|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
341-1298 |
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: 1549.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 341 IMKEKPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTLDYVEQVIKAE 420
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 421 RPNGVLLAFGGQTALNCGIDLERAGVFSKYNVKILGTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVYSVAEALQAAEV 500
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 501 LGYPVMARAAFSLGGLGSGFASNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLG 578
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 579 IHTGESIVVAPSQTLSNCEYNMLRTTALKVIRHFGVVGECNIQYALNPESEEFFIIEVNARLSRSSALASKATGYPLAYV 658
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 659 AAKLALGIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFVRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVD 738
Cdd:TIGR01369 321 AAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 739 ETVTGFDPYIKEVK-----EGELTQATDKRIFVLAAAIKANYSVEKLHDLTKIDPWFLNKMKNIIDFL-NVMELQGNNLT 812
Cdd:TIGR01369 401 IGATGFDLPDREVEpdedlWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEeELEEVKLTDLD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 813 YSQLLFAKKLGFSDRAIAAAIKSTDLVVRSQREHLGVTPFVKQIDTVAGEWPAGTNYLYLTYNANCHDIEFPGNFMIVV- 891
Cdd:TIGR01369 481 PELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVl 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 892 GSGVYRIGSSVEFDWCAVGCLRELRNLGRQTIMINYNPETVSTDYDMSDRLYFEEISFEIVMDIYQIENADGIILSMGGQ 971
Cdd:TIGR01369 561 GSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 972 LPNNIAMDLHRQQARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAM 1051
Cdd:TIGR01369 641 TPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1052 NVAYSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVAADGEILCMAVSEHVENAGVHSGDATLVTPPQDINAET 1131
Cdd:TIGR01369 721 EIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1132 LEKIKGIVRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMTVEPVDVL--HGC 1209
Cdd:TIGR01369 801 VDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEP 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1210 GKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKKAILLSIGSFKHKVELLPSIRDLA 1289
Cdd:TIGR01369 881 KYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLA 960
|
....*....
gi 34398211 1290 KMGYKLYAS 1298
Cdd:TIGR01369 961 EKGYKLYAT 969
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
347-1297 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1339.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 347 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTLDYVEQVIKAERPNGVL 426
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 427 LAFGGQTALNCGIDLERAGVFSKYNVKILGTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVYSVAEALQAAEVLGYPVM 506
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 507 ARAAFSLGGLGSGFASNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGES 584
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 585 IVVAPSQTLSNCEYNMLRTTALKVIRHFGVV-GECNIQYALNPESEEFFIIEVNARLSRSSALASKATGYPLAYVAAKLA 663
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 664 LGIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFVRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVTG 743
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 744 FDPYIK------EVKEgELTQATDKRIFVLAAAIKANYSVEKLHDLTKIDPWFLNKMKNIIDFLNVMELQGNNLTYSQLL 817
Cdd:PRK05294 408 LDEDLFeeesleELRE-ELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLR 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 818 FAKKLGFSDRAIAAAIKSTDLVVRSQREHLGVTPFVKQIDTVAGEWPAGTNYLYLTYNANCHDIEFPGNFMIVVGSGVYR 897
Cdd:PRK05294 487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 898 IGSSVEFDWCAVGCLRELRNLGRQTIMINYNPETVSTDYDMSDRLYFEEISFEIVMDIYQIENADGIILSMGGQLPNNIA 977
Cdd:PRK05294 567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 978 MDLHRQQARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSN 1057
Cdd:PRK05294 647 KALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDE 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1058 QDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDINAETLEKIK 1136
Cdd:PRK05294 727 EELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEdVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIR 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1137 GIVRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMTVEPVDVLHGC--GKVGV 1214
Cdd:PRK05294 806 EYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPYVAV 885
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1215 KVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKK-AILLSIgSFKHKVELLPSIRDLAKMGY 1293
Cdd:PRK05294 886 KEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLELGF 964
|
....
gi 34398211 1294 KLYA 1297
Cdd:PRK05294 965 KILA 968
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
352-893 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 639.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 352 LGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTLDYVEQVIKAERPNGVLLAFGG 431
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 432 QTALNCGIDLERAGVFSkyNVKILGTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVYSVAEALQAAEVLGYPVMARAAF 511
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 512 SLGGLGSGFASNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGESIVVAP 589
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 590 SQTLSNCEYNMLRTTALKVIRHFGVVGECNIQYALNpeSEEFFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 669
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 670 DIKNSvTGvttacFEPSLDYCVVKIPRWDLSKFVRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVTG--FDPY 747
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 748 I--KEVKEGELTQATDKRIFVLAAAIKANYSVEKLHDLTKIDPWFLNKMKNIIDFLnvMELQGNNLTYSQLLFAKKLGFS 825
Cdd:COG0458 391 VadDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDE--IELEEIILVINTLLGAKSLGDS 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34398211 826 DRAIAAAIKSTDLVVRSQREHLGVTPFVKQIDTVAGEWPAGTNYLYLTYNANCHDIEFPGNFMIVVGS 893
Cdd:COG0458 469 DGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-314 |
9.61e-130 |
|
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: 403.16 E-value: 9.61e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVPtendidtlglPNHFEwTDGISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:TIGR01368 47 QIVVFTYPLIGNYGVN----------DEDAE-SKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 81 KKIRDNGSVLGRIAySLPIPNDKLNLL-----DPNSRNLVDECSVKKPIVYNPKGSP--RICAIDCGLKLNQIRCFVSRG 153
Cdd:TIGR01368 116 KKIREKGTMKGVIS-TEDSNDEELVEKarvspDITGINLVAEVSTKEPYTWGQRGGKgkRVVVIDFGVKRNILRRLVKRG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 154 ARVELVPWNYDFSSI---DFDGLFISNGPGDPVVCEQLVTQIQNFMKKKntPIFGICLGHQLLSTAIGCKTFKMKYGNRG 230
Cdd:TIGR01368 195 CEVTVVPYDTDAEEIkkyNPDGIFLSNGPGDPAAVEPAIETIRKLLEKI--PIFGICLGHQLLALAFGAKTYKMKFGHRG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 231 HNLPCVHHGTGRCFMTSQNHGFAVDVTTLPS-EWEPLFTNANDHTNEGIVHKSKPYFSVQFHPEHTAGPEDLELLFDVFL 309
Cdd:TIGR01368 273 GNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFI 352
|
....*
gi 34398211 310 DTVKE 314
Cdd:TIGR01368 353 DLMKK 357
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-310 |
1.17e-129 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 402.92 E-value: 1.17e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVpteNDIDtlglpnhFEwTDGISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:PRK12564 51 QIVTFTYPLIGNYGV---NRED-------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 81 KKIRDNGSVLGRIAySLPIPNDKL-----NLLDPNSRNLVDECSVKKPIVY---NPKGSPRICAIDCGLKLNQIRCFVSR 152
Cdd:PRK12564 120 RKLREKGAMKGVIA-TEDFDAEELlekarAFPGLLGLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAER 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 153 GARVELVPWNYDFSSI---DFDGLFISNGPGDPVVCEQLVTQIQNFMKKKnTPIFGICLGHQLLSTAIGCKTFKMKYGNR 229
Cdd:PRK12564 199 GCRVTVVPATTTAEEIlalNPDGVFLSNGPGDPAALDYAIEMIRELLEKK-IPIFGICLGHQLLALALGAKTYKMKFGHR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 230 GHNLPCVHHGTGRCFMTSQNHGFAVDVTTLPSEWEPLFTNANDHTNEGIVHKSKPYFSVQFHPEHTAGPEDLELLFDVFL 309
Cdd:PRK12564 278 GANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFV 357
|
.
gi 34398211 310 D 310
Cdd:PRK12564 358 E 358
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-313 |
1.65e-125 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 392.08 E-value: 1.65e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVpteNDIDtlglpnhFEwTDGISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:COG0505 51 QIVTFTYPHIGNYGV---NDED-------FE-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 81 KKIRDNGSVLGRIAySLPIPNDKL-----NLLDPNSRNLVDECSVKKPIVY--NPKGSPRICAIDCGLKLNQIRCFVSRG 153
Cdd:COG0505 120 RHLREKGAMKGVIS-TGDLDIEELlekarAAPGMEGLDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 154 ARVELVPWNYDFSSI---DFDGLFISNGPGDPVVCEQLVTQIQNFMKKKnTPIFGICLGHQLLSTAIGCKTFKMKYGNRG 230
Cdd:COG0505 199 CRVTVVPATTSAEEIlalNPDGVFLSNGPGDPAALDYAIETIRELLGKG-IPIFGICLGHQLLALALGAKTYKLKFGHRG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 231 HNLPCVHHGTGRCFMTSQNHGFAVDVTTLP-SEWEPLFTNANDHTNEGIVHKSKPYFSVQFHPEHTAGPEDLELLFDVFL 309
Cdd:COG0505 278 ANHPVKDLETGRVEITSQNHGFAVDEDSLPaTDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFI 357
|
....
gi 34398211 310 DTVK 313
Cdd:COG0505 358 ELME 361
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
134-309 |
2.17e-96 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 305.96 E-value: 2.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 134 ICAIDCGLKLNQIRCFVSRGARVELVPWNYDFS---SIDFDGLFISNGPGDPVVCEQLVTQIQNFMKKKNtPIFGICLGH 210
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeilKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKI-PIFGICLGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 211 QLLSTAIGCKTFKMKYGNRGHNLPCVHHGTGRCFMTSQNHGFAVDVTTLPSEWEPLFTNANDHTNEGIVHKSKPYFSVQF 290
Cdd:cd01744 80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159
|
170
....*....|....*....
