|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
344-1276 |
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: 1519.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 344 ERPRKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSTGLADKVYFLPLTPEYVEQVIKAERPN 423
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 424 GVLLTFGGQTALNCGVELDRSGIFSKYNVKIMGTPIQSIIETEDRKIFAERVAQIGEKVAPSEAVYSVKEALDAATKLGY 503
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 504 PVMARAAFSLGGLGSGFANNEKELQELAQQAFAHS--NQLIVDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHT 581
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 582 GESIVVAPSQTLSNREYNMLRSTAIKVIRHFGIVGECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAK 661
Cdd:TIGR01369 244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 662 LCLAIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFTRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETV 741
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 742 NGFDPYIKPV-----REEELIQATDKRIFVLSAALKANYTVEKLHELTKIDPWFLNKMKNIIGYLNFLEEQGNN-LDRNM 815
Cdd:TIGR01369 404 TGFDLPDREVepdedLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTdLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 816 LLQAKKLGFSDKQIAAAIKVTDLVIRKQREEMKVISFVKQIDTVAGEWPATTNYLYLTYNAEDHDIDFPGGFTIVV-GSG 894
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 895 VYRIGSSVEFDLCAVGCLRELRKLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVEGIILSMGGQLPN 974
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 975 NIAMDLHRQQAKVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIEFCDEVGYPCLVRPSYVLSGAAMNVA 1054
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1055 YSNQDLETYLNAASFVSKEHPVVISKFLTEAKEIDVDAVAADGEILCMAVSEHVENAGVHSGDATLVTPPQDINAETLVK 1134
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1135 IKGIVRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMPVEPVEVL--HGCGKV 1212
Cdd:TIGR01369 804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEPKYV 883
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450127 1213 GVKVPQFSFSRLAGADVQLGVEMASTGEVACQGDNRYEAYLKAMMSTGFQIPKKAILLSIGSFK 1276
Cdd:TIGR01369 884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDK 947
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
347-1272 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1308.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 347 RKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSTGLADKVYFLPLTPEYVEQVIKAERPNGVL 426
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 427 LTFGGQTALNCGVELDRSGIFSKYNVKIMGTPIQSIIETEDRKIFAERVAQIGEKVAPSEAVYSVKEALDAATKLGYPVM 506
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 507 ARAAFSLGGLGSGFANNEKELQELAQQAFAHS--NQLIVDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGES 584
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 585 IVVAPSQTLSNREYNMLRSTAIKVIRHFGIV-GECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLC 663
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 664 LAIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFTRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVNG 743
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 744 FDPYIKPVR-----EEELIQATDKRIFVLSAALKANYTVEKLHELTKIDPWFLNKMKNIIGYLNFLEEQGNNLDRNMLLQ 818
Cdd:PRK05294 408 LDEDLFEEEsleelREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLRE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 819 AKKLGFSDKQIAAAIKVTDLVIRKQREEMKVISFVKQIDTVAGEWPATTNYLYLTYNAEDHDIDFPGGFTIVVGSGVYRI 898
Cdd:PRK05294 488 AKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNRI 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 899 GSSVEFDLCAVGCLRELRKLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVEGIILSMGGQLPNNIAM 978
Cdd:PRK05294 568 GQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLAK 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 979 DLHRQQAKVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIEFCDEVGYPCLVRPSYVLSGAAMNVAYSNQ 1058
Cdd:PRK05294 648 ALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEE 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1059 DLETYLNAASFVSKEHPVVISKFLTEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDINAETLVKIKG 1137
Cdd:PRK05294 728 ELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEdVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIRE 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1138 IVRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMPVEPVEVLHGC--GKVGVK 1215
Cdd:PRK05294 807 YTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPYVAVK 886
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 86450127 1216 VPQFSFSRLAGADVQLGVEMASTGEVACQGDNRYEAYLKAMMSTGFQIPKK-AILLSI 1272
Cdd:PRK05294 887 EAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV 944
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
347-1266 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1012.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 347 RKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSTGLADKVYFLPLTPEYVEQVIKAERPNGVL 426
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 427 LTFGGQTALNCGVELDRSGIFSKYNVKIMGTPIQSIIETEDRKIFAERVAQIGEKVAPSEAVYSVKEALDAATKLGYPVM 506
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 507 ARAAFSLGGLGSGFANNEKELQELAQQAFAHS--NQLIVDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGES 584
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQASpiHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 585 IVVAPSQTLSNREYNMLRSTAIKVIRHFGIVGECNIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLCL 664
Cdd:PRK12815 248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 665 AIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFTRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVNGF 744
Cdd:PRK12815 328 GYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 745 DPYIK--PVREEELIQ----ATDKRIFVLSAALKANYTVEKLHELTKIDPWFLNKMKNIIGYLNFLEEQGNNLDRNMLLQ 818
Cdd:PRK12815 408 SLPIElsGKSDEELLQdlrhPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLDLSADLLRK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 819 AKKLGFSDKQIAAAIKVTDLVIRKQREEMKVISFVKQIDTVAGEWPATTNYLYLTYNAEDhDIDFPGG--FTIVVGSGVY 896
Cdd:PRK12815 488 VKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGES-EAEPSSEkkKVLILGSGPI 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 897 RIGSSVEFDLCAVGCLRELRKLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVEGIILSMGGQLPNNI 976
Cdd:PRK12815 567 RIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAINL 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 977 AMDLHRQQAKVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIEFCDEVGYPCLVRPSYVLSGAAMNVAYS 1056
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYD 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1057 NQDLETYLNAAsfVSKEHPVVISKFLtEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDINAETLVKI 1135
Cdd:PRK12815 727 EPALEAYLAEN--ASQLYPILIDQFI-DGKEYEVDAI-SDGEdVTIPGIIEHIEQAGVHSGDSIAVLPPQSLSEEQQEKI 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1136 KGIVRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMPVE----PVEVLHGCGK 1211
Cdd:PRK12815 803 RDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAelgyPNGLWPGSPF 882
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 86450127 1212 VGVKVPQFSFSRLAGADVQLGVEMASTGEVACQGDNRYEAYLKAMMSTGFQIPKK 1266
Cdd:PRK12815 883 IHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSY 937
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
347-1265 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 838.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 347 RKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSTGLADKVYFLPLTPEYVEQVIKAERPNGVL 426
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 427 LTFGGQTALNCGVELDRSGIFSKYNVKIMGTPIQSIIETEDRKIFAERVAQIGEKVAPSEAVYSVKEALDAATKLG-YPV 505
