgsdadiviWDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTA 446
|
....*..
gi 665391904 1819 GFGQNVR 1825
Cdd:TIGR02033 447 GAGRFVK 453
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
1479-1824 |
2.54e-44 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 166.86 E-value: 2.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFT-QFQELAkAGARCDYALYVGASDDnw 1557
Cdd:PRK00369 46 LPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITeKLAELE-YYSRVDYFVYSGVTKD-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1558 aqVNELASHA-CGLKMYLND--TFGTLKLSDMTSW------QRHLSHWPKRSPIV-CHAErqstAAVIMLAHLLDRsVHI 1627
Cdd:PRK00369 123 --PEKVDKLPiAGYKIFPEDleREETFRVLLKSRKlkilhpEVPLALKSNRKLRRnCWYE----IAALYYVKDYQN-VHI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1628 CHVARKEEIQLirsAKEKGVkvTCEVCPHHLFlstkdVERLGHGMSEVRPLLCSPEDQEALWENIDYIDVFATDHAPHTL 1707
Cdd:PRK00369 196 THASNPRTVRL---AKELGF--TVDITPHHLL-----VNGEKDCLTKVNPPIRDINERLWLLQALSEVDAIASDHAPHSS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1708 AEKRSERP--PPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNLPDQaqtYVEVDLDEEWTITGNE------ 1779
Cdd:PRK00369 266 FEKLQPYEvcPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGIPYG---EIKEGYRANFTVIQFEdwryst 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 665391904 1780 MKSKSGWTPFEGTKVKGRVHRVVLRGEVAFVDGQVLvqPGFGQNV 1824
Cdd:PRK00369 343 KYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVF--PVKGINP 385
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
1479-1807 |
1.16e-43 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 165.42 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGARCDYALYVGASDDNWA 1558
Cdd:PRK01211 45 LPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1559 QVNELAShacGLKMYLNDTFGTL----------KLSDM-----------------TSWQRHLSHWPKRSPIVCHAErqst 1611
Cdd:PRK01211 125 ILDERSI---GLKVYMGGTTNTNgtdieggeikKINEAnipvffhaelseclrkhQFESKNLRDHDLARPIECEIK---- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1612 aAVIMLAHLLDRSVHICHVarkeeiqlirSAKEKGVKVTCEVCPHHLFLStkDVERLGhGMSEVRPLLCSPEDQEALWEn 1691
Cdd:PRK01211 198 -AVKYVKNLDLKTKIIAHV----------SSIDVIGRFLREVTPHHLLLN--DDMPLG-SYGKVNPPLRDRWTQERLLE- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1692 iDYI----DVFATDHAPHTLAEKRS-ERPPPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNLPDQA----- 1761
Cdd:PRK01211 263 -EYIsgrfDILSSDHAPHTEEDKQEfEYAKSGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIKKGKieegy 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 665391904 1762 -QTYVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKgRVHRVVLRGEV 1807
Cdd:PRK01211 342 dADFMAFDFTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEV 387
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1475-1825 |
6.59e-43 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 164.87 E-value: 6.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1475 RIVkLPGFIDVHVHLREP---GATHKEDFASGTAAALAGGVTLVC--AMPNTNPSIvdRETFTQFQELAKAGARCDYALY 1549
Cdd:PRK13404 50 RLV-LPGGVDSHCHIDQPsgdGIMMADDFYTGTVSAAFGGTTTVIpfAAQHRGQSL--REAVEDYHRRAAGKAVIDYAFH 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1550 VGASDDNWAQVNE-----LASHACGLKMYLndTFGTLKLSD-------------------------MTSW--QRHLS--- 1594
Cdd:PRK13404 127 LIVADPTEEVLTEelpalIAQGYTSFKVFM--TYDDLKLDDrqildvlavarrhgamvmvhaenhdMIAWltKRLLAagl 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1595 -----HWPKRSPIVchaERQSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERlg 1669
Cdd:PRK13404 205 tapkyHAISRPMLA---EREATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDR-- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1670 HGMSEVRpLLCSP-----EDQEALWENID--YIDVFATDHAPHTLAEKRSERP----------PPGFPGVETILPLLLQA 1732
Cdd:PRK13404 280 PGMEGAK-YICSPpprdkANQEAIWNGLAdgTFEVFSSDHAPFRFDDTDGKLAaganpsfkaiANGIPGIETRLPLLFSE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1733 -VHEGRLTMEDIKRKFHRNPKIIFNL-PDQAQTYVEVDLD-------EEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVL 1803
Cdd:PRK13404 359 gVVKGRISLNRFVALTSTNPAKLYGLyPRKGAIAIGADADiaiwdpdREVTITNADLHHAADYTPYEGMRVTGWPVTVLS 438
|
410 420
....*....|....*....|..
gi 665391904 1804 RGEVAFVDGQVLVQPGFGQNVR 1825
Cdd:PRK13404 439 RGRVVVEDGELVAERGSGQFLA 460
|
|
| pyrB |
PRK13814 |
aspartate carbamoyltransferase; |
1919-2215 |
7.08e-43 |
|
aspartate carbamoyltransferase;
Pssm-ID: 139876 [Multi-domain] Cd Length: 310 Bit Score: 159.88 E-value: 7.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1919 HILAVDMFNKDHLNDIFNLAQLLKLRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNITSSVKK 1998
Cdd:PRK13814 7 HLLNMRSLTRDHIEKLIQRANYFLTQGMEKNSVFETLKGHVVANLFFEPSTRTRNSFEIAAKRLGAMVLNPNLKISAISK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1999 GESLEDSIKVVSSYA-DVVVLRHP---SPGAVARaaTFSRKPLINAGDGVGEHPTQALLDIFTIREEFGTVNGLTITMVG 2074
Cdd:PRK13814 87 GETLFDTIKTLEAMGvYFFIVRHSeneTPEQIAK--QLSSGVVINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2075 DLKNGRTVHSLAR-LLTLYNVNLQYVAPNSLqMPDEvvqfVHQRGVKQLfaRDLKNVLPDTDVLYMTRIQRERFDNVEDY 2153
Cdd:PRK13814 165 DIRHSRVANSLMDgLVTMGVPEIRLVGPSSL-LPDK----VGNDSIKKF--TELKPSLLNSDVIVTLRLQKERHDNSVDI 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391904 2154 EKCCGHLVLTPEHMMRAKKRSIVLHPLP--RLNEISREIDSDPRAAYFRQAEYGMYIRMALLAM 2215
Cdd:PRK13814 238 DAFRGSFRLTPEKLYSAKPDAIVMHPGPvnREVEINSDVADNQQSVILQQVRNGVAMRMAVLEL 301
|
|
| PRK00779 |
PRK00779 |
ornithine carbamoyltransferase; Provisional |
1914-2214 |
9.08e-43 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 234835 [Multi-domain] Cd Length: 304 Bit Score: 159.49 E-value: 9.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1914 SLMGKHILAVDMFNKDHLNDIFNLAQLLKlRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNIT 1993
Cdd:PRK00779 1 MLMGRHFLSLDDLSPEELEELLDLAAELK-KKRKAGEPHPPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIFLSPRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1994 SSVKKGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINA-GDgvGEHPTQALLDIFTIREEFGTVNGLTITM 2072
Cdd:PRK00779 80 TQLGRGEPIEDTARVLSRYVDAIMIRTFEHETLEELAEYSTVPVINGlTD--LSHPCQILADLLTIYEHRGSLKGLKVAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2073 VGDlknGRTV-HSLARLLTLYNVNLQYVAPNSLQMPDEVV-QFVHQRGVKQLFARDLKNVLPDTDVLY--------MTRI 2142
Cdd:PRK00779 158 VGD---GNNVaNSLLLAAALLGFDLRVATPKGYEPDPEIVeKIAKETGASIEVTHDPKEAVKGADVVYtdvwvsmgQEAE 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665391904 2143 QRERFDNVEDYEkccghlvLTPEHMMRAKKRSIVLHPLP--RLNEISRE-IDSdPRAAYFRQAEYGMYIRMALLA 2214
Cdd:PRK00779 235 AEERLKAFAPYQ-------VNEELMALAKPDAIFMHCLPahRGEEVTDEvIDG-PQSVVWDEAENRLHAQKALLA 301
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1327-1453 |
3.91e-41 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 147.83 E-value: 3.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1327 NAVLLSIGSFKhKMELLPSIRDLAKMGYKLYASMGTGDFYAEHGVNVESVQWTFDKTTPDDingelRHLAEFLANKQFDL 1406
Cdd:cd01423 1 KGILISIGSYS-KPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK-----PSLRELLAEGKIDL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 665391904 1407 VINLPMSGGGARRVSsfmthGYRTRRLAVDYSIPLVTDVKCTKLLVE 1453
Cdd:cd01423 75 VINLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
|
|
| OTCace |
pfam00185 |
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain; |
2069-2216 |
5.15e-37 |
|
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
Pssm-ID: 425511 [Multi-domain] Cd Length: 154 Bit Score: 137.36 E-value: 5.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2069 TITMVGDlKNGRTVHSLARLLTLYNVNLQYVAPNSLQMPDEVV----QFVHQRGVKQLFARDLKNVLPDTDVLYMTRIQ- 2143
Cdd:pfam00185 1 KIAYVGD-GHNNVAHSLIIAAAKLGMDVRLATPKGYPPDPEVLdkakKIAEKSGGSIEITDDPAEAVKGADVVYTDVWQs 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665391904 2144 ----RERFDNVEDYEKCCghlvLTPEHMMRAKKRSIVLHPLP--RLNEISREIDSDPRAAYFRQAEYGMYIRMALLAMV 2216
Cdd:pfam00185 80 mgqeKEREERLKAFKPYQ----VNEELMKLAKKDAIFMHCLPahRGEEVTDDVFDGPRSVVFDQAENRLHAQKALLALL 154
|
|
| PLN02795 |
PLN02795 |
allantoinase |
1477-1818 |
9.56e-36 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 144.15 E-value: 9.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1477 VKLPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMP-NTNPSIVDRETFTQFQELAKAGARCDYALYVGASDD 1555
Cdd:PLN02795 96 VVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1556 NWAQVNELASH----ACGLKMYL-----ND---TFGT---LKLSDMTSWQRH-LSHWPKRSPIVCHAERQSTAAVIMlAH 1619
Cdd:PLN02795 176 NAHNASVLEELldagALGLKSFMcpsgiNDfpmTTAThikAALPVLAKYGRPlLVHAEVVSPVESDSRLDADPRSYS-TY 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1620 LLDR----------------------------SVHICHVAR-KEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERlGH 1670
Cdd:PLN02795 255 LKSRppsweqeairqllevakdtrpggvaegaHVHIVHLSDaESSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPD-GD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1671 GMSEVRPLLCSPEDQEALWENI--DYIDVFATDHAPHTLAEKRSE-----RPPPGFPGVETILPLLLQAVHEGRLTMEDI 1743
Cdd:PLN02795 334 TRYKCAPPIRDAANRELLWKALldGDIDMLSSDHSPSPPDLKLLEegnflRAWGGISSLQFVLPATWTAGRAYGLTLEQL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1744 KRKFHRNPKIIFNLPD--------QAQTYV-----EVDLDEEWTItgnEMKSKSgWTPFEGTKVKGRVHRVVLRGEVAFV 1810
Cdd:PLN02795 414 ARWWSERPAKLAGLDSkgaiapgkDADIVVwdpeaEFVLDESYPI---YHKHKS-LSPYLGTKLSGKVIATFVRGNLVFL 489
|
....*...
