|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
346-1295 |
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: 1531.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 346 ERPRKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPN 425
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 426 GVLLTFGGQTALNCGVELEKSGIFAKYNVRIMGTPIQSIIETEDRKIFADRVAEIGEKVAPSEAVYSVKEALQAAEKLGY 505
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 506 PVMARAAFSLGGLGSGFANNETELQVLAQQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHT 583
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 584 GESIVVAPSQTLSNNEYNMLRTTAIKVIRHFGVVGECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAK 663
Cdd:TIGR01369 244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 664 LSLAIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFTKVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENV 743
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 744 NGFDPYIKPVKDGE-----LIQATDKRIFVLAAAIKENYTIERLYQLTNIDPWFLNKMKNIIDYLNVLEKHGNN-LDRNM 817
Cdd:TIGR01369 404 TGFDLPDREVEPDEdlwraLKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTdLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 818 ILEAKKLGFSDKQIAAAIKSTDLMVRKQREEMKVVPFVKQIDTVAGEWPATTNYLYLTYNADCHDLDFSGNFTIVV-GSG 896
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 897 VYRIGSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVDGIILSMGGQLPN 976
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 977 NIAMDLHRQKANVLGTSPECIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVA 1056
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1057 YSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVAADGEILCMAVSEHVENAGVHSGDATLVTPPQDINAETLEK 1136
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1137 IKEITRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMHVEPVEVL--HGCGKV 1214
Cdd:TIGR01369 804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEPKYV 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1215 GVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKRAILLSIGSFKHKVELLPSIRDLAKMG 1294
Cdd:TIGR01369 884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963
|
.
gi 86450145 1295 Y 1295
Cdd:TIGR01369 964 Y 964
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
349-1295 |
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 86450145 349 RKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVL 428
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 429 LTFGGQTALNCGVELEKSGIFAKYNVRIMGTPIQSIIETEDRKIFADRVAEIGEKVAPSEAVYSVKEALQAAEKLGYPVM 508
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 509 ARAAFSLGGLGSGFANNETELQVLAQQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGES 586
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 587 IVVAPSQTLSNNEYNMLRTTAIKVIRHFGVV-GECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 665
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 666 LAIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFTKVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNG 745
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 746 FDPYIKPVKDGE-----LIQATDKRIFVLAAAIKENYTIERLYQLTNIDPWFLNKMKNIIDYLNVLEKHGNNLDRNMILE 820
Cdd:PRK05294 408 LDEDLFEEESLEelreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLRE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 821 AKKLGFSDKQIAAAIKSTDLMVRKQREEMKVVPFVKQIDTVAGEWPATTNYLYLTYNADCHDLDFSGNFTIVVGSGVYRI 900
Cdd:PRK05294 488 AKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNRI 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 901 GSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVDGIILSMGGQLPNNIAM 980
Cdd:PRK05294 568 GQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLAK 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 981 DLHRQKANVLGTSPECIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQ 1060
Cdd:PRK05294 648 ALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEE 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1061 DLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDINAETLEKIKE 1139
Cdd:PRK05294 728 ELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEdVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIRE 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1140 ITRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMHVEPVEVLHGC--GKVGVK 1217
Cdd:PRK05294 807 YTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPYVAVK 886
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450145 1218 VPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKR-AILLSIGSfKHKVELLPSIRDLAKMGY 1295
Cdd:PRK05294 887 EAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSVRD-RDKEEVVELAKRLLELGF 964
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
354-895 |
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: 651.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 354 LGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVLLTFGG 433
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 434 QTALNCGVELEKSGIFAkyNVRIMGTPIQSIIETEDRKIFADRVAEIGEKVAPSEAVYSVKEALQAAEKLGYPVMARAAF 513
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 514 SLGGLGSGFANNETELQVLAQQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGESIVVAP 591
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 592 SQTLSNNEYNMLRTTAIKVIRHFGVVGECNIQYALNpeSEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLAIPLP 671
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 672 DIKNSvTGvttacFEPSLDYCVVKIPRWDLAKFTKVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNGfDPYIK 751
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPG-TVLLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 752 PVKDGE-----LIQATDKRIFVLAAAIKENYTIERLYQLTNIDPWFLNKMKNIIdyLNVLEKHGNNLDRNMILEAKKLGF 826
Cdd:COG0458 390 LVADDDkeealLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPII--VDEIELEEIILVINTLLGAKSLGD 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450145 827 SDKQIAAAIKSTDLMVRKQREEMKVVPFVKQIDTVAGEWPATTNYLYLTYNADCHDLDFSGNFTIVVGS 895
Cdd:COG0458 468 SDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-315 |
1.24e-127 |
|
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: 397.38 E-value: 1.24e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIPsqkeiddfgmPKHFEwTKGITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:TIGR01368 47 QIVVFTYPLIGNYGVN----------DEDAE-SKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 81 KKIRENGSILGRITYEIPSDLQISNLKLVDPNLR--NLVAECSVSTVQTFNM--NGSPRICAIDCGLKLNQIRCFVRRGV 156
Cdd:TIGR01368 116 KKIREKGTMKGVISTEDSNDEELVEKARVSPDITgiNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 157 RVDLVPWNH---ELNKKEFDGLFISNGPGDPVMCETTVKQISKIMQEseIPIFGICLGHQLLATAIGCKTYKMKYGNRGH 233
Cdd:TIGR01368 196 EVTVVPYDTdaeEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLEK--IPIFGICLGHQLLALAFGAKTYKMKFGHRGG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 234 NLPCLHHGTGRCFMTSQNHGFAVDANTLP-DDWESLFTNVNDHSNEGIIHKQKPYFSVQFHPEHTAGPEDLEMLFDVFVD 312
Cdd:TIGR01368 274 NHPVKDLITGRVEITSQNHGYAVDPDSLPaGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFID 353
|
...
gi 86450145 313 EVK 315
Cdd:TIGR01368 354 LMK 356
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-312 |
7.77e-127 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 395.21 E-value: 7.77e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIPSqkeiDDFgmpkhfEwTKGITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:PRK12564 51 QIVTFTYPLIGNYGVNR----EDF------E-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 81 KKIRENGSILGRITYEiPSDLQisnlKLVD-----PNL--RNLVAEcsVSTVQTFNMNGSP-----RICAIDCGLKLNQI 148
Cdd:PRK12564 120 RKLREKGAMKGVIATE-DFDAE----ELLEkarafPGLlgLDLVKE--VSTKEPYPWPGPGgelkyKVVAIDFGVKRNIL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 149 RCFVRRGVRVDLVPWN---HELNKKEFDGLFISNGPGDPVMCETTVKQISKIMqESEIPIFGICLGHQLLATAIGCKTYK 225
Cdd:PRK12564 193 RELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAALDYAIEMIRELL-EKKIPIFGICLGHQLLALALGAKTYK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 226 MKYGNRGHNLPCLHHGTGRCFMTSQNHGFAVDANTLPDDWESLFTNVNDHSNEGIIHKQKPYFSVQFHPEHTAGPEDLEM 305
Cdd:PRK12564 272 MKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAY 351
|
....*..
gi 86450145 306 LFDVFVD 312
Cdd:PRK12564 352 LFDEFVE 358
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-315 |
5.59e-123 |
|
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: 385.14 E-value: 5.59e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIPSqkeiDDFgmpkhfEwTKGITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:COG0505 51 QIVTFTYPHIGNYGVND----EDF------E-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 81 KKIRENGSILGRITYEipsDLQISNLK-----LVDPNLRNLVAEcsVSTVQTFNMNGSP----RICAIDCGLKLNQIRCF 151
Cdd:COG0505 120 RHLREKGAMKGVISTG---DLDIEELLekaraAPGMEGLDLVKE--VSTKEPYEWTEAPgagfHVVALDFGVKRNILREL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 152 VRRGVRVDLVPWN---HELNKKEFDGLFISNGPGDPVMCETTVKQISKIMqESEIPIFGICLGHQLLATAIGCKTYKMKY 228
Cdd:COG0505 195 AERGCRVTVVPATtsaEEILALNPDGVFLSNGPGDPAALDYAIETIRELL-GKGIPIFGICLGHQLLALALGAKTYKLKF 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 229 GNRGHNLPCLHHGTGRCFMTSQNHGFAVDANTLPD-DWESLFTNVNDHSNEGIIHKQKPYFSVQFHPEHTAGPEDLEMLF 307
Cdd:COG0505 274 GHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLF 353
|
....*...
gi 86450145 308 DVFVDEVK 315
Cdd:COG0505 354 DRFIELME 361
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
136-311 |
6.78e-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: 304.42 E-value: 6.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 136 ICAIDCGLKLNQIRCFVRRGVRVDLVPWNH---ELNKKEFDGLFISNGPGDPVMCETTVKQISKIMqESEIPIFGICLGH 212
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTdaeEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLL-GKKIPIFGICLGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 213 QLLATAIGCKTYKMKYGNRGHNLPCLHHGTGRCFMTSQNHGFAVDANTLPDDWESLFTNVNDHSNEGIIHKQKPYFSVQF 292
Cdd:cd01744 80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159
|
170
....*....|....*....
