|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
345-1298 |
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: 1546.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 345 ERPKKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPN 424
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 425 GVLLTFGGQTALNCGVELERAKIFTKYNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAPSEAVYSVAEALEAAETLGY 504
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 505 PVMARAAFSLGGLGSGFANNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHT 582
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 583 GESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAK 662
Cdd:TIGR01369 244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 663 LSLGVALPLIKNTVTGVTTACFEPSLGYCVVKIPRWDLSKFIRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETV 742
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 743 TGFDPYLKEVK-----EEELIQATDKRMFVLAAALKAKYSIEKLYNLTKIDPWFLNKMKNIIDFLNLLESQGNN-LDHSM 816
Cdd:TIGR01369 404 TGFDLPDREVEpdedlWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTdLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 817 LLQAKKLGFSDKAIATAIKSTDLVVRSHREQLGVIPFVKQIDTVAGEWPATTNYLYLTYNATTHDIEFPGNFTIVV-GSG 895
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 896 VYRIGSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENPDGIILSMGGQLPN 975
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 976 NIAMDLHRQQARVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLRSAINFCDEVGYPCLVRPSYVLSGAAMNVA 1055
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1056 YSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVAADGEILCMAVSEHVENAGVHSGDATLVTPPQDLNRETLEK 1135
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1136 IKEITRDLAALLDVTGPFNMQLIAKNNQLKVIECNVRVSRSFPFVSKTLNHDFVATATQAIIGMAVEPVDIL--HGCGKV 1213
Cdd:TIGR01369 804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEPKYV 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1214 GVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKKAILLSIGSFKHKVELLPSIRELANLG 1293
Cdd:TIGR01369 884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963
|
....*
gi 86450129 1294 YKLYA 1298
Cdd:TIGR01369 964 YKLYA 968
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
348-1298 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1343.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 348 KKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVL 427
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 428 LTFGGQTALNCGVELERAKIFTKYNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAPSEAVYSVAEALEAAETLGYPVM 507
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 508 ARAAFSLGGLGSGFANNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGES 585
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 586 IVVAPSQTLSNREYNMLRTTAIKVIRHFGVV-GECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 664
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 665 LGVALPLIKNTVTGVTTACFEPSLGYCVVKIPRWDLSKFIRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVTG 744
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 745 FDPYLKEVK-----EEELIQATDKRMFVLAAALKAKYSIEKLYNLTKIDPWFLNKMKNIIDFLNLLESQGNNLDHSMLLQ 819
Cdd:PRK05294 408 LDEDLFEEEsleelREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLRE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 820 AKKLGFSDKAIATAIKSTDLVVRSHREQLGVIPFVKQIDTVAGEWPATTNYLYLTYNATTHDIEFPGNFTIVVGSGVYRI 899
Cdd:PRK05294 488 AKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNRI 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 900 GSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENPDGIILSMGGQLPNNIAM 979
Cdd:PRK05294 568 GQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLAK 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 980 DLHRQQARVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLRSAINFCDEVGYPCLVRPSYVLSGAAMNVAYSNQ 1059
Cdd:PRK05294 648 ALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEE 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1060 DLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDLNRETLEKIKE 1138
Cdd:PRK05294 728 ELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEdVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIRE 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1139 ITRDLAALLDVTGPFNMQLIAKNNQLKVIECNVRVSRSFPFVSKTLNHDFVATATQAIIGMAVEPVDILHGC--GKVGVK 1216
Cdd:PRK05294 807 YTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPYVAVK 886
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1217 VPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKK-AILLSIGSfKHKVELLPSIRELANLGYK 1295
Cdd:PRK05294 887 EAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSVRD-RDKEEVVELAKRLLELGFK 965
|
...
gi 86450129 1296 LYA 1298
Cdd:PRK05294 966 ILA 968
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
353-894 |
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: 646.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 353 LGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVLLTFGG 432
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 433 QTALNCGVELERAKIFTkyNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAPSEAVYSVAEALEAAETLGYPVMARAAF 512
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 513 SLGGLGSGFANNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGESIVVAP 590
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 591 SQTLSNREYNMLRTTAIKVIRHFGVVGECNIQYALNpeSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGVALP 670
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 671 LIKNTvTGvttacFEPSLGYCVVKIPRWDLSKFIRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVTG----FD 746
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvllSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 747 PYLKEVKEEELIQATDKRMFVLAAALKAKYSIEKLYNLTKIDPWFLNKMKNIIDFLNLLESQGNNLDHsmLLQAKKLGFS 826
Cdd:COG0458 391 VADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINT--LLGAKSLGDS 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450129 827 DKAIATAIKSTDLVVRSHREQLGVIPFVKQIDTVAGEWPATTNYLYLTYNATTHDIEFPGNFTIVVGS 894
Cdd:COG0458 469 DGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-312 |
2.78e-136 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 420.64 E-value: 2.78e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVpteNDidvnglpkhfEWIE--GISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRA 78
Cdd:PRK12564 51 QIVTFTYPLIGNYGV---NR----------EDFEsdRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 79 LTKKIRENGTILGRIAYEIPKPDISL----NFVDPNTRNLVAECSVKKPIVY---NPNGSPRICAIDCGLKLNQIRCFVA 151
Cdd:PRK12564 118 LTRKLREKGAMKGVIATEDFDAEELLekarAFPGLLGLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 152 RGARVELVPWNYD----LNVaNFDGLFISNGPGDPVVCKDTVTQIQKILkESEIPIFGICLGHQLLSAAIGCKTYKMKYG 227
Cdd:PRK12564 198 RGCRVTVVPATTTaeeiLAL-NPDGVFLSNGPGDPAALDYAIEMIRELL-EKKIPIFGICLGHQLLALALGAKTYKMKFG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 228 NRGHNLPCIHHGTGRCFMTSQNHGFAVDAGTLPAEWEILFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPEDLELLFDV 307
Cdd:PRK12564 276 HRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDE 355
|
....*
gi 86450129 308 FLEAV 312
Cdd:PRK12564 356 FVELM 360
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-313 |
3.06e-131 |
|
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: 407.10 E-value: 3.06e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVpteNDIDVnglpkhfewiE--GISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRA 78
Cdd:COG0505 51 QIVTFTYPHIGNYGV---NDEDF----------EsdRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 79 LTKKIRENGTILGRIAYEIPKPDISL----NFVDPNTRNLVAECSVKKPIVY--NPNGSPRICAIDCGLKLNQIRCFVAR 152
Cdd:COG0505 118 LTRHLREKGAMKGVISTGDLDIEELLekarAAPGMEGLDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAER 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 153 GARVELVPWNYD----LNVaNFDGLFISNGPGDPVVCKDTVTQIQKILkESEIPIFGICLGHQLLSAAIGCKTYKMKYGN 228
Cdd:COG0505 198 GCRVTVVPATTSaeeiLAL-NPDGVFLSNGPGDPAALDYAIETIRELL-GKGIPIFGICLGHQLLALALGAKTYKLKFGH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 229 RGHNLPCIHHGTGRCFMTSQNHGFAVDAGTLPA-EWEILFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPEDLELLFDV 307
Cdd:COG0505 276 RGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDR 355
|
....*.
gi 86450129 308 FLEAVK 313
Cdd:COG0505 356 FIELME 361
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-313 |
1.56e-129 |
|
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: 402.39 E-value: 1.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVPtendidvnglPKHFEWIeGISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRALT 80
Cdd:TIGR01368 47 QIVVFTYPLIGNYGVN----------DEDAESK-GIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 81 KKIRENGTILGRIAYEIPKPDISLNF--VDPNTR--NLVAECSVKKPIVYNP--NGSPRICAIDCGLKLNQIRCFVARGA 154
Cdd:TIGR01368 116 KKIREKGTMKGVISTEDSNDEELVEKarVSPDITgiNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 155 RVELVPWNYDLNVA---NFDGLFISNGPGDPVVCKDTVTQIQKILkeSEIPIFGICLGHQLLSAAIGCKTYKMKYGNRGH 231
Cdd:TIGR01368 196 EVTVVPYDTDAEEIkkyNPDGIFLSNGPGDPAAVEPAIETIRKLL--EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 232 NLPCIHHGTGRCFMTSQNHGFAVDAGTLPA-EWEILFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPEDLELLFDVFLE 310
Cdd:TIGR01368 274 NHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFID 353
|
...
gi 86450129 311 AVK 313
Cdd:TIGR01368 354 LMK 356
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
134-309 |
1.47e-98 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 311.74 E-value: 1.47e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 134 ICAIDCGLKLNQIRCFVARGARVELVPWNYDLNVA---NFDGLFISNGPGDPVVCKDTVTQIQKILkESEIPIFGICLGH 210
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlklDPDGIFLSNGPGDPALLDEAIKTVRKLL-GKKIPIFGICLGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 211 QLLSAAIGCKTYKMKYGNRGHNLPCIHHGTGRCFMTSQNHGFAVDAGTLPAEWEILFTNANDNTNEGIIHKSKPYFSVQF 290
Cdd:cd01744 80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159
|
170
....*....|....*....