gi 665391904 1811 DGQVLVQP 1818
Cdd:PLN02795 490 EGKHAKQA 497
|
|
| pyrB |
PRK13376 |
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase ... |
1914-2218 |
3.93e-32 |
|
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase regulatory subunit; Provisional
Pssm-ID: 237369 [Multi-domain] Cd Length: 525 Bit Score: 133.73 E-value: 3.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1914 SLMGKHILAVDMFNKDHLNDIFNLAQLLKLRGTKDRPVDELLPGKI---MASVFYEVSTRTQCSFA-AAMLRLGGRVISM 1989
Cdd:PRK13376 4 DFLGRTLAVIEDLSVEEQLFLYEKTRELKQRWYEGEDVSEFRIKKRdvgIYIVFVEPSTRTKESFInAAKFHKNVKVNIF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1990 DNITSSVKKGESLEDSIKVVSSYAD--VVVLRHPSPG----------AVARAATFSRKPLINAGDGVGEHPTQALLDIFT 2057
Cdd:PRK13376 84 DSEHSSFNKQESYTDTFNMLTGYSDysIFIVRTRLEGvcrlleekvsEFASRNGIEVPAFINAGDGKHEHPTQELLDEFT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2058 IREEFGTVNG-LTITMVGDLKNGRTVHSLARLLTLY-NVNLQYVAPNSLQMPDEVVQFVHQRGVKQLFARDLKNVLPDTD 2135
Cdd:PRK13376 164 FLEQNNFDNSfIHIALVGDLLHGRTVHSKVNGLKIFkNVKVDLIAPEELAMPEHYVEKMKKNGFEVRIFSSIEEYLSQKD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2136 VL---YMTRIQRERFdnvedyekccGHLVLTPEHMMRakkRSIVL---------------HPLPRLN---EISREIDSDP 2194
Cdd:PRK13376 244 VAkiwYFTRLQLERM----------GEDILEKEHILR---KAVTFrkefldklpegvkfyHPLPRHKvypTIPTFLDTLP 310
|
330 340
....*....|....*....|....
gi 665391904 2195 RAAYFRQAEYGMYIRMALLAMVVG 2218
Cdd:PRK13376 311 LNGWETQAINGYWVRIVLLSMLGG 334
|
|
| PLN02342 |
PLN02342 |
ornithine carbamoyltransferase |
1875-2218 |
6.07e-32 |
|
ornithine carbamoyltransferase
Pssm-ID: 177976 [Multi-domain] Cd Length: 348 Bit Score: 129.52 E-value: 6.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1875 GANFLRPNSPSPRIRLDSASNTTLREYLQRTTNS-NPVAHSLMGKHILAVDMFNKDHLNDIFNLAQLLKLR-GTKDR--- 1949
Cdd:PLN02342 2 FFSLRRARSPSAVSSSSRARRGLVVCAASSSAAApSPIKGKSKPKHFLHIDDFDKEEILGLLDRAKEVKALlKSGDRsfq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1950 PvdelLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNITSSVKKGESLEDSIKVVSSYADVVVLRHPSPGAVARA 2029
Cdd:PLN02342 82 P----FKGKSMAMIFTKPSMRTRVSFETGFFLLGGHALYLGPDDIQLGKREETRDIARVLSRYNDIIMARVFAHQDVLDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2030 ATFSRKPLINAGDGVgEHPTQALLDIFTIREEFGTVNGLTITMVGDLKNgrTVHSLARLLTLYNVNLQYVAPNSLQMPDE 2109
Cdd:PLN02342 158 AEYSSVPVINGLTDY-NHPCQIMADALTIIEHIGRLEGTKVVYVGDGNN--IVHSWLLLAAVLPFHFVCACPKGYEPDAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2110 VVQFVHQRGVKQLFAR-DLKNVLPDTDVLY------MTriQRERFDN-VEDYEkccGHLVltPEHMM-RAKKRSIVLHPL 2180
Cdd:PLN02342 235 TVEKARAAGISKIEITnDPAEAVKGADVVYtdvwasMG--QKEEAEKrKKAFQ---GFQV--NEALMkLAGPQAYFMHCL 307
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 665391904 2181 P--RLNEISREIDSDPRAAYFRQAEYGMYIRMALLAMVVG 2218
Cdd:PLN02342 308 PaeRGVEVTDGVMEAPNSIVFPQAENRMHAQNAIMLHQLG 347
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
815-892 |
7.81e-32 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 119.79 E-value: 7.81e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665391904 815 EQLSEPTDRRPFVIAAALQLGMSLRELHQLTNIDYWFLEKLERIILLQSLLTRNGSRTDAALLLKAKRFGFSDKQIAK 892
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDAELLREAKRLGFSDRQIAK 78
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1469-1809 |
1.27e-31 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 130.75 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1469 DCMTSRRIVKLPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMP-NTNPSIVDRETFTQFQELAKAGARCDYA 1547
Cdd:PRK08044 42 EVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1548 LYVGASDDNWAQVNELASHA----------CGLKMYLNDtfgtlkLSDMTSWQ-----RHLSHWPKrsPIVCHAER---- 1608
Cdd:PRK08044 122 QLGGLVSYNLDRLHELDEVGvvgfkcfvatCGDRGIDND------FRDVNDWQfykgaQKLGELGQ--PVLVHCENalic 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1609 -----------QSTAA-----------------VIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFL 1660
Cdd:PRK08044 194 delgeeakregRVTAHdyvasrpvfteveairrVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1661 STKDVERLGhgmsevrPLL-CSP-----EDQEALWENI--DYIDVFATDHAPHT--LAEKRSERPPPGFPGVETILPLLL 1730
Cdd:PRK08044 274 DTDQFEEIG-------TLAkCSPpirdlENQKGMWEKLfnGEIDCLVSDHSPCPpeMKAGNIMEAWGGIAGLQNCMDVMF 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1731 -QAVHEGRLTMEDIKRKFHRNPKIIFNL-------PDQAQTYVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVV 1802
Cdd:PRK08044 347 dEAVQKRGMSLPMFGKLMATNAADIFGLqqkgriaPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTI 426
|
....*..
gi 665391904 1803 LRGEVAF 1809
Cdd:PRK08044 427 LRGDVIY 433
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
1480-1798 |
2.94e-31 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 128.95 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1480 PGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNT-----NPSIVDR-------------------------E 1529
Cdd:PRK07369 57 PGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTfppldNPATLARlqqqaqqippvqlhfwgaltlggqgK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1530 TFTQFQELAKAGArcdyalyVGASDD----NWAQVNELAShacglkmYLNdtfgtlklsdmtSWQRHLSHWPKRS----- 1600
Cdd:PRK07369 137 QLTELAELAAAGV-------VGFTDGqpleNLALLRRLLE-------YLK------------PLGKPVALWPCDRslagn 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1601 ---------------PIVCHAERQSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDV 1665
Cdd:PRK07369 191 gvmregllalrlglpGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEAL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1666 E------RLghgmsevRPLLCSPEDQEALWENID--YIDVFATDHAPHTLAEKR---SErPPPGFPGVETILPLLLQA-V 1733
Cdd:PRK07369 271 AsydpnlRL-------DPPLGNPSDRQALIEGVRtgVIDAIAIDHAPYTYEEKTvafAE-APPGAIGLELALPLLWQNlV 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665391904 1734 HEGRLTMEDIKRKFHRNPKIIFNL------PDQAQTYVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRV 1798
Cdd:PRK07369 343 ETGELSALQLWQALSTNPARCLGQeppslaPGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRV 413
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
1476-1809 |
7.19e-31 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 127.87 E-value: 7.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1476 IVKLPGFIDVHVHLREPGATHKEDFASGTAAALAGGVT-LVCAmPNTNP-----SIVDRETFtQFQELAKAGARCDYALY 1549
Cdd:PRK07627 51 LIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTsLVCP-PDTDPvldepGLVEMLKF-RARNLNQAHVYPLGALT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1550 VGASDDNWAQVNELASHAC-GLK---------------MYLNDTFGtlklsdMTSWQRHLSHWPKR-------------- 1599
Cdd:PRK07627 129 VGLKGEVLTEMVELTEAGCvGFSqanvpvvdtqvllraLQYASTFG------FTVWLRPLDAFLGRggvaasgavasrlg 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1600 -SPIVCHAERQSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLSTKDVerlGHGMSEVR-- 1676
Cdd:PRK07627 203 lSGVPVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDI---GYFDSQFRld 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1677 PLLCSPEDQEALWENI--DYIDVFATDHAPHTLAEKR---SErPPPGFPGVETILPLLLQAVHEGRLTMEDIKRKFHRNP 1751
Cdd:PRK07627 280 PPLRSQRDREAIRAALadGTIDAICSDHTPVDDDEKLlpfAE-ATPGATGLELLLPLTLKWADEAKVPLARALARITSAP 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665391904 1752 KIIFNLPdqAQTYVE--------VDLDEEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAF 1809
Cdd:PRK07627 359 ARVLGLP--AGRLAEgapadlcvFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAF 422
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
1457-1809 |
2.13e-29 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 123.61 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1457 MNGGKPPMKTHTDCmtsRRIVKLPGFIDVHVHLREPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVD--------- 1527
Cdd:PRK09059 40 GNQGAPEGAEIVDC---AGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDvalvefvkr 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1528 --RET-------------------FTQFQELAKAGArcdYALYVGASDDNWAQV-----------NELASHACGLKmYLN 1575
Cdd:PRK09059 117 taRDTaivnihpaaaitkglageeMTEFGLLRAAGA---VAFTDGRRSVANTQVmrraltyardfDAVIVHETRDP-DLG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1576 DTfGTLKLSDMTSWQrHLSHWPKRSPIVChAERQstaavIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCP 1655
Cdd:PRK09059 193 GN-GVMNEGLFASWL-GLSGIPREAEVIP-LERD-----LRLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1656 HHLFLSTKDVerlghgmSEVR------PLLCSPEDQEALWENID--YIDVFATDHAPHTLAEKR---SErPPPGFPGVET 1724
Cdd:PRK09059 265 NHLSLNENDI-------GEYRtffklsPPLRTEDDRVAMVEAVAsgTIDIIVSSHDPQDVDTKRlpfSE-AAAGAIGLET 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1725 ILPLLLQAVHEGRLTMEDIKRKFHRNPKIIFNL------PDQAQTYVEVDLDEEWTITGNEMKSKSGWTPFEGTKVKGRV 1798
Cdd:PRK09059 337 LLAAALRLYHNGEVPLLRLIEALSTRPAEIFGLpagtlkPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRV 416
|
410
....*....|.