gi 86450145 293 HPEHTAGPEDLEMLFDVFV 311
Cdd:cd01744 160 HPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
469-671 |
2.26e-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: 2.26e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 469 DRKIFADRVAEIGEKVAPSEAVY--SVKEALQAAEKLGYPVMARAAFSLGGLGSGFANNETELQVLAQQALAHS------ 540
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 541 NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLgiHTGESIVVAPSQTLSNNEYNMLRTTAIKVIRHFGVVGEC 620
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 86450145 621 NIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLAIPLP 671
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
139-312 |
2.90e-61 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 207.48 E-value: 2.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 139 IDCGL--KLNQIRCFVRRGVRVDLVPWNH---ELNKKEFDGLFISNGPGDPVMCETTVKQISKIMqESEIPIFGICLGHQ 213
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREAR-ELKIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 214 LLATAIGCKTYKMK-YGNRGHNLPCLH------HGTGRCFMTSQNHGFAVDANTLPDDWESLFTNVNDHSNEGIIHKQKP 286
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*.
gi 86450145 287 YFSVQFHPEHTAGPEDLEMLFDVFVD 312
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
757-876 |
3.08e-51 |
|
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: 176.10 E-value: 3.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 757 ELIQATDKRIFVLAAAIKENYTIERLYQLTNIDPWFLNKMKNIIDYLNVLEKHG-NNLDRNMILEAKKLGFSDKQIAAAI 835
Cdd:smart01096 4 ELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGlDELDADLLRKAKRLGFSDRQIAKLL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 86450145 836 KSTDLMVRKQREEMKVVPFVKQIDTVAGEWPATTNYLYLTY 876
Cdd:smart01096 84 GVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
2.26e-35 |
|
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: 130.96 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIPSQKeiddfgmpkhFEWTKgITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:smart01097 49 QIVVFTYPLIGNYGVNDED----------FESDK-IQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALT 117
|
90
....*....|...
gi 86450145 81 KKIRENGSILGRI 93
Cdd:smart01097 118 RKLREKGAMKGVI 130
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1268-1295 |
3.72e-03 |
|
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: 38.43 E-value: 3.72e-03
10 20
....*....|....*....|....*...
gi 86450145 1268 RAILLSIGSFKhKVELLPSIRDLAKMGY 1295
Cdd:cd01423 1 KGILISIGSYS-KPELLPTAQKLSKLGY 27
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
346-1295 |
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: 1531.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 346 ERPRKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPN 425
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 426 GVLLTFGGQTALNCGVELEKSGIFAKYNVRIMGTPIQSIIETEDRKIFADRVAEIGEKVAPSEAVYSVKEALQAAEKLGY 505
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 506 PVMARAAFSLGGLGSGFANNETELQVLAQQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHT 583
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 584 GESIVVAPSQTLSNNEYNMLRTTAIKVIRHFGVVGECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAK 663
Cdd:TIGR01369 244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 664 LSLAIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFTKVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENV 743
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 744 NGFDPYIKPVKDGE-----LIQATDKRIFVLAAAIKENYTIERLYQLTNIDPWFLNKMKNIIDYLNVLEKHGNN-LDRNM 817
Cdd:TIGR01369 404 TGFDLPDREVEPDEdlwraLKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTdLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 818 ILEAKKLGFSDKQIAAAIKSTDLMVRKQREEMKVVPFVKQIDTVAGEWPATTNYLYLTYNADCHDLDFSGNFTIVV-GSG 896
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 897 VYRIGSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVDGIILSMGGQLPN 976
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 977 NIAMDLHRQKANVLGTSPECIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVA 1056
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1057 YSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVAADGEILCMAVSEHVENAGVHSGDATLVTPPQDINAETLEK 1136
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1137 IKEITRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMHVEPVEVL--HGCGKV 1214
Cdd:TIGR01369 804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEPKYV 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1215 GVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKRAILLSIGSFKHKVELLPSIRDLAKMG 1294
Cdd:TIGR01369 884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963
|
.
gi 86450145 1295 Y 1295
Cdd:TIGR01369 964 Y 964
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
349-1295 |
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 86450145 349 RKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVL 428
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 429 LTFGGQTALNCGVELEKSGIFAKYNVRIMGTPIQSIIETEDRKIFADRVAEIGEKVAPSEAVYSVKEALQAAEKLGYPVM 508
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 509 ARAAFSLGGLGSGFANNETELQVLAQQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGES 586
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 587 IVVAPSQTLSNNEYNMLRTTAIKVIRHFGVV-GECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 665
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 666 LAIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFTKVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNG 745
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 746 FDPYIKPVKDGE-----LIQATDKRIFVLAAAIKENYTIERLYQLTNIDPWFLNKMKNIIDYLNVLEKHGNNLDRNMILE 820
Cdd:PRK05294 408 LDEDLFEEESLEelreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLRE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 821 AKKLGFSDKQIAAAIKSTDLMVRKQREEMKVVPFVKQIDTVAGEWPATTNYLYLTYNADCHDLDFSGNFTIVVGSGVYRI 900
Cdd:PRK05294 488 AKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNRI 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 901 GSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVDGIILSMGGQLPNNIAM 980
Cdd:PRK05294 568 GQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLAK 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 981 DLHRQKANVLGTSPECIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQ 1060
Cdd:PRK05294 648 ALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEE 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1061 DLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDINAETLEKIKE 1139
Cdd:PRK05294 728 ELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEdVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIRE 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1140 ITRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMHVEPVEVLHGC--GKVGVK 1217
Cdd:PRK05294 807 YTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPYVAVK 886
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450145 1218 VPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKR-AILLSIGSfKHKVELLPSIRDLAKMGY 1295
Cdd:PRK05294 887 EAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSVRD-RDKEEVVELAKRLLELGF 964
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
349-1295 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1026.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 349 RKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVL 428
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 429 LTFGGQTALNCGVELEKSGIFAKYNVRIMGTPIQSIIETEDRKIFADRVAEIGEKVAPSEAVYSVKEALQAAEKLGYPVM 508
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 509 ARAAFSLGGLGSGFANNETELQVLAQQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGES 586
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQASpiHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 587 IVVAPSQTLSNNEYNMLRTTAIKVIRHFGVVGECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLSL 666
Cdd:PRK12815 248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 667 AIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFTKVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNGF 746
Cdd:PRK12815 328 GYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 747 DPYIK--PVKDGELIQ----ATDKRIFVLAAAIKENYTIERLYQLTNIDPWFLNKMKNIIDYLNVLEKHGNNLDRNMILE 820
Cdd:PRK12815 408 SLPIElsGKSDEELLQdlrhPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLDLSADLLRK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 821 AKKLGFSDKQIAAAIKSTDLMVRKQREEMKVVPFVKQIDTVAGEWPATTNYLYLTYNADChDLDFSGN--FTIVVGSGVY 898
Cdd:PRK12815 488 VKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGES-EAEPSSEkkKVLILGSGPI 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 899 RIGSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVDGIILSMGGQLPNNI 978
Cdd:PRK12815 567 RIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAINL 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 979 AMDLHRQKANVLGTSPECIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYS 1058
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYD 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1059 NQDLETYLNAAslVSKEHPVVISKFLqEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDINAETLEKI 1137
Cdd:PRK12815 727 EPALEAYLAEN--ASQLYPILIDQFI-DGKEYEVDAI-SDGEdVTIPGIIEHIEQAGVHSGDSIAVLPPQSLSEEQQEKI 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1138 KEITRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMHVE----PVEVLHGCGK 1213
Cdd:PRK12815 803 RDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAelgyPNGLWPGSPF 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1214 VGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKRAILLSIGSFKHKVELLPSIRDLAKM 1293
Cdd:PRK12815 883 IHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARRFAQL 962
|
..