gi 86450129 291 HPEHTAGPEDLELLFDVFL 309
Cdd:cd01744 160 HPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
468-670 |
2.84e-96 |
|
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: 306.92 E-value: 2.84e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 468 DRKIFSERVAEIGEKVAPSEAVY--SVAEALEAAETLGYPVMARAAFSLGGLGSGFANNQEELKILAKQALAHS------ 539
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 540 NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLgiHTGESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVVGEC 619
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 86450129 620 NIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGVALP 670
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
137-311 |
3.09e-63 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 213.25 E-value: 3.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 137 IDCGL--KLNQIRCFVARGARVELVPWNYDLNV---ANFDGLFISNGPGDPVVCKDTVTQIQKILkESEIPIFGICLGHQ 211
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTPAEEileENPDGIILSGGPGSPGAAGGAIEAIREAR-ELKIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 212 LLSAAIGCKTYKMK-YGNRGHNLPCIH------HGTGRCFMTSQNHGFAVDAGTLPAEWEILFTNANDNTNEGIIHKSKP 284
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*..
gi 86450129 285 YFSVQFHPEHTAGPEDLELLFDVFLEA 311
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
754-875 |
6.94e-50 |
|
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: 172.25 E-value: 6.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 754 EEELIQATDKRMFVLAAALKAKYSIEKLYNLTKIDPWFLNKMKNIIDFLNLLESQG-NNLDHSMLLQAKKLGFSDKAIAT 832
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGlDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 86450129 833 AIKSTDLVVRSHREQLGVIPFVKQIDTVAGEWPATTNYLYLTY 875
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
2.04e-36 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 134.04 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVpteNDIDvnglpkhFEWiEGISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRALT 80
Cdd:smart01097 49 QIVVFTYPLIGNYGV---NDED-------FES-DKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALT 117
|
90
....*....|...
gi 86450129 81 KKIRENGTILGRI 93
Cdd:smart01097 118 RKLREKGAMKGVI 130
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1267-1298 |
3.40e-06 |
|
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: 47.29 E-value: 3.40e-06
10 20 30
....*....|....*....|....*....|..
gi 86450129 1267 KAILLSIGSFKhKVELLPSIRELANLGYKLYA 1298
Cdd:cd01423 1 KGILISIGSYS-KPELLPTAQKLSKLGYKLYA 31
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
345-1298 |
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: 1546.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 345 ERPKKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPN 424
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 425 GVLLTFGGQTALNCGVELERAKIFTKYNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAPSEAVYSVAEALEAAETLGY 504
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 505 PVMARAAFSLGGLGSGFANNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHT 582
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 583 GESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAK 662
Cdd:TIGR01369 244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 663 LSLGVALPLIKNTVTGVTTACFEPSLGYCVVKIPRWDLSKFIRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETV 742
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 743 TGFDPYLKEVK-----EEELIQATDKRMFVLAAALKAKYSIEKLYNLTKIDPWFLNKMKNIIDFLNLLESQGNN-LDHSM 816
Cdd:TIGR01369 404 TGFDLPDREVEpdedlWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTdLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 817 LLQAKKLGFSDKAIATAIKSTDLVVRSHREQLGVIPFVKQIDTVAGEWPATTNYLYLTYNATTHDIEFPGNFTIVV-GSG 895
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 896 VYRIGSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENPDGIILSMGGQLPN 975
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 976 NIAMDLHRQQARVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLRSAINFCDEVGYPCLVRPSYVLSGAAMNVA 1055
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1056 YSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVAADGEILCMAVSEHVENAGVHSGDATLVTPPQDLNRETLEK 1135
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1136 IKEITRDLAALLDVTGPFNMQLIAKNNQLKVIECNVRVSRSFPFVSKTLNHDFVATATQAIIGMAVEPVDIL--HGCGKV 1213
Cdd:TIGR01369 804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEPKYV 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1214 GVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKKAILLSIGSFKHKVELLPSIRELANLG 1293
Cdd:TIGR01369 884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963
|
....*
gi 86450129 1294 YKLYA 1298
Cdd:TIGR01369 964 YKLYA 968
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
348-1298 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1343.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 348 KKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVL 427
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 428 LTFGGQTALNCGVELERAKIFTKYNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAPSEAVYSVAEALEAAETLGYPVM 507
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 508 ARAAFSLGGLGSGFANNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGES 585
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 586 IVVAPSQTLSNREYNMLRTTAIKVIRHFGVV-GECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 664
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 665 LGVALPLIKNTVTGVTTACFEPSLGYCVVKIPRWDLSKFIRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVTG 744
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 745 FDPYLKEVK-----EEELIQATDKRMFVLAAALKAKYSIEKLYNLTKIDPWFLNKMKNIIDFLNLLESQGNNLDHSMLLQ 819
Cdd:PRK05294 408 LDEDLFEEEsleelREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLRE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 820 AKKLGFSDKAIATAIKSTDLVVRSHREQLGVIPFVKQIDTVAGEWPATTNYLYLTYNATTHDIEFPGNFTIVVGSGVYRI 899
Cdd:PRK05294 488 AKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNRI 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 900 GSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENPDGIILSMGGQLPNNIAM 979
Cdd:PRK05294 568 GQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLAK 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 980 DLHRQQARVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLRSAINFCDEVGYPCLVRPSYVLSGAAMNVAYSNQ 1059
Cdd:PRK05294 648 ALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEE 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1060 DLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDLNRETLEKIKE 1138
Cdd:PRK05294 728 ELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEdVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIRE 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1139 ITRDLAALLDVTGPFNMQLIAKNNQLKVIECNVRVSRSFPFVSKTLNHDFVATATQAIIGMAVEPVDILHGC--GKVGVK 1216
Cdd:PRK05294 807 YTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPYVAVK 886
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1217 VPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKK-AILLSIGSfKHKVELLPSIRELANLGYK 1295
Cdd:PRK05294 887 EAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSVRD-RDKEEVVELAKRLLELGFK 965
|
...
gi 86450129 1296 LYA 1298
Cdd:PRK05294 966 ILA 968
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
348-1298 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1026.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 348 KKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVL 427
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 428 LTFGGQTALNCGVELERAKIFTKYNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAPSEAVYSVAEALEAAETLGYPVM 507
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 508 ARAAFSLGGLGSGFANNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGES 585
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQASpiHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 586 IVVAPSQTLSNREYNMLRTTAIKVIRHFGVVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSL 665
Cdd:PRK12815 248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 666 GVALPLIKNTVTGVTTACFEPSLGYCVVKIPRWDLSKFIRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVTGF 745
Cdd:PRK12815 328 GYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 746 DPYLKEVK--EEELIQ----ATDKRMFVLAAALKAKYSIEKLYNLTKIDPWFLNKMKNIIDFLNLLESQGNNLDHSMLLQ 819
Cdd:PRK12815 408 SLPIELSGksDEELLQdlrhPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLDLSADLLRK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 820 AKKLGFSDKAIATAIKSTDLVVRSHREQLGVIPFVKQIDTVAGEWPATTNYLYLTYNATThDIEFPGN--FTIVVGSGVY 897
Cdd:PRK12815 488 VKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGES-EAEPSSEkkKVLILGSGPI 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 898 RIGSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENPDGIILSMGGQLPNNI 977
Cdd:PRK12815 567 RIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAINL 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 978 AMDLHRQQARVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLRSAINFCDEVGYPCLVRPSYVLSGAAMNVAYS 1057
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYD 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1058 NQDLETYLNAAslVSKEHPVVISKFLqEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDLNRETLEKI 1136
Cdd:PRK12815 727 EPALEAYLAEN--ASQLYPILIDQFI-DGKEYEVDAI-SDGEdVTIPGIIEHIEQAGVHSGDSIAVLPPQSLSEEQQEKI 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1137 KEITRDLAALLDVTGPFNMQLIAKNNQLKVIECNVRVSRSFPFVSKTLNHDFVATATQAIIGM----AVEPVDILHGCGK 1212
Cdd:PRK12815 803 RDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKslaeLGYPNGLWPGSPF 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1213 VGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKKAILLSIGSFKHKVELLPSIRELANL 1292
Cdd:PRK12815 883 IHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARRFAQL 962
|
....*.
gi 86450129 1293 GYKLYA 1298
Cdd:PRK12815 963 GFKLLA 968
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
348-1298 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 856.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 348 KKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVL 427
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 428 LTFGGQTALNCGVELERAKIFTKYNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAPSEAVYSVAEALEAAETLG-YPV 506
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 507 MARAAFSLGGLGSGFANNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGE 584
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAASitSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 585 SIVVAPSQTLSNREYNMLRTTAIKVIRHFGVvgEC---NIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAA 661
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 662 KLSLGVALPLIKNTVTGVTTACFEPSLGYCVVKIPRWDLSKFIRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDET 741
Cdd:PLN02735 342 KLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 742 VTGFDPylKEVKE---------EELIQATDKRMFVLAAALKAKYSIEKLYNLTKIDPWFLNKMKNIIDFLNLLESQG-NN 811
Cdd:PLN02735 422 FSGWGC--AKVKEldwdweqlkYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSlSE 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 812 LDHSMLLQAKKLGFSDKAIATAIKSTDLVVRSHREQLGVIPFVKQIDTVAGEWPATTNYLYLTYNATTHDIEFPGNFTIV 891
Cdd:PLN02735 500 LSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLI 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 892 VGSGVYRIGSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENPDGIILSMGG 971
Cdd:PLN02735 580 LGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGG 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 972 QLPNNIAMDLHRQ-------------QARVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLRSAINFCDEVGYP 1038
Cdd:PLN02735 660 QTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYP 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1039 CLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVA-ADGEILCMAVSEHVENAGVHSG 1117
Cdd:PLN02735 740 VVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSG 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1118 DATLVTPPQDLNRETLEKIKEITRDLAALLDVTGPFNMQL-IAKNNQLKVIECNVRVSRSFPFVSKTLNHDFVATATQAI 1196
Cdd:PLN02735 820 DSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVM 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1197 IGMAV------EPVDILHgcgkVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKKA-I 1269
Cdd:PLN02735 900 SGKSLkdlgftEEVIPAH----VSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGtV 975
|
970 980
....*....|....*....|....*....