gi 34398211 291 HPEHTAGPEDLELLFDVFL 309
Cdd:cd01744 160 HPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
467-669 |
2.41e-95 |
|
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: 304.23 E-value: 2.41e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 467 DRKIFADRVGEIGEKVAPSEAVY--SVAEALQAAEVLGYPVMARAAFSLGGLGSGFASNQEELKILAKQALAHS------ 538
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 539 NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLgiHTGESIVVAPSQTLSNCEYNMLRTTALKVIRHFGVVGEC 618
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 34398211 619 NIQYALNPESEEFFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 669
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
137-310 |
5.54e-60 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 204.01 E-value: 5.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 137 IDCGL--KLNQIRCFVSRGARVELVPWNYDFSSID---FDGLFISNGPGDPVVCEQLVTQIQNFMKKKnTPIFGICLGHQ 211
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTPAEEILeenPDGIILSGGPGSPGAAGGAIEAIREARELK-IPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 212 LLSTAIGCKTFKMK-YGNRGHNLPCVH------HGTGRCFMTSQNHGFAVDVTTLPSEWEPLFTNANDHTNEGIVHKSKP 284
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*.
gi 34398211 285 YFSVQFHPEHTAGPEDLELLFDVFLD 310
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
755-874 |
1.62e-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: 174.17 E-value: 1.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 755 ELTQATDKRIFVLAAAIKANYSVEKLHDLTKIDPWFLNKMKNIIDFLN-VMELQGNNLTYSQLLFAKKLGFSDRAIAAAI 833
Cdd:smart01096 4 ELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKeLKKGGLDELDADLLRKAKRLGFSDRQIAKLL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 34398211 834 KSTDLVVRSQREHLGVTPFVKQIDTVAGEWPAGTNYLYLTY 874
Cdd:smart01096 84 GVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
4.71e-36 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 132.88 E-value: 4.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVpteNDIDtlglpnhFEwTDGISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:smart01097 49 QIVVFTYPLIGNYGV---NDED-------FE-SDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALT 117
|
90
....*....|...
gi 34398211 81 KKIRDNGSVLGRI 93
Cdd:smart01097 118 RKLREKGAMKGVI 130
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1266-1298 |
3.63e-07 |
|
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: 49.99 E-value: 3.63e-07
10 20 30
....*....|....*....|....*....|...
gi 34398211 1266 KAILLSIGSFKhKVELLPSIRDLAKMGYKLYAS 1298
Cdd:cd01423 1 KGILISIGSYS-KPELLPTAQKLSKLGYKLYAT 32
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
341-1298 |
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: 1549.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 341 IMKEKPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTLDYVEQVIKAE 420
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 421 RPNGVLLAFGGQTALNCGIDLERAGVFSKYNVKILGTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVYSVAEALQAAEV 500
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 501 LGYPVMARAAFSLGGLGSGFASNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLG 578
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 579 IHTGESIVVAPSQTLSNCEYNMLRTTALKVIRHFGVVGECNIQYALNPESEEFFIIEVNARLSRSSALASKATGYPLAYV 658
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 659 AAKLALGIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFVRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVD 738
Cdd:TIGR01369 321 AAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 739 ETVTGFDPYIKEVK-----EGELTQATDKRIFVLAAAIKANYSVEKLHDLTKIDPWFLNKMKNIIDFL-NVMELQGNNLT 812
Cdd:TIGR01369 401 IGATGFDLPDREVEpdedlWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEeELEEVKLTDLD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 813 YSQLLFAKKLGFSDRAIAAAIKSTDLVVRSQREHLGVTPFVKQIDTVAGEWPAGTNYLYLTYNANCHDIEFPGNFMIVV- 891
Cdd:TIGR01369 481 PELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVl 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 892 GSGVYRIGSSVEFDWCAVGCLRELRNLGRQTIMINYNPETVSTDYDMSDRLYFEEISFEIVMDIYQIENADGIILSMGGQ 971
Cdd:TIGR01369 561 GSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 972 LPNNIAMDLHRQQARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAM 1051
Cdd:TIGR01369 641 TPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1052 NVAYSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVAADGEILCMAVSEHVENAGVHSGDATLVTPPQDINAET 1131
Cdd:TIGR01369 721 EIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1132 LEKIKGIVRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMTVEPVDVL--HGC 1209
Cdd:TIGR01369 801 VDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEP 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1210 GKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKKAILLSIGSFKHKVELLPSIRDLA 1289
Cdd:TIGR01369 881 KYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLA 960
|
....*....
gi 34398211 1290 KMGYKLYAS 1298
Cdd:TIGR01369 961 EKGYKLYAT 969
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
347-1297 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1339.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 347 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTLDYVEQVIKAERPNGVL 426
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 427 LAFGGQTALNCGIDLERAGVFSKYNVKILGTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVYSVAEALQAAEVLGYPVM 506
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 507 ARAAFSLGGLGSGFASNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGES 584
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 585 IVVAPSQTLSNCEYNMLRTTALKVIRHFGVV-GECNIQYALNPESEEFFIIEVNARLSRSSALASKATGYPLAYVAAKLA 663
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 664 LGIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFVRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVTG 743
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 744 FDPYIK------EVKEgELTQATDKRIFVLAAAIKANYSVEKLHDLTKIDPWFLNKMKNIIDFLNVMELQGNNLTYSQLL 817
Cdd:PRK05294 408 LDEDLFeeesleELRE-ELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLR 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 818 FAKKLGFSDRAIAAAIKSTDLVVRSQREHLGVTPFVKQIDTVAGEWPAGTNYLYLTYNANCHDIEFPGNFMIVVGSGVYR 897
Cdd:PRK05294 487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 898 IGSSVEFDWCAVGCLRELRNLGRQTIMINYNPETVSTDYDMSDRLYFEEISFEIVMDIYQIENADGIILSMGGQLPNNIA 977
Cdd:PRK05294 567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 978 MDLHRQQARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSN 1057
Cdd:PRK05294 647 KALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDE 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1058 QDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDINAETLEKIK 1136
Cdd:PRK05294 727 EELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEdVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIR 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1137 GIVRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMTVEPVDVLHGC--GKVGV 1214
Cdd:PRK05294 806 EYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPYVAV 885
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1215 KVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKK-AILLSIgSFKHKVELLPSIRDLAKMGY 1293
Cdd:PRK05294 886 KEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLELGF 964
|
....
gi 34398211 1294 KLYA 1297
Cdd:PRK05294 965 KILA 968
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
347-1297 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1020.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 347 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTLDYVEQVIKAERPNGVL 426
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 427 LAFGGQTALNCGIDLERAGVFSKYNVKILGTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVYSVAEALQAAEVLGYPVM 506
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 507 ARAAFSLGGLGSGFASNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGES 584
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQASpiHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 585 IVVAPSQTLSNCEYNMLRTTALKVIRHFGVVGECNIQYALNPESEEFFIIEVNARLSRSSALASKATGYPLAYVAAKLAL 664
Cdd:PRK12815 248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 665 GIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFVRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVTGF 744
Cdd:PRK12815 328 GYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 745 DPYIKEVKEGE------LTQATDKRIFVLAAAIKANYSVEKLHDLTKIDPWFLNKMKNIIDFLNVMELQGNNLTYSQLLF 818
Cdd:PRK12815 408 SLPIELSGKSDeellqdLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLDLSADLLRK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 819 AKKLGFSDRAIAAAIKSTDLVVRSQREHLGVTPFVKQIDTVAGEWPAGTNYLYLTYNANChDIEFPGN--FMIVVGSGVY 896
Cdd:PRK12815 488 VKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGES-EAEPSSEkkKVLILGSGPI 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 897 RIGSSVEFDWCAVGCLRELRNLGRQTIMINYNPETVSTDYDMSDRLYFEEISFEIVMDIYQIENADGIILSMGGQLPNNI 976
Cdd:PRK12815 567 RIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAINL 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 977 AMDLHRQQARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYS 1056
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYD 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1057 NQDLETYLNAAslVSKEHPVVISKFLqEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDINAETLEKI 1135
Cdd:PRK12815 727 EPALEAYLAEN--ASQLYPILIDQFI-DGKEYEVDAI-SDGEdVTIPGIIEHIEQAGVHSGDSIAVLPPQSLSEEQQEKI 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1136 KGIVRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMTVE----PVDVLHGCGK 1211
Cdd:PRK12815 803 RDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAelgyPNGLWPGSPF 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1212 VGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKKAILLSIGSFKHKVELLPSIRDLAKM 1291
Cdd:PRK12815 883 IHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARRFAQL 962
|
....*.