gi 86450145 1294 GY 1295
Cdd:PRK12815 963 GF 964
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
349-1295 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 857.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 349 RKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVL 428
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 429 LTFGGQTALNCGVELEKSGIFAKYNVRIMGTPIQSIIETEDRKIFADRVAEIGEKVAPSEAVYSVKEALQAAEKLG-YPV 507
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 508 MARAAFSLGGLGSGFANNETELQVLAQQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGE 585
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAASitSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 586 SIVVAPSQTLSNNEYNMLRTTAIKVIRHFGVvgEC---NIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAA 662
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 663 KLSLAIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFTKVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDEN 742
Cdd:PLN02735 342 KLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 743 VNGFDPyiKPVK--DGELIQATDK-------RIFVLAAAIKENYTIERLYQLTNIDPWFLNKMKNIIDYLNVLE-KHGNN 812
Cdd:PLN02735 422 FSGWGC--AKVKelDWDWEQLKYKlrvpnpdRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKsRSLSE 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 813 LDRNMILEAKKLGFSDKQIAAAIKSTDLMVRKQREEMKVVPFVKQIDTVAGEWPATTNYLYLTYNADCHDLDFSGNFTIV 892
Cdd:PLN02735 500 LSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLI 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 893 VGSGVYRIGSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVDGIILSMGG 972
Cdd:PLN02735 580 LGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGG 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 973 QLPNNIAMDLHRQ-------------KANVLGTSPECIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYP 1039
Cdd:PLN02735 660 QTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYP 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1040 CLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVA-ADGEILCMAVSEHVENAGVHSG 1118
Cdd:PLN02735 740 VVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSG 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1119 DATLVTPPQDINAETLEKIKEITRDLAALLDVTGPFNMQL-IAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAI 1197
Cdd:PLN02735 820 DSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVM 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1198 IGMHV------EPVEVLHgcgkVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKRA-I 1270
Cdd:PLN02735 900 SGKSLkdlgftEEVIPAH----VSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGtV 975
|
970 980
....*....|....*....|....*
gi 86450145 1271 LLSIGSfKHKVELLPSIRDLAKMGY 1295
Cdd:PLN02735 976 FISLND-LTKPHLVPIARGFLELGF 999
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
354-895 |
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: 651.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 354 LGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPEYVEQVIKAERPNGVLLTFGG 433
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 434 QTALNCGVELEKSGIFAkyNVRIMGTPIQSIIETEDRKIFADRVAEIGEKVAPSEAVYSVKEALQAAEKLGYPVMARAAF 513
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 514 SLGGLGSGFANNETELQVLAQQALAHS--NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGESIVVAP 591
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 592 SQTLSNNEYNMLRTTAIKVIRHFGVVGECNIQYALNpeSEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLAIPLP 671
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 672 DIKNSvTGvttacFEPSLDYCVVKIPRWDLAKFTKVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNGfDPYIK 751
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPG-TVLLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 752 PVKDGE-----LIQATDKRIFVLAAAIKENYTIERLYQLTNIDPWFLNKMKNIIdyLNVLEKHGNNLDRNMILEAKKLGF 826
Cdd:COG0458 390 LVADDDkeealLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPII--VDEIELEEIILVINTLLGAKSLGD 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450145 827 SDKQIAAAIKSTDLMVRKQREEMKVVPFVKQIDTVAGEWPATTNYLYLTYNADCHDLDFSGNFTIVVGS 895
Cdd:COG0458 468 SDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
893-1295 |
1.89e-158 |
|
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: 485.92 E-value: 1.89e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 893 VGSGVYRIGSSVEFDWCAVGCLRELRNLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVDGIILSMGG 972
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 973 QLPNNIAMDLHRQKA----NVLGTSPECIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVL 1048
Cdd:COG0458 81 QTALNLAVELEEAGIlegvKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1049 SGAAMNVAYSNQDLETYLNAASLVSKEHPVVISKFLQEAKEIDVDAVA-ADGEILCMAVSEHVENAGVHSGDATLVTPPQ 1127
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRdGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1128 DINAETLEKIKEITRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMHVEPVEV 1207
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1208 LHGC----GKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPkRAILLSIGSFKHKVEL 1283
Cdd:COG0458 321 DTGFeptlDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP-GTVLLSLVADDDKEEA 399
|
410
....*....|..
gi 86450145 1284 LPSIRDLAKMGY 1295
Cdd:COG0458 400 LLLARRLARLGF 411
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-315 |
1.24e-127 |
|
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: 397.38 E-value: 1.24e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIPsqkeiddfgmPKHFEwTKGITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:TIGR01368 47 QIVVFTYPLIGNYGVN----------DEDAE-SKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 81 KKIRENGSILGRITYEIPSDLQISNLKLVDPNLR--NLVAECSVSTVQTFNM--NGSPRICAIDCGLKLNQIRCFVRRGV 156
Cdd:TIGR01368 116 KKIREKGTMKGVISTEDSNDEELVEKARVSPDITgiNLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVKRNILRRLVKRGC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 157 RVDLVPWNH---ELNKKEFDGLFISNGPGDPVMCETTVKQISKIMQEseIPIFGICLGHQLLATAIGCKTYKMKYGNRGH 233
Cdd:TIGR01368 196 EVTVVPYDTdaeEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLEK--IPIFGICLGHQLLALAFGAKTYKMKFGHRGG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 234 NLPCLHHGTGRCFMTSQNHGFAVDANTLP-DDWESLFTNVNDHSNEGIIHKQKPYFSVQFHPEHTAGPEDLEMLFDVFVD 312
Cdd:TIGR01368 274 NHPVKDLITGRVEITSQNHGYAVDPDSLPaGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFID 353
|
...
gi 86450145 313 EVK 315
Cdd:TIGR01368 354 LMK 356
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-312 |
7.77e-127 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 395.21 E-value: 7.77e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIPSqkeiDDFgmpkhfEwTKGITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:PRK12564 51 QIVTFTYPLIGNYGVNR----EDF------E-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 81 KKIRENGSILGRITYEiPSDLQisnlKLVD-----PNL--RNLVAEcsVSTVQTFNMNGSP-----RICAIDCGLKLNQI 148
Cdd:PRK12564 120 RKLREKGAMKGVIATE-DFDAE----ELLEkarafPGLlgLDLVKE--VSTKEPYPWPGPGgelkyKVVAIDFGVKRNIL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 149 RCFVRRGVRVDLVPWN---HELNKKEFDGLFISNGPGDPVMCETTVKQISKIMqESEIPIFGICLGHQLLATAIGCKTYK 225
Cdd:PRK12564 193 RELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAALDYAIEMIRELL-EKKIPIFGICLGHQLLALALGAKTYK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 226 MKYGNRGHNLPCLHHGTGRCFMTSQNHGFAVDANTLPDDWESLFTNVNDHSNEGIIHKQKPYFSVQFHPEHTAGPEDLEM 305
Cdd:PRK12564 272 MKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAY 351
|
....*..
gi 86450145 306 LFDVFVD 312
Cdd:PRK12564 352 LFDEFVE 358
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-315 |
5.59e-123 |
|
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: 385.14 E-value: 5.59e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIPSqkeiDDFgmpkhfEwTKGITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:COG0505 51 QIVTFTYPHIGNYGVND----EDF------E-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 81 KKIRENGSILGRITYEipsDLQISNLK-----LVDPNLRNLVAEcsVSTVQTFNMNGSP----RICAIDCGLKLNQIRCF 151
Cdd:COG0505 120 RHLREKGAMKGVISTG---DLDIEELLekaraAPGMEGLDLVKE--VSTKEPYEWTEAPgagfHVVALDFGVKRNILREL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 152 VRRGVRVDLVPWN---HELNKKEFDGLFISNGPGDPVMCETTVKQISKIMqESEIPIFGICLGHQLLATAIGCKTYKMKY 228
Cdd:COG0505 195 AERGCRVTVVPATtsaEEILALNPDGVFLSNGPGDPAALDYAIETIRELL-GKGIPIFGICLGHQLLALALGAKTYKLKF 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 229 GNRGHNLPCLHHGTGRCFMTSQNHGFAVDANTLPD-DWESLFTNVNDHSNEGIIHKQKPYFSVQFHPEHTAGPEDLEMLF 307
Cdd:COG0505 274 GHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLF 353
|
....*...
gi 86450145 308 DVFVDEVK 315
Cdd:COG0505 354 DRFIELME 361
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
1-317 |
2.83e-98 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 317.99 E-value: 2.83e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIPsqkEIDdfgmpkhFEwTKGITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:PRK12838 49 QIVVFTYPLIGNYGIN---ADD-------YE-SKQPQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 81 KKIRENGSILGRITYEIPSDLQISNLKLVDPnlRNLVAECSVSTVQTFNmNGSPRICAIDCGLKLNQIRCFVRRGVRVDL 160
Cdd:PRK12838 118 KHIREKGTMKASITTTDDAHAFDQIKALVLP--KNVVAQVSTKEPYTYG-NGGKHVALIDFGYKKSILRSLSKRGCKVTV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 161 VPWN------HELNkkeFDGLFISNGPGDPVMCETTVKQISKIMQEseIPIFGICLGHQLLATAIGCKTYKMKYGNRGHN 234
Cdd:PRK12838 195 LPYDtsleeiKNLN---PDGIVLSNGPGDPKELQPYLPEIKKLISS--YPILGICLGHQLIALALGADTEKLPFGHRGAN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 235 LPCLHHGTGRCFMTSQNHGFAVDANTLPDD-WESLFTNVNDHSNEGIIHKQKPYFSVQFHPEHTAGPEDLEMLFDVFVDE 313
Cdd:PRK12838 270 HPVIDLTTGRVWMTSQNHGYVVDEDSLDGTpLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEM 349
|
....
gi 86450145 314 VKSR 317
Cdd:PRK12838 350 MEKA 353
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
136-311 |
6.78e-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: 304.42 E-value: 6.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 136 ICAIDCGLKLNQIRCFVRRGVRVDLVPWNH---ELNKKEFDGLFISNGPGDPVMCETTVKQISKIMqESEIPIFGICLGH 212
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTdaeEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLL-GKKIPIFGICLGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 213 QLLATAIGCKTYKMKYGNRGHNLPCLHHGTGRCFMTSQNHGFAVDANTLPDDWESLFTNVNDHSNEGIIHKQKPYFSVQF 292
Cdd:cd01744 80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159
|
170
....*....|....*....