gi 86450129 1270 LLSIGSfKHKVELLPSIRELANLGYKLYA 1298
Cdd:PLN02735 976 FISLND-LTKPHLVPIARGFLELGFRIVS 1003
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
353-894 |
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: 646.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 353 LGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVLLTFGG 432
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 433 QTALNCGVELERAKIFTkyNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAPSEAVYSVAEALEAAETLGYPVMARAAF 512
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 513 SLGGLGSGFANNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGESIVVAP 590
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 591 SQTLSNREYNMLRTTAIKVIRHFGVVGECNIQYALNpeSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGVALP 670
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 671 LIKNTvTGvttacFEPSLGYCVVKIPRWDLSKFIRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVTG----FD 746
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvllSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 747 PYLKEVKEEELIQATDKRMFVLAAALKAKYSIEKLYNLTKIDPWFLNKMKNIIDFLNLLESQGNNLDHsmLLQAKKLGFS 826
Cdd:COG0458 391 VADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINT--LLGAKSLGDS 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450129 827 DKAIATAIKSTDLVVRSHREQLGVIPFVKQIDTVAGEWPATTNYLYLTYNATTHDIEFPGNFTIVVGS 894
Cdd:COG0458 469 DGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
892-1298 |
2.21e-159 |
|
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: 488.23 E-value: 2.21e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 892 VGSGVYRIGSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENPDGIILSMGG 971
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 972 QLPNNIAMDLHRQQA----RVLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLRSAINFCDEVGYPCLVRPSYVL 1047
Cdd:COG0458 81 QTALNLAVELEEAGIlegvKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1048 SGAAMNVAYSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVA-ADGEILCMAVSEHVENAGVHSGDATLVTPPQ 1126
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRdGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1127 DLNRETLEKIKEITRDLAALLDVTGPFNMQLIAKNNQLKVIECNVRVSRSFPFVSKTLNHDFVATATQAIIGMAVEPVDI 1206
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1207 LHG----CGKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKKaILLSIGSFKHKVEL 1282
Cdd:COG0458 321 DTGfeptLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDKEEA 399
|
410
....*....|....*.
gi 86450129 1283 LPSIRELANLGYKLYA 1298
Cdd:COG0458 400 LLLARRLARLGFLIEA 415
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-312 |
2.78e-136 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 420.64 E-value: 2.78e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVpteNDidvnglpkhfEWIE--GISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRA 78
Cdd:PRK12564 51 QIVTFTYPLIGNYGV---NR----------EDFEsdRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 79 LTKKIRENGTILGRIAYEIPKPDISL----NFVDPNTRNLVAECSVKKPIVY---NPNGSPRICAIDCGLKLNQIRCFVA 151
Cdd:PRK12564 118 LTRKLREKGAMKGVIATEDFDAEELLekarAFPGLLGLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 152 RGARVELVPWNYD----LNVaNFDGLFISNGPGDPVVCKDTVTQIQKILkESEIPIFGICLGHQLLSAAIGCKTYKMKYG 227
Cdd:PRK12564 198 RGCRVTVVPATTTaeeiLAL-NPDGVFLSNGPGDPAALDYAIEMIRELL-EKKIPIFGICLGHQLLALALGAKTYKMKFG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 228 NRGHNLPCIHHGTGRCFMTSQNHGFAVDAGTLPAEWEILFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPEDLELLFDV 307
Cdd:PRK12564 276 HRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDE 355
|
....*
gi 86450129 308 FLEAV 312
Cdd:PRK12564 356 FVELM 360
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-313 |
3.06e-131 |
|
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: 407.10 E-value: 3.06e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVpteNDIDVnglpkhfewiE--GISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRA 78
Cdd:COG0505 51 QIVTFTYPHIGNYGV---NDEDF----------EsdRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 79 LTKKIRENGTILGRIAYEIPKPDISL----NFVDPNTRNLVAECSVKKPIVY--NPNGSPRICAIDCGLKLNQIRCFVAR 152
Cdd:COG0505 118 LTRHLREKGAMKGVISTGDLDIEELLekarAAPGMEGLDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAER 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 153 GARVELVPWNYD----LNVaNFDGLFISNGPGDPVVCKDTVTQIQKILkESEIPIFGICLGHQLLSAAIGCKTYKMKYGN 228
Cdd:COG0505 198 GCRVTVVPATTSaeeiLAL-NPDGVFLSNGPGDPAALDYAIETIRELL-GKGIPIFGICLGHQLLALALGAKTYKLKFGH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 229 RGHNLPCIHHGTGRCFMTSQNHGFAVDAGTLPA-EWEILFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPEDLELLFDV 307
Cdd:COG0505 276 RGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDR 355
|
....*.
gi 86450129 308 FLEAVK 313
Cdd:COG0505 356 FIELME 361
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-313 |
1.56e-129 |
|
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: 402.39 E-value: 1.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVPtendidvnglPKHFEWIeGISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRALT 80
Cdd:TIGR01368 47 QIVVFTYPLIGNYGVN----------DEDAESK-GIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 81 KKIRENGTILGRIAYEIPKPDISLNF--VDPNTR--NLVAECSVKKPIVYNP--NGSPRICAIDCGLKLNQIRCFVARGA 154
Cdd:TIGR01368 116 KKIREKGTMKGVISTEDSNDEELVEKarVSPDITgiNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 155 RVELVPWNYDLNVA---NFDGLFISNGPGDPVVCKDTVTQIQKILkeSEIPIFGICLGHQLLSAAIGCKTYKMKYGNRGH 231
Cdd:TIGR01368 196 EVTVVPYDTDAEEIkkyNPDGIFLSNGPGDPAAVEPAIETIRKLL--EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 232 NLPCIHHGTGRCFMTSQNHGFAVDAGTLPA-EWEILFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPEDLELLFDVFLE 310
Cdd:TIGR01368 274 NHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFID 353
|
...
gi 86450129 311 AVK 313
Cdd:TIGR01368 354 LMK 356
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
1-313 |
8.08e-102 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 328.00 E-value: 8.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVpteNDIDvnglpkhFEWIEgISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRALT 80
Cdd:PRK12838 49 QIVVFTYPLIGNYGI---NADD-------YESKQ-PQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 81 KKIRENGTILGRIAyeiPKPDISLNFVDPN---TRNLVAECSVKKPIVYnPNGSPRICAIDCGLKLNQIRCFVARGARVE 157
Cdd:PRK12838 118 KHIREKGTMKASIT---TTDDAHAFDQIKAlvlPKNVVAQVSTKEPYTY-GNGGKHVALIDFGYKKSILRSLSKRGCKVT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 158 LVPWN---YDLNVANFDGLFISNGPGDPVVCKDTVTQIQKILkeSEIPIFGICLGHQLLSAAIGCKTYKMKYGNRGHNLP 234
Cdd:PRK12838 194 VLPYDtslEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLI--SSYPILGICLGHQLIALALGADTEKLPFGHRGANHP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 235 CIHHGTGRCFMTSQNHGFAVDAGTL-PAEWEILFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPEDLELLFDVFLEAVK 313
Cdd:PRK12838 272 VIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMME 351
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
134-309 |
1.47e-98 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 311.74 E-value: 1.47e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 134 ICAIDCGLKLNQIRCFVARGARVELVPWNYDLNVA---NFDGLFISNGPGDPVVCKDTVTQIQKILkESEIPIFGICLGH 210
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlklDPDGIFLSNGPGDPALLDEAIKTVRKLL-GKKIPIFGICLGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 211 QLLSAAIGCKTYKMKYGNRGHNLPCIHHGTGRCFMTSQNHGFAVDAGTLPAEWEILFTNANDNTNEGIIHKSKPYFSVQF 290
Cdd:cd01744 80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159
|
170
....*....|....*....
gi 86450129 291 HPEHTAGPEDLELLFDVFL 309
Cdd:cd01744 160 HPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
468-670 |
2.84e-96 |
|
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: 306.92 E-value: 2.84e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 468 DRKIFSERVAEIGEKVAPSEAVY--SVAEALEAAETLGYPVMARAAFSLGGLGSGFANNQEELKILAKQALAHS------ 539
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 540 NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLgiHTGESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVVGEC 619
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 86450129 620 NIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGVALP 670
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
333-736 |
8.07e-86 |
|
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: 303.07 E-value: 8.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 333 LTYKPRSDVLLSERPKKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPE 412
Cdd:TIGR01369 540 STYEGERDDVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFE 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 413 YVEQVIKAERPNGVLLTFGGQTALNCGVELERAkiftkyNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAPSEAVYSV 492
Cdd:TIGR01369 620 DVMNIIELEKPEGVIVQFGGQTPLNLAKALEEA------GVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSV 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 493 AEALEAAETLGYPVMARAAFSLGGLGSGFANNQEELKILAKQALAHSNQ--LIIDKSLRGWKEVEYEVVRDafDNCITVC 570
Cdd:TIGR01369 694 EEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAVSD--GEEVLIP 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 571 N-MENLDPLGIHTGESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVVGECNIQYALnpESEQYYIIEVNARLSRSSALAS 649
Cdd:TIGR01369 772 GiMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGEVYVIEVNPRASRTVPFVS 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 650 KATGYPLAYVAAKLSLG---VALPLIKntvtgvttacfEPSLGYCVVKIPRWDLSKFIRVSKNIGSSMKSVGEVMAIGRN 726
Cdd:TIGR01369 850 KATGVPLAKLAVRVMLGkklEELGVGK-----------EKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRD 918
|
410
....*....|
gi 86450129 727 FEEAFQKALR 736
Cdd:TIGR01369 919 LAEAFLKAQL 928
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
334-734 |
3.53e-81 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 289.56 E-value: 3.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 334 TYKPRSDVLLSERPKKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEY 413
Cdd:PRK12815 542 TYFGESEAEPSSEKKKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLED 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 414 VEQVIKAERPNGVLLTFGGQTALNCGVELErakiftKYNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAPSEAVYSVA 493
Cdd:PRK12815 622 VLNVAEAENIKGVIVQFGGQTAINLAKGLE------EAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEE 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 494 EALEAAETLGYPVMARAAFSLGGLGSGFANNQEELKILAKQALAHSNQLIIDKSLRGwKEVEYEVVRDAFDncITVCN-M 572
Cdd:PRK12815 696 EAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPILIDQFIDG-KEYEVDAISDGED--VTIPGiI 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 573 ENLDPLGIHTGESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVVGECNIQYALnpESEQYYIIEVNARLSRSSALASKAT 652
Cdd:PRK12815 773 EHIEQAGVHSGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL--ANDEIYVLEVNPRASRTVPFVSKAT 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 653 GYPLAYVAAKLSLGvalpliKNTVTGVTTACFEPSLGYCVVKIPRWDLSKFIRVSKNIGSSMKSVGEVMAIGRNFEEAFQ 732
Cdd:PRK12815 851 GVPLAKLATKVLLG------KSLAELGYPNGLWPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALY 924
|
..