gi 34398211 1292 GYKLYA 1297
Cdd:PRK12815 963 GFKLLA 968
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
347-1298 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 858.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 347 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTLDYVEQVIKAERPNGVL 426
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 427 LAFGGQTALNCGIDLERAGVFSKYNVKILGTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVYSVAEALQAAEVLG-YPV 505
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 506 MARAAFSLGGLGSGFASNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGE 583
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAASitSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 584 SIVVAPSQTLSNCEYNMLRTTALKVIRHFGVvgEC---NIQYALNPESEEFFIIEVNARLSRSSALASKATGYPLAYVAA 660
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 661 KLALGIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLSKFVRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDet 740
Cdd:PLN02735 342 KLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLE-- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 741 vTGFD----PYIKEVkEGELTQATDK-------RIFVLAAAIKANYSVEKLHDLTKIDPWFLNKMKNIID---FLNVMEL 806
Cdd:PLN02735 420 -TGFSgwgcAKVKEL-DWDWEQLKYKlrvpnpdRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDveqFLKSRSL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 807 qgNNLTYSQLLFAKKLGFSDRAIAAAIKSTDLVVRSQREHLGVTPFVKQIDTVAGEWPAGTNYLYLTYNANCHDIEFPGN 886
Cdd:PLN02735 498 --SELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKK 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 887 FMIVVGSGVYRIGSSVEFDWCAVGCLRELRNLGRQTIMINYNPETVSTDYDMSDRLYFEEISFEIVMDIYQIENADGIIL 966
Cdd:PLN02735 576 KVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIV 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 967 SMGGQLPNNIAMDLHRQ-------------QARVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEE 1033
Cdd:PLN02735 656 QFGGQTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKR 735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1034 VGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVA-ADGEILCMAVSEHVENAG 1112
Cdd:PLN02735 736 IGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAG 815
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1113 VHSGDATLVTPPQDINAETLEKIKGIVRDLAALLDVTGPFNMQL-IAKNNELKVIECNVRVSRSFPFVSKTLNHDF---- 1187
Cdd:PLN02735 816 VHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLakya 895
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1188 ---VATATRAIIGMTVEPVDvlhgcGKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIP 1264
Cdd:PLN02735 896 slvMSGKSLKDLGFTEEVIP-----AHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLP 970
|
970 980 990
....*....|....*....|....*....|....*
gi 34398211 1265 KKA-ILLSIGSfKHKVELLPSIRDLAKMGYKLYAS 1298
Cdd:PLN02735 971 LSGtVFISLND-LTKPHLVPIARGFLELGFRIVST 1004
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
352-893 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 639.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 352 LGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTLDYVEQVIKAERPNGVLLAFGG 431
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 432 QTALNCGIDLERAGVFSkyNVKILGTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVYSVAEALQAAEVLGYPVMARAAF 511
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 512 SLGGLGSGFASNQEELKILAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGESIVVAP 589
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 590 SQTLSNCEYNMLRTTALKVIRHFGVVGECNIQYALNpeSEEFFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 669
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 670 DIKNSvTGvttacFEPSLDYCVVKIPRWDLSKFVRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVTG--FDPY 747
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 748 I--KEVKEGELTQATDKRIFVLAAAIKANYSVEKLHDLTKIDPWFLNKMKNIIDFLnvMELQGNNLTYSQLLFAKKLGFS 825
Cdd:COG0458 391 VadDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDE--IELEEIILVINTLLGAKSLGDS 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34398211 826 DRAIAAAIKSTDLVVRSQREHLGVTPFVKQIDTVAGEWPAGTNYLYLTYNANCHDIEFPGNFMIVVGS 893
Cdd:COG0458 469 DGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
891-1297 |
2.28e-161 |
|
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: 493.63 E-value: 2.28e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 891 VGSGVYRIGSSVEFDWCAVGCLRELRNLGRQTIMINYNPETVSTDYDMSDRLYFEEISFEIVMDIYQIENADGIILSMGG 970
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 971 QLPNNIAMDLHRQQA----RVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVL 1046
Cdd:COG0458 81 QTALNLAVELEEAGIlegvKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1047 SGAAMNVAYSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVA-ADGEILCMAVSEHVENAGVHSGDATLVTPPQ 1125
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRdGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1126 DINAETLEKIKGIVRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMTVEPVDV 1205
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1206 LHG----CGKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRHEAYLKAMMSTGFQIPKKaILLSIGSFKHKVEL 1281
Cdd:COG0458 321 DTGfeptLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDKEEA 399
|
410
....*....|....*.
gi 34398211 1282 LPSIRDLAKMGYKLYA 1297
Cdd:COG0458 400 LLLARRLARLGFLIEA 415
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-314 |
9.61e-130 |
|
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: 403.16 E-value: 9.61e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVPtendidtlglPNHFEwTDGISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:TIGR01368 47 QIVVFTYPLIGNYGVN----------DEDAE-SKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 81 KKIRDNGSVLGRIAySLPIPNDKLNLL-----DPNSRNLVDECSVKKPIVYNPKGSP--RICAIDCGLKLNQIRCFVSRG 153
Cdd:TIGR01368 116 KKIREKGTMKGVIS-TEDSNDEELVEKarvspDITGINLVAEVSTKEPYTWGQRGGKgkRVVVIDFGVKRNILRRLVKRG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 154 ARVELVPWNYDFSSI---DFDGLFISNGPGDPVVCEQLVTQIQNFMKKKntPIFGICLGHQLLSTAIGCKTFKMKYGNRG 230
Cdd:TIGR01368 195 CEVTVVPYDTDAEEIkkyNPDGIFLSNGPGDPAAVEPAIETIRKLLEKI--PIFGICLGHQLLALAFGAKTYKMKFGHRG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 231 HNLPCVHHGTGRCFMTSQNHGFAVDVTTLPS-EWEPLFTNANDHTNEGIVHKSKPYFSVQFHPEHTAGPEDLELLFDVFL 309
Cdd:TIGR01368 273 GNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFI 352
|
....*
gi 34398211 310 DTVKE 314
Cdd:TIGR01368 353 DLMKK 357
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-310 |
1.17e-129 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 402.92 E-value: 1.17e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVpteNDIDtlglpnhFEwTDGISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:PRK12564 51 QIVTFTYPLIGNYGV---NRED-------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 81 KKIRDNGSVLGRIAySLPIPNDKL-----NLLDPNSRNLVDECSVKKPIVY---NPKGSPRICAIDCGLKLNQIRCFVSR 152
Cdd:PRK12564 120 RKLREKGAMKGVIA-TEDFDAEELlekarAFPGLLGLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAER 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 153 GARVELVPWNYDFSSI---DFDGLFISNGPGDPVVCEQLVTQIQNFMKKKnTPIFGICLGHQLLSTAIGCKTFKMKYGNR 229
Cdd:PRK12564 199 GCRVTVVPATTTAEEIlalNPDGVFLSNGPGDPAALDYAIEMIRELLEKK-IPIFGICLGHQLLALALGAKTYKMKFGHR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 230 GHNLPCVHHGTGRCFMTSQNHGFAVDVTTLPSEWEPLFTNANDHTNEGIVHKSKPYFSVQFHPEHTAGPEDLELLFDVFL 309
Cdd:PRK12564 278 GANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFV 357
|
.
gi 34398211 310 D 310
Cdd:PRK12564 358 E 358
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-313 |
1.65e-125 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 392.08 E-value: 1.65e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVpteNDIDtlglpnhFEwTDGISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:COG0505 51 QIVTFTYPHIGNYGV---NDED-------FE-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 81 KKIRDNGSVLGRIAySLPIPNDKL-----NLLDPNSRNLVDECSVKKPIVY--NPKGSPRICAIDCGLKLNQIRCFVSRG 153
Cdd:COG0505 120 RHLREKGAMKGVIS-TGDLDIEELlekarAAPGMEGLDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 154 ARVELVPWNYDFSSI---DFDGLFISNGPGDPVVCEQLVTQIQNFMKKKnTPIFGICLGHQLLSTAIGCKTFKMKYGNRG 230
Cdd:COG0505 199 CRVTVVPATTSAEEIlalNPDGVFLSNGPGDPAALDYAIETIRELLGKG-IPIFGICLGHQLLALALGAKTYKLKFGHRG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 231 HNLPCVHHGTGRCFMTSQNHGFAVDVTTLP-SEWEPLFTNANDHTNEGIVHKSKPYFSVQFHPEHTAGPEDLELLFDVFL 309
Cdd:COG0505 278 ANHPVKDLETGRVEITSQNHGFAVDEDSLPaTDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFI 357
|
....
gi 34398211 310 DTVK 313
Cdd:COG0505 358 ELME 361
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
134-309 |
2.17e-96 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 305.96 E-value: 2.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 134 ICAIDCGLKLNQIRCFVSRGARVELVPWNYDFS---SIDFDGLFISNGPGDPVVCEQLVTQIQNFMKKKNtPIFGICLGH 210
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeilKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKI-PIFGICLGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 211 QLLSTAIGCKTFKMKYGNRGHNLPCVHHGTGRCFMTSQNHGFAVDVTTLPSEWEPLFTNANDHTNEGIVHKSKPYFSVQF 290
Cdd:cd01744 80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159
|
170
....*....|....*....