gi 86450145 293 HPEHTAGPEDLEMLFDVFV 311
Cdd:cd01744 160 HPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
469-671 |
2.26e-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: 2.26e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 469 DRKIFADRVAEIGEKVAPSEAVY--SVKEALQAAEKLGYPVMARAAFSLGGLGSGFANNETELQVLAQQALAHS------ 540
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 541 NQLIIDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLgiHTGESIVVAPSQTLSNNEYNMLRTTAIKVIRHFGVVGEC 620
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 86450145 621 NIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLAIPLP 671
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
334-737 |
1.25e-84 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 299.61 E-value: 1.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 334 LSYKPKPEFVNFERPRKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLPLTPE 413
Cdd:TIGR01369 540 STYEGERDDVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFE 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 414 YVEQVIKAERPNGVLLTFGGQTALNCGVELEKSGifakynVRIMGTPIQSIIETEDRKIFADRVAEIGEKVAPSEAVYSV 493
Cdd:TIGR01369 620 DVMNIIELEKPEGVIVQFGGQTPLNLAKALEEAG------VPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSV 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 494 KEALQAAEKLGYPVMARAAFSLGGLGSGFANNETELQVLAQQALAHSNQ--LIIDKSLRGWKEVEYEVVRDafDNCITVC 571
Cdd:TIGR01369 694 EEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAVSD--GEEVLIP 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 572 N-MENLDPLGIHTGESIVVAPSQTLSNNEYNMLRTTAIKVIRHFGVVGECNIQYALnpESEEYYIIEVNARLSRSSALAS 650
Cdd:TIGR01369 772 GiMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGEVYVIEVNPRASRTVPFVS 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 651 KATGYPLAYVAAKLSLAIPLPDIknsvtGVTtacFEPSLDYCVVKIPRWDLAKFTKVSKNIGSSMKSVGEVMAIGRNFEE 730
Cdd:TIGR01369 850 KATGVPLAKLAVRVMLGKKLEEL-----GVG---KEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAE 921
|
....*..
gi 86450145 731 AFQKALR 737
Cdd:TIGR01369 922 AFLKAQL 928
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-311 |
2.88e-63 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 220.82 E-value: 2.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIPSQKeiddfgmpkhFEWTKgITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:CHL00197 53 QIVTFTYPEIGNTGINLED----------IESVK-IQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 81 KKIRENGSILGRITYE----------IPSDLQISNLKLVDPNLRNLVAECSVSTVQTFN-------MNGSP-RICAIDCG 142
Cdd:CHL00197 122 QHLRRFGTMNGCISNQnlnlsylrakIKESPHMPSSDLIPRVTTSSYYEWDEKSHPSFYladnkrpHSSYQlKIIVIDFG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 143 LKLNQIRCFVRRGVRVDLVPWN---HELNKKEFDGLFISNGPGDPVMCETTVKQISKIMQESeIPIFGICLGHQLLATAI 219
Cdd:CHL00197 202 VKYNILRRLKSFGCSITVVPATspyQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYN-IPIFGICMGHQILSLAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 220 GCKTYKMKYGNRGhnlpcLHHGTG---RCFMTSQNHGFAVDANTL-PDDWESLFTNVNDHSNEGIIHKQKPYFSVQFHPE 295
Cdd:CHL00197 281 EAKTFKLKFGHRG-----LNHPSGlnqQVEITSQNHGFAVNLESLaKNKFYITHFNLNDGTVAGISHSPKPYFSVQYHPE 355
|
330
....*....|....*.
gi 86450145 296 HTAGPEDLEMLFDVFV 311
Cdd:CHL00197 356 ASPGPHDADYLFEYFI 371
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
139-312 |
2.90e-61 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 207.48 E-value: 2.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 139 IDCGL--KLNQIRCFVRRGVRVDLVPWNH---ELNKKEFDGLFISNGPGDPVMCETTVKQISKIMqESEIPIFGICLGHQ 213
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREAR-ELKIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 214 LLATAIGCKTYKMK-YGNRGHNLPCLH------HGTGRCFMTSQNHGFAVDANTLPDDWESLFTNVNDHSNEGIIHKQKP 286
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*.
gi 86450145 287 YFSVQFHPEHTAGPEDLEMLFDVFVD 312
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
757-876 |
3.08e-51 |
|
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: 176.10 E-value: 3.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 757 ELIQATDKRIFVLAAAIKENYTIERLYQLTNIDPWFLNKMKNIIDYLNVLEKHG-NNLDRNMILEAKKLGFSDKQIAAAI 835
Cdd:smart01096 4 ELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGlDELDADLLRKAKRLGFSDRQIAKLL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 86450145 836 KSTDLMVRKQREEMKVVPFVKQIDTVAGEWPATTNYLYLTY 876
Cdd:smart01096 84 GVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
1-307 |
6.72e-50 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 182.87 E-value: 6.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIpsqkEIDDfgmpkhfEWTKGITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:PLN02771 103 QFVLMTNPHIGNTGV----NFDD-------EESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAIT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 81 KKIRENGSILGRITYE-IPSD---LQIS-NLKLVDPNLRNLVAeCS--------VSTVQTFNMNG----SPRICAIDCGL 143
Cdd:PLN02771 172 RRLREDGSLIGVLSTEdSKTDeelLKMSrSWDIVGIDLISGVS-CKspyewvdkTNPEWDFNTNSrdgeSYHVIAYDFGI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 144 KLNQIRCFVRRGVRVDLVPWN---HELNKKEFDGLFISNGPGDPVMCETTVKQISKIMqeSEIPIFGICLGHQLLATAIG 220
Cdd:PLN02771 251 KHNILRRLASYGCKITVVPSTwpaSEALKMKPDGVLFSNGPGDPSAVPYAVETVKELL--GKVPVFGICMGHQLLGQALG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 221 CKTYKMKYGNRGHNLPCLHHGTGRCFMTSQNHGFAVDANTLPDDWESLFTNVNDHSNEGIIHKQKPYFSVQFHPEHTAGP 300
Cdd:PLN02771 329 GKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGP 408
|
....*..
gi 86450145 301 EDLEMLF 307
Cdd:PLN02771 409 HDSDNAF 415
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
3.17e-38 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 139.00 E-value: 3.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIPsqkeiddfgmPKHFEwTKGITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:pfam00988 45 QIVVFTYPLIGNYGVN----------PEDFE-SDKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALT 113
|
90
....*....|...
gi 86450145 81 KKIRENGSILGRI 93
Cdd:pfam00988 114 RKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
2.26e-35 |
|
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: 130.96 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1 QILVLTYPLVGNYGIPSQKeiddfgmpkhFEWTKgITVAGLVVGEICSTPSHFRKTSTLDQWMKENEIPGISDIDTRSLT 80
Cdd:smart01097 49 QIVVFTYPLIGNYGVNDED----------FESDK-IQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALT 117
|
90
....*....|...
gi 86450145 81 KKIRENGSILGRI 93
Cdd:smart01097 118 RKLREKGAMKGVI 130
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
757-833 |
3.54e-33 |
|
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: 122.87 E-value: 3.54e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86450145 757 ELIQATDKRIFVLAAAIKENYTIERLYQLTNIDPWFLNKMKNIIDYLNVLEKHGNNLDRNMILEAKKLGFSDKQIAA 833
Cdd:pfam02787 2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDAELLREAKRLGFSDRQIAK 78
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
156-295 |
2.33e-22 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 95.68 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 156 VRVDLVPWNhELNKKEFDGLFISNGPGDPV---MCETTVKQISKimqesEIPIFGICLGHQLLATAIGCKTYKMKYGNRG 232
Cdd:cd01743 28 VRNDEITLE-ELELLNPDAIVISPGPGHPEdagISLEIIRALAG-----KVPILGVCLGHQAIAEAFGGKVVRAPEPMHG 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86450145 233 HNLPCLHHGTGRCFMTSQN------HGFAVDANTLPDDWEslftnVNDHSNEGII----HKQKPYFSVQFHPE 295
Cdd:cd01743 102 KTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLE-----VTASTEDGVImalrHRDLPIYGVQFHPE 169
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
984-1175 |
3.35e-20 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 91.86 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 984 RQKANVLGTSPECIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLE 1063
Cdd:COG0439 36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1064 TYLNAAS----LVSKEHPVVISKFLqEAKEIDVDAVAADGEILCMAVSEHvENAGVHSGDATLVTPPqDINAETLEKIKE 1139
Cdd:COG0439 116 AALAEARaeakAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGE 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 86450145 1140 ITRDLAALLDV-TGPFNMQ-LIAKNNELKVIECNVRVS 1175
Cdd:COG0439 193 LVARALRALGYrRGAFHTEfLLTPDGEPYLIEINARLG 230
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
156-295 |
1.54e-18 |
|
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: 85.09 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 156 VRVDLVPWNhELNKKEFDGLFISNGPGDPV---MCETTVKQISKimqesEIPIFGICLGHQLLATAIGCKTYKMKYgnrg 232
Cdd:COG0512 28 VRNDEITLE-EIEALAPDGIVLSPGPGTPEeagISLEVIRAFAG-----KIPILGVCLGHQAIGEAFGGKVVRAPE---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 233 hnlpcLHHGtgrcfMTSQ-------------N-------HGFAVDANTLPDDWEslftnVNDHSNEGII----HKQKPYF 288
Cdd:COG0512 98 -----PMHG-----KTSPithdgsglfaglpNpftatryHSLVVDRETLPDELE-----VTAWTEDGEImgirHRELPIE 162
|
....*..