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 506 MARAAFSLGGLGSGFANNEKELQELAQQAFAHS--NQLIVDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGE 583
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAASitSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 584 SIVVAPSQTLSNREYNMLRSTAIKVIRHFGIvgEC---NIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAA 660
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 661 KLCLAIPLPDIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFTRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDET 740
Cdd:PLN02735 342 KLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 741 VNGFDPyiKPVRE---------EELIQATDKRIFVLSAALKANYTVEKLHELTKIDPWFLNKMKNIIGYLNFLEEQG-NN 810
Cdd:PLN02735 422 FSGWGC--AKVKEldwdweqlkYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSlSE 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 811 LDRNMLLQAKKLGFSDKQIAAAIKVTDLVIRKQREEMKVISFVKQIDTVAGEWPATTNYLYLTYNAEDHDIDFPGGFTIV 890
Cdd:PLN02735 500 LSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLI 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 891 VGSGVYRIGSSVEFDLCAVGCLRELRKLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVEGIILSMGG 970
Cdd:PLN02735 580 LGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGG 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 971 QLPNNIAMDLHRQ-------------QAKVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIEFCDEVGYP 1037
Cdd:PLN02735 660 QTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYP 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1038 CLVRPSYVLSGAAMNVAYSNQDLETYLNAASFVSKEHPVVISKFLTEAKEIDVDAVA-ADGEILCMAVSEHVENAGVHSG 1116
Cdd:PLN02735 740 VVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSG 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1117 DATLVTPPQDINAETLVKIKGIVRDLAALLDVTGPFNMQL-IAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAI 1195
Cdd:PLN02735 820 DSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVM 899
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450127 1196 IGMPV------EPVEVLHgcgkVGVKVPQFSFSRLAGADVQLGVEMASTGEVACQGDNRYEAYLKAMMSTGFQIPK 1265
Cdd:PLN02735 900 SGKSLkdlgftEEVIPAH----VSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPL 971
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
352-893 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 650.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 352 LGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSTGLADKVYFLPLTPEYVEQVIKAERPNGVLLTFGG 431
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 432 QTALNCGVELDRSGIFSkyNVKIMGTPIQSIIETEDRKIFAERVAQIGEKVAPSEAVYSVKEALDAATKLGYPVMARAAF 511
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 512 SLGGLGSGFANNEKELQELAQQAFAHS--NQLIVDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLGIHTGESIVVAP 589
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 590 SQTLSNREYNMLRSTAIKVIRHFGIVGECNIQYALNpeSEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLCLAIPLP 669
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 670 DIKNSvTGvttacFEPSLDYCVVKIPRWDLAKFTRVSKNIGSSMKSVGEVMAIGRNFEEAFQKALRMVDETVNG--FDPY 747
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 748 IKPVREEE--LIQATDKRIFVLSAALKANYTVEKLHELTKIDPWFLNKMKNIIgyLNFLEEQGNNLDRNMLLQAKKLGFS 825
Cdd:COG0458 391 VADDDKEEalLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPII--VDEIELEEIILVINTLLGAKSLGDS 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450127 826 DKQIAAAIKVTDLVIRKQREEMKVISFVKQIDTVAGEWPATTNYLYLTYNAEDHDIDFPGGFTIVVGS 893
Cdd:COG0458 469 DGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
891-1269 |
2.02e-148 |
|
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: 458.96 E-value: 2.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 891 VGSGVYRIGSSVEFDLCAVGCLRELRKLGRSTIMINYNPETVSTDYDMCDRLYFEEISFEVVMDIYQIENVEGIILSMGG 970
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 971 QLPNNIAMDLHRQQA----KVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIEFCDEVGYPCLVRPSYVL 1046
Cdd:COG0458 81 QTALNLAVELEEAGIlegvKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1047 SGAAMNVAYSNQDLETYLNAASFVSKEHPVVISKFLTEAKEIDVDAVA-ADGEILCMAVSEHVENAGVHSGDATLVTPPQ 1125
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRdGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1126 DINAETLVKIKGIVRDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAIIGMPVEPVEV 1205
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450127 1206 LHG----CGKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACQGDNRYEAYLKAMMSTGFQIPKKAIL 1269
Cdd:COG0458 321 DTGfeptLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLL 388
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-312 |
3.51e-128 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 398.68 E-value: 3.51e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1 QILVLTYPLIGNYGVPSADeideyglpkhFEwFDGISIAGLVVGEACITPSHWRQTCTLSKWMEAQGIPGISDIDTRALT 80
Cdd:PRK12564 51 QIVTFTYPLIGNYGVNRED----------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 81 KKIRENGSILGKIIYEQPDIK--IDMKLTDPNL--RNLVAECSVRTVKTFNASGS---PRICAIDCGLKLNQIRCFIARG 153
Cdd:PRK12564 120 RKLREKGAMKGVIATEDFDAEelLEKARAFPGLlgLDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILRELAERG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 154 ARVDLVPWNH------NLNPnefDGLFLSNGPGDPIVCSDTVKQIEKIISTsNIPIFGICLGHQLLATAIGCKTYKLKYG 227
Cdd:PRK12564 200 CRVTVVPATTtaeeilALNP---DGVFLSNGPGDPAALDYAIEMIRELLEK-KIPIFGICLGHQLLALALGAKTYKMKFG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 228 NRGHNLPCIHHGTGRCFMTSQNHGFAVDAKTLPKDWEPLFTNVNDKSNEGIVHAEKPYFSVQFHPEHTPGPEDLELLFDV 307
Cdd:PRK12564 276 HRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDE 355
|
....*
gi 86450127 308 FLNAI 312
Cdd:PRK12564 356 FVELM 360
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-313 |
1.74e-126 |
|
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: 393.92 E-value: 1.74e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1 QILVLTYPLIGNYGVPsadeideyglPKHFEwFDGISIAGLVVGEACITPSHWRQTCTLSKWMEAQGIPGISDIDTRALT 80
Cdd:TIGR01368 47 QIVVFTYPLIGNYGVN----------DEDAE-SKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 81 KKIRENGSILGKIIYEQPDIK--IDMKLTDPNLR--NLVAECSVRTVKTFNASGSP--RICAIDCGLKLNQIRCFIARGA 154
Cdd:TIGR01368 116 KKIREKGTMKGVISTEDSNDEelVEKARVSPDITgiNLVAEVSTKEPYTWGQRGGKgkRVVVIDFGVKRNILRRLVKRGC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 155 RVDLVPWNH------NLNPnefDGLFLSNGPGDPIVCSDTVKQIEKIISTsnIPIFGICLGHQLLATAIGCKTYKLKYGN 228
Cdd:TIGR01368 196 EVTVVPYDTdaeeikKYNP---DGIFLSNGPGDPAAVEPAIETIRKLLEK--IPIFGICLGHQLLALAFGAKTYKMKFGH 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 229 RGHNLPCIHHGTGRCFMTSQNHGFAVDAKTLPK-DWEPLFTNVNDKSNEGIVHAEKPYFSVQFHPEHTPGPEDLELLFDV 307
Cdd:TIGR01368 271 RGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDE 350
|
....*.
gi 86450127 308 FLNAIK 313
Cdd:TIGR01368 351 FIDLMK 356
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-313 |
6.88e-125 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 389.77 E-value: 6.88e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1 QILVLTYPLIGNYGVPSADeideyglpkhFEwFDGISIAGLVVGEACITPSHWRQTCTLSKWMEAQGIPGISDIDTRALT 80
Cdd:COG0505 51 QIVTFTYPHIGNYGVNDED----------FE-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 81 KKIRENGSILGKIIYEQPDIKIDMKL----TDPNLRNLVAECSVRTVKTFNASG--SPRICAIDCGLKLNQIRCFIARGA 154
Cdd:COG0505 120 RHLREKGAMKGVISTGDLDIEELLEKaraaPGMEGLDLVKEVSTKEPYEWTEAPgaGFHVVALDFGVKRNILRELAERGC 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 155 RVDLVPWN------HNLNPnefDGLFLSNGPGDPIVCSDTVKQIEKIIsTSNIPIFGICLGHQLLATAIGCKTYKLKYGN 228
Cdd:COG0505 200 RVTVVPATtsaeeiLALNP---DGVFLSNGPGDPAALDYAIETIRELL-GKGIPIFGICLGHQLLALALGAKTYKLKFGH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 229 RGHNLPCIHHGTGRCFMTSQNHGFAVDAKTLPK-DWEPLFTNVNDKSNEGIVHAEKPYFSVQFHPEHTPGPEDLELLFDV 307
Cdd:COG0505 276 RGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDR 355
|
....*.