gi 34398211 291 HPEHTAGPEDLELLFDVFL 309
Cdd:cd01744 160 HPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
467-669 |
2.41e-95 |
|
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: 304.23 E-value: 2.41e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 467 DRKIFADRVGEIGEKVAPSEAVY--SVAEALQAAEVLGYPVMARAAFSLGGLGSGFASNQEELKILAKQALAHS------ 538
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 539 NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLgiHTGESIVVAPSQTLSNCEYNMLRTTALKVIRHFGVVGEC 618
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 34398211 619 NIQYALNPESEEFFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 669
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
1-314 |
5.78e-95 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 309.13 E-value: 5.78e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVpteNDIDtlglpnhFEWTDgISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:PRK12838 49 QIVVFTYPLIGNYGI---NADD-------YESKQ-PQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 81 KKIRDNGSVLGRIAYSLPIPNDKLNLLDPNSRNLVDECSVKKPIVYnPKGSPRICAIDCGLKLNQIRCFVSRGARVELVP 160
Cdd:PRK12838 118 KHIREKGTMKASITTTDDAHAFDQIKALVLPKNVVAQVSTKEPYTY-GNGGKHVALIDFGYKKSILRSLSKRGCKVTVLP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 161 WNYDFSSI---DFDGLFISNGPGDPVVCEQLVTQI-QNFMkkkNTPIFGICLGHQLLSTAIGCKTFKMKYGNRGHNLPCV 236
Cdd:PRK12838 197 YDTSLEEIknlNPDGIVLSNGPGDPKELQPYLPEIkKLIS---SYPILGICLGHQLIALALGADTEKLPFGHRGANHPVI 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34398211 237 HHGTGRCFMTSQNHGFAVDVTTL-PSEWEPLFTNANDHTNEGIVHKSKPYFSVQFHPEHTAGPEDLELLFDVFLDTVKE 314
Cdd:PRK12838 274 DLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEK 352
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
332-735 |
5.11e-83 |
|
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: 294.98 E-value: 5.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 332 LSYKPKPELIMKEKPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTLD 411
Cdd:TIGR01369 540 STYEGERDDVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFE 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 412 YVEQVIKAERPNGVLLAFGGQTALNCGIDLERAGvfskynVKILGTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVYSV 491
Cdd:TIGR01369 620 DVMNIIELEKPEGVIVQFGGQTPLNLAKALEEAG------VPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSV 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 492 AEALQAAEVLGYPVMARAAFSLGGLGSGFASNQEELKILAKQALAHSNQ--LIIDKSLRGWKEVEYEVVRDafDNCITVC 569
Cdd:TIGR01369 694 EEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAVSD--GEEVLIP 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 570 N-MENLDPLGIHTGESIVVAPSQTLSNCEYNMLRTTALKVIRHFGVVGECNIQYALnpESEEFFIIEVNARLSRSSALAS 648
Cdd:TIGR01369 772 GiMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGEVYVIEVNPRASRTVPFVS 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 649 KATGYPLAYVAAKLALGIPLPDIknsvtGVTtacFEPSLDYCVVKIPRWDLSKFVRVSKNIGSSMKSVGEVMAIGRNFEE 728
Cdd:TIGR01369 850 KATGVPLAKLAVRVMLGKKLEEL-----GVG---KEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAE 921
|
....*..
gi 34398211 729 AFQKALR 735
Cdd:TIGR01369 922 AFLKAQL 928
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
333-733 |
1.46e-78 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 281.86 E-value: 1.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 333 SYKPKPELIMKEKPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTLDY 412
Cdd:PRK12815 542 TYFGESEAEPSSEKKKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLED 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 413 VEQVIKAERPNGVLLAFGGQTALNCGIDLERAGvfskynVKILGTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVYSVA 492
Cdd:PRK12815 622 VLNVAEAENIKGVIVQFGGQTAINLAKGLEEAG------LTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEE 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 493 EALQAAEVLGYPVMARAAFSLGGLGSGFASNQEELKILAKQALAHSNQLIIDKSLRGwKEVEYEVVRDAFDncITVCN-M 571
Cdd:PRK12815 696 EAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPILIDQFIDG-KEYEVDAISDGED--VTIPGiI 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 572 ENLDPLGIHTGESIVVAPSQTLSNCEYNMLRTTALKVIRHFGVVGECNIQYALnpESEEFFIIEVNARLSRSSALASKAT 651
Cdd:PRK12815 773 EHIEQAGVHSGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL--ANDEIYVLEVNPRASRTVPFVSKAT 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 652 GYPLAYVAAKLALGIPLPDIKNSVTgvttacFEPSLDYCVVKIPRWDLSKFVRVSKNIGSSMKSVGEVMAIGRNFEEAFQ 731
Cdd:PRK12815 851 GVPLAKLATKVLLGKSLAELGYPNG------LWPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALY 924
|
..
gi 34398211 732 KA 733
Cdd:PRK12815 925 KG 926
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-317 |
3.78e-67 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 231.99 E-value: 3.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVPTEnDIDTLGlpnhfewtdgISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:CHL00197 53 QIVTFTYPEIGNTGINLE-DIESVK----------IQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 81 KKIRDNGSVLG--------------RIAYSLPIPNdkLNLLDPNSRNLV---DECSVKK-PIVYNPK---GSP-RICAID 138
Cdd:CHL00197 122 QHLRRFGTMNGcisnqnlnlsylraKIKESPHMPS--SDLIPRVTTSSYyewDEKSHPSfYLADNKRphsSYQlKIIVID 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 139 CGLKLNQIRCFVSRGARVELVPWNYDFSSIDF---DGLFISNGPGDPVVCEQLVTQIQNFMKKkNTPIFGICLGHQLLST 215
Cdd:CHL00197 200 FGVKYNILRRLKSFGCSITVVPATSPYQDILSyqpDGILLSNGPGDPSAIHYGIKTVKKLLKY-NIPIFGICMGHQILSL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 216 AIGCKTFKMKYGNRGHNlpcvhHGTG---RCFMTSQNHGFAVDVTTLPSewEPLFT---NANDHTNEGIVHKSKPYFSVQ 289
Cdd:CHL00197 279 ALEAKTFKLKFGHRGLN-----HPSGlnqQVEITSQNHGFAVNLESLAK--NKFYIthfNLNDGTVAGISHSPKPYFSVQ 351
|
330 340
....*....|....*....|....*...
gi 34398211 290 FHPEHTAGPEDLELLFDVFLDTVKEYQN 317
Cdd:CHL00197 352 YHPEASPGPHDADYLFEYFIEIIKHSKS 379
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
137-310 |
5.54e-60 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 204.01 E-value: 5.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 137 IDCGL--KLNQIRCFVSRGARVELVPWNYDFSSID---FDGLFISNGPGDPVVCEQLVTQIQNFMKKKnTPIFGICLGHQ 211
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTPAEEILeenPDGIILSGGPGSPGAAGGAIEAIREARELK-IPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 212 LLSTAIGCKTFKMK-YGNRGHNLPCVH------HGTGRCFMTSQNHGFAVDVTTLPSEWEPLFTNANDHTNEGIVHKSKP 284
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*.
gi 34398211 285 YFSVQFHPEHTAGPEDLELLFDVFLD 310
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
755-874 |
1.62e-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: 174.17 E-value: 1.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 755 ELTQATDKRIFVLAAAIKANYSVEKLHDLTKIDPWFLNKMKNIIDFLN-VMELQGNNLTYSQLLFAKKLGFSDRAIAAAI 833
Cdd:smart01096 4 ELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKeLKKGGLDELDADLLRKAKRLGFSDRQIAKLL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 34398211 834 KSTDLVVRSQREHLGVTPFVKQIDTVAGEWPAGTNYLYLTY 874
Cdd:smart01096 84 GVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
1-305 |
2.74e-50 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 184.03 E-value: 2.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVPTENdidtlglpnhfEWTDGISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:PLN02771 103 QFVLMTNPHIGNTGVNFDD-----------EESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAIT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 81 KKIRDNGSVLGRIAYSLPIPNDKLNLL----DPNSRNLVDECSVKKPIVYNPKGSP--------------RICAIDCGLK 142
Cdd:PLN02771 172 RRLREDGSLIGVLSTEDSKTDEELLKMsrswDIVGIDLISGVSCKSPYEWVDKTNPewdfntnsrdgesyHVIAYDFGIK 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 143 LNQIRCFVSRGARVELVPWNYDFSS---IDFDGLFISNGPGDPVVCEQLVTQIQNFMKKknTPIFGICLGHQLLSTAIGC 219
Cdd:PLN02771 252 HNILRRLASYGCKITVVPSTWPASEalkMKPDGVLFSNGPGDPSAVPYAVETVKELLGK--VPVFGICMGHQLLGQALGG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 220 KTFKMKYGNRGHNLPCVHHGTGRCFMTSQNHGFAVDVTTLPSEWEPLFTNANDHTNEGIVHKSKPYFSVQFHPEHTAGPE 299
Cdd:PLN02771 330 KTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPH 409
|
....*.
gi 34398211 300 DLELLF 305
Cdd:PLN02771 410 DSDNAF 415
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
6.80e-39 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 140.92 E-value: 6.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVPTENdidtlglpnhFEwTDGISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:pfam00988 45 QIVVFTYPLIGNYGVNPED----------FE-SDKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALT 113
|
90
....*....|...
gi 34398211 81 KKIRDNGSVLGRI 93
Cdd:pfam00988 114 RKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
4.71e-36 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 132.88 E-value: 4.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1 QILVLTYPMIGNYGVpteNDIDtlglpnhFEwTDGISVAGLVVGEICNTPSHWRQTRTLSKWMEDYGVAGISDIDTRALT 80
Cdd:smart01097 49 QIVVFTYPLIGNYGV---NDED-------FE-SDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALT 117
|
90
....*....|...