gi 665391904 1799 HRVVLRGEVAF 1809
Cdd:PRK09059 417 VRTIVAGKTVY 427
|
|
| PRK02102 |
PRK02102 |
ornithine carbamoyltransferase; Validated |
1911-2181 |
6.92e-28 |
|
ornithine carbamoyltransferase; Validated
Pssm-ID: 179366 [Multi-domain] Cd Length: 331 Bit Score: 116.91 E-value: 6.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1911 VAHSLMGKHILAVDMFNKDHLNDIFNLAQLLKlRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMD 1990
Cdd:PRK02102 1 MAFNLKGRSFLKLLDFTPEEIEYLIDLSIELK-AAKKAGIEHQYLEGKNIALIFEKTSTRTRCAFEVAAIDLGAHVTYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1991 NITSSVKKGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINAGDGVgEHPTQALLDIFTIREEFGTVNGLTI 2070
Cdd:PRK02102 80 PNDSQLGKKESIEDTARVLGRMYDGIEYRGFKQEIVEELAKYSGVPVWNGLTDE-WHPTQMLADFMTMKEHFGPLKGLKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2071 TMVGDLKNgRTVHSLARLLTLYNVNLQYVAPNSLQMPDEVV----QFVHQRGVKQLFARDLKNVLPDTDVLYmTRI---- 2142
Cdd:PRK02102 159 AYVGDGRN-NMANSLMVGGAKLGMDVRICAPKELWPEEELValarEIAKETGAKITITEDPEEAVKGADVIY-TDVwvsm 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 665391904 2143 -----QRERFDnvedyekccghlVLTP----EHMMRA--KKRSIVLHPLP 2181
Cdd:PRK02102 237 geedeWEERIK------------LLKPyqvnMDLMKAtgNPDVIFMHCLP 274
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1341-1443 |
4.36e-23 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 95.25 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1341 ELLPSIRDLAKMGYKLYASMGTGDFYAEHGVNVESVQWtfdKTTPDDINGELRHLAeFLANKQFDLVINLPMSGGGARRv 1420
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVE---KTGEGRPGGRVQIGD-LIKNGEIDLVINTLYPFKATVH- 75
|
90 100
....*....|....*....|...
gi 665391904 1421 ssfmtHGYRTRRLAVDYSIPLVT 1443
Cdd:pfam02142 76 -----DGYAIRRAAENIDIPGPT 93
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
1050-1261 |
1.55e-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: 93.78 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1050 GTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAS 1129
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1130 E----VSREHPVVISKFLtEAKEIDVDAVASDGRILCMAVSEHvENAGVHSGDATLVTPPqDLNAETLEAIKRITCDLAS 1205
Cdd:COG0439 123 AeakaGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGELVARALR 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 665391904 1206 VLDV-TGPFNMQ-LIAKNNELKVIECNVRVSrsfpfvsktldHDFVATATRAIVGLDV 1261
Cdd:COG0439 200 ALGYrRGAFHTEfLLTPDGEPYLIEINARLG-----------GEHIPPLTELATGVDL 246
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1084-1265 |
2.02e-20 |
|
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: 91.60 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1084 NLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASEVSRE----HPVVISKFLTEAKEIDVDAVAsDGR 1159
Cdd:pfam02786 26 TEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnPQVLVEKSLKGPKHIEYQVLR-DAH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1160 ILCMAVSEhVENA-GVHSGDATLVTPPQDLNAETLEAIKRITCDLASVLDVTGPFNMQLI--AKNNELKVIECNVRVSRS 1236
Cdd:pfam02786 105 GNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFAldPFSGEYYFIEMNTRLQVE 183
|
170 180
....*....|....*....|....*....
gi 665391904 1237 FPFVSKTLDHDFVATATRAIVGldvEPLD 1265
Cdd:pfam02786 184 HALAEKATGYDLAKEAAKIALG---YPLP 209
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1341-1443 |
6.51e-19 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 83.29 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1341 ELLPSIRDLAKMGYKLYASMGTGDFYAEHGVNVEsvqwtfdKTTPDDINGELRHLAEFLANKQFDLVINLPMSGGgarrv 1420
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVV-------KTLHPKVHGGIPQILDLIKNGEIDLVINTLYPFE----- 68
|
90 100
....*....|....*....|...
gi 665391904 1421 SSFMTHGYRTRRLAVDYSIPLVT 1443
Cdd:smart00851 69 AQAHEDGYSIRRAAENIDIPGPT 91
|
|
| PRK14805 |
PRK14805 |
ornithine carbamoyltransferase; Provisional |
1918-2219 |
3.85e-18 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 237819 [Multi-domain] Cd Length: 302 Bit Score: 87.44 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1918 KHILAVDMFNKDHLNDIFNLAQLLKLRGTKDRPVdelLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNITSSVK 1997
Cdd:PRK14805 2 KHLLSIKELTQQQLLDLLALAKTIKANPAEYRQA---LAGKSVVMLFEKPSLRTRVSFDIGINKLGGHCLYLDQQNGALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1998 KGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINAGDGVgEHPTQALLDIFTIREEFGTVNGLTITMVGDLK 2077
Cdd:PRK14805 79 KRESVADFAANLSCWADAIVARVFSHSTIEQLAEHGSVPVINALCDL-YHPCQALADFLTLAEQFGDVSKVKLAYVGDGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2078 NgrTVHSLARLLTLYNVNLQYVAPNSlQMPD-EVV----QFVHQRGVKQLFARDLkNVLPDTDVLYM-TRIQRERFDNVE 2151
Cdd:PRK14805 158 N--VTHSLMYGAAILGATMTVICPPG-HFPDgQIVaeaqELAAKSGGKLVLTSDI-EAIEGHDAIYTdTWISMGDDTPLA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2152 DYEKCCGHLVLTPEHMMRAKKRSiVLHPLP--RLNEISREIDSDPRAAYFRQAEYGMYIRMALLAMVVGG 2219
Cdd:PRK14805 234 EIKAKFAPYQVNKALMEKAGATF-VMHCQPahRGVEITSEVMDGEGSLILQQAENRMHAQNAVLVTLLSQ 302
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
195-355 |
9.43e-18 |
|
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: 84.61 E-value: 9.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 195 RIAILDCGL---KLNQL--RCLLQRGASVT--------LLPWSARLEDeqFDALFLSNGPGNPESCDQIVQQVRKVIE-- 259
Cdd:COG0518 1 KILILDHDPfggQYPGLiaRRLREAGIELDvlrvyageILPYDPDLED--PDGLILSGGPMSVYDEDPWLEDEPALIRea 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 260 -EGQKPVFGICLGHQLLAKAIGCSTYKMKYGNRG-------------HNLPclhrATGRCLMTsqnHGYAVDleQLPDGW 325
Cdd:COG0518 79 fELGKPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelteadplfAGLP----DEFTVWMS---HGDTVT--ELPEGA 149
|
170 180 190
....*....|....*....|....*....|
gi 665391904 326 SELFVNANDgTNEGIVHaSKPYFSVQFHPE 355
Cdd:COG0518 150 EVLASSDNC-PNQAFRY-GRRVYGVQFHPE 177
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
211-355 |
1.01e-17 |
|
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: 82.97 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 211 LLQRGASVTLLPWSARLEDE----QFDALFLSNGPGNPEScDQIVQQVRKVIEeGQKPVFGICLGHQLLAKAIGCSTYKM 286
Cdd:cd01743 18 LRELGAEVVVVRNDEITLEElellNPDAIVISPGPGHPED-AGISLEIIRALA-GKVPILGVCLGHQAIAEAFGGKVVRA 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665391904 287 KYGNRGHNLPCLHRATGRCLMTSQN------HGYAVDLEQLPDgwsELFVNANDGTNE--GIVHASKPYFSVQFHPE 355
Cdd:cd01743 96 PEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPD---LLEVTASTEDGVimALRHRDLPIYGVQFHPE 169
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
530-724 |
1.57e-17 |
|
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: 84.92 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 530 ERVNEIGEQVAPSEAVYSVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQALAH------SSQLIVDKS 603
Cdd:COG0439 60 EALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEakagspNGEVLVEEF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 604 LKGwKEVEYEVVrdAYNNCITVCNM---ENFDPLGIHTGEsivVAPSQtLSDREYQMLRSTALKVIRHFGVV-GECNIQY 679
Cdd:COG0439 140 LEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEF 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 665391904 680 ALCPHSEqYYIIEVNARLS--RSSALASKATGYPLAYVAAKLALGLP 724
Cdd:COG0439 213 LLTPDGE-PYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
225-355 |
2.15e-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: 79.31 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 225 ARLEDEQFDALFLSNGPGNPES---CDQIVQQVRkvieeGQKPVFGICLGHQLLAKAIGCSTYKMKY---G--------N 290
Cdd:COG0512 36 EEIEALAPDGIVLSPGPGTPEEagiSLEVIRAFA-----GKIPILGVCLGHQAIGEAFGGKVVRAPEpmhGktspithdG 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665391904 291 RG--HNLPCLHRATgRclmtsqnhgY---AVDLEQLPDgwsELFVNA--NDGTNEGIVHASKPYFSVQFHPE 355
Cdd:COG0512 111 SGlfAGLPNPFTAT-R---------YhslVVDRETLPD---ELEVTAwtEDGEIMGIRHRELPIEGVQFHPE 169
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
1329-1443 |
4.58e-16 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 75.98 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1329 VLLSIgSFKHKMELLPSIRDLAKMGYKLYASMGTGDFYAEHGVNVESVqwtfdkttpDDINGELRHLAEFLANKQFDLVI 1408
Cdd:cd01424 3 VFISV-ADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVV---------NKVSEGRPNIVDLIKNGEIQLVI 72
|
90 100 110
....*....|....*....|....*....|....*
gi 665391904 1409 NLPmSGGGARRvssfmtHGYRTRRLAVDYSIPLVT 1443
Cdd:cd01424 73 NTP-SGKRAIR------DGFSIRRAALEYKVPYFT 100
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
1479-1824 |
3.25e-15 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 81.04 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREP--GATHKEDFASGTAAALAGGVTLVC--AMPnTNPSIVdrETFTQFQELAKAGArCDYALYVGAS- 1553
Cdd:PLN02942 56 MPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTMHIdfVIP-VNGNLL--AGYEAYEKKAEKSC-MDYGFHMAITk 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1554 -DDNWAQVNELASHACGL---KMYLNDTfGTLKLSD---MTSWQRHLS-------------------------------- 1594
Cdd:PLN02942 132 wDDTVSRDMETLVKEKGInsfKFFMAYK-GSLMVTDellLEGFKRCKSlgalamvhaengdavfegqkrmielgitgpeg 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1595 HWPKRSPIVchaERQSTAAVIMLAHLLDRSVHICHVARKEEIQLIRSAKEKGVKVTCEVCPHHLFLstkDVERL------ 1668
Cdd:PLN02942 211 HALSRPPLL---EGEATARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVL---DDSKLwdpdft 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1669 ---GHGMSevrPLLCSPEDQEALWENID--YIDVFATDHAPHTLAEKRS-----ERPPPGFPGVETILPLLLQA-VHEGR 1737
Cdd:PLN02942 285 iasKYVMS---PPIRPAGHGKALQAALSsgILQLVGTDHCPFNSTQKAFgkddfRKIPNGVNGIEERMHLVWDTmVESGQ 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1738 LTMEDIKRKFHRNPKIIFNL-PDQAQTYVEVDLD-------EEWTITGNEMKSKSGWTPFEGTKVKGRVHRVVLRGEVAF 1809
Cdd:PLN02942 362 ISPTDYVRVTSTECAKIFNIyPRKGAILAGSDADiiilnpnSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVW 441
|
410
....*....|....*
gi 665391904 1810 VDGQVLVQPGFGQNV 1824
Cdd:PLN02942 442 ENGELKVVRGSGRYI 456
|
|
| PRK01713 |
PRK01713 |
ornithine carbamoyltransferase; Provisional |
1911-2213 |
5.55e-15 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 167263 [Multi-domain] Cd Length: 334 Bit Score: 78.49 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1911 VAHSLMGKHILAVDMFNKDHLNDIFNLAQLLKlRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMD 1990
Cdd:PRK01713 1 MAFNLKNRHLLSLVNHTEREIKYLLDLSRDLK-RAKYAGTEQQRLKGKNIALIFEKTSTRTRCAFEVAAYDQGAQVTYID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1991 NITSSVKKGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINagdGVGE--HPTQALLDIFTIREEFGT-VNG 2067
Cdd:PRK01713 80 PNSSQIGHKESMKDTARVLGRMYDAIEYRGFKQSIVNELAEYAGVPVFN---GLTDefHPTQMLADVLTMIENCDKpLSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2068 LTITMVGDLKNGRTvHSLARLLTLYNVNLQYVAPNSLQMPDEVV----QFVHQRGVKQLFARDLKNVLPDTDVLYMT--- 2140
Cdd:PRK01713 157 ISYVYIGDARNNMG-NSLLLIGAKLGMDVRICAPKALLPEASLVemceKFAKESGARITVTDDIDKAVKGVDFVHTDvwv 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2141 ------RIQRERFDNVEDYEkccghlvLTPEHMMRAKKRSI-VLHPLPRLN---------------------EISREIDS 2192
Cdd:PRK01713 236 smgeplETWGERIKLLMPYQ-------VTPELMKRTGNPKVkFMHCLPAFHnsetkvgrqiaekypelangiEVTEDVFE 308
|
330 340
....*....|....*....|.