gi 86450127 308 FLNAIK 313
Cdd:COG0505 356 FIELME 361
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
1-313 |
4.98e-99 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 319.91 E-value: 4.98e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1 QILVLTYPLIGNYGVPSADeideyglpkhFEWFDgISIAGLVVGEACITPSHWRQTCTLSKWMEAQGIPGISDIDTRALT 80
Cdd:PRK12838 49 QIVVFTYPLIGNYGINADD----------YESKQ-PQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 81 KKIRENGSILGKIIYEQPDIKIDMKLTDPNLRNLVAECSVRTVKTFNASGsPRICAIDCGLKLNQIRCFIARGARVDLVP 160
Cdd:PRK12838 118 KHIREKGTMKASITTTDDAHAFDQIKALVLPKNVVAQVSTKEPYTYGNGG-KHVALIDFGYKKSILRSLSKRGCKVTVLP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 161 WN------HNLNPnefDGLFLSNGPGDPIVCSDTVKQIEKIISTsnIPIFGICLGHQLLATAIGCKTYKLKYGNRGHNLP 234
Cdd:PRK12838 197 YDtsleeiKNLNP---DGIVLSNGPGDPKELQPYLPEIKKLISS--YPILGICLGHQLIALALGADTEKLPFGHRGANHP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 235 CIHHGTGRCFMTSQNHGFAVDAKTL-PKDWEPLFTNVNDKSNEGIVHAEKPYFSVQFHPEHTPGPEDLELLFDVFLNAIK 313
Cdd:PRK12838 272 VIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMME 351
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
134-309 |
1.59e-95 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 303.26 E-value: 1.59e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 134 ICAIDCGLKLNQIRCFIARGARVDLVPWNH------NLNPnefDGLFLSNGPGDPIVCSDTVKQIEKIIStSNIPIFGIC 207
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTdaeeilKLDP---DGIFLSNGPGDPALLDEAIKTVRKLLG-KKIPIFGIC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 208 LGHQLLATAIGCKTYKLKYGNRGHNLPCIHHGTGRCFMTSQNHGFAVDAKTLPKDWEPLFTNVNDKSNEGIVHAEKPYFS 287
Cdd:cd01744 77 LGHQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFS 156
|
170 180
....*....|....*....|..
gi 86450127 288 VQFHPEHTPGPEDLELLFDVFL 309
Cdd:cd01744 157 VQFHPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
467-669 |
2.89e-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: 303.84 E-value: 2.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 467 DRKIFAERVAQIGEKVAPSEAVY--SVKEALDAATKLGYPVMARAAFSLGGLGSGFANNEKELQELAQQAFAHS------ 538
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 539 NQLIVDKSLRGWKEVEYEVVRDAFDNCITVCNMENLDPLgiHTGESIVVAPSQTLSNREYNMLRSTAIKVIRHFGIVGEC 618
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 86450127 619 NIQYALNPESEEYYIIEVNARLSRSSALASKATGYPLAYVAAKLCLAIPLP 669
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
334-735 |
7.08e-83 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 294.21 E-value: 7.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 334 YTPKPEFINFERPRKILILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSTGLADKVYFLPLTPEYV 413
Cdd:TIGR01369 542 YEGERDDVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDV 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 414 EQVIKAERPNGVLLTFGGQTALNCGVELDRSGifskynVKIMGTPIQSIIETEDRKIFAERVAQIGEKVAPSEAVYSVKE 493
Cdd:TIGR01369 622 MNIIELEKPEGVIVQFGGQTPLNLAKALEEAG------VPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEE 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 494 ALDAATKLGYPVMARAAFSLGGLGSGFANNEKELQELAQQAFAHSNQ--LIVDKSLRGWKEVEYEVVRDafDNCITVCN- 570
Cdd:TIGR01369 696 AVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAVSD--GEEVLIPGi 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 571 MENLDPLGIHTGESIVVAPSQTLSNREYNMLRSTAIKVIRHFGIVGECNIQYALnpESEEYYIIEVNARLSRSSALASKA 650
Cdd:TIGR01369 774 MEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGEVYVIEVNPRASRTVPFVSKA 851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 651 TGYPLAYVAAKLCLAIPLPDIknsvtGVTtacFEPSLDYCVVKIPRWDLAKFTRVSKNIGSSMKSVGEVMAIGRNFEEAF 730
Cdd:TIGR01369 852 TGVPLAKLAVRVMLGKKLEEL-----GVG---KEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAF 923
|
....*
gi 86450127 731 QKALR 735
Cdd:TIGR01369 924 LKAQL 928
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-320 |
2.78e-67 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 232.38 E-value: 2.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1 QILVLTYPLIGNYGVPSADEIDEYglpkhfewfdgISIAGLVVGEACITPSHWRQTCTLSKWMEAQGIPGISDIDTRALT 80
Cdd:CHL00197 53 QIVTFTYPEIGNTGINLEDIESVK-----------IQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 81 KKIRENGSILGKI-------IYEQPDIKIDMKLTDPNLRNLVA--------ECSVR----TVKTFNASGSP-RICAIDCG 140
Cdd:CHL00197 122 QHLRRFGTMNGCIsnqnlnlSYLRAKIKESPHMPSSDLIPRVTtssyyewdEKSHPsfylADNKRPHSSYQlKIIVIDFG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 141 LKLNQIRCFIARGARVDLVP-------WNhNLNPnefDGLFLSNGPGDPIVCSDTVKQIEKIIStSNIPIFGICLGHQLL 213
Cdd:CHL00197 202 VKYNILRRLKSFGCSITVVPatspyqdIL-SYQP---DGILLSNGPGDPSAIHYGIKTVKKLLK-YNIPIFGICMGHQIL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 214 ATAIGCKTYKLKYGNRGhnlpcIHHGTG---RCFMTSQNHGFAVDAKTLPKDwePLFT---NVNDKSNEGIVHAEKPYFS 287
Cdd:CHL00197 277 SLALEAKTFKLKFGHRG-----LNHPSGlnqQVEITSQNHGFAVNLESLAKN--KFYIthfNLNDGTVAGISHSPKPYFS 349
|
330 340 350
....*....|....*....|....*....|...
gi 86450127 288 VQFHPEHTPGPEDLELLFDVFlnaikIRLMKKS 320
Cdd:CHL00197 350 VQYHPEASPGPHDADYLFEYF-----IEIIKHS 377
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
137-311 |
3.25e-59 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 201.70 E-value: 3.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 137 IDCGL--KLNQIRCFIARGARVDLVPWNHNLN---PNEFDGLFLSNGPGDPIVCSDTVKQIEKIIsTSNIPIFGICLGHQ 211
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTPAEeilEENPDGIILSGGPGSPGAAGGAIEAIREAR-ELKIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 212 LLATAIGCKTYKLK-YGNRGHNLPCIH------HGTGRCFMTSQNHGFAVDAKTLPKDWEPLFTNVNDKSNEGIVHAEKP 284
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*..
gi 86450127 285 YFSVQFHPEHTPGPEDLELLFDVFLNA 311
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
1-305 |
2.54e-53 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 192.89 E-value: 2.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1 QILVLTYPLIGNYGVPSADEideyglpKHFEWFdgisIAGLVVGEACITPSHWRQTCTLSKWMEAQGIPGISDIDTRALT 80
Cdd:PLN02771 103 QFVLMTNPHIGNTGVNFDDE-------ESRQCF----LAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAIT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 81 KKIRENGSILGKIIYEqpDIKIDMKLTDPNLR------NLVAECSVRTV-----KT-----FNASG----SPRICAIDCG 140
Cdd:PLN02771 172 RRLREDGSLIGVLSTE--DSKTDEELLKMSRSwdivgiDLISGVSCKSPyewvdKTnpewdFNTNSrdgeSYHVIAYDFG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 141 LKLNQIRCFIARGARVDLVPWNH------NLNPnefDGLFLSNGPGDPIVCSDTVKQIEKIIStsNIPIFGICLGHQLLA 214
Cdd:PLN02771 250 IKHNILRRLASYGCKITVVPSTWpasealKMKP---DGVLFSNGPGDPSAVPYAVETVKELLG--KVPVFGICMGHQLLG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 215 TAIGCKTYKLKYGNRGHNLPCIHHGTGRCFMTSQNHGFAVDAKTLPKDWEPLFTNVNDKSNEGIVHAEKPYFSVQFHPEH 294
Cdd:PLN02771 325 QALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEA 404
|
330
....*....|.