gi 86450145 289 SVQFHPE 295
Cdd:COG0512 163 GVQFHPE 169
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1025-1195 |
7.08e-18 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 83.51 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1025 NLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKE----HPVVISKFLQEAKEIDVDaVAADGE 1100
Cdd:pfam02786 26 TEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnPQVLVEKSLKGPKHIEYQ-VLRDAH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1101 ILCMAVSEhVENA-GVHSGDATLVTPPQDINAETLEKIKEITRDLAALLDVTGPFNMQLI--AKNNELKVIECNVRVSRS 1177
Cdd:pfam02786 105 GNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFAldPFSGEYYFIEMNTRLQVE 183
|
170
....*....|....*...
gi 86450145 1178 FPFVSKTLNHDFVATATR 1195
Cdd:pfam02786 184 HALAEKATGYDLAKEAAK 201
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
135-313 |
3.13e-16 |
|
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: 79.22 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 135 RICAIDC----GLKLNQIRCFVR------RGVRV---DLVPWNHELNkkEFDGLFISNGPG---DPVMCETTVKQISKIM 198
Cdd:COG0518 1 KILILDHdpfgGQYPGLIARRLReagielDVLRVyagEILPYDPDLE--DPDGLILSGGPMsvyDEDPWLEDEPALIREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 199 QESEIPIFGICLGHQLLATAIGCKTYKMKYGNRG-------HNLPCLHH--GTGRCFMTsqnHGFAVDanTLPDDWESLF 269
Cdd:COG0518 79 FELGKPVLGICYGAQLLAHALGGKVEPGPGREIGwapveltEADPLFAGlpDEFTVWMS---HGDTVT--ELPEGAEVLA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 86450145 270 TNVNDHsNEGIIHKqKPYFSVQFHPEHTagPEDLEMLFDVFVDE 313
Cdd:COG0518 154 SSDNCP-NQAFRYG-RRVYGVQFHPEVT--HTMMEAWLEERADE 193
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
154-306 |
3.85e-15 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 75.04 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 154 RGVRVDLVPWN---HELNKKEFDGLFISNGPgDPVMCETTVKQISKIMqESEIPIFGICLGHQLLATAIGCKTYKMKYGN 230
Cdd:TIGR00888 21 LGVYSELVPNTtplEEIREKNPKGIILSGGP-SSVYAENAPRADEKIF-ELGVPVLGICYGMQLMAKQLGGEVGRAEKRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 231 RGH------NLPCLHHGTGRCFMTSQNHGFAVDAntLPDDWESLFTnvNDHS-NEGIIHKQKPYFSVQFHPEHTAGPEDL 303
Cdd:TIGR00888 99 YGKaeleilDEDDLFRGLPDESTVWMSHGDKVKE--LPEGFKVLAT--SDNCpVAAMAHEEKPIYGVQFHPEVTHTEYGN 174
|
...
gi 86450145 304 EML 306
Cdd:TIGR00888 175 ELL 177
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
166-306 |
4.14e-15 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 80.15 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 166 ELNKKEFDGLFISNGPGDPV---MCETTVKQISKimqesEIPIFGICLGHQLLATAIGCKTYKMKYGNRGHNLPCLHHGT 242
Cdd:PRK14607 39 EIEALNPSHIVISPGPGRPEeagISVEVIRHFSG-----KVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGK 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450145 243 GrCFMTSQN-------HGFAVDANTLPDDWEslftnVNDHSNEGII----HKQKPYFSVQFHPEHTAGPEDLEML 306
Cdd:PRK14607 114 G-LFRGIPNptvatryHSLVVEEASLPECLE-----VTAKSDDGEImgirHKEHPIFGVQFHPESILTEEGKRIL 182
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
475-669 |
2.06e-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: 74.91 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 475 DRVAEIGEKVAPSEAVYSVKEALQAAEKLGYPVMARAAFSLGGLGSGFANNETELQVLAQQALAHSN------QLIIDKS 548
Cdd:COG0439 60 EALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKagspngEVLVEEF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 549 LRGwKEVEYEVVrdAFDNCITVCNM---ENLDPLGIHTGEsivVAPSQtLSNNEYNMLRTTAIKVIRHFGVV-GECNIQY 624
Cdd:COG0439 140 LEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEF 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 86450145 625 ALNPEsEEYYIIEVNARLS--RSSALASKATGYPLAYVAAKLSLAIP 669
Cdd:COG0439 213 LLTPD-GEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
146-295 |
5.35e-14 |
|
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: 71.74 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 146 NQIRCFVRRGVRVdLVPWNHELNKKEFDGLF-----ISNGPGDPVMCETTVKQISKImqESEIPIFGICLGHQLLATAIG 220
Cdd:TIGR00566 14 NLVQYFCELGAEV-VVKRNDSLTLQEIEALLpllivISPGPCTPNEAGISLEAIRHF--AGKLPILGVCLGHQAMGQAFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 221 CKTYKMKYGNRGHNLPCLHHGTGRC------FMTSQNHGFAVDANTLPDDWESLFTNVNDHSNEGIIHKQKPYFSVQFHP 294
Cdd:TIGR00566 91 GDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHP 170
|
.
gi 86450145 295 E 295
Cdd:TIGR00566 171 E 171
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
173-315 |
9.35e-14 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 70.93 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 173 DGLFISNGPGDP----VMCEttvkqiskIMQE--SEIPIFGICLGHQLLATAIGC-----------KTYKMKYGNRG--H 233
Cdd:PRK05670 45 DAIVLSPGPGTPaeagISLE--------LIREfaGKVPILGVCLGHQAIGEAFGGkvvrakeimhgKTSPIEHDGSGifA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 234 NLPclhhgtgRCFMTSQNHGFAVDANTLPDDWEslftnVNDHSNEGII----HKQKPYFSVQFHPEHTAGPEDLEMLfDV 309
Cdd:PRK05670 117 GLP-------NPFTVTRYHSLVVDRESLPDCLE-----VTAWTDDGEImgvrHKELPIYGVQFHPESILTEHGHKLL-EN 183
|
....*.
gi 86450145 310 FVDEVK 315
Cdd:PRK05670 184 FLELAR 189
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
171-296 |
1.08e-13 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 70.74 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 171 EFDGLFISNGP------GDPVMcETTVKQISKIMqESEIPIFGICLGHQLLATAIGCKTYKMKYG-----------NRGH 233
Cdd:cd01741 46 DYDGLVILGGPmsvdedDYPWL-KKLKELIRQAL-AAGKPVLGICLGHQLLARALGGKVGRNPKGweigwfpvtltEAGK 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86450145 234 NLPcLHHGTGRCFMTSQNHGFAVDAntLPDDWESLFTnvNDHSNEGIIHKQKPYFSVQFHPEH 296
Cdd:cd01741 124 ADP-LFAGLPDEFPVFHWHGDTVVE--LPPGAVLLAS--SEACPNQAFRYGDRALGLQFHPEE 181
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
155-297 |
1.41e-12 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 67.57 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 155 GVRVDLVPwNH----ELnKKEFDGLFISNGPGdpvMceTTVKQISKIMQESEIPIFGICLGHQLLATAIGCKTYKMKYGN 230
Cdd:PRK00758 23 GVDAKIIP-NTtpveEI-KAFEDGLILSGGPD---I--ERAGNCPEYLKELDVPILGICLGHQLIAKAFGGEVGRGEYGE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450145 231 RGH-NLPCLHH-----GTGRCFMTSQNHGFAVdaNTLPDDWESLftnvnDHSN----EGIIHKQKPYFSVQFHPE--HT 297
Cdd:PRK00758 96 YALvEVEILDEddilkGLPPEIRVWASHADEV--KELPDGFEIL-----ARSDicevEAMKHKEKPIYGVQFHPEvaHT 167
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
151-295 |
1.56e-12 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 67.58 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 151 FVRRGVRVdLVPWNHELNKKEFDGL-----FISNGPGDPVMCETTVKQISKImqESEIPIFGICLGHQLLATAIGCKTYK 225
Cdd:PRK06774 19 FCELGTEV-MVKRNDELQLTDIEQLapshlVISPGPCTPNEAGISLAVIRHF--ADKLPILGVCLGHQALGQAFGARVVR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450145 226 MKYGNRGHNLPCLHHGTG------RCFMTSQNHGFAVDANTLPDDWE-SLFTNVNDHSNE--GIIHKQKPYFSVQFHPE 295
Cdd:PRK06774 96 ARQVMHGKTSAICHSGQGvfrglnQPLTVTRYHSLVIAADSLPGCFElTAWSERGGEMDEimGIRHRTLPLEGVQFHPE 174
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
152-297 |
2.05e-12 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 67.18 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 152 VRR----GVRVDLVPWN---HELNKKEFDGLFISNGP------GDPvmcettvkQISKIMQESEIPIFGICLGHQLLATA 218
Cdd:cd01742 15 ARRvrelGVYSEILPNTtplEEIKLKNPKGIILSGGPssvyeeDAP--------RVDPEIFELGVPVLGICYGMQLIAKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 219 IGCKTYKMKYGNRGH------NLPCLHHGTGRCFMTSQNHGFAVDAntLPDDWESLFTNVNDHsNEGIIHKQKPYFSVQF 292
Cdd:cd01742 87 LGGKVERGDKREYGKaeieidDSSPLFEGLPDEQTVWMSHGDEVVK--LPEGFKVIASSDNCP-VAAIANEEKKIYGVQF 163
|
....*..