gi 86450129 733 KA 734
Cdd:PRK12815 925 KG 926
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-314 |
1.22e-66 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 230.45 E-value: 1.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVPTEnDIDVNGlpkhfewiegISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRALT 80
Cdd:CHL00197 53 QIVTFTYPEIGNTGINLE-DIESVK----------IQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 81 KKIRENGTILGRIAYE----------------IPKPDISLN--------FVDPNTRNLVAECSVKKPIVYnpngSPRICA 136
Cdd:CHL00197 122 QHLRRFGTMNGCISNQnlnlsylrakikesphMPSSDLIPRvttssyyeWDEKSHPSFYLADNKRPHSSY----QLKIIV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 137 IDCGLKLNQIRCFVARGARVELVPWNYDL---NVANFDGLFISNGPGDPVVCKDTVTQIQKILKESeIPIFGICLGHQLL 213
Cdd:CHL00197 198 IDFGVKYNILRRLKSFGCSITVVPATSPYqdiLSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYN-IPIFGICMGHQIL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 214 SAAIGCKTYKMKYGNRGhnlpcIHHGTG---RCFMTSQNHGFAVDAGTLpAEWEILFT--NANDNTNEGIIHKSKPYFSV 288
Cdd:CHL00197 277 SLALEAKTFKLKFGHRG-----LNHPSGlnqQVEITSQNHGFAVNLESL-AKNKFYIThfNLNDGTVAGISHSPKPYFSV 350
|
330 340
....*....|....*....|....*.
gi 86450129 289 QFHPEHTAGPEDLELLFDVFLEAVKH 314
Cdd:CHL00197 351 QYHPEASPGPHDADYLFEYFIEIIKH 376
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
137-311 |
3.09e-63 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 213.25 E-value: 3.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 137 IDCGL--KLNQIRCFVARGARVELVPWNYDLNV---ANFDGLFISNGPGDPVVCKDTVTQIQKILkESEIPIFGICLGHQ 211
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTPAEEileENPDGIILSGGPGSPGAAGGAIEAIREAR-ELKIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 212 LLSAAIGCKTYKMK-YGNRGHNLPCIH------HGTGRCFMTSQNHGFAVDAGTLPAEWEILFTNANDNTNEGIIHKSKP 284
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*..
gi 86450129 285 YFSVQFHPEHTAGPEDLELLFDVFLEA 311
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
1-305 |
6.85e-52 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 188.65 E-value: 6.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVPTENdidvnglpkhfEWIEGISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRALT 80
Cdd:PLN02771 103 QFVLMTNPHIGNTGVNFDD-----------EESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAIT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 81 KKIRENGTILGRIAYEIPKPDISLNFV----DPNTRNLVAECSVKKPIV----------YNPNG----SPRICAIDCGLK 142
Cdd:PLN02771 172 RRLREDGSLIGVLSTEDSKTDEELLKMsrswDIVGIDLISGVSCKSPYEwvdktnpewdFNTNSrdgeSYHVIAYDFGIK 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 143 LNQIRCFVARGARVELVPWNYDLNVA---NFDGLFISNGPGDPVVCKDTVTQIQKILkeSEIPIFGICLGHQLLSAAIGC 219
Cdd:PLN02771 252 HNILRRLASYGCKITVVPSTWPASEAlkmKPDGVLFSNGPGDPSAVPYAVETVKELL--GKVPVFGICMGHQLLGQALGG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 220 KTYKMKYGNRGHNLPCIHHGTGRCFMTSQNHGFAVDAGTLPAEWEILFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPE 299
Cdd:PLN02771 330 KTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPH 409
|
....*.
gi 86450129 300 DLELLF 305
Cdd:PLN02771 410 DSDNAF 415
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
754-875 |
6.94e-50 |
|
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: 172.25 E-value: 6.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 754 EEELIQATDKRMFVLAAALKAKYSIEKLYNLTKIDPWFLNKMKNIIDFLNLLESQG-NNLDHSMLLQAKKLGFSDKAIAT 832
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGlDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 86450129 833 AIKSTDLVVRSHREQLGVIPFVKQIDTVAGEWPATTNYLYLTY 875
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
2.20e-38 |
|
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: 139.38 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVPTEnDIDVnglpkhfewiEGISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRALT 80
Cdd:pfam00988 45 QIVVFTYPLIGNYGVNPE-DFES----------DKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALT 113
|
90
....*....|...
gi 86450129 81 KKIRENGTILGRI 93
Cdd:pfam00988 114 RKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
2.04e-36 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 134.04 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1 QILVLTYPMIGNYGVpteNDIDvnglpkhFEWiEGISVAGLVVGEICTTPSHWGQTRTLSKWMEDQGIPGISDIDTRALT 80
Cdd:smart01097 49 QIVVFTYPLIGNYGV---NDED-------FES-DKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALT 117
|
90
....*....|...
gi 86450129 81 KKIRENGTILGRI 93
Cdd:smart01097 118 RKLREKGAMKGVI 130
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
755-831 |
2.98e-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: 120.17 E-value: 2.98e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86450129 755 EELIQATDKRMFVLAAALKAKYSIEKLYNLTKIDPWFLNKMKNIIDFLNLLESQGNNLDHSMLLQAKKLGFSDKAIA 831
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDAELLREAKRLGFSDRQIA 77
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
153-293 |
3.50e-22 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 95.29 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 153 GARVELVPWN----YDLNVANFDGLFISNGPGDPVVCKDTVTQIQKILKEseIPIFGICLGHQLLSAAIGCKTYKMKYGN 228
Cdd:cd01743 22 GAEVVVVRNDeitlEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGK--VPILGVCLGHQAIAEAFGGKVVRAPEPM 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450129 229 RGHNLPCIHHGTGRCFMTSQN------HGFAVDAGTLPAEWEIlfTNANDntnEGII----HKSKPYFSVQFHPE 293
Cdd:cd01743 100 HGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLEV--TASTE---DGVImalrHRDLPIYGVQFHPE 169
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
990-1174 |
4.97e-19 |
|
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: 88.39 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 990 GTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLRSAINFCDEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAS 1069
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1070 ----LVSKEHPVVISKFLqEAKEIDVDAVAADGEILCMAVSEHvENAGVHSGDATLVTPPqDLNRETLEKIKEITRDLAA 1145
Cdd:COG0439 123 aeakAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGELVARALR 199
|
170 180 190
....*....|....*....|....*....|.
gi 86450129 1146 LLDV-TGPFNMQ-LIAKNNQLKVIECNVRVS 1174
Cdd:COG0439 200 ALGYrRGAFHTEfLLTPDGEPYLIEINARLG 230
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
133-296 |
3.81e-17 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 81.92 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 133 RICAIDCG-------------LKLNQIRCFVARGARVELVPWNYDLnvANFDGLFISNGPG----DPVVCKDTVTQIQKI 195
Cdd:COG0518 1 KILILDHDpfggqypgliarrLREAGIELDVLRVYAGEILPYDPDL--EDPDGLILSGGPMsvydEDPWLEDEPALIREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 196 LkESEIPIFGICLGHQLLSAAIGCKTYKMKYGNRG-------------HNLPcihhGTGRCFMTsqnHGFAVDagTLPAE 262
Cdd:COG0518 79 F-ELGKPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelteadplfAGLP----DEFTVWMS---HGDTVT--ELPEG 148
|
170 180 190
....*....|....*....|....*....|....
gi 86450129 263 WEILFTNANDnTNEGIIHkSKPYFSVQFHPEHTA 296
Cdd:COG0518 149 AEVLASSDNC-PNQAFRY-GRRVYGVQFHPEVTH 180
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1024-1192 |
6.63e-17 |
|
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: 80.81 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1024 NLRSAINFCDEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKE----HPVVISKFLQEAKEIDVDaVAADGE 1099
Cdd:pfam02786 26 TEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnPQVLVEKSLKGPKHIEYQ-VLRDAH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1100 ILCMAVSEhVENA-GVHSGDATLVTPPQDLNRETLEKIKEITRDLAALLDVTGPFNMQLI--AKNNQLKVIECNVRVSRS 1176
Cdd:pfam02786 105 GNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFAldPFSGEYYFIEMNTRLQVE 183
|
170
....*....|....*.