gi 86450127 295 TPGPEDLELLF 305
Cdd:PLN02771 405 SPGPHDSDNAF 415
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
753-874 |
8.56e-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: 174.95 E-value: 8.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 753 EEELIQATDKRIFVLSAALKANYTVEKLHELTKIDPWFLNKMKNIIGYLNFLEEQG-NNLDRNMLLQAKKLGFSDKQIAA 831
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGlDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 86450127 832 AIKVTDLVIRKQREEMKVISFVKQIDTVAGEWPATTNYLYLTY 874
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
1.61e-39 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 142.85 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1 QILVLTYPLIGNYGVPSADeideyglpkhFEwFDGISIAGLVVGEACITPSHWRQTCTLSKWMEAQGIPGISDIDTRALT 80
Cdd:pfam00988 45 QIVVFTYPLIGNYGVNPED----------FE-SDKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALT 113
|
90
....*....|...
gi 86450127 81 KKIRENGSILGKI 93
Cdd:pfam00988 114 RKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
8.63e-37 |
|
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: 135.19 E-value: 8.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1 QILVLTYPLIGNYGVPSADeideyglpkhFEWfDGISIAGLVVGEACITPSHWRQTCTLSKWMEAQGIPGISDIDTRALT 80
Cdd:smart01097 49 QIVVFTYPLIGNYGVNDED----------FES-DKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALT 117
|
90
....*....|...
gi 86450127 81 KKIRENGSILGKI 93
Cdd:smart01097 118 RKLREKGAMKGVI 130
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
754-831 |
2.96e-34 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 125.95 E-value: 2.96e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450127 754 EELIQATDKRIFVLSAALKANYTVEKLHELTKIDPWFLNKMKNIIGYLNFLEEQGNNLDRNMLLQAKKLGFSDKQIAA 831
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDAELLREAKRLGFSDRQIAK 78
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
153-293 |
1.98e-20 |
|
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: 90.29 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 153 GARVDLVPwNHNLNPNE-----FDGLFLSNGPGDP---IVCSDTVKQIEKiistsNIPIFGICLGHQLLATAIGCKTYKL 224
Cdd:cd01743 22 GAEVVVVR-NDEITLEElellnPDAIVISPGPGHPedaGISLEIIRALAG-----KVPILGVCLGHQAIAEAFGGKVVRA 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450127 225 KYGNRGHNLPCIHHGTGRCFMTSQN------HGFAVDAKTLPKDWEplftnVNDKSNEGIVHA----EKPYFSVQFHPE 293
Cdd:cd01743 96 PEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLE-----VTASTEDGVIMAlrhrDLPIYGVQFHPE 169
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
989-1173 |
8.51e-19 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 87.62 E-value: 8.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 989 GTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIEFCDEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAS 1068
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1069 ----FVSKEHPVVISKFLtEAKEIDVDAVAADGEILCMAVSEHvENAGVHSGDATLVTPPqDINAETLVKIKGIVRDLAA 1144
Cdd:COG0439 123 aeakAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGELVARALR 199
|
170 180 190
....*....|....*....|....*....|.
gi 86450127 1145 LLDV-TGPFNMQ-LIAKNNELKVIECNVRVS 1173
Cdd:COG0439 200 ALGYrRGAFHTEfLLTPDGEPYLIEINARLG 230
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
133-296 |
5.62e-17 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 81.53 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 133 RICAIDCGLKLNQI-----RCFIARGARVDLV------PWNHNLNPNEFDGLFLSNGPG---DPIVCSDTVKQIEKIIST 198
Cdd:COG0518 1 KILILDHDPFGGQYpgliaRRLREAGIELDVLrvyageILPYDPDLEDPDGLILSGGPMsvyDEDPWLEDEPALIREAFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 199 SNIPIFGICLGHQLLATAIGCKTYKLKYGNRG-------------HNLPcihhGTGRCFMTsqnHGFAVDakTLPKDWEP 265
Cdd:COG0518 81 LGKPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelteadplfAGLP----DEFTVWMS---HGDTVT--ELPEGAEV 151
|
170 180 190
....*....|....*....|....*....|.
gi 86450127 266 LFTNVNDKsNEGIVHaEKPYFSVQFHPEHTP 296
Cdd:COG0518 152 LASSDNCP-NQAFRY-GRRVYGVQFHPEVTH 180
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1023-1201 |
7.13e-16 |
|
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: 77.73 E-value: 7.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1023 NLKSAIEFCDEVGYPCLVRPSYVLSGAAMNVAYSNQDL----ETYLNAASFVSKEHPVVISKFLTEAKEIDVDaVAADGE 1098
Cdd:pfam02786 26 TEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELaelfALALAEAPAAFGNPQVLVEKSLKGPKHIEYQ-VLRDAH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1099 ILCMAVSEhVENA-GVHSGDATLVTPPQDINAETLVKIKGIVRDLAALLDVTGPFNMQLI--AKNNELKVIECNVRVSRS 1175
Cdd:pfam02786 105 GNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFAldPFSGEYYFIEMNTRLQVE 183
|
170 180
....*....|....*....|....*.
gi 86450127 1176 FPFVSKTLNHDFVATATRAIIGMPVE 1201
Cdd:pfam02786 184 HALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
473-667 |
1.12e-15 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 78.38 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 473 ERVAQIGEKVAPSEAVYSVKEALDAATKLGYPVMARAAFSLGGLGSGFANNEKELQELAQQAFAHSN------QLIVDKS 546
Cdd:COG0439 60 EALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKagspngEVLVEEF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 547 LRGwKEVEYEVVrdAFDNCITVCNM---ENLDPLGIHTGEsivVAPSQtLSNREYNMLRSTAIKVIRHFGIV-GECNIQY 622
Cdd:COG0439 140 LEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEF 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 86450127 623 ALNPEsEEYYIIEVNARLS--RSSALASKATGYPLAYVAAKLCLAIP 667
Cdd:COG0439 213 LLTPD-GEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
171-314 |
4.63e-15 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 74.89 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 171 DGLFLSNGPGdpivcSDTVKQIEKIISTSNIPIFGICLGHQLLATAIGCKTYKLKYGNRG--------HNLPCIhhGTGR 242
Cdd:PRK00758 43 DGLILSGGPD-----IERAGNCPEYLKELDVPILGICLGHQLIAKAFGGEVGRGEYGEYAlveveildEDDILK--GLPP 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450127 243 CFMTSQNHGFAVdaKTLPKDWEPLFTNVNDKsNEGIVHAEKPYFSVQFHPE--HTPGPEdlellfDVFLNAIKI 314
Cdd:PRK00758 116 EIRVWASHADEV--KELPDGFEILARSDICE-VEAMKHKEKPIYGVQFHPEvaHTEYGE------EIFKNFLEI 180
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
155-293 |
1.51e-14 |
|
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: 73.53 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 155 RVDLVPWNHnLNPNEFDGLFLSNGPGDP---IVCSDTVKQIEKiistsNIPIFGICLGHQLLATAIGCKTYKLKYgnrgh 231
Cdd:COG0512 29 RNDEITLEE-IEALAPDGIVLSPGPGTPeeaGISLEVIRAFAG-----KIPILGVCLGHQAIGEAFGGKVVRAPE----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 232 nlpcIHHGtgrcfMTSQ-------------N-------HGFAVDAKTLPKDWEplftnVNDKSNEGIV----HAEKPYFS 287
Cdd:COG0512 98 ----PMHG-----KTSPithdgsglfaglpNpftatryHSLVVDRETLPDELE-----VTAWTEDGEImgirHRELPIEG 163
|
....*.