gi 86450145 293 HPE--HT 297
Cdd:cd01742 164 HPEvtHT 170
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
148-295 |
4.38e-12 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 67.00 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 148 IRCFVRRGVRVDLVpwNHELNKKEFDGLFISNGPGDPVMCETTVKQIsKIMQESEIPIFGICLGHQLLATAIGC------ 221
Cdd:PRK07765 25 VEAEVWRNDDPRLA--DEAAVAAQFDGVLLSPGPGTPERAGASIDMV-RACAAAGTPLLGVCLGHQAIGVAFGAtvdrap 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 222 -----KTYKMKYGNRG--HNLPclhhgtgRCFMTSQNHGFAVDANTLPDDWEslftnVNDHSNEGII----HKQKPYFSV 290
Cdd:PRK07765 102 ellhgKTSSVHHTGVGvlAGLP-------DPFTATRYHSLTILPETLPAELE-----VTARTDSGVImavrHRELPIHGV 169
|
....*
gi 86450145 291 QFHPE 295
Cdd:PRK07765 170 QFHPE 174
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
989-1180 |
6.45e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 68.37 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 989 VLGTSPECIDSAENRFKFSRMLDRKGILQPRWKELTNLKS--AIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYL 1066
Cdd:PRK12767 98 VLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDfkAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1067 NAASlvskehPVVISKFLQEaKEIDVDA-VAADGEILCMAVSEHVEnagVHSGDAtlvtppqdINAETLE--KIKEITRD 1143
Cdd:PRK12767 178 EYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGET--------SKGVTVKdpELFKLAER 239
|
170 180 190
....*....|....*....|....*....|....*..
gi 86450145 1144 LAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPF 1180
Cdd:PRK12767 240 LAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
1014-1158 |
9.59e-12 |
|
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: 64.58 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1014 GILQPRWKELTNLKSAIDFCEEVGYPCLV---RPSYvlSGAAMNVAYSNQDLETYLNAAslvsKEHPVVISKFLQEAKEI 1090
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEEL----GDGPVIVEEFVPFDREL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450145 1091 DVDAV-AADGEILCMAVSEHVEnagvHSGDATLVTPPQDINAETLEKIKEITRDLAALLDVTGPFNMQL 1158
Cdd:pfam02222 78 SVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
173-306 |
6.06e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 63.28 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 173 DGLFISNGPGDPVMCETTVKQISKImqESEIPIFGICLGHQLLATAIGCKTYKMKYGNRGHNLPCLHHGTG------RCF 246
Cdd:PRK07649 45 DFLMISPGPCSPNEAGISMEVIRYF--AGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTifsdipNPF 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450145 247 MTSQNHGFAVDANTLPDDWEslftnVNDHSNEG----IIHKQKPYFSVQFHPEHTAGPEDLEML 306
Cdd:PRK07649 123 TATRYHSLIVKKETLPDCLE-----VTSWTEEGeimaIRHKTLPIEGVQFHPESIMTSHGKELL 181
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
460-642 |
1.98e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 64.66 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 460 PIQSIIETEDRKIFADR-VAEIGEKVAP--SEAVYSVKEALQAAEKLGYPVMARAAFSLGGLGSGFANNETEL------- 529
Cdd:PRK06111 105 PSADIIAKMGSKIEARRaMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELtkafesn 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 530 QVLAQQALAHSnQLIIDKSLRGWKEVEYEVVRDAFDNCitvcnmenldplgIHTGE---SI------VV--APSQTLSNN 598
Cdd:PRK06111 185 KKRAANFFGNG-EMYIEKYIEDPRHIEIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPFLDEE 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 86450145 599 EYNMLRTTAIKVIRHFGVVGECNIQYaLNPESEEYYIIEVNARL 642
Cdd:PRK06111 251 TRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFYFLEMNTRL 293
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
175-295 |
3.06e-10 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 61.05 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 175 LFISNGPGDPVMCETTVKQISKIMqeSEIPIFGICLGHQLLATAIGCKTYKMKYGNRGHNLPCLHhgTGRCFMTSQN--- 251
Cdd:PRK08857 47 LVISPGPCTPNEAGISLQAIEHFA--GKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSVFKGLNnpl 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 86450145 252 -----HGFAVDANTLPDDWE-SLFTNVNDHSNE---GIIHKQKPYFSVQFHPE 295
Cdd:PRK08857 123 tvtryHSLVVKNDTLPECFElTAWTELEDGSMDeimGFQHKTLPIEAVQFHPE 175
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
152-295 |
5.94e-10 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 60.13 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 152 VRRGVRVDLVpwnhELNKKEFDGLFISNGPGDPVMCETTVKQISKIMqeSEIPIFGICLGHQLLATAIGCKTYKMKYGNR 231
Cdd:CHL00101 28 VCRNDEIDLS----KIKNLNIRHIIISPGPGHPRDSGISLDVISSYA--PYIPILGVCLGHQSIGYLFGGKIIKAPKPMH 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450145 232 G------HNLPCLHHGTGRCFMTSQNHGFAVDANTLPDDWEslftnVNDHSNEGII----HKQKPY-FSVQFHPE 295
Cdd:CHL00101 102 GktskiyHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSPLE-----ITAWTEDGLImacrHKKYKMlRGIQFHPE 171
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
146-295 |
1.22e-09 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 59.16 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 146 NQIRCFVRRGVRVdLVPWNHELNKKEFDGL-----FISNGPGDPVMCETTVKQISKImqESEIPIFGICLGHQLLATAIG 220
Cdd:PRK08007 14 NLYQYFCELGADV-LVKRNDALTLADIDALkpqkiVISPGPCTPDEAGISLDVIRHY--AGRLPILGVCLGHQAMAQAFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 221 CKTYKMKYGNRGHNLPCLHHGTG------RCFMTSQNHGFAVDANTLPDDWEslfTNVNDHSNE--GIIHKQKPYFSVQF 292
Cdd:PRK08007 91 GKVVRAAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGVQF 167
|
...
gi 86450145 293 HPE 295
Cdd:PRK08007 168 HPE 170
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
350-661 |
2.29e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 60.67 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 350 KILILGSGGlsigqagefdysGSQAIKALKEEKIQTILINPNIATVQTSKGLADKVYFLP--LTPEYVEQVI---KAERP 424
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPkvTDPNYIDRLLdicKKEKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 425 NGVLLTFggqtalncgvELEKSGI------FAKYNVRIMGTPiQSIIET-EDRKIFADRVAEIGEKVAPSEAVYSVKEAL 497
Cdd:PRK12767 71 DLLIPLI----------DPELPLLaqnrdrFEEIGVKVLVSS-KEVIEIcNDKWLTYEFLKENGIPTPKSYLPESLEDFK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 498 QA--AEKLGYPVMARAAFSLGGLGSGFANNETELQVLaqqaLAHSNQLIIDKSLRGwKEVEYEVVRDAFDNCITVCNMEN 575
Cdd:PRK12767 140 AAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL----LEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 576 LDPLGIHTGESIVVapsqtlsnnEYNMLRTTAIKVIRHFGVVGECNIQYALNPEseEYYIIEVNARLSrssalaskaTGY 655
Cdd:PRK12767 215 IEVRAGETSKGVTV---------KDPELFKLAERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFG---------GGY 274
|
....*.
gi 86450145 656 PLAYVA 661
Cdd:PRK12767 275 PLSYMA 280
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
460-667 |
2.70e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 61.31 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 460 PIQSIIETEDRKIFADRVA-EIGEKVAPSE--AVYSVKEALQAAEKLGYPVMARAAFSLGGLGSGFANNETELQV---LA 533
Cdd:PRK12833 108 PDAQTIRTMGDKARARRTArRAGVPTVPGSdgVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpLA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 534 Q---QALAHSNQLIIDKSLRGWKEVEYEVVRDAFDnciTVCNMENLDPLGIHTGESIVVAPSQTLSNNEYNMLRTTAIKV 610
Cdd:PRK12833 188 QreaQAAFGDGGVYLERFIARARHIEVQILGDGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRL 264
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 86450145 611 IRHFGVVGECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLayVAAKLSLA 667
Cdd:PRK12833 265 ARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDL--VQEMLRIA 319
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
166-295 |
4.21e-09 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 58.27 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 166 ELNKKEFDGLFISNGPGDPVMCETTVKQISKImqESEIPIFGICLGHQLLATAIGCKTYKMKYG-NRGHNLPCLH----- 239
Cdd:PLN02335 57 ELKRKNPRGVLISPGPGTPQDSGISLQTVLEL--GPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYdekge 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86450145 240 ----HGTGRCFMTSQNHGFAVDANTLPDDWESLFTNVNDHSNEGIIHKQKPYFS-VQFHPE 295
Cdd:PLN02335 135 eglfSGLPNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPE 195
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
148-221 |
4.33e-09 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 55.68 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 148 IRCFVRRGVRVDLVPWNH-----ELNKKEFDGLFISNGPGDPVMCETTVKQISKIMQ--ESEIPIFGICLGHQLLATAIG 220
Cdd:cd01653 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPDDLARDEALLALLREaaAAGKPILGICLGAQLLVLGVQ 97
|
.