gi 665391904 2193 DPRAAYFRQAEYGMYIRMALL 2213
Cdd:PRK01713 309 SPMNIAFEQAENRMHTIKAVM 329
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
1482-1751 |
6.28e-15 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 77.37 E-value: 6.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1482 FIDVHVHLREPGATH------------------KEDFASGTAAALAGGVTLVCAMPNTNPSIVDRETFTQFQELAKAGAR 1543
Cdd:cd01292 1 FIDTHVHLDGSALRGtrlnlelkeaeelspedlYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1544 CDYALYVGASDDNWAQVNELASH------------ACGLKMYLNDTFGTLKLSdmtSWQRHLSHWPKR-SPIVCHAErQS 1610
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEDAEALllellrrglelgAVGLKLAGPYTATGLSDE---SLRRVLEEARKLgLPVVIHAG-EL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1611 TAAVIML-----AHLLDRSVHICHVAR--KEEIQLIrsakeKGVKVTCEVCPHHLFLSTKDverlghgmsevrpllcsPE 1683
Cdd:cd01292 157 PDPTRALedlvaLLRLGGRVVIGHVSHldPELLELL-----KEAGVSLEVCPLSNYLLGRD-----------------GE 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665391904 1684 DQEALWENIDY--IDVFATDHAPHTLAekrserpppgfpgveTILPLLLQ-AVHEGRL--TMEDIKRKFHRNP 1751
Cdd:cd01292 215 GAEALRRLLELgiRVTLGTDGPPHPLG---------------TDLLALLRlLLKVLRLglSLEEALRLATINP 272
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
195-357 |
8.36e-15 |
|
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: 74.97 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 195 RIAILDC------GLKLNQLRCLLQRGASVTLLPWSAR---LEDEQFDALFLSNGPGNPESCD-----QIVQQVRKVIEE 260
Cdd:cd01741 1 RILILQHdtpegpGLFEDLLREAGAETIEIDVVDVYAGellPDLDDYDGLVILGGPMSVDEDDypwlkKLKELIRQALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 261 GqKPVFGICLGHQLLAKAIGCSTYKMKYG-----------NRGHNLPcLHRATGRCLMTSQNHGYAVDLeqLPDGWSELF 329
Cdd:cd01741 81 G-KPVLGICLGHQLLARALGGKVGRNPKGweigwfpvtltEAGKADP-LFAGLPDEFPVFHWHGDTVVE--LPPGAVLLA 156
|
170 180
....*....|....*....|....*...
gi 665391904 330 vnANDGTNEGIVHASKPYFSVQFHPEHH 357
Cdd:cd01741 157 --SSEACPNQAFRYGDRALGLQFHPEER 182
|
|
| PRK12562 |
PRK12562 |
ornithine carbamoyltransferase subunit F; Provisional |
1918-2218 |
1.65e-14 |
|
ornithine carbamoyltransferase subunit F; Provisional
Pssm-ID: 105755 Cd Length: 334 Bit Score: 77.02 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1918 KHILAVDMFNKDHLNDIFNLAQLLKLRGTKDRPVDELlPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNITSSVK 1997
Cdd:PRK12562 7 KHFLKLLDFTPAELNSLLQLAAKLKADKKNGKEVARL-TGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1998 KGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINaGDGVGEHPTQALLDIFTIREEF--GTVNGLTITMVGD 2075
Cdd:PRK12562 86 HKESIKDTARVLGRMYDGIQYRGHGQEVVETLAEYAGVPVWN-GLTNEFHPTQLLADLLTMQEHLpgKAFNEMTLVYAGD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2076 LKNGRTvHSLARLLTLYNVNLQYVAPNSL----QMPDEVVQFVHQRGVKQLFARDLKNVLPDTDVLY------MTRIQR- 2144
Cdd:PRK12562 165 ARNNMG-NSMLEAAALTGLDLRLVAPQACwpeaSLVAECSALAQKHGGKITLTEDIAAGVKGADFIYtdvwvsMGEPKEk 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2145 --ERFDNVEDYEKCCGHLVLTPEHMMRakkrsiVLHPLPRLN--------------------EISREIDSDPRAAYFRQA 2202
Cdd:PRK12562 244 waERIALLRGYQVNSKMMALTGNPQVK------FLHCLPAFHddqttlgkkmakefglhggmEVTDEVFESPASIVFDQA 317
|
330
....*....|....*.
gi 665391904 2203 EYGMYIRMALLAMVVG 2218
Cdd:PRK12562 318 ENRMHTIKAVMVATLA 333
|
|
| PRK04523 |
PRK04523 |
N-acetylornithine carbamoyltransferase; Reviewed |
1918-2219 |
2.10e-14 |
|
N-acetylornithine carbamoyltransferase; Reviewed
Pssm-ID: 235304 [Multi-domain] Cd Length: 335 Bit Score: 76.71 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1918 KHILAVDMFNKDHLNDIFNLAQLLKlrgtkDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNITSS-- 1995
Cdd:PRK04523 4 KHFLNTQDWSRAELDALLTQAAAFK-----RNKLGSALKGKSIALVFFNPSLRTRTSFELGAFQLGGHAVVLQPGKDAwp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1996 -------VKKGESLE---DSIKVVSSYADVVVLRHPSPG-------------AVARAATFsrkPLINAGDGVgeHPTQAL 2052
Cdd:PRK04523 79 iefelgaVMDGETEEhirEVARVLSRYVDLIGVRAFPKFvdwskdrqdqvlnSFAKYSTV---PVINMETIT--HPCQEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2053 LDIFTIREEFG-TVNGLT--ITMVGDLK--NGRTVHSLARLLTLYNVNLQYVAPNSLQMPDEVV-----QFVHQRGVKQL 2122
Cdd:PRK04523 154 AHALALQEHFGtTLRGKKyvLTWTYHPKplNTAVANSALLIATRLGMDVTLLCPTPDYILDERYmdwaeQNAAESGGSLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2123 FARDLKNVLPDTDVLY--------------MTRIQRERFDnvedyekccgHLVLTPEHMMRAKKrSIVLHPLP-RLN-EI 2186
Cdd:PRK04523 234 VSHDIDSAYAGADVVYakswgalpffgnwePEKPIRDQYQ----------HFIVDERKMALTNN-GVFSHCLPlRRNvKV 302
|
330 340 350
....*....|....*....|....*....|...
gi 665391904 2187 SREIDSDPRAAYFRQAEYGMYIRMALLAMVVGG 2219
Cdd:PRK04523 303 TDAVMDSPNCIAIDEAENRLHVQKAIMAALASQ 335
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
196-369 |
2.61e-14 |
|
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: 73.50 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 196 IAILDCGLKLNQL--RCLLQRGASVTLLPWSARLE---DEQFDALFLSNGP-----GNPESCDQivqqvrKVIEEGqKPV 265
Cdd:TIGR00888 1 ILVLDFGSQYTQLiaRRLRELGVYSELVPNTTPLEeirEKNPKGIILSGGPssvyaENAPRADE------KIFELG-VPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 266 FGICLGHQLLAKAIGCSTYKMKYGNRGH------NLPCLHRATGRCLMTSQNHGYAVdlEQLPDGWSELFVNANdGTNEG 339
Cdd:TIGR00888 74 LGICYGMQLMAKQLGGEVGRAEKREYGKaeleilDEDDLFRGLPDESTVWMSHGDKV--KELPEGFKVLATSDN-CPVAA 150
|
170 180 190
....*....|....*....|....*....|....
gi 665391904 340 IVHASKPYFSVQFHPEHHAGPQDTE----FLFDV 369
Cdd:TIGR00888 151 MAHEEKPIYGVQFHPEVTHTEYGNEllenFVYDV 184
|
|
| PRK03515 |
PRK03515 |
ornithine carbamoyltransferase subunit I; Provisional |
1918-2101 |
1.25e-13 |
|
ornithine carbamoyltransferase subunit I; Provisional
Pssm-ID: 179587 [Multi-domain] Cd Length: 336 Bit Score: 74.37 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1918 KHILAVDMFNKDHLNDIFNLAQLLKlRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNITSSVK 1997
Cdd:PRK03515 7 RHFLRLLDFTPAELNSLLQLAAKLK-ADKKNGKEEQKLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1998 KGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINagdGVGE--HPTQALLDIFTIREEF--GTVNGLTITMV 2073
Cdd:PRK03515 86 HKESIKDTARVLGRMYDGIQYRGYGQEIVETLAEYAGVPVWN---GLTNefHPTQLLADLLTMQEHLpgKAFNEMTLAYA 162
|
170 180 190
....*....|....*....|....*....|
gi 665391904 2074 GDLKN--GRTVHSLARLLTLynvNLQYVAP 2101
Cdd:PRK03515 163 GDARNnmGNSLLEAAALTGL---DLRLVAP 189
|
|
| PRK04284 |
PRK04284 |
ornithine carbamoyltransferase; Provisional |
1912-2193 |
1.77e-13 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 235269 [Multi-domain] Cd Length: 332 Bit Score: 74.01 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1912 AHSLMGKHILAVDMFNKDHLNDIFNLAQLLKlRGTKDRPVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDN 1991
Cdd:PRK04284 1 MKNLRNRSFLTLLDFTPKEIEYLLDLSEDLK-RAKYAGIEVQKLKGKNIALIFEKDSTRTRCAFEVAAYDQGAHVTYLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1992 ITSSVKKGESLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINaGDGVGEHPTQALLDIFTIREEF-GTVNGLTI 2070
Cdd:PRK04284 80 TGSQMGKKESTKDTARVLGGMYDGIEYRGFSQRTVETLAEYSGVPVWN-GLTDEDHPTQVLADFLTAKEHLkKPYKDIKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2071 TMVGDLKNgRTVHSLARLLTLYNVNLQYVAPNSLQMPDEVV----QFVHQRGVKQLFARDLKNVLPDTDVLYM------- 2139
Cdd:PRK04284 159 TYVGDGRN-NVANALMQGAAIMGMDFHLVCPKELNPDDELLnkckEIAAETGGKITITDDIDEGVKGSDVIYTdvwvsmg 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 665391904 2140 --TRIQRERFDNVEDYEkccghlvLTPEHMMRAK-KRSIVLHPLPRLNEISREIDSD 2193
Cdd:PRK04284 238 epDEVWEERIKLLKPYQ-------VNKEMMKKTGnPNAIFEHCLPSFHDLDTKVGKE 287
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
196-357 |
2.92e-13 |
|
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: 70.26 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 196 IAILDCGLKLNQL--RCLLQRGASVTLLPWS---ARLEDEQFDALFLSNGP-----GNPESCDqivqqvRKVIEEGqKPV 265
Cdd:cd01742 1 ILILDFGSQYTHLiaRRVRELGVYSEILPNTtplEEIKLKNPKGIILSGGPssvyeEDAPRVD------PEIFELG-VPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 266 FGICLGHQLLAKAIGcstykmkygnrGHNLPCLHRATGRCLMTSQ-----------------NHGYAVdlEQLPDGWsEL 328
Cdd:cd01742 74 LGICYGMQLIAKALG-----------GKVERGDKREYGKAEIEIDdssplfeglpdeqtvwmSHGDEV--VKLPEGF-KV 139
|
170 180 190
....*....|....*....|....*....|
gi 665391904 329 FVNANDGTNEGIVHASKPYFSVQFHPE-HH 357
Cdd:cd01742 140 IASSDNCPVAAIANEEKKIYGVQFHPEvTH 169
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
515-792 |
3.17e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 74.29 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 515 PIQSIIETEDRKLFAER-VNEIGEQVAP--SEAVYSVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEEEL------- 584
Cdd:PRK06111 105 PSADIIAKMGSKIEARRaMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELtkafesn 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 585 QSLAQQALAHSSqLIVDKSLKGWKEVEYEVVRDAYNNCitvcnmenfdplgIHTGE---SI------VV--APSQTLSDR 653
Cdd:PRK06111 185 KKRAANFFGNGE-MYIEKYIEDPRHIEIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPFLDEE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 654 EYQMLRSTALKVIRHFGVVGECNIQYaLCPHSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGLPLP----DIK 729
Cdd:PRK06111 251 TRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSftqdDIK 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 730 nsVTGNTTAC---------FEPSLDycvvKIPRWDLAK--FVRVSKHIGSSMK-------SVGEVMAIGRNFEEAFQK-- 789
Cdd:PRK06111 330 --RSGHAIEVriyaedpktFFPSPG----KITDLTLPGgeGVRHDHAVENGVTvtpfydpMIAKLIAHGETREEAISRlh 403
|
....