gi 86450127 288 VQFHPE 293
Cdd:COG0512 164 VQFHPE 169
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
134-304 |
8.18e-14 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 71.19 E-value: 8.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 134 ICAIDCGLKLNQIrcfIARGAR-----VDLVPWNHNL------NPNefdGLFLSNGPGdpIVCSDTVKQIEKIISTSNIP 202
Cdd:TIGR00888 1 ILVLDFGSQYTQL---IARRLRelgvySELVPNTTPLeeirekNPK---GIILSGGPS--SVYAENAPRADEKIFELGVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 203 IFGICLGHQLLATAIGCKTYKLKYGNRGH------NLPCIHHGTGRCFMTSQNHGFAVdaKTLPKDWEPLFTNVNDKsNE 276
Cdd:TIGR00888 73 VLGICYGMQLMAKQLGGEVGRAEKREYGKaeleilDEDDLFRGLPDESTVWMSHGDKV--KELPEGFKVLATSDNCP-VA 149
|
170 180
....*....|....*....|....*...
gi 86450127 277 GIVHAEKPYFSVQFHPEHTPGPEDLELL 304
Cdd:TIGR00888 150 AMAHEEKPIYGVQFHPEVTHTEYGNELL 177
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
165-365 |
9.26e-14 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 75.52 E-value: 9.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 165 LNPnefDGLFLSNGPGDPI---VCSDTVKQIEKiistsNIPIFGICLGHQLLATAIGCKTYKLKYGNRGHNLPCIHHGTG 241
Cdd:PRK14607 43 LNP---SHIVISPGPGRPEeagISVEVIRHFSG-----KVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 242 rCFMTSQN-------HGFAVDAKTLPKDWEplftnVNDKSNEG----IVHAEKPYFSVQFHPEhTPGPEDLELLFDVFLN 310
Cdd:PRK14607 115 -LFRGIPNptvatryHSLVVEEASLPECLE-----VTAKSDDGeimgIRHKEHPIFGVQFHPE-SILTEEGKRILKNFLN 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 86450127 311 aikirlMKKSDISIKNVlierLKYTPKPEFINFERPRKIL-ILGSGGLSIGQAGEF 365
Cdd:PRK14607 188 ------YQREEIDIKSY----LKKLVEGEDLSFEEAEDVMeDITDGNATDAQIAGF 233
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
150-296 |
1.26e-13 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 70.64 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 150 IAR-----GARVDLVPWN---HNLNPNEFDGLFLSNGPgdPIVCSDTVKQIEKIISTSNIPIFGICLGHQLLATAIGCKT 221
Cdd:cd01742 14 IARrvrelGVYSEILPNTtplEEIKLKNPKGIILSGGP--SSVYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALGGKV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 222 YKLKYGNRGHNLPCIHHGTG---------RCFMtsqNHGFAVDAktLPKDWEPLFTNVNDKsNEGIVHAEKPYFSVQFHP 292
Cdd:cd01742 92 ERGDKREYGKAEIEIDDSSPlfeglpdeqTVWM---SHGDEVVK--LPEGFKVIASSDNCP-VAAIANEEKKIYGVQFHP 165
|
....*.
gi 86450127 293 E--HTP 296
Cdd:cd01742 166 EvtHTE 171
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
167-294 |
1.23e-12 |
|
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: 67.66 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 167 PNEFDGLFLSNGPGDPIVC-----SDTVKQIEKIIsTSNIPIFGICLGHQLLATAIGCKTYKLKYG-----------NRG 230
Cdd:cd01741 44 LDDYDGLVILGGPMSVDEDdypwlKKLKELIRQAL-AAGKPVLGICLGHQLLARALGGKVGRNPKGweigwfpvtltEAG 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450127 231 HNLPcIHHGTGRCFMTSQNHGFAVDAktLPKDWEPLFTnvNDKSNEGIVHAEKPYFSVQFHPEH 294
Cdd:cd01741 123 KADP-LFAGLPDEFPVFHWHGDTVVE--LPPGAVLLAS--SEACPNQAFRYGDRALGLQFHPEE 181
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
144-293 |
1.77e-12 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 67.51 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 144 NQIRCFIARGARVdLVPWNHNLNPNEFDGLF-----LSNGPGDPIVCSDTVKQIEKIisTSNIPIFGICLGHQLLATAIG 218
Cdd:TIGR00566 14 NLVQYFCELGAEV-VVKRNDSLTLQEIEALLpllivISPGPCTPNEAGISLEAIRHF--AGKLPILGVCLGHQAMGQAFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 219 CKTYKLKYGNRGHNLPCIHHGTGRC------FMTSQNHGFAVDAKTLPKDWEPLFTNVNDKSNEGIVHAEKPYFSVQFHP 292
Cdd:TIGR00566 91 GDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHP 170
|
.
gi 86450127 293 E 293
Cdd:TIGR00566 171 E 171
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
458-640 |
6.12e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 69.29 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 458 PIQSIIETEDRKIFAER-VAQIGEKVAP--SEAVYSVKEALDAATKLGYPVMARAAFSLGGLGSGFANNEKEL------- 527
Cdd:PRK06111 105 PSADIIAKMGSKIEARRaMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELtkafesn 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 528 QELAQQAFAHSnQLIVDKSLRGWKEVEYEVVRDAFDNCitvcnmenldplgIHTGE---SI------VV--APSQTLSNR 596
Cdd:PRK06111 185 KKRAANFFGNG-EMYIEKYIEDPRHIEIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPFLDEE 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 86450127 597 EYNMLRSTAIKVIRHFGIVGECNIQYaLNPESEEYYIIEVNARL 640
Cdd:PRK06111 251 TRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFYFLEMNTRL 293
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
169-293 |
7.59e-12 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 66.23 E-value: 7.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 169 EFDGLFLSNGPGDPI---VCSDTVKQIEKiistSNIPIFGICLGHQLLATAIGC-----------KTYKLKYGNRGhnlp 234
Cdd:PRK07765 46 QFDGVLLSPGPGTPEragASIDMVRACAA----AGTPLLGVCLGHQAIGVAFGAtvdrapellhgKTSSVHHTGVG---- 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86450127 235 cIHHGTGRCFMTSQNHGFAVDAKTLPKDWEplftnVNDKSNEGIV----HAEKPYFSVQFHPE 293
Cdd:PRK07765 118 -VLAGLPDPFTATRYHSLTILPETLPAELE-----VTARTDSGVImavrHRELPIHGVQFHPE 174
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
165-293 |
9.88e-12 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 65.15 E-value: 9.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 165 LNPnefDGLFLSNGPGDPivcsDTVKQIEKIIST--SNIPIFGICLGHQLLATAIGCKTYKLKYGNRGHNLPCIHHGTG- 241
Cdd:PRK05670 42 LNP---DAIVLSPGPGTP----AEAGISLELIREfaGKVPILGVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGi 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86450127 242 -----RCFMTSQNHGFAVDAKTLPKDWEplftnVNDKSNEGIV----HAEKPYFSVQFHPE 293
Cdd:PRK05670 115 faglpNPFTVTRYHSLVVDRESLPDCLE-----VTAWTDDGEImgvrHKELPIYGVQFHPE 170
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
986-1178 |
1.67e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 67.22 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 986 KVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIEFCD--EVGYPCLVRPSYVLSGAAMNVAYSNQDLETY 1063
Cdd:PRK12767 97 KVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAkgELQFPLFVKPRDGSASIGVFKVNDKEELEFL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1064 LNAASfvskehPVVISKFLtEAKEIDVDA-VAADGEILCMAVSEHVEnagVHSGDA-TLVTPPQDinaetlvKIKGIVRD 1141
Cdd:PRK12767 177 LEYVP------NLIIQEFI-EGQEYTVDVlCDLNGEVISIVPRKRIE---VRAGETsKGVTVKDP-------ELFKLAER 239
|
170 180 190
....*....|....*....|....*....|....*..