gi 86450129 1177 FPFVSKTLNHDFVATA 1192
Cdd:pfam02786 184 HALAEKATGYDLAKEA 199
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
164-293 |
7.04e-17 |
|
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: 80.08 E-value: 7.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 164 DLNVANFDGLFISNGPGDPV---VCKDTVTQIQKilkesEIPIFGICLGHQLLSAAIGCKTYKMKYgnrghnlpcIHHGt 240
Cdd:COG0512 37 EIEALAPDGIVLSPGPGTPEeagISLEVIRAFAG-----KIPILGVCLGHQAIGEAFGGKVVRAPE---------PMHG- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450129 241 grcfMTSQ-------------N-------HGFAVDAGTLPAEWEIlftNANDNTNE--GIIHKSKPYFSVQFHPE 293
Cdd:COG0512 102 ----KTSPithdgsglfaglpNpftatryHSLVVDRETLPDELEV---TAWTEDGEimGIRHRELPIEGVQFHPE 169
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
474-666 |
4.73e-16 |
|
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: 79.53 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 474 ERVAEIGEKVAPSEAVYSVAEALEAAETLGYPVMARAAFSLGGLGSGFANNQEELKILAKQALAHSN------QLIIDKS 547
Cdd:COG0439 60 EALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKagspngEVLVEEF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 548 LRGwKEVEYEVVrdAFDNCITVCNM---ENLDPLGIHTGEsivVAPSQtLSNREYNMLRTTAIKVIRHFGVV-GECNIQY 623
Cdd:COG0439 140 LEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEF 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 86450129 624 ALNPESEqYYIIEVNARLS--RSSALASKATGYPLAYVAAKLSLG 666
Cdd:COG0439 213 LLTPDGE-PYLIEINARLGgeHIPPLTELATGVDLVREQIRLALG 256
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
168-310 |
1.35e-14 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 73.35 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 168 ANFDGLFISNGPGdpvvcKDTVTQIQKILKESEIPIFGICLGHQLLSAAIGCKTYKMKYGNRG--------HNLPCIhhG 239
Cdd:PRK00758 40 AFEDGLILSGGPD-----IERAGNCPEYLKELDVPILGICLGHQLIAKAFGGEVGRGEYGEYAlveveildEDDILK--G 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450129 240 TGRCFMTSQNHGFAVDagTLPAEWEILftnANDNT--NEGIIHKSKPYFSVQFHPE--HTagpEDLELLFDVFLE 310
Cdd:PRK00758 113 LPPEIRVWASHADEVK--ELPDGFEIL---ARSDIceVEAMKHKEKPIYGVQFHPEvaHT---EYGEEIFKNFLE 179
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
167-294 |
1.40e-13 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 70.74 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 167 VANFDGLFISNGPGDPVVC-----KDTVTQIQKILkESEIPIFGICLGHQLLSAAIGCKTYKMKYG-----------NRG 230
Cdd:cd01741 44 LDDYDGLVILGGPMSVDEDdypwlKKLKELIRQAL-AAGKPVLGICLGHQLLARALGGKVGRNPKGweigwfpvtltEAG 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450129 231 HNLPcIHHGTGRCFMTSQNHGFAVDAgtLPAEWEILFTNAnDNTNEGIIhKSKPYFSVQFHPEH 294
Cdd:cd01741 123 KADP-LFAGLPDEFPVFHWHGDTVVE--LPPGAVLLASSE-ACPNQAFR-YGDRALGLQFHPEE 181
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
157-304 |
2.19e-13 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 70.04 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 157 ELVPWNY---DLNVANFDGLFISNGPgDPVVCKDTVTQIQKILkESEIPIFGICLGHQLLSAAIGCKTYKMKYGNRGH-- 231
Cdd:TIGR00888 26 ELVPNTTpleEIREKNPKGIILSGGP-SSVYAENAPRADEKIF-ELGVPVLGICYGMQLMAKQLGGEVGRAEKREYGKae 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86450129 232 ----NLPCIHHGTGRCFMTSQNHGFAVDAgtLPAEWEILFTNANdNTNEGIIHKSKPYFSVQFHPEHTAGPEDLELL 304
Cdd:TIGR00888 104 leilDEDDLFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDN-CPVAAMAHEEKPIYGVQFHPEVTHTEYGNELL 177
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
144-310 |
2.22e-13 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 70.28 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 144 NQIRCFVARGARVeLVPWNYDLNVANFDGL-----FISNGPGDPVVCKDTVTQIQKIlkESEIPIFGICLGHQLLSAAIG 218
Cdd:PRK06774 14 NLYQYFCELGTEV-MVKRNDELQLTDIEQLapshlVISPGPCTPNEAGISLAVIRHF--ADKLPILGVCLGHQALGQAFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 219 CKTYKMKYGNRG------HNLPCIHHGTGRCFMTSQNHGFAVDAGTLPAEWEIL-FTNANDNTNE--GIIHKSKPYFSVQ 289
Cdd:PRK06774 91 ARVVRARQVMHGktsaicHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTaWSERGGEMDEimGIRHRTLPLEGVQ 170
|
170 180
....*....|....*....|.
gi 86450129 290 FHPEHTAGPEDLELLfDVFLE 310
Cdd:PRK06774 171 FHPESILSEQGHQLL-DNFLK 190
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
169-304 |
3.24e-13 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 73.98 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 169 NFDGLFISNGPGDPVVCKDTVTQIQKILKEseIPIFGICLGHQLLSAAIGCKTYKMKYGNRGHNLPCIHHGTGrCFMTSQ 248
Cdd:PRK14607 44 NPSHIVISPGPGRPEEAGISVEVIRHFSGK--VPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKG-LFRGIP 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86450129 249 N-------HGFAVDAGTLPAEWEILfTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPEDLELL 304
Cdd:PRK14607 121 NptvatryHSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPESILTEEGKRIL 182
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
167-293 |
5.17e-13 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 69.69 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 167 VANFDGLFISNGPGDPV---VCKDTVtqiqKILKESEIPIFGICLGHQLLSAAIGC-----------KTYKMKYGNRGhn 232
Cdd:PRK07765 44 AAQFDGVLLSPGPGTPEragASIDMV----RACAAAGTPLLGVCLGHQAIGVAFGAtvdrapellhgKTSSVHHTGVG-- 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450129 233 lpcIHHGTGRCFMTSQNHGFAVDAGTLPAEWEILftnanDNTNEGII----HKSKPYFSVQFHPE 293
Cdd:PRK07765 118 ---VLAGLPDPFTATRYHSLTILPETLPAELEVT-----ARTDSGVImavrHRELPIHGVQFHPE 174
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
459-760 |
5.92e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 72.75 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 459 PIQSIIETEDRKIFSER-VAEIGEKVAP--SEAVYSVAEALEAAETLGYPVMARAAFSLGGLGSGFANNQEELkilaKQA 535
Cdd:PRK06111 105 PSADIIAKMGSKIEARRaMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEL----TKA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 536 LAhSNQ-----------LIIDKSLRGWKEVEYEVVRDAFDNCitvcnmenldplgIHTGE---SI------VV--APSQT 593
Cdd:PRK06111 181 FE-SNKkraanffgngeMYIEKYIEDPRHIEIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 594 LSNREYNMLRTTAIKVIRHFGVVGECNIQYaLNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGVALPLIK 673
Cdd:PRK06111 247 LDEETRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQ 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 674 NTVTGVTTA-----------CFEPSLGycvvKIPRWDLSK--FIRVSKNIGSSMK-------SVGEVMAIGRNFEEAFQK 733
Cdd:PRK06111 326 DDIKRSGHAievriyaedpkTFFPSPG----KITDLTLPGgeGVRHDHAVENGVTvtpfydpMIAKLIAHGETREEAISR 401
|
330 340 350
....*....|....*....|....*....|.
gi 86450129 734 ALRMVDE-TVTGFD---PYLKEVKEEELIQA 760
Cdd:PRK06111 402 LHDALEElKVEGIKtniPLLLQVLEDPVFKA 432
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
145-313 |
9.28e-13 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 68.23 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 145 QIRCFvarGARVELVPwNYDLNVA-----NFDGLFISNGPGDPV---VCKDtvtqiqkILKE--SEIPIFGICLGHQLLS 214
Cdd:PRK05670 18 YLGEL---GAEVVVYR-NDEITLEeiealNPDAIVLSPGPGTPAeagISLE-------LIREfaGKVPILGVCLGHQAIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 215 AAIGC-----------KTYKMKYGNRGhnlpcIHHGTGRCFMTSQNHGFAVDAGTLPAEWEILFTnANDNTNEGIIHKSK 283
Cdd:PRK05670 87 EAFGGkvvrakeimhgKTSPIEHDGSG-----IFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAW-TDDGEIMGVRHKEL 160
|
170 180 190
....*....|....*....|....*....|
gi 86450129 284 PYFSVQFHPEHTAGPEDLELLfDVFLEAVK 313
Cdd:PRK05670 161 PIYGVQFHPESILTEHGHKLL-ENFLELAR 189
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
153-295 |
1.48e-12 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 67.56 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 153 GARVELVPWNYDLNVA---NFDGLFISNGP------GDPVVCKDtvtqiqkiLKESEIPIFGICLGHQLLSAAIGCKTYK 223
Cdd:cd01742 22 GVYSEILPNTTPLEEIklkNPKGIILSGGPssvyeeDAPRVDPE--------IFELGVPVLGICYGMQLIAKALGGKVER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 224 MKYGNRGHNLPCIHHGTG---------RCFMtsqNHGFAVDAgtLPAEWEILFTNANdNTNEGIIHKSKPYFSVQFHPE- 293
Cdd:cd01742 94 GDKREYGKAEIEIDDSSPlfeglpdeqTVWM---SHGDEVVK--LPEGFKVIASSDN-CPVAAIANEEKKIYGVQFHPEv 167
|
...