gi 665391904 790 -ALR 792
Cdd:PRK06111 404 dALE 407
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
233-355 |
4.23e-13 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 69.77 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 233 DALFLSNGPGNPE---SCDQIVQQVRkvieeGQKPVFGICLGHQLLAKAIGcstykmkyGNRGHNLPCLHRATGrcLMTS 309
Cdd:PRK05670 45 DAIVLSPGPGTPAeagISLELIREFA-----GKVPILGVCLGHQAIGEAFG--------GKVVRAKEIMHGKTS--PIEH 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391904 310 QNHG-------------Y---AVDLEQLPDgwsELFVNA--NDGTNEGIVHASKPYFSVQFHPE 355
Cdd:PRK05670 110 DGSGifaglpnpftvtrYhslVVDRESLPD---CLEVTAwtDDGEIMGVRHKELPIYGVQFHPE 170
|
|
| PRK14804 |
PRK14804 |
ornithine carbamoyltransferase; Provisional |
1918-2203 |
3.59e-12 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 173265 [Multi-domain] Cd Length: 311 Bit Score: 69.67 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1918 KHILAVDMFNKDHLNDIFNLAQLLKlrgtKDR-PVDELLPGKIMASVFYEVSTRTQCSFAAAMLRLGGRVISMDNITSSV 1996
Cdd:PRK14804 7 KHLISWEDWSDSEILDLLDFAVHVK----KNRvNYAGHMSGRSLAMLFQKTSTRTRVSFEVAMTEMGGHGIYLDWMASNF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1997 KKGEsLEDSIKVVSSYADVVVLRHPSPGAVARAATFSRKPLINAGDGVGeHPTQALLDIFTIREEFGTV--NGLTITMVG 2074
Cdd:PRK14804 83 QLSD-IDLEARYLSRNVSVIMARLKKHEDLLVMKNGSQVPVINGCDNMF-HPCQSLADIMTIALDSPEIplNQKQLTYIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 2075 DLKNgrTVHSLARLLTLYNVNLQYVAPNSLQ--MPDEVVQFVHQRGVKQlFARDLKNVLPDTDVLYM-TRIQRERFDNVE 2151
Cdd:PRK14804 161 VHNN--VVNSLIGITAALGIHLTLVTPIAAKenIHAQTVERAKKKGTLS-WEMNLHKAVSHADYVYTdTWLDMEFFNDPS 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 665391904 2152 DYEKCCGHLVLTPEHMMRA----KKRSIVLHPLP--RLNEISREIDSDPRAAYFRQAE 2203
Cdd:PRK14804 238 YADKKKQRMELMMPYQINSslmeKTNAKVMHDMPihAGYEITREVVLSDRSIIFQQAE 295
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1047-1239 |
1.17e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 68.37 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1047 KVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLQSAIE--FCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETY 1124
Cdd:PRK12767 97 KVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAalAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1125 LNAASEVsrehpvVISKFLtEAKEIDVDA-VASDGRILCMAVSEHVEnagVHSGDA-TLVTppqDLNAETLEAIKRItcd 1202
Cdd:PRK12767 177 LEYVPNL------IIQEFI-EGQEYTVDVlCDLNGEVISIVPRKRIE---VRAGETsKGVT---VKDPELFKLAERL--- 240
|
170 180 190
....*....|....*....|....*....|....*..
gi 665391904 1203 lASVLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPF 1239
Cdd:PRK12767 241 -AEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
1479-1806 |
1.58e-11 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 68.58 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLREPGATHKeDFASGTAAALAGGVTLVCAMPNTNPSIVDRET--FTQFQELAKAGARCDyALYVGASDDN 1556
Cdd:PRK08417 29 LPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTPAIDNEIAleLINSAQRELPMQIFP-SIRALDEDGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1557 WAQVNELASH-ACGLkmYLNDTFGTLKLSDMTSWQRHLShwpkrSPIVCHAERQSTAAV-IMLAHLLDRSV--------- 1625
Cdd:PRK08417 107 LSNIATLLKKgAKAL--ELSSDLDANLLKVIAQYAKMLD-----VPIFCRCEDSSFDDSgVMNDGELSFELglpgipsia 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1626 HICHVARKEE-------------------IQLIRSAKEKGVKVTCEVCPHHLFLSTKDVERLGHGmSEVRPLLCSPEDQE 1686
Cdd:PRK08417 180 ETKEVAKMKElakfyknkvlfdtlalprsLELLDKFKSEGEKLLKEVSIHHLILDDSACENFNTA-AKLNPPLRSKEDRL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1687 ALWENID--YIDVFATDHAPHTLAEKRS--ERPPPGFPGVETILPLLLQAVH-EGRLTMEDIKRKFHRNPKIIFNLP-DQ 1760
Cdd:PRK08417 259 ALLEALKegKIDFLTSLHSAKSNSKKDLafDEAAFGIDSICEYFSLCYTYLVkEGIITWSELSRFTSYNPAQFLGLNsGE 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 665391904 1761 AQTYVEVDL---DEEWTITGNEMKSksgwtPFEGTKVKGRVHRVVLRGE 1806
Cdd:PRK08417 339 IEVGKEADLvlfDPNESTIIDDNFS-----LYSGDELYGKIEAVIIKGK 382
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
230-355 |
2.17e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 65.46 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 230 EQFDALFLSNGPGNPESCDQIVQQVRKVIEEGqKPVFGICLGHQLLAKAIGCS-----------TYKMKYGNRG--HNLP 296
Cdd:PRK07765 45 AQFDGVLLSPGPGTPERAGASIDMVRACAAAG-TPLLGVCLGHQAIGVAFGATvdrapellhgkTSSVHHTGVGvlAGLP 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665391904 297 CLHRATgrclmtsQNHGYAVDLEQLPDgwsELFVNANdgTNEGIV----HASKPYFSVQFHPE 355
Cdd:PRK07765 124 DPFTAT-------RYHSLTILPETLPA---ELEVTAR--TDSGVImavrHRELPIHGVQFHPE 174
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
233-355 |
8.91e-11 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 67.05 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 233 DALFLSNGPGNPES---CDQIVQQVRKVIeegqkPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPCLHRATG------ 303
Cdd:PRK14607 46 SHIVISPGPGRPEEagiSVEVIRHFSGKV-----PILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGlfrgip 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 665391904 304 RCLMTSQNHGYAVDLEQLPDGWsELFVNANDGTNEGIVHASKPYFSVQFHPE 355
Cdd:PRK14607 121 NPTVATRYHSLVVEEASLPECL-EVTAKSDDGEIMGIRHKEHPIFGVQFHPE 171
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
405-716 |
1.08e-10 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 65.29 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 405 KVLILGSGGlsigqagefdysGSQAIKAMRES----NIQTVLINPNIATVQtskgMADKCYFLP--LTPHYVEQVI---K 475
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSllkgRVIGADISELAPALY----FADKFYVVPkvTDPNYIDRLLdicK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 476 SERPNGVLLTFGGQTALNCgvqlERAGVFSKYNVRILGTPiQSIIET-EDRKLFAERVNEIGEQVAPSEAVYSVAQAL-- 552
Cdd:PRK12767 67 KEKIDLLIPLIDPELPLLA----QNRDRFEEIGVKVLVSS-KEVIEIcNDKWLTYEFLKENGIPTPKSYLPESLEDFKaa 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 553 DAASRLGYPVMARAAFSLGGLGSGFANNEEELQSLaqqaLAHSSQLIVDKSLKGwKEVEYEVVRDAYNNCITVCNMENFD 632
Cdd:PRK12767 142 LAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL----LEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 633 PLGihtGESivvapSQTLSdREYQMLRSTALKVIRHFGVVGECNIQYALCPhsEQYYIIEVNARLSrssalaskaTGYPL 712
Cdd:PRK12767 217 VRA---GET-----SKGVT-VKDPELFKLAERLAEALGARGPLNIQCFVTD--GEPYLFEINPRFG---------GGYPL 276
|
....
gi 665391904 713 AYVA 716
Cdd:PRK12767 277 SYMA 280
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
505-795 |
1.12e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 66.31 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 505 SKYNVRILGTPIQSIIETEDRKLFAERVNEIGEQVAP-SE-AVYSVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEE 582
Cdd:PRK08462 98 SHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDES 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 583 ELQS--LAQQALAHSS----QLIVDKSLKGWKEVEYEVVRDAYNNCITV----CNMENfdplgiHTGESIVVAPSQTLSD 652
Cdd:PRK08462 178 DLENlyLAAESEALSAfgdgTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVLDE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 653 REYQMLRSTALKVIRHFGVVGECNIQYaLCPHSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGLPLPD----- 727
Cdd:PRK08462 252 KTRERLHETAIKAAKAIGYEGAGTFEF-LLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSqesik 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 728 -----IKNSVTGNTTACFEPsldyCVVKIPRWDL--AKFVRVSKHIGS---------SMksVGEVMAIGRNFEEAFQKAL 791
Cdd:PRK08462 331 lkghaIECRITAEDPKKFYP----SPGKITKWIApgGRNVRMDSHAYAgyvvppyydSM--IGKLIVWGEDRNRAIAKMK 404
|
....