gi 86450127 1142 LAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPF 1178
Cdd:PRK12767 240 LAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
153-293 |
5.76e-10 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 63.78 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 153 GARVDLVPWNHN---LNPNEFDGLFLSNGPGDP--IVCSDTVKqiekIISTSNIPIFGICLGHQLLATAIGCKTYKLKY- 226
Cdd:PRK13566 550 GAEVTTVRYGFAeemLDRVNPDLVVLSPGPGRPsdFDCKATID----AALARNLPIFGVCLGLQAIVEAFGGELGQLAYp 625
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450127 227 --G------NRGHNLpcIHHGTGRCFMTSQNHGFAVDAKTLPKDWEplftnVNDKSNEGIV----HAEKPYFSVQFHPE 293
Cdd:PRK13566 626 mhGkpsrirVRGPGR--LFSGLPEEFTVGRYHSLFADPETLPDELL-----VTAETEDGVImaieHKTLPVAAVQFHPE 697
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
458-640 |
1.24e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 62.08 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 458 PIQSIIETEDRKIFAERVAQI-GEKVAPSE--AVYSVKEALDAATKLGYPVMARAAFSLGGLGSGFANNEKEL------- 527
Cdd:PRK12833 108 PDAQTIRTMGDKARARRTARRaGVPTVPGSdgVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLaaelpla 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 528 QELAQQAFAhSNQLIVDKSLRGWKEVEYEVVRDAFDnciTVCNMENLDPLGIHTGESIVVAPSQTLSNREYNMLRSTAIK 607
Cdd:PRK12833 188 QREAQAAFG-DGGVYLERFIARARHIEVQILGDGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVR 263
|
170 180 190
....*....|....*....|....*....|...
gi 86450127 608 VIRHFGIVGECNIQYALNPESEEYYIIEVNARL 640
Cdd:PRK12833 264 LARQVGYRGAGTLEYLFDDARGEFYFIEMNTRI 296
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
164-304 |
1.35e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 59.05 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 164 NLNPnefDGLFLSNGPGDPIVCSDTVKQIEKIisTSNIPIFGICLGHQLLATAIG---CKTYKLKYGNRG---HNLPCIH 237
Cdd:PRK07649 41 NMKP---DFLMISPGPCSPNEAGISMEVIRYF--AGKIPIFGVCLGHQSIAQVFGgevVRAERLMHGKTSlmhHDGKTIF 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86450127 238 HGTGRCFMTSQNHGFAVDAKTLPKDWEplftnVNDKSNEG----IVHAEKPYFSVQFHPEHTPGPEDLELL 304
Cdd:PRK07649 116 SDIPNPFTATRYHSLIVKKETLPDCLE-----VTSWTEEGeimaIRHKTLPIEGVQFHPESIMTSHGKELL 181
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
173-309 |
1.35e-09 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 59.10 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 173 LFLSNGPGDPIVCSDTVKQIEKIisTSNIPIFGICLGHQLLATAIGCKTYKLKYGNRG------HNLPCIHHGTGRCFMT 246
Cdd:PRK06774 47 LVISPGPCTPNEAGISLAVIRHF--ADKLPILGVCLGHQALGQAFGARVVRARQVMHGktsaicHSGQGVFRGLNQPLTV 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450127 247 SQNHGFAVDAKTLPKDWE-PLFTNVNDKSNE--GIVHAEKPYFSVQFHPEHTPGPEDLELLfDVFL 309
Cdd:PRK06774 125 TRYHSLVIAADSLPGCFElTAWSERGGEMDEimGIRHRTLPLEGVQFHPESILSEQGHQLL-DNFL 189
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
1012-1156 |
1.60e-09 |
|
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: 58.42 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1012 GILQPRWKELTNLKSAIEFCDEVGYPCLV---RPSYvlSGAAMNVAYSNQDLETYLNAAsfvsKEHPVVISKFLTEAKEI 1088
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEEL----GDGPVIVEEFVPFDREL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450127 1089 DVDAV-AADGEILCMAVSEHVEnagvHSGDATLVTPPQDINAETLVKIKGIVRDLAALLDVTGPFNMQL 1156
Cdd:pfam02222 78 SVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
446-640 |
1.75e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 61.68 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 446 IFSKYNVKIMGTPIQSIIETEDRKIFAERVAQIGEKVAP-SE-AVYSVKEALDAATKLGYPVMARAAFSLGGLGSGFANN 523
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 524 EKELQEL-------AQQAFAhSNQLIVDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGESIVVAPSQT 592
Cdd:PRK08462 176 ESDLENLylaaeseALSAFG-DGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVV 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 86450127 593 LSNREYNMLRSTAIKVIRHFGIVGECNIQYALNpESEEYYIIEVNARL 640
Cdd:PRK08462 249 LDEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRL 295
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
344-678 |
2.01e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 61.10 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 344 ERPRKILILGS--GGLSIgqagefdysgsqaIKALKEEKIQTILINPNIATVQTSTGLADKVYFLPL----TPEYVEQVI 417
Cdd:COG3919 3 TMRFRVVVLGGdiNALAV-------------ARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDpgddPEAFVDALL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 418 K-AERPN-GVLLTFGGQTALNCGVELDRsgiFSKYnVKIMGTPIQSIIETEDRKIFAERVAQIGEKVAPSEAVYSVKEAL 495
Cdd:COG3919 70 ElAERHGpDVLIPTGDEYVELLSRHRDE---LEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 496 DAATKLGYPVMARAA--------FSLGGLGSGFANNEKELQELAQQAFAHSNQLIV-------DKSLRGwkeveYEVVRD 560
Cdd:COG3919 146 ALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAGYELIVqeyipgdDGEMRG-----LTAYVD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 561 AFDNCITVCNMENL--DPLGIhtGESIVVapsQTLSNREynmLRSTAIKVIRHFGIVGECNIQYALNPESEEYYIIEVNA 638
Cdd:COG3919 221 RDGEVVATFTGRKLrhYPPAG--GNSAAR---ESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINP 292
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 86450127 639 RLSRSSALASKAtGYPLAYVAAKLCLAIPLPDIKNSVTGV 678
Cdd:COG3919 293 RFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREGV 331
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
165-310 |
3.13e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 57.96 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 165 LNPNEfdgLFLSNGPGDPIVCSDTVKQIEKIisTSNIPIFGICLGHQLLATAIGCKTYKLKYGNRGHNLPCIHhgTGRCF 244
Cdd:PRK08857 42 LNPTH---LVISPGPCTPNEAGISLQAIEHF--AGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSV 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450127 245 MTSQN--------HGFAVDAKTLPKDWE-PLFTNVNDKSNE---GIVHAEKPYFSVQFHPEHTPGPEDLELLFDvFLN 310
Cdd:PRK08857 115 FKGLNnpltvtryHSLVVKNDTLPECFElTAWTELEDGSMDeimGFQHKTLPIEAVQFHPESIKTEQGHQLLAN-FLA 191
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
348-659 |
3.93e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 59.90 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 348 KILILGSGGlsigqagefdysGSQAIKALKEE----KIQTILINPNIATVQtstgLADKVYFLP--LTPEYVEQVI---K 418
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSllkgRVIGADISELAPALY----FADKFYVVPkvTDPNYIDRLLdicK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 419 AERPNGVLLTFGGQTALNCGvELDRsgiFSKYNVKIMGTPiQSIIET-EDRKIFAERVAQIGEKVAPSEAVYSVKEAL-- 495
Cdd:PRK12767 67 KEKIDLLIPLIDPELPLLAQ-NRDR---FEEIGVKVLVSS-KEVIEIcNDKWLTYEFLKENGIPTPKSYLPESLEDFKaa 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 496 DAATKLGYPVMARAAFSLGGLGSGFANNEKELQelaqQAFAHSNQLIVDKSLRGwKEVEYEVVRDAFDNCITVCNMENLD 575
Cdd:PRK12767 142 LAKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 576 PLGihtGESivvapSQTLSnREYNMLRSTAIKVIRHFGIVGECNIQYALNPEseEYYIIEVNARLSrssalaskaTGYPL 655
Cdd:PRK12767 217 VRA---GET-----SKGVT-VKDPELFKLAERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFG---------GGYPL 276
|
....