gi 34398211 81 KKIRDNGSVLGRI 93
Cdd:smart01097 118 RKLREKGAMKGVI 130
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
755-831 |
3.88e-32 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 119.79 E-value: 3.88e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34398211 755 ELTQATDKRIFVLAAAIKANYSVEKLHDLTKIDPWFLNKMKNIIDFLNVMELQGNNLTYSQLLFAKKLGFSDRAIAA 831
Cdd:pfam02787 2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDAELLREAKRLGFSDRQIAK 78
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
989-1173 |
7.10e-20 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 90.70 E-value: 7.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 989 GTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAS 1068
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1069 ----LVSKEHPVVISKFLqEAKEIDVDAVAADGEILCMAVSEHvENAGVHSGDATLVTPPqDINAETLEKIKGIVRDLAA 1144
Cdd:COG0439 123 aeakAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGELVARALR 199
|
170 180 190
....*....|....*....|....*....|.
gi 34398211 1145 LLDV-TGPFNMQ-LIAKNNELKVIECNVRVS 1173
Cdd:COG0439 200 ALGYrRGAFHTEfLLTPDGEPYLIEINARLG 230
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
153-293 |
6.55e-19 |
|
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: 85.66 E-value: 6.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 153 GARVELVPWN----YDFSSIDFDGLFISNGPGDPVVCEQLVTQIQNFmkKKNTPIFGICLGHQLLSTAIGCKTFKMKYGN 228
Cdd:cd01743 22 GAEVVVVRNDeitlEELELLNPDAIVISPGPGHPEDAGISLEIIRAL--AGKVPILGVCLGHQAIAEAFGGKVVRAPEPM 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34398211 229 RGHNLPCVHHGTGRCFMTSQN------HGFAVDVTTLPSEWEplftnANDHTNEGIV----HKSKPYFSVQFHPE 293
Cdd:cd01743 100 HGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLE-----VTASTEDGVImalrHRDLPIYGVQFHPE 169
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1023-1201 |
3.71e-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: 81.58 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1023 NLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKE----HPVVISKFLQEAKEIDVDaVAADGE 1098
Cdd:pfam02786 26 TEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnPQVLVEKSLKGPKHIEYQ-VLRDAH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1099 ILCMAVSEhVENA-GVHSGDATLVTPPQDINAETLEKIKGIVRDLAALLDVTGPFNMQLI--AKNNELKVIECNVRVSRS 1175
Cdd:pfam02786 105 GNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFAldPFSGEYYFIEMNTRLQVE 183
|
170 180
....*....|....*....|....*.
gi 34398211 1176 FPFVSKTLNHDFVATATRAIIGMTVE 1201
Cdd:pfam02786 184 HALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
164-293 |
4.10e-15 |
|
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: 75.07 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 164 DFSSIDFDGLFISNGPGDPV---VCEQLvtqIQNFMKKKntPIFGICLGHQllstAIGcktfkMKYGNRGHNLPCVHHGt 240
Cdd:COG0512 37 EIEALAPDGIVLSPGPGTPEeagISLEV---IRAFAGKI--PILGVCLGHQ----AIG-----EAFGGKVVRAPEPMHG- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34398211 241 grcfMTSQ-------------N-------HGFAVDVTTLPSEWEPlftNANDHTNE--GIVHKSKPYFSVQFHPE 293
Cdd:COG0512 102 ----KTSPithdgsglfaglpNpftatryHSLVVDRETLPDELEV---TAWTEDGEimGIRHRELPIEGVQFHPE 169
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
468-667 |
1.25e-14 |
|
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: 75.29 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 468 RKIFAdrvgEIGEKVAPSEAVYSVAEALQAAEVLGYPVMARAAFSLGGLGSGFASNQEELKILAKQALAHSN------QL 541
Cdd:COG0439 59 REALA----AAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKagspngEV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 542 IIDKSLRGwKEVEYEVVrdAFDNCITVCNM---ENLDPLGIHTGEsivVAPSQtLSNCEYNMLRTTALKVIRHFGVV-GE 617
Cdd:COG0439 135 LVEEFLEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 34398211 618 CNIQYALNPEsEEFFIIEVNARLS--RSSALASKATGYPLAYVAAKLALGIP 667
Cdd:COG0439 208 FHTEFLLTPD-GEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
157-296 |
3.92e-14 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 73.06 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 157 ELVPWNYDFSsiDFDGLFISNGPGDPVVCEQLVTQIQNFMK---KKNTPIFGICLGHQLLSTAIGCKTFKMKYGNRG--- 230
Cdd:COG0518 38 EILPYDPDLE--DPDGLILSGGPMSVYDEDPWLEDEPALIReafELGKPVLGICYGAQLLAHALGGKVEPGPGREIGwap 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34398211 231 ----------HNLPcvhhGTGRCFMTsqnHGFAvdVTTLPSEWEPLFTNANDHtNEGIVHkSKPYFSVQFHPEHTA 296
Cdd:COG0518 116 velteadplfAGLP----DEFTVWMS---HGDT--VTELPEGAEVLASSDNCP-NQAFRY-GRRVYGVQFHPEVTH 180
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
171-293 |
6.91e-14 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 71.31 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 171 DGLFISNGPGDPV---VCEQLvtqIQNFmkKKNTPIFGICLGHQLLSTAIGC-----------KTFKMKYGNRG--HNLP 234
Cdd:PRK05670 45 DAIVLSPGPGTPAeagISLEL---IREF--AGKVPILGVCLGHQAIGEAFGGkvvrakeimhgKTSPIEHDGSGifAGLP 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34398211 235 cvhhgtgRCFMTSQNHGFAVDVTTLPSEWEPlftNANDHTNE--GIVHKSKPYFSVQFHPE 293
Cdd:PRK05670 120 -------NPFTVTRYHSLVVDRESLPDCLEV---TAWTDDGEimGVRHKELPIYGVQFHPE 170
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
153-315 |
1.44e-12 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 67.57 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 153 GARVELVPWNYDFSSID--FDGLFISNGPGdpvvcEQLVTQIQNFMKKKNTPIFGICLGHQLLSTAIGCKTFKMKYGNRG 230
Cdd:PRK00758 23 GVDAKIIPNTTPVEEIKafEDGLILSGGPD-----IERAGNCPEYLKELDVPILGICLGHQLIAKAFGGEVGRGEYGEYA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 231 H-NLPCVHH-----GTGRCFMTSQNHgfAVDVTTLPSEWEPLftnANDHT--NEGIVHKSKPYFSVQFHPE--HTagpED 300
Cdd:PRK00758 98 LvEVEILDEddilkGLPPEIRVWASH--ADEVKELPDGFEIL---ARSDIceVEAMKHKEKPIYGVQFHPEvaHT---EY 169
|
170
....*....|....*
gi 34398211 301 LELLFDVFLDTVKEY 315
Cdd:PRK00758 170 GEEIFKNFLEICGKY 184
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
173-304 |
1.75e-12 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 71.67 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 173 LFISNGPGDPVVCEQLVTQIQNFMKKknTPIFGICLGHQLLSTAIGCKTFKMKYGNRGHNLPCVHHGTGrCFMTSQN--- 249
Cdd:PRK14607 48 IVISPGPGRPEEAGISVEVIRHFSGK--VPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKG-LFRGIPNptv 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 34398211 250 ----HGFAVDVTTLPSEWEPLfTNANDHTNEGIVHKSKPYFSVQFHPEHTAGPEDLELL 304
Cdd:PRK14607 125 atryHSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPESILTEEGKRIL 182
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
144-293 |
2.02e-12 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 67.12 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 144 NQIRCFVSRGARVeLVPWNYDFSSIDFDGLF-----ISNGPGDPVVCEQLVTQIQNFMKKknTPIFGICLGHQLLSTAIG 218
Cdd:TIGR00566 14 NLVQYFCELGAEV-VVKRNDSLTLQEIEALLpllivISPGPCTPNEAGISLEAIRHFAGK--LPILGVCLGHQAMGQAFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 219 CKTFKMKYGNRGHNLPCVHHGTGRC------FMTSQNHGFAVDVTTLPSEWEPLFTNANDHTNEGIVHKSKPYFSVQFHP 292
Cdd:TIGR00566 91 GDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHP 170
|
.