gi 665391904 792 RMVD 795
Cdd:PRK08462 405 RALK 408
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
191-355 |
1.28e-10 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 66.86 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 191 GKGPRIAILDC------GLKlNQLRcllQRGASVTLLPWS---ARLEDEQFDALFLSNGPGNPESCDqiVQQVRKVIEEG 261
Cdd:PRK13566 524 GEGKRVLLVDHedsfvhTLA-NYFR---QTGAEVTTVRYGfaeEMLDRVNPDLVVLSPGPGRPSDFD--CKATIDAALAR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 262 QKPVFGICLGHQLLAKAIGCS----TYKMkygnrgHNLPCLHRATGRCLMTS---------QNHGYAVDLEQLPDgwsEL 328
Cdd:PRK13566 598 NLPIFGVCLGLQAIVEAFGGElgqlAYPM------HGKPSRIRVRGPGRLFSglpeeftvgRYHSLFADPETLPD---EL 668
|
170 180
....*....|....*....|....*....
gi 665391904 329 FVNA--NDGTNEGIVHASKPYFSVQFHPE 355
Cdd:PRK13566 669 LVTAetEDGVIMAIEHKTLPVAAVQFHPE 697
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
230-370 |
1.53e-10 |
|
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: 153216 [Multi-domain] Cd Length: 189 Bit Score: 62.59 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 230 EQFDALFLSNGP--------GNPESCDQIVQQVRKVIE--------EGQKPVFGICLGHQLLAKAIGcstykmkyGNrgh 293
Cdd:cd01745 52 ELLDGLLLTGGGdvdpplygEEPHPELGPIDPERDAFElallraalERGKPILGICRGMQLLNVALG--------GT--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 294 nlpcLHratgRCLMTSQNHGYAVDleQLPDGWSELFVnANDGTNEGIVHASKPY-FSVQFHPEHHAgPQDTEF--LFDVF 370
Cdd:cd01745 121 ----LY----QDIRVNSLHHQAIK--RLADGLRVEAR-APDGVIEAIESPDRPFvLGVQWHPEWLA-DTDPDSlkLFEAF 188
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
544-815 |
2.48e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 65.16 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 544 AVYSVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEEEL-------QSLAQQALAhSSQLIVDKSLKGWKEVEYEVVR 616
Cdd:PRK12833 140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLaaelplaQREAQAAFG-DGGVYLERFIARARHIEVQILG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 617 DAYNnciTVCNMENFDPLGIHTGESIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYALCPHSEQYYIIEVNAR 696
Cdd:PRK12833 219 DGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 697 LSRSSALASKATGYPLAYVAAKLALGLPLPDIKNSVTGNTTAC------------FEPSLDycVVKIPRWDLAKFVRVSK 764
Cdd:PRK12833 296 IQVEHPVTEAITGIDLVQEMLRIADGEPLRFAQGDIALRGAALecrinaedplrdFFPNPG--RIDALVWPQGPGVRVDS 373
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 665391904 765 HIGSSMKS-------VGEVMAIGRNFEEAFQKALRMVDSDVLGFDPDVVPLNKEQLAE 815
Cdd:PRK12833 374 LLYPGYRVppfydslLAKLIVHGEDRAAALARAARALRELRIDGMKTTAPLHRALLAD 431
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
195-371 |
8.23e-10 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 60.25 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 195 RIAILDCGLKLNQL--RCLLQRGASVTLLPWSARLED--EQFDALFLSNGP-----GNpesCDQIvqqvrkvIEEGQKPV 265
Cdd:PRK00758 1 KIVVVDNGGQYNHLihRTLRYLGVDAKIIPNTTPVEEikAFEDGLILSGGPdieraGN---CPEY-------LKELDVPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 266 FGICLGHQLLAKAIGCSTYKMKYGNRG--------HNLPClhRATGRCLMTSQNHGYAVdlEQLPDGWSELfvnANDGT- 336
Cdd:PRK00758 71 LGICLGHQLIAKAFGGEVGRGEYGEYAlveveildEDDIL--KGLPPEIRVWASHADEV--KELPDGFEIL---ARSDIc 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 665391904 337 -NEGIVHASKPYFSVQFHPE-HHagpqdTEFLFDVFM 371
Cdd:PRK00758 144 eVEAMKHKEKPIYGVQFHPEvAH-----TEYGEEIFK 175
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
196-275 |
1.05e-09 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 57.99 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 196 IAILDCGLKLNQ-----LRCLLQRGASVTLLPWS-----ARLEDEQFDALFLSNGPGNP---ESCDQIVQQVRKVIEEGq 262
Cdd:cd01653 1 VAVLLFPGFEELelaspLDALREAGAEVDVVSPDggpveSDVDLDDYDGLILPGGPGTPddlARDEALLALLREAAAAG- 79
|
90
....*....|...
gi 665391904 263 KPVFGICLGHQLL 275
Cdd:cd01653 80 KPILGICLGAQLL 92
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
499-726 |
1.26e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 63.20 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 499 ERAGVFSKYNVRILGtPIQSIIETEDRKLFAER-VNEIGEQVAP-SEA-VYSVAQALDAASRLGYPVMARAAFSLGGLGS 575
Cdd:PRK07178 89 ELAEICAERGIKFIG-PSAEVIRRMGDKTEARRaMIKAGVPVTPgSEGnLADLDEALAEAERIGYPVMLKATSGGGGRGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 576 GFANNEEEL-------QSLAQQALAhSSQLIVDKSLKGWKEVEYEVVRDAYNNCITV----CNMENfdplgiHTGESIVV 644
Cdd:PRK07178 168 RRCNSREELeqnfprvISEATKAFG-SAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 645 APSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYaLCPHSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGLP 724
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEF-LLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
..
gi 665391904 725 LP 726
Cdd:PRK07178 320 LS 321
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
235-366 |
1.27e-09 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 59.88 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 235 LFLSNGPGNPESCDQIVQQVRKVieEGQKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPCLHRATG------RCLMT 308
Cdd:PRK06774 47 LVISPGPCTPNEAGISLAVIRHF--ADKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGvfrglnQPLTV 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665391904 309 SQNHGYAVDLEQLPD-----GWSElfvnaNDGTNE---GIVHASKPYFSVQFHPEHHAGPQDTEFL 366
Cdd:PRK06774 125 TRYHSLVIAADSLPGcfeltAWSE-----RGGEMDeimGIRHRTLPLEGVQFHPESILSEQGHQLL 185
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
254-355 |
3.01e-09 |
|
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: 59.19 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 254 VRKVIEEGqKPVFGICLGHQLLAKAIGCSTY---KMKYGNRGHNLPC----------LHRATGRCL--MTSQN------- 311
Cdd:pfam07722 98 IRAALARG-KPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshaVNVEPGSLLasLLGSEefrvnsl 176
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 665391904 312 HGYAVDleQLPDGWsELFVNANDGTNEGIVHASKPYF--SVQFHPE 355
Cdd:pfam07722 177 HHQAID--RLAPGL-RVEAVAPDGTIEAIESPNAKGFalGVQWHPE 219
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
196-275 |
3.13e-09 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 56.05 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 196 IAILDCGLKLNQ-----LRCLLQRGASVTLLPWS-----ARLEDEQFDALFLSNGPGNPE---SCDQIVQQVRKVIEEGq 262
Cdd:cd03128 1 VAVLLFGGSEELelaspLDALREAGAEVDVVSPDggpveSDVDLDDYDGLILPGGPGTPDdlaWDEALLALLREAAAAG- 79
|
90
....*....|...
gi 665391904 263 KPVFGICLGHQLL 275
Cdd:cd03128 80 KPVLGICLGAQLL 92
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
230-355 |
3.61e-09 |
|
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: 58.65 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 230 EQFDALFL--SNGPGNPESCDQIVQQVRKVieEGQKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPCLHRATGRC-- 305
Cdd:TIGR00566 40 EALLPLLIviSPGPCTPNEAGISLEAIRHF--AGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFrg 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 665391904 306 ----LMTSQNHGYAVDLEQLPDGWSelfVNANDGTNE---GIVHASKPYFSVQFHPE 355
Cdd:TIGR00566 118 lfnpLTATRYHSLVVEPETLPTCFP---VTAWEEENIeimAIRHRDLPLEGVQFHPE 171
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
524-766 |
9.35e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 59.94 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 524 DRKLFAERVNEIGEQVAPSEAVYSVAQALDAASRLGYPVMARAA--------FSLGGLGSGFANNEEELQSLAQQALAHS 595
Cdd:COG3919 117 DKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 596 SQLIVDKSLKGwkEVEYEVVRDAYnncitvCNmENFDPLGIHTGESIVVAPSQ--------TLSDREyqmLRSTALKVIR 667
Cdd:COG3919 197 YELIVQEYIPG--DDGEMRGLTAY------VD-RDGEVVATFTGRKLRHYPPAggnsaareSVDDPE---LEEAARRLLE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 668 HFGVVGECNIQYALCPHSEQYYIIEVNARLSRSSALASKAtGYPLAYVAAKLALGLPLPDIKNSVTGNTTACFEPSLDYC 747
Cdd:COG3919 265 ALGYHGFANVEFKRDPRDGEYKLIEINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREGVLWRVLPGDLLLR 343
|
250 260
....*....|....*....|.
gi 665391904 748 VVKIPRW--DLAKFVRVSKHI 766
Cdd:COG3919 344 YLRDGELrkRLRELLRRGKVV 364
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
235-366 |
1.72e-08 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 56.81 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 235 LFLSNGPGNPESCDQIVQQVRKVIeeGQKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPCLHraTGRCLMTSQN--- 311
Cdd:PRK08857 47 LVISPGPCTPNEAGISLQAIEHFA--GKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSVFKGLNnpl 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665391904 312 -----HGYAVDLEQLPD-----GWSELfvnaNDGTNE---GIVHASKPYFSVQFHPEHHAGPQDTEFL 366
Cdd:PRK08857 123 tvtryHSLVVKNDTLPEcfeltAWTEL----EDGSMDeimGFQHKTLPIEAVQFHPESIKTEQGHQLL 186
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
1073-1217 |
4.17e-08 |
|
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: 54.95 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1073 GILQPRWKELTNLQSAIEFCEEVGYPCLV---RPSYvlSGAAMNVAYSNQDLETYLNAASEVsrehPVVISKFLTEAKEI 1149
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEELGDG----PVIVEEFVPFDREL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665391904 1150 DVDAVAS-DGRILCMAVSEHVEnagvHSGDATLVTPPQDLNAETLEAIKRITCDLASVLDVTGPFNMQL 1217
Cdd:pfam02222 78 SVLVVRSvDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
211-355 |
6.28e-08 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 54.92 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 211 LLQRGASVTLlpwsarledEQFDAL-----FLSNGPGNPESCDQIVQQVRKVieEGQKPVFGICLGHQLLAKAIGCSTYK 285
Cdd:PRK08007 27 LVKRNDALTL---------ADIDALkpqkiVISPGPCTPDEAGISLDVIRHY--AGRLPILGVCLGHQAMAQAFGGKVVR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665391904 286 MKYGNRGHNLPCLHRATG------RCLMTSQNHGYAVDLEQLPDGWSelfVNANDGTNE--GIVHASKPYFSVQFHPE 355
Cdd:PRK08007 96 AAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGVQFHPE 170
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
544-792 |
9.95e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 57.03 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 544 AVYSVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQALAHSS------QLIVDKSLKGWKEVEYEVVRD 617
Cdd:PRK05586 137 EIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKaafgddSMYIEKFIENPKHIEFQILGD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 618 AYNNCITV----CNMENfdplgiHTGESIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYALCPHSEqYYIIEV 693
Cdd:PRK05586 217 NYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGN-FYFMEM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 694 NARLSRSSALASKATGYPLAYVAAKLALGLPL----PDIKnsVTGNTTAC----------FEPS---------------- 743
Cdd:PRK05586 290 NTRIQVEHPITEMITGVDLVKEQIKIAYGEKLsikqEDIK--INGHSIECrinaedpkngFMPCpgkieelyipgglgvr 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 665391904 744 LD---YCVVKIPrwdlakfvrvskHIGSSMksVGEVMAIGRNFEEAFQKALR 792
Cdd:PRK05586 368 VDsavYSGYTIP------------PYYDSM--IGKLIVYGKDREEAIQKMKR 405
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
1477-1732 |
1.21e-07 |
|
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.