gi 86450127 656 AYVA 659
Cdd:PRK12767 277 SYMA 280
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
146-219 |
6.42e-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: 54.91 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 146 IRCFIARGARVDLVPWNH-----NLNPNEFDGLFLSNGPGDPIVCSDTVKQIEKIIS--TSNIPIFGICLGHQLLATAIG 218
Cdd:cd01653 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPDDLARDEALLALLREaaAAGKPILGICLGAQLLVLGVQ 97
|
.
gi 86450127 219 C 219
Cdd:cd01653 98 F 98
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
446-672 |
9.09e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 59.35 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 446 IFSKYNVKIMGtPIQSIIETEDRKIFAERVAQ-IGEKVAP-SEA-VYSVKEALDAATKLGYPVMARAAFSLGGLGSGFAN 522
Cdd:PRK07178 93 ICAERGIKFIG-PSAEVIRRMGDKTEARRAMIkAGVPVTPgSEGnLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 523 NEKEL-------QELAQQAFAhSNQLIVDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGESIVVAPSQ 591
Cdd:PRK07178 172 SREELeqnfprvISEATKAFG-SAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 592 TLSNREYNMLRSTAIKVIRHFGIVGECNIQYALNPESeEYYIIEVNARLSRSSALASKATGYPLAY----VAAKLCLAIP 667
Cdd:PRK07178 245 QLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADG-EVYFMEMNTRVQVEHTITEEITGIDIVReqirIASGLPLSYK 323
|
....*
gi 86450127 668 LPDIK 672
Cdd:PRK07178 324 QEDIQ 328
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
144-310 |
1.85e-08 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 55.69 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 144 NQIRCFIARGARVdLVPWNHNLNPNEFDGL-----FLSNGPGDPIVCSDTVKQIEKIisTSNIPIFGICLGHQLLATAIG 218
Cdd:PRK08007 14 NLYQYFCELGADV-LVKRNDALTLADIDALkpqkiVISPGPCTPDEAGISLDVIRHY--AGRLPILGVCLGHQAMAQAFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 219 CKTYKLKYGNRGHNLPCIHHGTG------RCFMTSQNHGFAVDAKTLPKDWEplfTNVNDKSNE--GIVHAEKPYFSVQF 290
Cdd:PRK08007 91 GKVVRAAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGVQF 167
|
170 180
....*....|....*....|
gi 86450127 291 HPEHTPGPEDLELLFDvFLN 310
Cdd:PRK08007 168 HPESILSEQGHQLLAN-FLH 186
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
164-293 |
2.28e-08 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 55.51 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 164 NLNPNefdGLFLSNGPGDPI---VCSDTVKQIekiisTSNIPIFGICLGHQLLATAIGCKTYKLKYGNRGhNLPCIHHGT 240
Cdd:CHL00101 41 NLNIR---HIIISPGPGHPRdsgISLDVISSY-----APYIPILGVCLGHQSIGYLFGGKIIKAPKPMHG-KTSKIYHNH 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450127 241 GRCFMTSQN-------HGFAVDAKTLPKDWEplftnVNDKSNEGIVHA--EKPY---FSVQFHPE 293
Cdd:CHL00101 112 DDLFQGLPNpftatryHSLIIDPLNLPSPLE-----ITAWTEDGLIMAcrHKKYkmlRGIQFHPE 171
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
146-213 |
3.94e-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: 52.20 E-value: 3.94e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450127 146 IRCFIARGARVDLVPWNH-----NLNPNEFDGLFLSNGPGDPIVCSDTVKQIEKIIS--TSNIPIFGICLGHQLL 213
Cdd:cd03128 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPDDLAWDEALLALLREaaAAGKPVLGICLGAQLL 92
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
469-640 |
5.93e-08 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 57.46 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 469 KIFAERVAQ-IGEKVAPS--EAVYSVKEALDAATKLGYPVMARAAFSLGGLGSGFANNEKELQEL-------AQQAFAhS 538
Cdd:PRK12999 120 KVAARNAAIkAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAferakreAKAAFG-N 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 539 NQLIVDKSLRGWKEVEYEVVRDAFDNCitvcnmenldplgIHTGE---SI------VV--APSQTLSNREYNMLRSTAIK 607
Cdd:PRK12999 199 DEVYLEKYVENPRHIEVQILGDKHGNV-------------VHLYErdcSVqrrhqkVVeiAPAPGLSEELRERICEAAVK 265
|
170 180 190
....*....|....*....|....*....|...
gi 86450127 608 VIRHFGIVGECNIQYALNPESeEYYIIEVNARL 640
Cdd:PRK12999 266 LARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
168-293 |
9.22e-08 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 56.78 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 168 NEFDGLFLSNGPGDPIVCSDTVKQIEKIISTSNIPIFGICLGHQLLATAIGC-----------KTYKLKY-GNR-GHNLP 234
Cdd:PLN02889 130 KAFDNIVISPGPGSPTCPADIGICLRLLLECRDIPILGVCLGHQALGYVHGArivhapepvhgRLSEIEHnGCRlFDDIP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 235 cihHGTGRCFMTSQNHGFAVDAKTLPKDWEPL------------------------------------------------ 266
Cdd:PLN02889 210 ---SGRNSGFKVVRYHSLVIDAESLPKELVPIawtsssdtlsflesqksglvpdayesqigqsgssdpfssklkngtswp 286
|
170 180 190
....*....|....*....|....*....|.
gi 86450127 267 FTNVNDKSNE----GIVHAEKPYFSVQFHPE 293
Cdd:PLN02889 287 SSHSERMQNGkilmGIMHSTRPHYGLQFHPE 317
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
449-640 |
1.16e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 56.15 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 449 KYNVKIMGtPIQSIIETEDRKIFAERVAQ-IGEKVAP--SEAVYSVKEALDAATKLGYPVMARAAFSLGGLGSGFANNEK 525
Cdd:PRK08654 97 KAGIVFIG-PSSDVIEAMGSKINAKKLMKkAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 526 ELQE-------LAQQAFAHSNQLIvDKSLRGWKEVEYEVVRDAFDNCITVCNMEnldpLGI---HTgESIVVAPSQTLSN 595
Cdd:PRK08654 176 ELEDaiestqsIAQSAFGDSTVFI-EKYLEKPRHIEIQILADKHGNVIHLGDRE----CSIqrrHQ-KLIEEAPSPIMTP 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 86450127 596 REYNMLRSTAIKVIRHFGIVGECNIQYALnpESEEYYIIEVNARL 640
Cdd:PRK08654 250 ELRERMGEAAVKAAKAINYENAGTVEFLY--SNGNFYFLEMNTRL 292
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
200-308 |
4.61e-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: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 200 NIPIFGICLGHQLLATAIGCKTYKLKYGNrghnlpCIHHgtgrcfmtsQnhgfAVdaKTLPKDWEPLFTnvndkSNEGIV 279
Cdd:cd01745 100 GKPILGICRGMQLLNVALGGTLYQDIRVN------SLHH---------Q----AI--KRLADGLRVEAR-----APDGVI 153
|
90 100 110
....*....|....*....|....*....|....*
gi 86450127 280 HA-----EKPYFSVQFHPE-HTPGPEDLELLFDVF 308
Cdd:cd01745 154 EAiespdRPFVLGVQWHPEwLADTDPDSLKLFEAF 188
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
150-296 |
4.91e-07 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 53.90 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 150 IARgaRV-------DLVPWNH------NLNPNefdGLFLSNGPGDpiVCSDTVKQIEKIISTSNIPIFGICLGHQLLATA 216
Cdd:PRK00074 19 IAR--RVrelgvysEIVPYDIsaeeirAFNPK---GIILSGGPAS--VYEEGAPRADPEIFELGVPVLGICYGMQLMAHQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 217 IGCK---TYKLKYGN---RGHNLPCIHHGTGR---CFMtsqNHGFAVDAktLPKDWEPLFTNVNdKSNEGIVHAEKPYFS 287
Cdd:PRK00074 92 LGGKverAGKREYGRaelEVDNDSPLFKGLPEeqdVWM---SHGDKVTE--LPEGFKVIASTEN-CPIAAIANEERKFYG 165
|
170
....*....|.