gi 86450145 221 C 221
Cdd:cd01653 98 F 98
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
448-674 |
1.20e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 58.96 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 448 IFAKYNVRIMGtPIQSIIETEDRKIFADRVA-EIGEKVAP-SEA-VYSVKEALQAAEKLGYPVMARAAFSLGGLGSGFAN 524
Cdd:PRK07178 93 ICAERGIKFIG-PSAEVIRRMGDKTEARRAMiKAGVPVTPgSEGnLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 525 NETEL-----QVL--AQQALAhSNQLIIDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGESIVVAPSQ 593
Cdd:PRK07178 172 SREELeqnfpRVIseATKAFG-SAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 594 TLSNNEYNMLRTTAIKVIRHFGVVGECNIQYALNPESeEYYIIEVNARLSRSSALASKATGYPLAY----VAAKLSLAIP 669
Cdd:PRK07178 245 QLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADG-EVYFMEMNTRVQVEHTITEEITGIDIVReqirIASGLPLSYK 323
|
....*
gi 86450145 670 LPDIK 674
Cdd:PRK07178 324 QEDIQ 328
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
148-215 |
1.52e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 53.36 E-value: 1.52e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450145 148 IRCFVRRGVRVDLVPWNH-----ELNKKEFDGLFISNGPGDPVMCETTVKQISKIMQ--ESEIPIFGICLGHQLL 215
Cdd:cd03128 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPDDLAWDEALLALLREaaAAGKPVLGICLGAQLL 92
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
346-680 |
1.55e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 58.40 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 346 ERPRKILILGS--GGLSIgqagefdysgsqaIKALKEEKIQTILINPN-IATVQTSKgLADKVYFLPL----TPEYVEQV 418
Cdd:COG3919 3 TMRFRVVVLGGdiNALAV-------------ARSLGEAGVRVIVVDRDpLGPAARSR-YVDEVVVVPDpgddPEAFVDAL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 419 IK-AERPN-GVLLTFGGQTAL---NCGVELEKsgifakyNVRIMGTPIQSIIETEDRKIFADRVAEIGEKVAPSEAVYSV 493
Cdd:COG3919 69 LElAERHGpDVLIPTGDEYVEllsRHRDELEE-------HYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 494 KEALQAAEKLGYPVMARAA--------FSLGGLGSGFANNETELQVLAQQALAHSNQLII-------DKSLRGwkeveYE 558
Cdd:COG3919 142 DDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAGYELIVqeyipgdDGEMRG-----LT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 559 VVRDAFDNCITVCNMENL--DPLGIhtGESIVVapsQTLSNNEynmLRTTAIKVIRHFGVVGECNIQYALNPESEEYYII 636
Cdd:COG3919 217 AYVDRDGEVVATFTGRKLrhYPPAG--GNSAAR---ESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLI 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 86450145 637 EVNARLSRSSALASKAtGYPLAYVAAKLSLAIPLPDIKNSVTGV 680
Cdd:COG3919 289 EINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREGV 331
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
448-642 |
2.06e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 58.22 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 448 IFAKYNVRIMGTPIQSIIETEDRKIFADRVAEIGEKVAP-SE-AVYSVKEALQAAEKLGYPVMARAAFSLGGLGSGFANN 525
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 526 ETELQ--VLAQQALAHS----NQLIIDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGESIVVAPSQTL 595
Cdd:PRK08462 176 ESDLEnlYLAAESEALSafgdGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 86450145 596 SNNEYNMLRTTAIKVIRHFGVVGECNIQYALNpESEEYYIIEVNARL 642
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRL 295
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
165-295 |
4.61e-08 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 57.62 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 165 HELNKKEFDGLFISNGPGDPVmcETTVKQISKIMQESEIPIFGICLGHQLLATAIGcktykmkyGNRGH-NLPC------ 237
Cdd:PRK13566 563 EMLDRVNPDLVVLSPGPGRPS--DFDCKATIDAALARNLPIFGVCLGLQAIVEAFG--------GELGQlAYPMhgkpsr 632
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 238 --------LHHGTGRCFMTSQNHGFAVDANTLPDDWEslftnVNDHSNEGII----HKQKPYFSVQFHPE 295
Cdd:PRK13566 633 irvrgpgrLFSGLPEEFTVGRYHSLFADPETLPDELL-----VTAETEDGVImaieHKTLPVAAVQFHPE 697
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
169-350 |
2.71e-07 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 55.24 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 169 KKEFDGLFISNGPGDPvMCETTVKQISKIMQE-SEIPIFGICLGHQLLATAIGCKTYKMKYGNRGHNLPCLHHG------ 241
Cdd:PLN02889 129 EKAFDNIVISPGPGSP-TCPADIGICLRLLLEcRDIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGcrlfdd 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 242 --TGR--CFMTSQNHGFAVDANTLPDD-----W----------ESLFTNVNDHSNE------------------------ 278
Cdd:PLN02889 208 ipSGRnsGFKVVRYHSLVIDAESLPKElvpiaWtsssdtlsflESQKSGLVPDAYEsqigqsgssdpfssklkngtswps 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 279 -------------GIIHKQKPYFSVQFHPEHTA---GPEDLEMLFDVFVD-----------EVKSRLSGKMQKTI----- 326
Cdd:PLN02889 288 shsermqngkilmGIMHSTRPHYGLQFHPESIAtcyGRQIFKNFREITQDywlrlrstslrRRNSNLTANMQVPDasqlf 367
|
250 260
....*....|....*....|....*...
gi 86450145 327 ----RQSLIDKLSYKPKPEFVNFERPRK 350
Cdd:PLN02889 368 kvprRGQLGNGEDALGNRELSRRAQLRG 395
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
443-741 |
4.17e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 53.95 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 443 LEKSGIFAKY----NVRIMGtPIQSIIETEDRKIFADRV-AEIGEKVAP-SE-AVYSVKEALQAAEKLGYPVMARAAFSL 515
Cdd:PRK05586 85 LSENSKFAKMckecNIVFIG-PDSETIELMGNKSNAREImIKAGVPVVPgSEgEIENEEEALEIAKEIGYPVMVKASAGG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 516 GGLGSGFANNETELQVLAQQALAHS------NQLIIDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGE 585
Cdd:PRK05586 164 GGRGIRIVRSEEELIKAFNTAKSEAkaafgdDSMYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 586 SIVVAPSQTLSNNEYNMLRTTAIKVIRHFGVVGECNIQYALNpESEEYYIIEVNARLSRSSALASKATGYPLA----YVA 661
Cdd:PRK05586 238 VLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVkeqiKIA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 662 AKLSLAIPLPDIKnsVTGVTTAC----------FEPS----------------LD---YCVVKIPR-WDlakftkvskni 711
Cdd:PRK05586 317 YGEKLSIKQEDIK--INGHSIECrinaedpkngFMPCpgkieelyipgglgvrVDsavYSGYTIPPyYD----------- 383
|
330 340 350
....*....|....*....|....*....|
gi 86450145 712 gsSMksVGEVMAIGRNFEEAFQKALRMVDE 741
Cdd:PRK05586 384 --SM--IGKLIVYGKDREEAIQKMKRALGE 409
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
203-311 |
5.71e-07 |
|
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: 51.42 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 203 IPIFGICLGHQLLATAIGcktykmkyGNrghnlpcLHhgtgRCFMTSQNHGFAVDAntLPDDWEslftnVNDHSNEGII- 281
Cdd:cd01745 101 KPILGICRGMQLLNVALG--------GT-------LY----QDIRVNSLHHQAIKR--LADGLR-----VEARAPDGVIe 154
|
90 100 110
....*....|....*....|....*....|....*.