gi 86450129 294 -HT 295
Cdd:cd01742 168 tHT 170
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
144-293 |
6.00e-12 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 65.97 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 144 NQIRCFVARGARVeLVPWNYDLNVANFDGLF-----ISNGPGDPvvckDTVTQIQKILKE--SEIPIFGICLGHQLLSAA 216
Cdd:TIGR00566 14 NLVQYFCELGAEV-VVKRNDSLTLQEIEALLpllivISPGPCTP----NEAGISLEAIRHfaGKLPILGVCLGHQAMGQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 217 IGCKTYKMKYGNRGHNLPCIHHGTGRC------FMTSQNHGFAVDAGTLPAEWEILFTNANDNTNEGIIHKSKPYFSVQF 290
Cdd:TIGR00566 89 FGGDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQF 168
|
...
gi 86450129 291 HPE 293
Cdd:TIGR00566 169 HPE 171
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
144-304 |
3.11e-11 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 63.78 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 144 NQIRCFVARGARVeLVPWNYDLNVANFDGL-----FISNGPGDPVVCKDTVTQIQKIlkESEIPIFGICLGHQLLSAAIG 218
Cdd:PRK08007 14 NLYQYFCELGADV-LVKRNDALTLADIDALkpqkiVISPGPCTPDEAGISLDVIRHY--AGRLPILGVCLGHQAMAQAFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 219 CKTYKMKYGNRGHNLPCIHHGTG------RCFMTSQNHGFAVDAGTLPAEWEIlftNANDNTNE--GIIHKSKPYFSVQF 290
Cdd:PRK08007 91 GKVVRAAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFEV---TAWSETREimGIRHRQWDLEGVQF 167
|
170
....*....|....
gi 86450129 291 HPEHTAGPEDLELL 304
Cdd:PRK08007 168 HPESILSEQGHQLL 181
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
349-674 |
3.99e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 66.06 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 349 KVLILGSGGlsigqagefdysGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLP--LTPEYVEQVI---KAERP 423
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPkvTDPNYIDRLLdicKKEKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 424 NGVLLTFGgqtalncgVEL----ERAKIFTKYNVKIMGTPiQSIIET-EDRKIFSERVAEIGEKVAPSEAVYSVAEALEA 498
Cdd:PRK12767 71 DLLIPLID--------PELpllaQNRDRFEEIGVKVLVSS-KEVIEIcNDKWLTYEFLKENGIPTPKSYLPESLEDFKAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 499 --AETLGYPVMARAAFSLGGLGSGFANNQEELKilakQALAHSNQLIIDKSLRGwKEVEYEVVRDAFDNCITVCNMENLD 576
Cdd:PRK12767 142 laKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 577 PLGihtGESivvapSQTLSnREYNMLRTTAIKVIRHFGVVGECNIQYALNPEseQYYIIEVNARLSrssalaskaTGYPL 656
Cdd:PRK12767 217 VRA---GET-----SKGVT-VKDPELFKLAERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFG---------GGYPL 276
|
330 340
....*....|....*....|
gi 86450129 657 AYVAaklslGVALP--LIKN 674
Cdd:PRK12767 277 SYMA-----GANEPdwIIRN 291
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
988-1179 |
1.01e-10 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 64.52 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 988 VLGTSPESIDCAENRFKFSRMLDRKGILQPRWKELTNLRS--AINFCDEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYL 1065
Cdd:PRK12767 98 VLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDfkAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1066 NAASlvskehPVVISKFLQEaKEIDVDA-VAADGEILCMAVSEHVEnagVHSGDA-TLVTPPQDlnretleKIKEITRDL 1143
Cdd:PRK12767 178 EYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETsKGVTVKDP-------ELFKLAERL 240
|
170 180 190
....*....|....*....|....*....|....*.
gi 86450129 1144 AALLDVTGPFNMQLIAKNNQLKVIECNVRVSRSFPF 1179
Cdd:PRK12767 241 AEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
149-304 |
1.21e-10 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 62.20 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 149 FVARGARVELVPwNYDLNVA-----NFDGLFISNGPGDPVVCKDTVTQIQKILkeSEIPIFGICLGHQLLSAAIGCKTYK 223
Cdd:PRK08857 19 FCELGAQVKVVR-NDEIDIDgiealNPTHLVISPGPCTPNEAGISLQAIEHFA--GKLPILGVCLGHQAIAQVFGGQVVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 224 MKYGNRGHNLPCIHhgTGRCFMTSQN--------HGFAVDAGTLPAEWEIL-FTNANDNTNE---GIIHKSKPYFSVQFH 291
Cdd:PRK08857 96 ARQVMHGKTSPIRH--TGRSVFKGLNnpltvtryHSLVVKNDTLPECFELTaWTELEDGSMDeimGFQHKTLPIEAVQFH 173
|
170
....*....|...
gi 86450129 292 PEHTAGPEDLELL 304
Cdd:PRK08857 174 PESIKTEQGHQLL 186
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
344-708 |
2.18e-10 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 64.18 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 344 SERPKKVLILGS--GGLSIgqagefdysgsqaIKALKEEKIQTILINPN-IATVQTSKgLADKVYFLPL----TPEYVEQ 416
Cdd:COG3919 2 MTMRFRVVVLGGdiNALAV-------------ARSLGEAGVRVIVVDRDpLGPAARSR-YVDEVVVVPDpgddPEAFVDA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 417 VIK-AERPN-GVLLTFGgqtalNCGVEL--ERAKIFTKYnVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAPSEAVYSV 492
Cdd:COG3919 68 LLElAERHGpDVLIPTG-----DEYVELlsRHRDELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 493 AEALEAAETLGYPVMARAA--------FSLGGLGSGFANNQEELKILAKQALAHSNQLII-------DKSLRGwkeveYE 557
Cdd:COG3919 142 DDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAGYELIVqeyipgdDGEMRG-----LT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 558 VVRDAFDNCITVCNMENL--DPLGIhtGESIVVapsQTLSNREynmLRTTAIKVIRHFGVVGECNIQYALNPESEQYYII 635
Cdd:COG3919 217 AYVDRDGEVVATFTGRKLrhYPPAG--GNSAAR---ESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLI 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450129 636 EVNARLSRSSALASKAtGYPLAYVAAKLSLGVALPLIKNTVTGVTTACFEPSLGYCVVKIPRW--DLSKFIRVSK 708
Cdd:COG3919 289 EINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREGVLWRVLPGDLLLRYLRDGELrkRLRELLRRGK 362
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
164-293 |
3.48e-10 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 60.91 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 164 DLN-VANFDGLFISNGPGDPVVCKDTVTQIQKILKESEIpiFGICLGHQLLSAAIGCKTYkmkygnrghNLPCIHHGTGR 242
Cdd:PRK06895 37 DLDeVENFSHILISPGPDVPRAYPQLFAMLERYHQHKSI--LGVCLGHQTLCEFFGGELY---------NLNNVRHGQQR 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86450129 243 CFMTSQN----------------HGFAVDAGTLPAEWEILFTnANDNTNEGIIHKSKPYFSVQFHPE 293
Cdd:PRK06895 106 PLKVRSNsplfdglpeefniglyHSWAVSEENFPTPLEITAV-CDENVVMAMQHKTLPIYGVQFHPE 171
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
1013-1157 |
5.74e-10 |
|
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: 59.57 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1013 GILQPRWKELTNLRSAINFCDEVGYPCLV---RPSYvlSGAAMNVAYSNQDLETYLNAAslvsKEHPVVISKFLQEAKEI 1089
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEEL----GDGPVIVEEFVPFDREL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450129 1090 DVDAV-AADGEILCMAVSEHVEnagvHSGDATLVTPPQDLNRETLEKIKEITRDLAALLDVTGPFNMQL 1157
Cdd:pfam02222 78 SVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
445-740 |
1.49e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 62.07 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 445 AKIFTKYNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAP-SE-AVYSVAEALEAAETLGYPVMARAAFSLGGLGSGFA 522
Cdd:PRK08462 94 VEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 523 NNQEELK--ILAKQALAHS----NQLIIDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGESIVVAPSQ 592
Cdd:PRK08462 174 EDESDLEnlYLAAESEALSafgdGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 593 TLSNREYNMLRTTAIKVIRHFGVVGECNIQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGVALP-- 670
Cdd:PRK08462 248 VLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPsq 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 671 --------LIKNTVTGVTTACFEPSLGycvvKIPRWDL--SKFIRVSKNIGS---------SMksVGEVMAIGRNFEEAF 731
Cdd:PRK08462 327 esiklkghAIECRITAEDPKKFYPSPG----KITKWIApgGRNVRMDSHAYAgyvvppyydSM--IGKLIVWGEDRNRAI 400
|
....*....