Pssm-ID: 238619 Cd Length: 335 Bit Score: 56.14 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1477 VKLPGFIDVHVHLREpGATHKedFASGTAAAlAGGVTLVcaMPNTNPSIVDRETFTQF-QELAKA--GARCDY--ALYVg 1551
Cdd:cd01294 1 LTIPRPDDMHLHLRD-GAMLK--LVLPYTAR-GFSRAIV--MPNLKPPVTTTADALAYrERILAAdpGPNFTPlmTLYL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1552 aSDDNWAQVNELASHAC---GLKMY--------------LNDTFGTL----KLsDMtswqrhlshwpkrsPIVCHAERQS 1610
Cdd:cd01294 74 -TENTTPEELREAKKKGgirGVKLYpagattnsqggvtdLEKIYPVLeamqKL-GM--------------PLLVHGEVPD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1611 TAAVIM------LAHLLD-RS------VHICHVARKEEIQLIRSAKEKgvkVTCEVCPHHLFLSTKDVerLGHGMSEV-- 1675
Cdd:cd01294 138 FKIDVLdreakfIPVLEPlAQrfpklkIVLEHITTADAVEYVKSCNEN---VAATITPHHLLLTRDDL--LGGGLNPHly 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391904 1676 -RPLLCSPEDQEALWENI--DYIDVF-ATDHAPHTLAEKRSerpPPGFPGVET---ILPLLLQA 1732
Cdd:cd01294 213 cKPVAKRPEDREALRKAAtsGHPKFFlGSDSAPHPKSNKES---SCGCAGIFSapiALPYLAEV 273
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
543-739 |
2.11e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 56.15 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 543 EAVYSVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEEEL-------QSLAQQALAHSSQLIvDKSLKGWKEVEYEVV 615
Cdd:PRK08654 136 EGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELedaiestQSIAQSAFGDSTVFI-EKYLEKPRHIEIQIL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 616 RDAYNNCITVCNMEnfdpLGI---HTgESIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYaLCPHSEqYYIIE 692
Cdd:PRK08654 215 ADKHGNVIHLGDRE----CSIqrrHQ-KLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEF-LYSNGN-FYFLE 287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 665391904 693 VNARLSRSSALASKATGYPLAYVAAKLALGLPLP----DIKnsVTGNTTAC 739
Cdd:PRK08654 288 MNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSfkqeDIT--IRGHAIEC 336
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
211-355 |
2.15e-07 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 53.27 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 211 LLQRGASVTLlpwsARLEDEQFDALFLSNGPGNPESCDQIVQQVRKVieEGQKPVFGICLGHQLLAKAIGCSTYKM---- 286
Cdd:PRK07649 27 VVKRNDEVTI----SDIENMKPDFLMISPGPCSPNEAGISMEVIRYF--AGKIPIFGVCLGHQSIAQVFGGEVVRAerlm 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665391904 287 --KYGNRGHNLPCLHRATGRCLMTSQNHGYAVDLEQLPDGWsELFVNANDGTNEGIVHASKPYFSVQFHPE 355
Cdd:PRK07649 101 hgKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKETLPDCL-EVTSWTEEGEIMAIRHKTLPIEGVQFHPE 170
|
|
| PRK07200 |
PRK07200 |
aspartate/ornithine carbamoyltransferase family protein; Validated |
1962-2068 |
1.47e-06 |
|
aspartate/ornithine carbamoyltransferase family protein; Validated
Pssm-ID: 235961 [Multi-domain] Cd Length: 395 Bit Score: 52.82 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1962 SVFYEVSTRTQCSFAAAMLRLGGRVISMDNITSSVKKGESLEDSIKVVSSYADVVVLR------------HPSPGAVA-- 2027
Cdd:PRK07200 64 SVFRDNSTRTRFSYASACNLLGLEVQDLDEGKSQIAHGETVRETANMISFMADVIGIRddmyigkgnaymREVGAAVDdg 143
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 665391904 2028 -RAATFSRKP-LINAGDGVgEHPTQALLDIFTIREEFGTVNGL 2068
Cdd:PRK07200 144 yKQGVLPQRPtLVNLQCDI-DHPTQSMADLLHLIEHFGGLENL 185
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
230-355 |
2.52e-06 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 50.12 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 230 EQFDALFLSNGPGNPESCDQIVQQVRKVIEegQKPVFGICLGHQLLAKAIGCSTYkmkygnrghNLPCLHRATGRCLMTS 309
Cdd:PRK06895 42 ENFSHILISPGPDVPRAYPQLFAMLERYHQ--HKSILGVCLGHQTLCEFFGGELY---------NLNNVRHGQQRPLKVR 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665391904 310 QN----------------HGYAVDLEQLPDgwsELFVNA--NDGTNEGIVHASKPYFSVQFHPE 355
Cdd:PRK06895 111 SNsplfdglpeefniglyHSWAVSEENFPT---PLEITAvcDENVVMAMQHKTLPIYGVQFHPE 171
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1479-1807 |
3.72e-06 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 51.35 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1479 LPGFIDVHVHLR--------EPGATHKEDFASGTAAALAGGVTLVCAMPNTNPSIVDRetftqfqeLAKA---------- 1540
Cdd:pfam01979 3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEA--------LLEAaeelplglrf 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1541 -GARCDYA-LYVGASDDNWAQvnELASHACGLKMYLND-TFGTLKLSDMTS-------------------WQRHLSHWPK 1598
Cdd:pfam01979 75 lGPGCSLDtDGELEGRKALRE--KLKAGAEFIKGMADGvVFVGLAPHGAPTfsddelkaaleeakkyglpVAIHALETKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1599 -----RSPIVCHAERQSTAAVIMLAHLLDRS----VHICHVARKEEIQLIRSAKEKGVkVTCevcphhlflsTKDVERLG 1669
Cdd:pfam01979 153 evedaIAAFGGGIEHGTHLEVAESGGLLDIIklilAHGVHLSPTEANLLAEHLKGAGV-AHC----------PFSNSKLR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1670 HGMSEVRPLLCSpedqealweniDYIDVFATDHAPH----TLAEkrserpppgfpgvETILPLLLQAVHEGRLTMEDIKR 1745
Cdd:pfam01979 222 SGRIALRKALED-----------GVKVGLGTDGAGSgnslNMLE-------------ELRLALELQFDPEGGLSPLEALR 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665391904 1746 KFHRNPKIIFNLPDQAQTyVEV----DLdeewTITGNEMKSksgwtPFEGTKVKGRVHRVVLRGEV 1807
Cdd:pfam01979 278 MATINPAKALGLDDKVGS-IEVgkdaDL----VVVDLDPLA-----AFFGLKPDGNVKKVIVKGKI 333
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
534-697 |
4.45e-06 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 52.06 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 534 EIGEQVAPS--EAVYSVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEEEL-------QSLAQQALAhSSQLIVDKSL 604
Cdd:PRK12999 129 KAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELeeaferaKREAKAAFG-NDEVYLEKYV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 605 KGWKEVEYEVVRDAYNNCitvcnmenfdplgIHTGE---SI------VV--APSQTLSDREYQMLRSTALKVIRHFGVVG 673
Cdd:PRK12999 208 ENPRHIEVQILGDKHGNV-------------VHLYErdcSVqrrhqkVVeiAPAPGLSEELRERICEAAVKLARAVGYVN 274
|
170 180
....*....|....*....|....
gi 665391904 674 ECNIQYALCPHSeQYYIIEVNARL 697
Cdd:PRK12999 275 AGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
544-697 |
5.93e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 51.34 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 544 AVYSVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQALAHS------SQLIVDKSLKGWKEVEYEVVRD 617
Cdd:PRK08591 137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAkaafgnPGVYMEKYLENPRHIEIQVLAD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 618 AYNNcitvcnmenfdplGIHTGE---SI------VV--APSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYaLCPHSE 686
Cdd:PRK08591 217 GHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKNG 282
|
170
....*....|.
gi 665391904 687 QYYIIEVNARL 697
Cdd:PRK08591 283 EFYFIEMNTRI 293
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
235-355 |
1.46e-05 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 48.64 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 235 LFLSNGPGNPESCDQIVQQVRKVIEEgqKPVFGICLGHQLLAKAIGCSTYKMKYG-NRGHNLPCLHRATGRCLMTS---- 309
Cdd:PLN02335 66 VLISPGPGTPQDSGISLQTVLELGPL--VPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYDEKGEEGLFSglpn 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 665391904 310 -----QNHGYAVDLEQLPDGWSELFVNANDGTNEGIVHASKPYFS-VQFHPE 355
Cdd:PLN02335 144 pftagRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPE 195
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
648-734 |
2.67e-05 |
|
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: 45.68 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 648 QTLSDREyqMLRSTALKVIRHFGVVGECNIQYALcpHSEQYYIIEVNARLsrSSALA-SKATGYPLAYVAAKLALGLPLP 726
Cdd:pfam15632 41 QTLEDDP--ELIEAARRLAEAFGLDGLFNVQFRY--DGDGPKLLEINPRM--SGGIGySCLAGVNLPYLALKLLLGLETP 114
|
....*...
gi 665391904 727 DIKNSVTG 734
Cdd:pfam15632 115 DPVEPRLG 122
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
555-722 |
3.87e-05 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 48.66 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 555 ASRLGYPVMARAAFSLGGLGSGFANNEEELQ----SLAQQALAH--SSQLIVDKSLKGWKEVEYEVVRDAYNNCITVCnm 628
Cdd:PRK08463 148 ARKIGYPVILKASGGGGGRGIRVVHKEEDLEnafeSCKREALAYfnNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLC-- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 629 ENFDPLGIHTGESIVVAPSQTLSDREYQMLRSTALKVIRHFGVVGECNIQYALCPHSeQYYIIEVNARLSRSSALASKAT 708
Cdd:PRK08463 226 ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYN-RFYFMEMNTRIQVEHGVTEEIT 304
|
170
....*....|....