gi 34398211 293 E 293
Cdd:TIGR00566 171 E 171
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
169-293 |
2.76e-12 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 67.38 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 169 DFDGLFISNGPGDPV---VCEQLVTQIqnfmKKKNTPIFGICLGHQLLSTAIGC-----------KTFKMKYGNRGhnlp 234
Cdd:PRK07765 46 QFDGVLLSPGPGTPEragASIDMVRAC----AAAGTPLLGVCLGHQAIGVAFGAtvdrapellhgKTSSVHHTGVG---- 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34398211 235 cVHHGTGRCFMTSQNHGFAVDVTTLPSEWEplftnANDHTNEGIV----HKSKPYFSVQFHPE 293
Cdd:PRK07765 118 -VLAGLPDPFTATRYHSLTILPETLPAELE-----VTARTDSGVImavrHRELPIHGVQFHPE 174
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
173-309 |
5.62e-12 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 66.04 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 173 LFISNGPGDPVVCEQLVTQIQNFMKKknTPIFGICLGHQLLSTAIGCKTFKMKYGNRG------HNLPCVHHGTGRCFMT 246
Cdd:PRK06774 47 LVISPGPCTPNEAGISLAVIRHFADK--LPILGVCLGHQALGQAFGARVVRARQVMHGktsaicHSGQGVFRGLNQPLTV 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34398211 247 SQNHGFAVDVTTLPSEWE-PLFTNANDHTNE--GIVHKSKPYFSVQFHPEHTAGPEDLELLfDVFL 309
Cdd:PRK06774 125 TRYHSLVIAADSLPGCFElTAWSERGGEMDEimGIRHRTLPLEGVQFHPESILSEQGHQLL-DNFL 189
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
153-295 |
5.88e-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: 65.64 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 153 GARVELVPWNYDFSSI---DFDGLFISNGP------GDPVVCEQLVTQiqnfmkkkNTPIFGICLGHQLLSTAIGCKTFK 223
Cdd:cd01742 22 GVYSEILPNTTPLEEIklkNPKGIILSGGPssvyeeDAPRVDPEIFEL--------GVPVLGICYGMQLIAKALGGKVER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 224 MKYGNRGHNLPCVHHGTG---------RCFMtsqNHGfavD-VTTLPSEWEPLFTNANDHtNEGIVHKSKPYFSVQFHPE 293
Cdd:cd01742 94 GDKREYGKAEIEIDDSSPlfeglpdeqTVWM---SHG---DeVVKLPEGFKVIASSDNCP-VAAIANEEKKIYGVQFHPE 166
|
....
gi 34398211 294 --HT 295
Cdd:cd01742 167 vtHT 170
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
987-1178 |
1.31e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 67.22 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 987 VLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKS--AIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYL 1064
Cdd:PRK12767 98 VLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDfkAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1065 NAASlvskehPVVISKFLQEaKEIDVDA-VAADGEILCMAVSEHVEnagVHSGDAtlvtppqdINAETLE--KIKGIVRD 1141
Cdd:PRK12767 178 EYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGET--------SKGVTVKdpELFKLAER 239
|
170 180 190
....*....|....*....|....*....|....*..
gi 34398211 1142 LAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPF 1178
Cdd:PRK12767 240 LAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
157-304 |
2.73e-11 |
|
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: 63.87 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 157 ELVPWNYDFSSI-DFD--GLFISNGP-----GDPVVCEQLVTQIqnfmkkkNTPIFGICLGHQLLSTAIGCKTFKMKYGN 228
Cdd:TIGR00888 26 ELVPNTTPLEEIrEKNpkGIILSGGPssvyaENAPRADEKIFEL-------GVPVLGICYGMQLMAKQLGGEVGRAEKRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 229 RGH------NLPCVHHGTGRCFMTSQNHGFAVdvTTLPSEWEPLFTNANDhTNEGIVHKSKPYFSVQFHPEHTAGPEDLE 302
Cdd:TIGR00888 99 YGKaeleilDEDDLFRGLPDESTVWMSHGDKV--KELPEGFKVLATSDNC-PVAAMAHEEKPIYGVQFHPEVTHTEYGNE 175
|
..
gi 34398211 303 LL 304
Cdd:TIGR00888 176 LL 177
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
169-294 |
2.98e-11 |
|
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: 63.80 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 169 DFDGLFISNGPGDpVVCEQL--VTQIQNFMKK---KNTPIFGICLGHQLLSTAIGCKTFKMKYG-----------NRGHN 232
Cdd:cd01741 46 DYDGLVILGGPMS-VDEDDYpwLKKLKELIRQalaAGKPVLGICLGHQLLARALGGKVGRNPKGweigwfpvtltEAGKA 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34398211 233 LPcVHHGTGRCFMTSQNHGfavD-VTTLPSEWEPLFTNANDHtNEGIVhKSKPYFSVQFHPEH 294
Cdd:cd01741 125 DP-LFAGLPDEFPVFHWHG---DtVVELPPGAVLLASSEACP-NQAFR-YGDRALGLQFHPEE 181
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
1012-1156 |
9.50e-11 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 61.89 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1012 GILQPRWKELTNLKSAIDFCEEVGYPCLV---RPSYvlSGAAMNVAYSNQDLETYLNAAslvsKEHPVVISKFLQEAKEI 1088
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEEL----GDGPVIVEEFVPFDREL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34398211 1089 DVDAV-AADGEILCMAVSEHVEnagvHSGDATLVTPPQDINAETLEKIKGIVRDLAALLDVTGPFNMQL 1156
Cdd:pfam02222 78 SVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
170-293 |
2.60e-10 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 61.29 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 170 FDGLFISNGPGDPVVCEQLVTQIQNFMKKKNtpIFGICLGHQLLstaigCKTFkmkyGNRGHNLPCVHHGTGRCFMTSQN 249
Cdd:PRK06895 44 FSHILISPGPDVPRAYPQLFAMLERYHQHKS--ILGVCLGHQTL-----CEFF----GGELYNLNNVRHGQQRPLKVRSN 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34398211 250 ----------------HGFAVDVTTLPsewEPLFTNANDHTN--EGIVHKSKPYFSVQFHPE 293
Cdd:PRK06895 113 splfdglpeefniglyHSWAVSEENFP---TPLEITAVCDENvvMAMQHKTLPIYGVQFHPE 171
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
458-739 |
2.67e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 64.28 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 458 PIQSIIETEDRKIFADR-VGEIGEKVAP--SEAVYSVAEALQAAEVLGYPVMARAAFSLGGLGSGFASNQEELkilaKQA 534
Cdd:PRK06111 105 PSADIIAKMGSKIEARRaMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEL----TKA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 535 LAhSNQ-----------LIIDKSLRGWKEVEYEVVRDAFDNCitvcnmenldplgIHTGE---SI------VV--APSQT 592
Cdd:PRK06111 181 FE-SNKkraanffgngeMYIEKYIEDPRHIEIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 593 LSNCEYNMLRTTALKVIRHFGVVGECNIQYaLNPESEEFFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP--- 669
Cdd:PRK06111 247 LDEETRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSftq 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 670 -DIKnsVTGVTTAC---------FEPSLDycvvKIPRWDLSK--FVRVSKNIGSSMK-------SVGEVMAIGRNFEEAF 730
Cdd:PRK06111 326 dDIK--RSGHAIEVriyaedpktFFPSPG----KITDLTLPGgeGVRHDHAVENGVTvtpfydpMIAKLIAHGETREEAI 399
|
....*....
gi 34398211 731 QKALRMVDE 739
Cdd:PRK06111 400 SRLHDALEE 408
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
144-304 |
2.96e-10 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 61.09 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 144 NQIRCFVSRGARVeLVPWNYDFSSIDFDGL-----FISNGPGDPVVCEQLVTQIQNFMKKknTPIFGICLGHQLLSTAIG 218
Cdd:PRK08007 14 NLYQYFCELGADV-LVKRNDALTLADIDALkpqkiVISPGPCTPDEAGISLDVIRHYAGR--LPILGVCLGHQAMAQAFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 219 CKTFKMKYGNRGHNLPCVHHGTG------RCFMTSQNHGFAVDVTTLPSEWEplfTNANDHTNE--GIVHKSKPYFSVQF 290
Cdd:PRK08007 91 GKVVRAAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGVQF 167
|
170
....*....|....
gi 34398211 291 HPEHTAGPEDLELL 304
Cdd:PRK08007 168 HPESILSEQGHQLL 181
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
342-707 |
3.74e-10 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 63.41 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 342 MKEKPRKVLILGS--GGLSIgqagefdysgsqaIKALKEEKIQTILINPN-IATVQTSKgLADKVYFLPLT-------LD 411
Cdd:COG3919 1 AMTMRFRVVVLGGdiNALAV-------------ARSLGEAGVRVIVVDRDpLGPAARSR-YVDEVVVVPDPgddpeafVD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 412 YVEQVIKAERPnGVLLAFGgqtalNCGIDL--ERAGVFSKYnVKILGTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVY 489
Cdd:COG3919 67 ALLELAERHGP-DVLIPTG-----DEYVELlsRHRDELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 490 SVAEALQAAEVLGYPVMARAA--------FSLGGLGSGFASNQEELKILAKQALAHSNQLIIDkslrgwkeveyEVVrDA 561
Cdd:COG3919 140 SADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAGYELIVQ-----------EYI-PG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 562 FDNCITVCNM---ENLDPLGIHTGESIVVAPSQ----TLSNCEYNM-LRTTALKVIRHFGVVGECNIQYALNPESEEFFI 633
Cdd:COG3919 208 DDGEMRGLTAyvdRDGEVVATFTGRKLRHYPPAggnsAARESVDDPeLEEAARRLLEALGYHGFANVEFKRDPRDGEYKL 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34398211 634 IEVNARLSRSSALASKAtGYPLAYVAAKLALGIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRW--DLSKFVRVSK 707
Cdd:COG3919 288 IEINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREGVLWRVLPGDLLLRYLRDGELrkRLRELLRRGK 362
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
161-354 |
2.11e-09 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 62.17 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 161 WNYDFSSIDFDGLFISNGPGDPVVCEQLVTQIQNFMKKKNTPIFGICLGHQLLSTAIGCKTFKMKYGNRGHNLPCVHHG- 239
Cdd:PLN02889 123 YHYLYEEKAFDNIVISPGPGSPTCPADIGICLRLLLECRDIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGc 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 240 -------TGR--CFMTSQNHGFAVDVTTLPSEWEPL-FTNAND------------------------------------- 272
Cdd:PLN02889 203 rlfddipSGRnsGFKVVRYHSLVIDAESLPKELVPIaWTSSSDtlsflesqksglvpdayesqigqsgssdpfssklkng 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 273 ------HTNE--------GIVHKSKPYFSVQFHPEHTAGPEDLElLFDVFLDTVKEYQNGTIPKSINENLNNRLS--YKP 336
Cdd:PLN02889 283 tswpssHSERmqngkilmGIMHSTRPHYGLQFHPESIATCYGRQ-IFKNFREITQDYWLRLRSTSLRRRNSNLTAnmQVP 361
|
250
....*....|....*...