gi 86450129 732 QKALRMVDE 740
Cdd:PRK08462 401 AKMKRALKE 409
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
171-304 |
2.27e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 58.66 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 171 DGLFISNGPGDPVVCKDTVTQIQKIlkESEIPIFGICLGHQLLSAAIGCKTYKM------KYGNRGHNLPCIHHGTGRCF 244
Cdd:PRK07649 45 DFLMISPGPCSPNEAGISMEVIRYF--AGKIPIFGVCLGHQSIAQVFGGEVVRAerlmhgKTSLMHHDGKTIFSDIPNPF 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450129 245 MTSQNHGFAVDAGTLPAEWEIlftnaNDNTNEG----IIHKSKPYFSVQFHPEHTAGPEDLELL 304
Cdd:PRK07649 123 TATRYHSLIVKKETLPDCLEV-----TSWTEEGeimaIRHKTLPIEGVQFHPESIMTSHGKELL 181
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
146-213 |
4.30e-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: 55.68 E-value: 4.30e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450129 146 IRCFVARGARVELVPWN-----YDLNVANFDGLFISNGPGDPVVCKDTVTQIQKILK--ESEIPIFGICLGHQLL 213
Cdd:cd01653 18 LDALREAGAEVDVVSPDggpveSDVDLDDYDGLILPGGPGTPDDLARDEALLALLREaaAAGKPILGICLGAQLL 92
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
146-213 |
1.11e-08 |
|
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: 53.74 E-value: 1.11e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450129 146 IRCFVARGARVELVPWN-----YDLNVANFDGLFISNGPGDPVVCKDTVTQIQKILK--ESEIPIFGICLGHQLL 213
Cdd:cd03128 18 LDALREAGAEVDVVSPDggpveSDVDLDDYDGLILPGGPGTPDDLAWDEALLALLREaaAAGKPVLGICLGAQLL 92
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
153-293 |
1.12e-08 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 59.55 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 153 GARVELVPWNYDLNV---ANFDGLFISNGPGDPV--VCKDTVtqiqKILKESEIPIFGICLGHQLLSAAIGcktykmkyG 227
Cdd:PRK13566 550 GAEVTTVRYGFAEEMldrVNPDLVVLSPGPGRPSdfDCKATI----DAALARNLPIFGVCLGLQAIVEAFG--------G 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 228 NRGH-NLPC--------------IHHGTGRCFMTSQNHGFAVDAGTLPAEWEILFTnandnTNEGII----HKSKPYFSV 288
Cdd:PRK13566 618 ELGQlAYPMhgkpsrirvrgpgrLFSGLPEEFTVGRYHSLFADPETLPDELLVTAE-----TEDGVImaieHKTLPVAAV 692
|
....*
gi 86450129 289 QFHPE 293
Cdd:PRK13566 693 QFHPE 697
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
164-293 |
1.99e-08 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 56.34 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 164 DLNVANFDGLFISNGPGDPvvcKDTVTQIQKILK-ESEIPIFGICLGHQLLSAAIGCKTYKMKYG-NRGHNLPCIH---- 237
Cdd:PLN02335 57 ELKRKNPRGVLISPGPGTP---QDSGISLQTVLElGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYdekg 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86450129 238 -----HGTGRCFMTSQNHGFAVDAGTLPAEWEILFTNANDNTNEGIIHKSKPYFS-VQFHPE 293
Cdd:PLN02335 134 eeglfSGLPNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPE 195
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
167-293 |
2.52e-08 |
|
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: 55.73 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 167 VANFDGLFISNGP---------------GDPVVCKDTVTQ--IQKILKEsEIPIFGICLGHQLLSAAIGCKTY---KMKY 226
Cdd:pfam07722 56 LDRLDGLLLTGGPnvdphfygeepsesgGPYDPARDAYELalIRAALAR-GKPILGICRGFQLLNVALGGTLYqdiQEQP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 227 GNRGHNLPC----------IHHGTGRCF--MTSQN-------HGFAVDagTLPAEWEILFTnANDNTNEGIIHKSKPYF- 286
Cdd:pfam07722 135 GFTDHREHCqvapyapshaVNVEPGSLLasLLGSEefrvnslHHQAID--RLAPGLRVEAV-APDGTIEAIESPNAKGFa 211
|
....*...
gi 86450129 287 -SVQFHPE 293
Cdd:pfam07722 212 lGVQWHPE 219
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
443-671 |
2.62e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 57.80 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 443 ERAKIFTKYNVKIMGtPIQSIIETEDRKIFSERVA-EIGEKVAP-SEA-VYSVAEALEAAETLGYPVMARAAFSLGGLGS 519
Cdd:PRK07178 89 ELAEICAERGIKFIG-PSAEVIRRMGDKTEARRAMiKAGVPVTPgSEGnLADLDEALAEAERIGYPVMLKATSGGGGRGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 520 GFANNQEELK-------ILAKQALAhSNQLIIDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGESIVV 588
Cdd:PRK07178 168 RRCNSREELEqnfprviSEATKAFG-SAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 589 APSQTLSNREYNMLRTTAIKVIRHFGVVGECNIQYALNPESEqYYIIEVNARLSRSSALASKATGYPLayVAAKLSLGVA 668
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGE-VYFMEMNTRVQVEHTITEEITGIDI--VREQIRIASG 317
|
...
gi 86450129 669 LPL 671
Cdd:PRK07178 318 LPL 320
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
445-573 |
2.80e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 58.07 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 445 AKIFTKYNVKIMGtPIQSIIETEDRKIFSERV-AEIGEKVAP--SEAVYSVAEALEAAETLGYPVMARAAFSLGGLGSGF 521
Cdd:PRK08654 92 AKACEKAGIVFIG-PSSDVIEAMGSKINAKKLmKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRV 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 86450129 522 ANNQEELK--ILAKQALAHSN----QLIIDKSLRGWKEVEYEVVRDAFDNCITVCNME 573
Cdd:PRK08654 171 VYSEEELEdaIESTQSIAQSAfgdsTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRE 228
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
169-293 |
3.73e-08 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 54.74 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 169 NFDGLFISNGPGDPV---VCKDTVTQIQkilkeSEIPIFGICLGHQLLSAAIGCKTYKMKYGNRGhNLPCIHHGTGRCFM 245
Cdd:CHL00101 43 NIRHIIISPGPGHPRdsgISLDVISSYA-----PYIPILGVCLGHQSIGYLFGGKIIKAPKPMHG-KTSKIYHNHDDLFQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 86450129 246 TSQN-------HGFAVDAGTLPAEWEILfTNANDNTNEGIIHKSKPY-FSVQFHPE 293
Cdd:CHL00101 117 GLPNpftatryHSLIIDPLNLPSPLEIT-AWTEDGLIMACRHKKYKMlRGIQFHPE 171
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
170-296 |
7.55e-08 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 57.17 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 170 FDGLFISNGPGDPVVCKDTVTQIQKILKESEIPIFGICLGHQLL-----------SAAIGCKTYKMKY-GNR-GHNLPci 236
Cdd:PLN02889 132 FDNIVISPGPGSPTCPADIGICLRLLLECRDIPILGVCLGHQALgyvhgarivhaPEPVHGRLSEIEHnGCRlFDDIP-- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 237 hHGTGRCFMTSQNHGFAVDAGTLPAE-----W-------------------------------EILFTNANDNTNE---- 276
Cdd:PLN02889 210 -SGRNSGFKVVRYHSLVIDAESLPKElvpiaWtsssdtlsflesqksglvpdayesqigqsgsSDPFSSKLKNGTSwpss 288
|
170 180 190
....*....|....*....|....*....|..
gi 86450129 277 ------------GIIHKSKPYFSVQFHPEHTA 296
Cdd:PLN02889 289 hsermqngkilmGIMHSTRPHYGLQFHPESIA 320
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
459-671 |
1.39e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 55.53 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 459 PIQSIIETEDRKIFSERVA-EIGEKVAPSE--AVYSVAEALEAAETLGYPVMARAAFSLGGLGSGFANNQEELKI---LA 532
Cdd:PRK12833 108 PDAQTIRTMGDKARARRTArRAGVPTVPGSdgVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpLA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 533 K---QALAHSNQLIIDKSLRGWKEVEYEVVRDAFDnciTVCNMENLDPLGIHTGESIVVAPSQTLSNREYNMLRTTAIKV 609
Cdd:PRK12833 188 QreaQAAFGDGGVYLERFIARARHIEVQILGDGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRL 264
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86450129 610 IRHFGVVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGVALPL 671
Cdd:PRK12833 265 ARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRF 326
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
445-740 |
2.67e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 54.72 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 445 AKIFTKYNVKIMGTPIQSIIETEDRKIFSERVAEIGEKVAP-SE-AVYSVAEALEAAETLGYPVMARAAFSLGGLGSGFA 522
Cdd:PRK05586 92 AKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPgSEgEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 523 NNQEEL-------KILAKQALAhSNQLIIDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGESIVVAPS 591
Cdd:PRK05586 172 RSEEELikafntaKSEAKAAFG-DDSMYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQKVLEEAPS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 592 QTLSNREYNMLRTTAIKVIRHFGVVGECNIQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGVALPL 671
Cdd:PRK05586 245 PVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSI 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 672 ----IKntVTGVTTAC----------FEPSLG----YCVVKIPRWDLSKFIRVSKNIGSSMKS-VGEVMAIGRNFEEAFQ 732
Cdd:PRK05586 324 kqedIK--INGHSIECrinaedpkngFMPCPGkieeLYIPGGLGVRVDSAVYSGYTIPPYYDSmIGKLIVYGKDREEAIQ 401
|
....*...