gi 665391904 709 GYPLAYVAAKLALG 722
Cdd:PRK08463 305 GIDLIVRQIRIAAG 318
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
513-804 |
4.07e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 49.08 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 513 GTPIQSIIETEDRKLFAERVNEIGEQVAPSEAVYSVAQALDAASRLGYPVMARAAFSLGGLGSGFANNEEELQSLAQQAL 592
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 593 -AHSSQLIVDKSLKGwKEVEYEVVRDAYNNCITVCNMENFDPLGiHTGESIVVAPSQtLSDREYQMLRSTALKVIRHFGv 671
Cdd:PRK02186 176 rAGTRAALVQAYVEG-DEYSVETLTVARGHQVLGITRKHLGPPP-HFVEIGHDFPAP-LSAPQRERIVRTVLRALDAVG- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 672 vgecniqYALCP-------HSEQYYIIEVNARLSRS--SALASKATGYPLAYVAAKLALGLP----------------LP 726
Cdd:PRK02186 252 -------YAFGPahtelrvRGDTVVIIEINPRLAGGmiPVLLEEAFGVDLLDHVIDLHLGVAafadptakrygairfvLP 324
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665391904 727 DIKNSVTGnttACFEPSLDYCVVKIPRWDLAKFVRVSKHIGSSMKSVGEVMAIGRNFEEAFQKALRMVDSDVLGFDPD 804
Cdd:PRK02186 325 ARSGVLRG---LLFLPDDIAARPELRFHPLKQPGDALRLEGDFRDRIAAVVCAGDHRDSVAAAAERAVAGLSIDIGDA 399
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
1052-1211 |
5.90e-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: 47.76 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1052 SPESIDCAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPS---------YVLSGAAmnvaysnqDLE 1122
Cdd:COG0026 80 GPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggydgkgqVVIKSAA--------DLE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1123 TYLNAASEVsrehPVVISKFLTEAKEIDVDAVAS-DGRILCMAVsehVENagVH-SGDATLVTPPQDLNAETLEAIKRIT 1200
Cdd:COG0026 152 AAWAALGGG----PCILEEFVPFERELSVIVARSpDGEVATYPV---VEN--VHrNGILDESIAPARISEALAAEAEEIA 222
|
170
....*....|.
gi 665391904 1201 CDLASVLDVTG 1211
Cdd:COG0026 223 KRIAEALDYVG 233
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
216-355 |
6.06e-05 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 46.88 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 216 ASVT-LLPWSARLEDeqfdalflsngpgnpescdqivqQVRKVIEEGQkPVFGICLGHQLLAKAIGCstyKMKYGNRG-- 292
Cdd:PRK09065 65 AMVTdRLDWSERTAD-----------------------WLRQAAAAGM-PLLGICYGHQLLAHALGG---EVGYNPAGre 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665391904 293 ---HNLPCLHRATGRCLMT---SQNHGYAVDLE---QLPDGWSELFVNANDGTNegIVHASKPYFSVQFHPE 355
Cdd:PRK09065 118 sgtVTVELHPAAADDPLFAglpAQFPAHLTHLQsvlRLPPGAVVLARSAQDPHQ--AFRYGPHAWGVQFHPE 187
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
237-355 |
6.46e-05 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 45.88 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 237 LSNGPGNPESCDqIVQQVRKVIEEgQKPVFGICLGHQLLAKAIGCSTYKMKYGNRG------HNLPCLHRATGRCLMTSQ 310
Cdd:CHL00101 49 ISPGPGHPRDSG-ISLDVISSYAP-YIPILGVCLGHQSIGYLFGGKIIKAPKPMHGktskiyHNHDDLFQGLPNPFTATR 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 665391904 311 NHGYAVDLEQLPDgwsELFVNA--NDGTNEGIVHASKPY-FSVQFHPE 355
Cdd:CHL00101 127 YHSLIIDPLNLPS---PLEITAwtEDGLIMACRHKKYKMlRGIQFHPE 171
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
192-369 |
1.23e-04 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 46.99 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 192 KGPRIAILDCGLKLNQL--RCLLQRGASVTLLPWSA---RLEDEQFDALFLSNGP------GNPESCDQIVqqvrKVIEE 260
Cdd:PLN02347 9 YLDVVLILDYGSQYTHLitRRVRELGVYSLLLSGTAsldRIASLNPRVVILSGGPhsvhveGAPTVPEGFF----DYCRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 261 GQKPVFGICLGHQLLAKAIGCST---YKMKYGNRGHNLPCLHR-----ATGRCLMTSQNHGYavDLEQLPDGWsELFVNA 332
Cdd:PLN02347 85 RGVPVLGICYGMQLIVQKLGGEVkpgEKQEYGRMEIRVVCGSQlfgdlPSGETQTVWMSHGD--EAVKLPEGF-EVVAKS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 665391904 333 NDGTNEGIVHASKPYFSVQFHPEHHAGPQDTE----FLFDV 369
Cdd:PLN02347 162 VQGAVVAIENRERRIYGLQYHPEVTHSPKGMEtlrhFLFDV 202
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1047-1155 |
2.69e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 46.13 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1047 KVLGTSPESIDCAENRFKFSRMLDRKG--ILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETY 1124
Cdd:PRK08654 101 VFIGPSSDVIEAMGSKINAKKLMKKAGvpVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDA 180
|
90 100 110
....*....|....*....|....*....|....*
gi 665391904 1125 LNAASEVSR----EHPVVISKFLTEAKEIDVDAVA 1155
Cdd:PRK08654 181 IESTQSIAQsafgDSTVFIEKYLEKPRHIEIQILA 215
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
1329-1445 |
3.09e-04 |
|
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 238297 [Multi-domain] Cd Length: 112 Bit Score: 42.11 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1329 VLLSIgSFKHKMELLPSIRDLAKMGYKLYASMGTGDFYAEHGVNVESVQWTFDKTTPDDINGelrhlaeFLANKQFDLVI 1408
Cdd:cd00532 2 VFLSV-SDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEDGEPTVDAA-------IAEKGKFDVVI 73
|
90 100 110
....*....|....*....|....*....|....*..
gi 665391904 1409 NLPmsggGARRVSSFMTHGYRTRRLAVDYSIPLVTDV 1445
Cdd:cd00532 74 NLR----DPRRDRCTDEDGTALLRLARLYKIPVTTPN 106
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1072-1211 |
3.12e-04 |
|
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: 44.23 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1072 KGILQPRWKELTNLQSAiEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAseVSREHPVVISKFLtEAKEIDV 1151
Cdd:pfam07478 13 VTFTRADWKLNPKEWCA-QVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEA--FQYDEKVLVEEGI-EGREIEC 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665391904 1152 dAVASDGRILCMAVSEHVENAGV------HSGDATLVTPPQDLNAETLEAIKRITCDLASVLDVTG 1211
Cdd:pfam07478 89 -AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRG 153
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
226-355 |
3.17e-04 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 45.79 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 226 RLEDEQFDALFLSNGPGNPESCDQIVQQVRKVieEGQKPVFGICLGHQLLAKAIGcsTYKMKYGNRGHNLPCLHRATGRC 305
Cdd:PRK09522 43 RLATMSNPVLMLSPGPGVPSEAGCMPELLTRL--RGKLPIIGICLGHQAIVEAYG--GYVGQAGEILHGKASSIEHDGQA 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 665391904 306 LMTSQNHGYAVDL------EQLPDGwseLFVNAN-DGTNEGIVHASKPYFSVQFHPE 355
Cdd:PRK09522 119 MFAGLTNPLPVARyhslvgSNIPAG---LTINAHfNGMVMAVRHDADRVCGFQFHPE 172
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
1052-1230 |
6.18e-04 |
|
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: 43.87 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1052 SPESIDCAENRFKFSRMLDRKGILQPRWKELTNLQSAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASEV 1131
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 1132 SREHPV-VISKFLTEAKEIDVDAVASDGRIL-CMA--VSEHVENAGVHSGDATlvtppqdlNAETLEAIKRITCDLASV- 1206
Cdd:TIGR00768 159 NGPQNLfLVQEYIKKPGGRDIRVFVVGDEVVaAIYriTSGHWRSNLARGGKAE--------PCSLTEEIEELAIKAAKAl 230
|
170 180
....*....|....*....|....*
gi 665391904 1207 -LDVTGpfnMQLIAKNNELKVIECN 1230
Cdd:TIGR00768 231 gLDVAG---VDLLESEDGLLVNEVN 252
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
196-276 |
1.86e-03 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 41.71 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 196 IAILDCGL-KLNQLRCLLQR-GASVTllpWSARLED-EQFDALFLSnGPGNPESCDQ------IVQQVRKVIEEGqKPVF 266
Cdd:cd01748 1 IAIIDYGMgNLRSVANALERlGAEVI---ITSDPEEiLSADKLILP-GVGAFGDAMAnlrergLIEALKEAIASG-KPFL 75
|
90
....*....|
gi 665391904 267 GICLGHQLLA 276
Cdd:cd01748 76 GICLGMQLLF 85
|
|
| PfpI |
TIGR01382 |
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ... |
215-278 |
2.66e-03 |
|
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: 40.86 E-value: 2.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 215 GASVTLlpwSARLED---EQFDALFLSNGPGnPESC---DQIVQQVRKVIEEGqKPVFGICLGHQLLAKA 278
Cdd:TIGR01382 44 GYSVTV---DATIDEvnpEEYDALVIPGGRA-PEYLrlnNKAVRLVREFVEKG-KPVAAICHGPQLLISA 108
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1093-1157 |
3.28e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 42.13 E-value: 3.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665391904 1093 EEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASEVsrEHPVVISKFLtEAKEIDVDAVASD 1157
Cdd:PRK14570 168 EVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKY--DLTVVIEKFI-EAREIECSVIGNE 229
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
228-355 |
4.51e-03 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 42.14 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 228 EDEQFDALFLSNGPGNPESCDQIVQQVRKVIEEGQKPVFGICLGHQLLAKAIGCSTYKMK------------YGNR-GHN 294
Cdd:PLN02889 128 EEKAFDNIVISPGPGSPTCPADIGICLRLLLECRDIPILGVCLGHQALGYVHGARIVHAPepvhgrlseiehNGCRlFDD 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391904 295 LPClHRATGrcLMTSQNHGYAVDLEQLPD-----GW--------------SELFVNANDGTNE----------------- 338
Cdd:PLN02889 208 IPS-GRNSG--FKVVRYHSLVIDAESLPKelvpiAWtsssdtlsflesqkSGLVPDAYESQIGqsgssdpfssklkngts 284
|
170 180 190
....*....|....*....|....*....|...
gi 665391904 339 ----------------GIVHASKPYFSVQFHPE 355
Cdd:PLN02889 285 wpsshsermqngkilmGIMHSTRPHYGLQFHPE 317
|
|
| YajL |
COG0693 |
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ... |
229-278 |
5.62e-03 |
|
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];
Pssm-ID: 440457 [Multi-domain] Cd Length: 170 Bit Score: 39.70 E-value: 5.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 665391904 229 DEQFDALFLSNGPGNPES---CDQIVQQVRKVIEEGqKPVFGICLGHQLLAKA 278
Cdd:COG0693 62 PDDYDALVLPGGHGAPDDlreDPDVVALVREFYEAG-KPVAAICHGPAVLAAA 113
|
|
| DJ-1_PfpI |
pfam01965 |
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ... |
228-278 |
6.63e-03 |
|
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.
Pssm-ID: 396514 [Multi-domain] Cd Length: 165 Bit Score: 39.55 E-value: 6.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 665391904 228 EDEQFDALFLSNGPGNPES---CDQIVQQVRKVIEEGqKPVFGICLGHQLLAKA 278
Cdd:pfam01965 58 KPDDYDALVLPGGRAGPERlrdNEKLVEFVKDFYEKG-KPVAAICHGPQVLAAA 110
|
|
| GATase1_PfpI_like |
cd03134 |
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ... |
230-278 |
7.37e-03 |
|
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and 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. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.
Pssm-ID: 153228 [Multi-domain] Cd Length: 165 Bit Score: 39.45 E-value: 7.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 665391904 230 EQFDALFLsngPG--NPES---CDQIVQQVRKVIEEGqKPVFGICLGHQLLAKA 278
Cdd:cd03134 61 DDYDALVI---PGgtNPDKlrrDPDAVAFVRAFAEAG-KPVAAICHGPWVLISA 110
|
|
| |