gi 34398211 337 KPELIMKEKPRKVLILGS 354
Cdd:PLN02889 362 DASQLFKVPRRGQLGNGE 379
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
171-313 |
3.02e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 58.28 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 171 DGLFISNGPGDPVVCEQLVTQIQNFMKKknTPIFGICLGHQLLSTAIGCKTFKM------KYGNRGHNLPCVHHGTGRCF 244
Cdd:PRK07649 45 DFLMISPGPCSPNEAGISMEVIRYFAGK--IPIFGVCLGHQSIAQVFGGEVVRAerlmhgKTSLMHHDGKTIFSDIPNPF 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34398211 245 MTSQNHGFAVDVTTLPSEWEplftnANDHTNEG----IVHKSKPYFSVQFHPEHTAGPEDLELLFDvFLDTVK 313
Cdd:PRK07649 123 TATRYHSLIVKKETLPDCLE-----VTSWTEEGeimaIRHKTLPIEGVQFHPESIMTSHGKELLQN-FIRKYS 189
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
149-304 |
4.40e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 57.58 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 149 FVSRGARVELVPWNydfsSIDFDG--------LFISNGPGDPVVCEQLVTQIQNFMKKknTPIFGICLGHQLLSTAIGCK 220
Cdd:PRK08857 19 FCELGAQVKVVRND----EIDIDGiealnpthLVISPGPCTPNEAGISLQAIEHFAGK--LPILGVCLGHQAIAQVFGGQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 221 TFKMKYGNRGHNLPCVHhgTGRCFMTSQN--------HGFAVDVTTLPSEWE-PLFTNANDHTNE---GIVHKSKPYFSV 288
Cdd:PRK08857 93 VVRARQVMHGKTSPIRH--TGRSVFKGLNnpltvtryHSLVVKNDTLPECFElTAWTELEDGSMDeimGFQHKTLPIEAV 170
|
170
....*....|....*.
gi 34398211 289 QFHPEHTAGPEDLELL 304
Cdd:PRK08857 171 QFHPESIKTEQGHQLL 186
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
487-669 |
7.86e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 59.77 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 487 AVYSVAEALQAAEVLGYPVMARAAFSLGGLGSGFASNQEELKI---LAK---QALAHSNQLIIDKSLRGWKEVEYEVVRD 560
Cdd:PRK12833 140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpLAQreaQAAFGDGGVYLERFIARARHIEVQILGD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 561 AFDnciTVCNMENLDPLGIHTGESIVVAPSQTLSNCEYNMLRTTALKVIRHFGVVGECNIQYALNPESEEFFIIEVNARL 640
Cdd:PRK12833 220 GER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRI 296
|
170 180
....*....|....*....|....*....
gi 34398211 641 SRSSALASKATGYPLAYVAAKLALGIPLP 669
Cdd:PRK12833 297 QVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
146-213 |
1.74e-08 |
|
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: 53.76 E-value: 1.74e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34398211 146 IRCFVSRGARVELVPWN-----YDFSSIDFDGLFISNGPGDP---VVCEQLVTQIQNFMKKkNTPIFGICLGHQLL 213
Cdd:cd01653 18 LDALREAGAEVDVVSPDggpveSDVDLDDYDGLILPGGPGTPddlARDEALLALLREAAAA-GKPILGICLGAQLL 92
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
164-293 |
1.77e-08 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 55.89 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 164 DFSSID---FDGLFISNGPGDPV---VCEQLVTQIQNFmkkknTPIFGICLGHQLLSTAIGCKTFKMKYGNRG------H 231
Cdd:CHL00101 35 DLSKIKnlnIRHIIISPGPGHPRdsgISLDVISSYAPY-----IPILGVCLGHQSIGYLFGGKIIKAPKPMHGktskiyH 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34398211 232 NLPCVHHGTGRCFMTSQNHGFAVDVTTLPSewePLFTNAndHTNEGIV----HKSKPY-FSVQFHPE 293
Cdd:CHL00101 110 NHDDLFQGLPNPFTATRYHSLIIDPLNLPS---PLEITA--WTEDGLImacrHKKYKMlRGIQFHPE 171
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
448-739 |
1.98e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 58.22 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 448 SKYNVKILGTPIQSIIETEDRKIFADRVGEIGEKVAP-SE-AVYSVAEALQAAEVLGYPVMARAAFSLGGLGSGFASNQE 525
Cdd:PRK08462 98 SHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDES 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 526 ELK--ILAKQALAHS----NQLIIDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGESIVVAPSQTLSN 595
Cdd:PRK08462 178 DLEnlYLAAESEALSafgdGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVLDE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 596 CEYNMLRTTALKVIRHFGVVGECNIQYALNpESEEFFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPD----- 670
Cdd:PRK08462 252 KTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSqesik 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 671 -----IKNSVTGVTTACFEPsldyCVVKIPRWDL--SKFVRVSKNIGS---------SMksVGEVMAIGRNFEEAFQKAL 734
Cdd:PRK08462 331 lkghaIECRITAEDPKKFYP----SPGKITKWIApgGRNVRMDSHAYAgyvvppyydSM--IGKLIVWGEDRNRAIAKMK 404
|
....*
gi 34398211 735 RMVDE 739
Cdd:PRK08462 405 RALKE 409
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
146-213 |
5.87e-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: 51.43 E-value: 5.87e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34398211 146 IRCFVSRGARVELVPWN-----YDFSSIDFDGLFISNGPGDP---VVCEQLVTQIQNFMKKkNTPIFGICLGHQLL 213
Cdd:cd03128 18 LDALREAGAEVDVVSPDggpveSDVDLDDYDGLILPGGPGTPddlAWDEALLALLREAAAA-GKPVLGICLGAQLL 92
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1266-1298 |
3.63e-07 |
|
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: 49.99 E-value: 3.63e-07
10 20 30
....*....|....*....|....*....|...
gi 34398211 1266 KAILLSIGSFKhKVELLPSIRDLAKMGYKLYAS 1298
Cdd:cd01423 1 KGILISIGSYS-KPELLPTAQKLSKLGYKLYAT 32
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
442-669 |
6.02e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 53.57 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 442 ERAGVFSKYNVKILGtPIQSIIETEDRKIFADR-VGEIGEKVAP-SEA-VYSVAEALQAAEVLGYPVMARAAFSLGGLGS 518
Cdd:PRK07178 89 ELAEICAERGIKFIG-PSAEVIRRMGDKTEARRaMIKAGVPVTPgSEGnLADLDEALAEAERIGYPVMLKATSGGGGRGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 519 GFASNQEELK-------ILAKQALAhSNQLIIDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGESIVV 587
Cdd:PRK07178 168 RRCNSREELEqnfprviSEATKAFG-SAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 588 APSQTLSNCEYNMLRTTALKVIRHFGVVGECNIQYALNPESeEFFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIP 667
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADG-EVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
..
gi 34398211 668 LP 669
Cdd:PRK07178 320 LS 321
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
348-671 |
1.02e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 52.19 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 348 KVLILGSGGlsigqagefdysGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTLD--YVEQVI---KAERP 422
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPKVTDpnYIDRLLdicKKEKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 423 NGVLLafggqtalncGIDLE------RAGVFSKYNVKILGTPiQSIIET-EDRKIFADRVGEIGEKVAPSEAVYSVAEAL 495
Cdd:PRK12767 71 DLLIP----------LIDPElpllaqNRDRFEEIGVKVLVSS-KEVIEIcNDKWLTYEFLKENGIPTPKSYLPESLEDFK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 496 QA--AEVLGYPVMARAAFSLGGLGSGFASNQEELKilakQALAHSNQLIIDKSLRGwKEVEYEVVRDAFDNCITVCNMEN 573
Cdd:PRK12767 140 AAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 574 LDPLGihtGESivvapSQTLSnCEYNMLRTTALKVIRHFGVVGECNIQYALNPEseEFFIIEVNARLSrssalaskaTGY 653
Cdd:PRK12767 215 IEVRA---GET-----SKGVT-VKDPELFKLAERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFG---------GGY 274
|
330 340
....*....|....*....|....*..