gi 86450129 733 KALRMVDE 740
Cdd:PRK05586 402 KMKRALGE 409
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
153-296 |
1.18e-06 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153218 [Multi-domain] Cd Length: 273 Bit Score: 51.55 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 153 GARVelVPWNYDLNVANFDGLFIS-NG---PGDPVV-----CKDTVTQIQKILKESEI-----PIFGICLGHQLLS---- 214
Cdd:cd01747 33 GARV--VPIWINESEEYYDKLFKSiNGilfPGGAVDidtsgYARTAKIIYNLALERNDagdyfPVWGTCLGFELLTylts 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 215 ----AAIGCKT--YKMKYGNRGHNLPC----------IHHGTGRCFmTSQNHGFAV-----DAGTLPAEW-EILFTNAND 272
Cdd:cd01747 111 getlLLEATEAtnSALPLNFTEDALQSrlfkrfppdlLKSLATEPL-TMNNHRYGIspenfTENGLLSDFfNVLTTNDDW 189
|
170 180
....*....|....*....|....*..
gi 86450129 273 NTNEGII---HKSKPYFSVQFHPEHTA 296
Cdd:cd01747 190 NGVEFIStveAYKYPIYGVQWHPEKNA 216
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
488-641 |
2.43e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 51.73 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 488 AVYSVAEALEAAETLGYPVMARAAFSLGGLGSGFANNQEELKILAKQA-----LAHSN-QLIIDKSLRGWKEVEYEVVRD 561
Cdd:PRK08591 137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMAraeakAAFGNpGVYMEKYLENPRHIEIQVLAD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 562 AFDNcitvcnmenldplGIHTGE---SI------VV--APSQTLSNREYNMLRTTAIKVIRHFGVVGECNIQYaLNPESE 630
Cdd:PRK08591 217 GHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKNG 282
|
170
....*....|.
gi 86450129 631 QYYIIEVNARL 641
Cdd:PRK08591 283 EFYFIEMNTRI 293
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1267-1298 |
3.40e-06 |
|
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: 47.29 E-value: 3.40e-06
10 20 30
....*....|....*....|....*....|..
gi 86450129 1267 KAILLSIGSFKhKVELLPSIRELANLGYKLYA 1298
Cdd:cd01423 1 KGILISIGSYS-KPELLPTAQKLSKLGYKLYA 31
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
470-641 |
3.61e-06 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 51.68 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 470 KIFSERVA-EIGEKVAPS--EAVYSVAEALEAAETLGYPVMARAAFSLGGLGSGFANNQEEL-------KILAKQALAhS 539
Cdd:PRK12999 120 KVAARNAAiKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELeeaferaKREAKAAFG-N 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 540 NQLIIDKSLRGWKEVEYEVVRDAFDNCitvcnmenldplgIHTGE---SI------VV--APSQTLSNREYNMLRTTAIK 608
Cdd:PRK12999 199 DEVYLEKYVENPRHIEVQILGDKHGNV-------------VHLYErdcSVqrrhqkVVeiAPAPGLSEELRERICEAAVK 265
|
170 180 190
....*....|....*....|....*....|...
gi 86450129 609 VIRHFGVVGECNIQYALNPESeQYYIIEVNARL 641
Cdd:PRK12999 266 LARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
146-314 |
6.70e-06 |
|
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];
Pssm-ID: 441674 [Multi-domain] Cd Length: 231 Bit Score: 48.63 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 146 IRCFVARGARVELVPWNYDLN-----VANFDGLFIS-----------------NGPGDPVvcKDTVTQ--IQKILkESEI 201
Cdd:COG2071 21 VRAVRAAGGLPVLLPPVGDEEdldelLDRLDGLVLTggadvdpalygeephpeLGPIDPE--RDAFELalIRAAL-ERGK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 202 PIFGICLGHQLLSAAIGcktykmkyGN--------RGHNLPciHHGTGRCFMTSqnHGFAVDAGTLPAEW---EILFTN- 269
Cdd:COG2071 98 PVLGICRGMQLLNVALG--------GTlyqdlpdqVPGALD--HRQPAPRYAPR--HTVEIEPGSRLARIlgeEEIRVNs 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450129 270 ------------------ANDNTNEGIIHKSKPYF-SVQFHPEHTAG--PEDLElLFDVFLEAVKH 314
Cdd:COG2071 166 lhhqavkrlgpglrvsarAPDGVIEAIESPGAPFVlGVQWHPEWLAAsdPLSRR-LFEAFVEAARA 230
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
992-1151 |
3.97e-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: 47.38 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 992 SPESIDCAENRFKFSRMLDRKGILQPRWKELTNLRSAINFCDEVGYPCLVRPS---------YVLSGAAmnvaysnqDLE 1062
Cdd:COG0026 80 GPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggydgkgqVVIKSAA--------DLE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1063 TYLNAAslvsKEHPVVISKFLQEAKEIDVDAV-AADGEILCMAVsehVENagVH-SGDATLVTPPQDLNRETLEKIKEIT 1140
Cdd:COG0026 152 AAWAAL----GGGPCILEEFVPFERELSVIVArSPDGEVATYPV---VEN--VHrNGILDESIAPARISEALAAEAEEIA 222
|
170
....*....|.
gi 86450129 1141 RDLAALLDVTG 1151
Cdd:COG0026 223 KRIAEALDYVG 233
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
470-640 |
4.63e-05 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 48.15 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 470 KIFSERVA-EIGEKVAPS--EAVYSVAEALEAAETLGYPVMARAAFSLGGLGSGFANNQEELKIL-------AKQALAhS 539
Cdd:COG1038 119 KVAARAAAiEAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAfesarreAKAAFG-D 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 540 NQLIIDKSLRGWKEVEYEVVRDAFDNCitvcnmenldplgIHTGE---SI------VV--APSQTLSNREYNMLRTTAIK 608
Cdd:COG1038 198 DEVFLEKYIERPKHIEVQILGDKHGNI-------------VHLFErdcSVqrrhqkVVeiAPAPNLDEELREAICEAAVK 264
|
170 180 190
....*....|....*....|....*....|....*..
gi 86450129 609 VIRHfgvVGECNiqyA-----LNPESEQYYIIEVNAR 640
Cdd:COG1038 265 LAKA---VGYVN---AgtvefLVDDDGNFYFIEVNPR 295
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1012-1151 |
8.93e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 45.00 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 1012 KGILQPRWKELTNLRSAiNFCDEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAslVSKEHPVVISKFLqEAKEIDV 1091
Cdd:pfam07478 13 VTFTRADWKLNPKEWCA-QVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEA--FQYDEKVLVEEGI-EGREIEC 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450129 1092 dAVAADGEILCMAVSEHVENAGV------HSGDATLVTPPQDLNRETLEKIKEITRDLAALLDVTG 1151
Cdd:pfam07478 89 -AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRG 153
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
490-676 |
1.17e-03 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 42.88 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 490 YSVAEALEAAETLGYPVMARAAFSLGGLGSGFANNQEEL----KILAKQALAHSN--QLIIDKSLRGWKEVEYEVVRDAF 563
Cdd:PRK08463 139 ESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLenafESCKREALAYFNndEVFMEKYVVNPRHIEFQILGDNY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 564 DNCITVCnmENLDPLGIHTGESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVVGECNIQYALNpESEQYYIIEVNARLSR 643
Cdd:PRK08463 219 GNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD-DYNRFYFMEMNTRIQV 295
|
170 180 190
....*....|....*....|....*....|...
gi 86450129 644 SSALASKATGYPLAYVAAKLSLGVALPLIKNTV 676
Cdd:PRK08463 296 EHGVTEEITGIDLIVRQIRIAAGEILDLEQSDI 328
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
606-680 |
2.46e-03 |
|
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.
Pssm-ID: 434824 [Multi-domain] Cd Length: 131 Bit Score: 39.52 E-value: 2.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450129 606 AIKVIRHFGVVGECNIQYALNpeSEQYYIIEVNARLsrSSALA-SKATGYPLAYVAAKLSLGVALPLIKNTVTGVT 680
Cdd:pfam15632 53 ARRLAEAFGLDGLFNVQFRYD--GDGPKLLEINPRM--SGGIGySCLAGVNLPYLALKLLLGLETPDPVEPRLGLR 124
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
989-1095 |
3.71e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 41.51 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 989 LGTSPESIDCAENRFKFSRMLDRKG--ILQPRWKELTNLRSAINFCDEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLN 1066
Cdd:PRK08654 103 IGPSSDVIEAMGSKINAKKLMKKAGvpVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIE 182
|
90 100 110
....*....|....*....|....*....|...
gi 86450129 1067 AASLVSK----EHPVVISKFLQEAKEIDVDAVA 1095
Cdd:PRK08654 183 STQSIAQsafgDSTVFIEKYLEKPRHIEIQILA 215
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
992-1101 |
4.63e-03 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 40.41 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450129 992 SPESIDCAENRFKFSRMLDRKGILQPRWKELTNLRSAINFCDEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLV 1071
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQL 158
|
90 100 110
....*....|....*....|....*....|.
gi 86450129 1072 SKEHPV-VISKFLQEAKEIDVDAVAADGEIL 1101
Cdd:TIGR00768 159 NGPQNLfLVQEYIKKPGGRDIRVFVVGDEVV 189
|
|
| PRK08250 |
PRK08250 |
glutamine amidotransferase; Provisional |
166-220 |
9.87e-03 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181323 [Multi-domain] Cd Length: 235 Bit Score: 39.18 E-value: 9.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86450129 166 NVANFDGLFISNGPGDPVVCK------DTVTQIQKILK--ESEIPIFGICLGHQLLSAAIGCK 220
Cdd:PRK08250 42 NADGFDLLIVMGGPQSPRTTReecpyfDSKAEQRLINQaiKAGKAVIGVCLGAQLIGEALGAK 104
|
|
| |