gi 86450145 282 ---HKQKPY-FSVQFHPEHTAgPEDLEM--LFDVFV 311
Cdd:cd01745 155 aieSPDRPFvLGVQWHPEWLA-DTDPDSlkLFEAFV 189
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
460-574 |
6.25e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 53.45 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 460 PIQSIIETEDRKIFADRV-AEIGEKVAP--SEAVYSVKEALQAAEKLGYPVMARAAFSLGGLGSGFANNETEL------- 529
Cdd:PRK08654 105 PSSDVIEAMGSKINAKKLmKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELedaiest 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 86450145 530 QVLAQQALAHSNqLIIDKSLRGWKEVEYEVVRDAFDNCITVCNME 574
Cdd:PRK08654 185 QSIAQSAFGDST-VFIEKYLEKPRHIEIQILADKHGNVIHLGDRE 228
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
177-295 |
6.49e-07 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 51.87 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 177 ISNGPGDPVMCETTVKQISKIMQEsEIPIFGICLGHQLLATAIGCKTY---KMKYGNRGHNLPC----------LHHGTG 243
Cdd:pfam07722 81 ESGGPYDPARDAYELALIRAALAR-GKPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshaVNVEPG 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86450145 244 RCF--MTSQN-------HGFAVDanTLPDDWEslftnVNDHSNEGII----HKQKPYF--SVQFHPE 295
Cdd:pfam07722 160 SLLasLLGSEefrvnslHHQAID--RLAPGLR-----VEAVAPDGTIeaieSPNAKGFalGVQWHPE 219
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
172-295 |
7.03e-07 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 50.89 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 172 FDGLFISNGPGDPVMCETTVKQISKIMQESEIpiFGICLGHQLLATAIGCKTYkmkygnrghNLPCLHHGTGRCFMTSQN 251
Cdd:PRK06895 44 FSHILISPGPDVPRAYPQLFAMLERYHQHKSI--LGVCLGHQTLCEFFGGELY---------NLNNVRHGQQRPLKVRSN 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450145 252 ----------------HGFAVDANTLPDDWESlfTNVNDhsnEGII----HKQKPYFSVQFHPE 295
Cdd:PRK06895 113 splfdglpeefniglyHSWAVSEENFPTPLEI--TAVCD---ENVVmamqHKTLPIYGVQFHPE 171
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
993-1152 |
3.07e-06 |
|
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: 50.84 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 993 SPECIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPS---------YVLSGAAmnvaysnqDLE 1063
Cdd:COG0026 80 GPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggydgkgqVVIKSAA--------DLE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1064 TYLNAAslvsKEHPVVISKFLQEAKEIDVDAV-AADGEILCMAVsehVENagVH-SGDATLVTPPQDINAETLEKIKEIT 1141
Cdd:COG0026 152 AAWAAL----GGGPCILEEFVPFERELSVIVArSPDGEVATYPV---VEN--VHrNGILDESIAPARISEALAAEAEEIA 222
|
170
....*....|.
gi 86450145 1142 RDLAALLDVTG 1152
Cdd:COG0026 223 KRIAEALDYVG 233
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
454-642 |
4.03e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 50.96 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 454 VRIMGTpiqsiietedrKIFADRVA-EIGEKVAP-SE-AVYSVKEALQAAEKLGYPVMARAAFSLGGLGSGFANNETELQ 530
Cdd:PRK08591 110 IRLMGD-----------KVTAKATMkKAGVPVVPgSDgPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 531 VLAQQA-----LAHSN-QLIIDKSLRGWKEVEYEVVRDAFDNcitvcnmenldplGIHTGE---SI------VV--APSQ 593
Cdd:PRK08591 179 KAFSMAraeakAAFGNpGVYMEKYLENPRHIEIQVLADGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSP 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 86450145 594 TLSNNEYNMLRTTAIKVIRHFGVVGECNIQYaLNPESEEYYIIEVNARL 642
Cdd:PRK08591 246 AITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKNGEFYFIEMNTRI 293
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
471-642 |
4.23e-06 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 51.29 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 471 KIFADRVA-EIGEKVAPS--EAVYSVKEALQAAEKLGYPVMARAAFSLGGLGSGFANNETEL-------QVLAQQALAhS 540
Cdd:PRK12999 120 KVAARNAAiKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELeeaferaKREAKAAFG-N 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 541 NQLIIDKSLRGWKEVEYEVVRDAFDNCitvcnmenldplgIHTGE---SI------VV--APSQTLSNNEYNMLRTTAIK 609
Cdd:PRK12999 199 DEVYLEKYVENPRHIEVQILGDKHGNV-------------VHLYErdcSVqrrhqkVVeiAPAPGLSEELRERICEAAVK 265
|
170 180 190
....*....|....*....|....*....|...
gi 86450145 610 VIRHFGVVGECNIQYALNPESeEYYIIEVNARL 642
Cdd:PRK12999 266 LARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1013-1152 |
1.56e-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: 47.31 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1013 KGILQPRWKELTNLKSAiDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAslVSKEHPVVISKFLqEAKEIDV 1092
Cdd:pfam07478 13 VTFTRADWKLNPKEWCA-QVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEA--FQYDEKVLVEEGI-EGREIEC 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450145 1093 dAVAADGEILCMAVSEHVENAGV------HSGDATLVTPPQDINAETLEKIKEITRDLAALLDVTG 1152
Cdd:pfam07478 89 -AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRG 153
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
491-657 |
8.86e-05 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 46.73 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 491 YSVKEALQAAEKLGYPVMARAAFSLGGLGSGFANNETELQ----VLAQQALAHSN--QLIIDKSLRGWKEVEYEVVRDAF 564
Cdd:PRK08463 139 ESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLEnafeSCKREALAYFNndEVFMEKYVVNPRHIEFQILGDNY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 565 DNCITVCnmENLDPLGIHTGESIVVAPSQTLSNNEYNMLRTTAIKVIRHFGVVGECNIQYALNpESEEYYIIEVNARLSR 644
Cdd:PRK08463 219 GNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD-DYNRFYFMEMNTRIQV 295
|
170
....*....|...
gi 86450145 645 SSALASKATGYPL 657
Cdd:PRK08463 296 EHGVTEEITGIDL 308
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
471-641 |
3.23e-04 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 45.07 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 471 KIFADRVA-EIGEKVAPS--EAVYSVKEALQAAEKLGYPVMARAAFSLGGLGSGFANNETELQ---VLAQ-QALAH--SN 541
Cdd:COG1038 119 KVAARAAAiEAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEeafESARrEAKAAfgDD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 542 QLIIDKSLRGWKEVEYEVVRDAFDNCitvcnmenldplgIHTGE---SI------VV--APSQTLSNNEYNMLRTTAIKV 610
Cdd:COG1038 199 EVFLEKYIERPKHIEVQILGDKHGNI-------------VHLFErdcSVqrrhqkVVeiAPAPNLDEELREAICEAAVKL 265
|
170 180 190
....*....|....*....|....*....|....*.
gi 86450145 611 IRHfgvVGECNiqyA-----LNPESEEYYIIEVNAR 641
Cdd:COG1038 266 AKA---VGYVN---AgtvefLVDDDGNFYFIEVNPR 295
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
993-1171 |
5.74e-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: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 993 SPECIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLV 1072
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 1073 SKEHPV-VISKFLQEAKEIDVDAVAADGEIL-CMA--VSEHVENAGVHSGDATlvtppqdiNAETLEKIKEITRDLAAL- 1147
Cdd:TIGR00768 159 NGPQNLfLVQEYIKKPGGRDIRVFVVGDEVVaAIYriTSGHWRSNLARGGKAE--------PCSLTEEIEELAIKAAKAl 230
|
170 180
....*....|....*....|....*
gi 86450145 1148 -LDVTGpfnMQLIAKNNELKVIECN 1171
Cdd:TIGR00768 231 gLDVAG---VDLLESEDGLLVNEVN 252
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
990-1096 |
7.71e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 43.82 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 990 LGTSPECIDSAENRFKFSRMLDRKG--ILQPRWKELTNLKSAIDFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLN 1067
Cdd:PRK08654 103 IGPSSDVIEAMGSKINAKKLMKKAGvpVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIE 182
|
90 100 110
....*....|....*....|....*....|...
gi 86450145 1068 AASLVSK----EHPVVISKFLQEAKEIDVDAVA 1096
Cdd:PRK08654 183 STQSIAQsafgDSTVFIEKYLEKPRHIEIQILA 215
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
607-681 |
2.70e-03 |
|
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.
Pssm-ID: 434824 [Multi-domain] Cd Length: 131 Bit Score: 39.52 E-value: 2.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450145 607 AIKVIRHFGVVGECNIQYALNpeSEEYYIIEVNARLsrSSALA-SKATGYPLAYVAAKLSLAIPLPDIKNSVTGVT 681
Cdd:pfam15632 53 ARRLAEAFGLDGLFNVQFRYD--GDGPKLLEINPRM--SGGIGySCLAGVNLPYLALKLLLGLETPDPVEPRLGLR 124
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
181-323 |
3.11e-03 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 41.59 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450145 181 PGDPVMCETTVKQIskimQESEIPIFGICLGHQLLATAIGCKT---YKMKYGNRGHNLPCL-----HHGTGRCFMTSQNH 252
Cdd:PLN02347 69 EGAPTVPEGFFDYC----RERGVPVLGICYGMQLIVQKLGGEVkpgEKQEYGRMEIRVVCGsqlfgDLPSGETQTVWMSH 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86450145 253 GfaVDANTLPDDWESLFTNVNDhSNEGIIHKQKPYFSVQFHPEHTAGPEDLEMLFDVFVDEVKSRLSGKMQ 323
Cdd:PLN02347 145 G--DEAVKLPEGFEVVAKSVQG-AVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTADWKMQ 212
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1268-1295 |
3.72e-03 |
|
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: 38.43 E-value: 3.72e-03
10 20
....*....|....*....|....*...
gi 86450145 1268 RAILLSIGSFKhKVELLPSIRDLAKMGY 1295
Cdd:cd01423 1 KGILISIGSYS-KPELLPTAQKLSKLGY 27
|
|
| |