gi 34398211 654 PLAYVA---------AKLALGIPLPDI 671
Cdd:PRK12767 275 PLSYMAganepdwiiRNLLGGENEPII 301
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
153-293 |
1.47e-06 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 52.61 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 153 GARVELVPWNYD---FSSIDFDGLFISNGPGDPV--VCEQLVTQIqnfmKKKNTPIFGICLGHQLLSTAIGcktfkmkyG 227
Cdd:PRK13566 550 GAEVTTVRYGFAeemLDRVNPDLVVLSPGPGRPSdfDCKATIDAA----LARNLPIFGVCLGLQAIVEAFG--------G 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 228 NRGH-NLPC--------VHHGT------GRCFMTSQNHGFAVDVTTLPSEWEPLFTnandhTNEGIV----HKSKPYFSV 288
Cdd:PRK13566 618 ELGQlAYPMhgkpsrirVRGPGrlfsglPEEFTVGRYHSLFADPETLPDELLVTAE-----TEDGVImaieHKTLPVAAV 692
|
....*
gi 34398211 289 QFHPE 293
Cdd:PRK13566 693 QFHPE 697
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
172-293 |
1.86e-06 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 50.57 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 172 GLFISNGPGDPV---VCEQLVTQIQNFmkkknTPIFGICLGHQLLSTAIGCKTFKMKYG-NRGHNLPCVH---------H 238
Cdd:PLN02335 65 GVLISPGPGTPQdsgISLQTVLELGPL-----VPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYdekgeeglfS 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 34398211 239 GTGRCFMTSQNHGFAVDVTTLPSEWEPLFTNANDHTNEGIVHKSKPYFS-VQFHPE 293
Cdd:PLN02335 140 GLPNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPE 195
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
198-293 |
2.74e-06 |
|
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: 49.95 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 198 KKNTPIFGICLGHQLLSTAIGCKTF---KMKYGNRGHNLPC----------VHHGTGRCF--MTSQN-------HGFAVD 255
Cdd:pfam07722 103 ARGKPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshaVNVEPGSLLasLLGSEefrvnslHHQAID 182
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 34398211 256 vtTLPSEWEPLFTnANDHTNEGIVHKSKPYF--SVQFHPE 293
Cdd:pfam07722 183 --RLAPGLRVEAV-APDGTIEAIESPNAKGFalGVQWHPE 219
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
449-572 |
3.59e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 51.14 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 449 KYNVKILGtPIQSIIETEDRKIFADRV-GEIGEKVAP--SEAVYSVAEALQAAEVLGYPVMARAAFSLGGLGSGFASNQE 525
Cdd:PRK08654 97 KAGIVFIG-PSSDVIEAMGSKINAKKLmKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEE 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 34398211 526 ELK--ILAKQALAHSN----QLIIDKSLRGWKEVEYEVVRDAFDNCITVCNME 572
Cdd:PRK08654 176 ELEdaIESTQSIAQSAfgdsTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRE 228
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
444-739 |
4.43e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 50.87 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 444 AGVFSKYNVKILGtPIQSIIETEDRKIFADRV-GEIGEKVAP-SE-AVYSVAEALQAAEVLGYPVMARAAFSLGGLGSGF 520
Cdd:PRK05586 92 AKMCKECNIVFIG-PDSETIELMGNKSNAREImIKAGVPVVPgSEgEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 521 ASNQEEL-------KILAKQALAhSNQLIIDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGESIVVAP 589
Cdd:PRK05586 171 VRSEEELikafntaKSEAKAAFG-DDSMYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQKVLEEAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 590 SQTLSNCEYNMLRTTALKVIRHFGVVGECNIQYALNpESEEFFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPL- 668
Cdd:PRK05586 244 SPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLs 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 669 ---PDIKnsVTGVTTAC----------FEPS----------------LD---YCVVKIPR-WDlskfvrvsknigsSMks 715
Cdd:PRK05586 323 ikqEDIK--INGHSIECrinaedpkngFMPCpgkieelyipgglgvrVDsavYSGYTIPPyYD-------------SM-- 385
|
330 340
....*....|....*....|....
gi 34398211 716 VGEVMAIGRNFEEAFQKALRMVDE 739
Cdd:PRK05586 386 IGKLIVYGKDREEAIQKMKRALGE 409
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
198-308 |
6.30e-06 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 48.34 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 198 KKNTPIFGICLGHQLLSTAIGcktfkmkygnrghnlpcvhhGT-GRCFMTSQNHGFAVDvtTLPSEWEPLFTnANDHTNE 276
Cdd:cd01745 98 ERGKPILGICRGMQLLNVALG--------------------GTlYQDIRVNSLHHQAIK--RLADGLRVEAR-APDGVIE 154
|
90 100 110
....*....|....*....|....*....|....
gi 34398211 277 GIVHKSKPY-FSVQFHPEHTAGPEDLEL-LFDVF 308
Cdd:cd01745 155 AIESPDRPFvLGVQWHPEWLADTDPDSLkLFEAF 188
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
991-1150 |
2.92e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 47.76 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 991 SPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPS---------YVLSGAAmnvaysnqDLE 1061
Cdd:COG0026 80 GPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggydgkgqVVIKSAA--------DLE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1062 TYLNAAslvsKEHPVVISKFLQEAKEIDVDAV-AADGEILCMAVsehVENagVH-SGDATLVTPPQDINAETLEKIKGIV 1139
Cdd:COG0026 152 AAWAAL----GGGPCILEEFVPFERELSVIVArSPDGEVATYPV---VEN--VHrNGILDESIAPARISEALAAEAEEIA 222
|
170
....*....|.
gi 34398211 1140 RDLAALLDVTG 1150
Cdd:COG0026 223 KRIAEALDYVG 233
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1011-1150 |
6.06e-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: 45.39 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 1011 KGILQPRWKELTNLKSAiDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAslVSKEHPVVISKFLqEAKEIDV 1090
Cdd:pfam07478 13 VTFTRADWKLNPKEWCA-QVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEA--FQYDEKVLVEEGI-EGREIEC 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34398211 1091 dAVAADGEILCMAVSEHVENAGV------HSGDATLVTPPQDINAETLEKIKGIVRDLAALLDVTG 1150
Cdd:pfam07478 89 -AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRG 153
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
487-640 |
1.10e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 46.33 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 487 AVYSVAEALQAAEVLGYPVMARAAFSLGGLGSGFASNQEELKILAKQA-----LAHSN-QLIIDKSLRGWKEVEYEVVRD 560
Cdd:PRK08591 137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMAraeakAAFGNpGVYMEKYLENPRHIEIQVLAD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 561 AFDNcitvcnmenldplGIHTGE---SI------VV--APSQTLSNCEYNMLRTTALKVIRHFGVVGECNIQYaLNPESE 629
Cdd:PRK08591 217 GHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKNG 282
|
170
....*....|.
gi 34398211 630 EFFIIEVNARL 640
Cdd:PRK08591 283 EFYFIEMNTRI 293
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
988-1094 |
3.49e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 44.59 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 988 LGTSPESIDSAENRFKFSRMLDRKG--ILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLN 1065
Cdd:PRK08654 103 IGPSSDVIEAMGSKINAKKLMKKAGvpVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIE 182
|
90 100 110
....*....|....*....|....*....|...
gi 34398211 1066 AASLVSK----EHPVVISKFLQEAKEIDVDAVA 1094
Cdd:PRK08654 183 STQSIAQsafgDSTVFIEKYLEKPRHIEIQILA 215
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
456-745 |
4.50e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 44.84 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 456 GTPIQSIIETEDRKIFADRVGEIGEKVAPSEAVYSVAEALQAAEVLGYPVMARAAFSLGGLGSGF-ASNQEELKILAKQA 534
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLcASVAEAAAHCAALR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 535 LAHSNQLIIDKSLRGwKEVEYEVVRDAFDNCITVCNMENLDPLGiHTGESIVVAPSQTLSNCEYNMLRTtalkVIRHFGV 614
Cdd:PRK02186 176 RAGTRAALVQAYVEG-DEYSVETLTVARGHQVLGITRKHLGPPP-HFVEIGHDFPAPLSAPQRERIVRT----VLRALDA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 615 VGecniqYALNPESEEF-------FIIEVNARLSRS--SALASKATGYPLAYVAAKLALGIP----------------LP 669
Cdd:PRK02186 250 VG-----YAFGPAHTELrvrgdtvVIIEINPRLAGGmiPVLLEEAFGVDLLDHVIDLHLGVAafadptakrygairfvLP 324
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34398211 670 DIKNSVTGVTtacFEPSLDYCVVKIPRWDLSKFVRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVTGFD 745
Cdd:PRK02186 325 ARSGVLRGLL---FLPDDIAARPELRFHPLKQPGDALRLEGDFRDRIAAVVCAGDHRDSVAAAAERAVAGLSIDIG 397
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
605-679 |
5.31e-04 |
|
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: 41.44 E-value: 5.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34398211 605 ALKVIRHFGVVGECNIQYALNpeSEEFFIIEVNARLsrSSALA-SKATGYPLAYVAAKLALGIPLPDIKNSVTGVT 679
Cdd:pfam15632 53 ARRLAEAFGLDGLFNVQFRYD--GDGPKLLEINPRM--SGGIGySCLAGVNLPYLALKLLLGLETPDPVEPRLGLR 124
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
991-1100 |
5.81e-04 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 43.49 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34398211 991 SPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLV 1070
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQL 158
|
90 100 110
....*....|....*....|....*....|.
gi 34398211 1071 SKEHPV-VISKFLQEAKEIDVDAVAADGEIL 1100
Cdd:TIGR00768 159 NGPQNLfLVQEYIKKPGGRDIRVFVVGDEVV 189
|
|
| |