gi 86450127 288 VQFHPE--HTP 296
Cdd:PRK00074 166 VQFHPEvtHTP 176
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
451-739 |
7.07e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 53.18 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 451 NVKIMGtPIQSIIETEDRKIFAERV-AQIGEKVAP-SE-AVYSVKEALDAATKLGYPVMARAAFSLGGLGSGFANNEKEL 527
Cdd:PRK05586 99 NIVFIG-PDSETIELMGNKSNAREImIKAGVPVVPgSEgEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEEL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 528 -------QELAQQAFAhSNQLIVDKSLRGWKEVEYEVVRDAFDNCITV----CNMENldplgiHTGESIVVAPSQTLSNR 596
Cdd:PRK05586 178 ikafntaKSEAKAAFG-DDSMYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 597 EYNMLRSTAIKVIRHFGIVGECNIQYALNpESEEYYIIEVNARLSRSSALASKATGYPLAY----VAAKLCLAIPLPDIK 672
Cdd:PRK05586 251 LRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKeqikIAYGEKLSIKQEDIK 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 673 nsVTGVTTAC----------FEPS----------------LD---YCVVKIPR-WDlakftrvsknigsSMksVGEVMAI 722
Cdd:PRK05586 330 --INGHSIECrinaedpkngFMPCpgkieelyipgglgvrVDsavYSGYTIPPyYD-------------SM--IGKLIVY 392
|
330
....*....|....*..
gi 86450127 723 GRNFEEAFQKALRMVDE 739
Cdd:PRK05586 393 GKDREEAIQKMKRALGE 409
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
170-293 |
1.93e-06 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 49.74 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 170 FDGLFLSNGPGDPIVCSDTVKQIEKIISTSNIpiFGICLGHQLLATAIGCKTYklkygnrghNLPCIHHGTGRCFMTSQN 249
Cdd:PRK06895 44 FSHILISPGPDVPRAYPQLFAMLERYHQHKSI--LGVCLGHQTLCEFFGGELY---------NLNNVRHGQQRPLKVRSN 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450127 250 ----------------HGFAVDAKTLPKDWEplFTNVNDksnEGIVHAEK----PYFSVQFHPE 293
Cdd:PRK06895 113 splfdglpeefniglyHSWAVSEENFPTPLE--ITAVCD---ENVVMAMQhktlPIYGVQFHPE 171
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
200-293 |
2.34e-06 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 49.95 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 200 NIPIFGICLGHQLLATAIGCKTY---KLKYGNRGHNLPC----------IHHGTGRCF--MTSQN-------HGFAVDak 257
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshaVNVEPGSLLasLLGSEefrvnslHHQAID-- 182
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 86450127 258 TLPKDWEplftnVNDKSNEGIVHA------EKPYFSVQFHPE 293
Cdd:pfam07722 183 RLAPGLR-----VEAVAPDGTIEAiespnaKGFALGVQWHPE 219
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
469-639 |
2.78e-06 |
|
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: 52.00 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 469 KIFAERVAQ-IGEKVAPS--EAVYSVKEALDAATKLGYPVMARAAFSLGGLGSGFANNEKELQEL-------AQQAFAhS 538
Cdd:COG1038 119 KVAARAAAIeAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAfesarreAKAAFG-D 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 539 NQLIVDKSLRGWKEVEYEVVRDAFDNCitvcnmenldplgIHTGE---SI------VV--APSQTLSNREYNMLRSTAIK 607
Cdd:COG1038 198 DEVFLEKYIERPKHIEVQILGDKHGNI-------------VHLFErdcSVqrrhqkVVeiAPAPNLDEELREAICEAAVK 264
|
170 180 190
....*....|....*....|....*....|....*..
gi 86450127 608 VIRHfgiVGECNiqyA-----LNPESEEYYIIEVNAR 639
Cdd:COG1038 265 LAKA---VGYVN---AgtvefLVDDDGNFYFIEVNPR 295
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
469-640 |
5.09e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 50.57 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 469 KIFAERVAQ-IGEKVAP-SE-AVYSVKEALDAATKLGYPVMARAAFSLGGLGSGFANNEKELQEL-------AQQAFAhS 538
Cdd:PRK08591 116 KVTAKATMKkAGVPVVPgSDgPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAfsmaraeAKAAFG-N 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 539 NQLIVDKSLRGWKEVEYEVVRDAFDNcitvcnmenldplGIHTGE---SI------VV--APSQTLSNREYNMLRSTAIK 607
Cdd:PRK08591 195 PGVYMEKYLENPRHIEIQVLADGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVK 261
|
170 180 190
....*....|....*....|....*....|...
gi 86450127 608 VIRHFGIVGECNIQYaLNPESEEYYIIEVNARL 640
Cdd:PRK08591 262 AAKAIGYRGAGTIEF-LYEKNGEFYFIEMNTRI 293
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
172-293 |
5.38e-06 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 49.03 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 172 GLFLSNGPGDPIVCSDTVKQIEKIISTsnIPIFGICLGHQLLATAIGCKTYKLKYG-NRGHNLPCIH---------HGTG 241
Cdd:PLN02335 65 GVLISPGPGTPQDSGISLQTVLELGPL--VPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYdekgeeglfSGLP 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 86450127 242 RCFMTSQNHGFAVDAKTLPKDWEPLFTNVNDKSNEGIVHAEKPYFS-VQFHPE 293
Cdd:PLN02335 143 NPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPE 195
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
991-1150 |
2.70e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 47.76 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 991 SPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIEFCDEVGYPCLVRPS---------YVLSGAAmnvaysnqDLE 1061
Cdd:COG0026 80 GPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggydgkgqVVIKSAA--------DLE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1062 TYLNAAsfvsKEHPVVISKFLTEAKEIDVDAV-AADGEILCMAVsehVENagVH-SGDATLVTPPQDINAETLVKIKGIV 1139
Cdd:COG0026 152 AAWAAL----GGGPCILEEFVPFERELSVIVArSPDGEVATYPV---VEN--VHrNGILDESIAPARISEALAAEAEEIA 222
|
170
....*....|.
gi 86450127 1140 RDLAALLDVTG 1150
Cdd:COG0026 223 KRIAEALDYVG 233
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
175-333 |
1.08e-04 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 46.60 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 175 LSNGP------GDPIVCSDTVKQIEKiistSNIPIFGICLGHQLLATAIGCKT---YKLKYGNRGHNLPCI-----HHGT 240
Cdd:PLN02347 59 LSGGPhsvhveGAPTVPEGFFDYCRE----RGVPVLGICYGMQLIVQKLGGEVkpgEKQEYGRMEIRVVCGsqlfgDLPS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 241 GRCFMTSQNHGfaVDAKTLPKDWEplftnVNDKSNEGIVHA----EKPYFSVQFHPEHTPGPEDLELLFDVFLNAIKIrl 316
Cdd:PLN02347 135 GETQTVWMSHG--DEAVKLPEGFE-----VVAKSVQGAVVAienrERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGV-- 205
|
170
....*....|....*..
gi 86450127 317 mkKSDISIKNVLIERLK 333
Cdd:PLN02347 206 --TADWKMQDVLEEQIE 220
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
489-672 |
1.29e-04 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 45.96 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 489 YSVKEALDAATKLGYPVMARAAFSLGGLGSGFANNEKELQELAQ------QAFAHSNQLIVDKSLRGWKEVEYEVVRDAF 562
Cdd:PRK08463 139 ESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFEsckreaLAYFNNDEVFMEKYVVNPRHIEFQILGDNY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 563 DNCITVCnmENLDPLGIHTGESIVVAPSQTLSNREYNMLRSTAIKVIRHFGIVGECNIQYALNpESEEYYIIEVNARLSR 642
Cdd:PRK08463 219 GNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD-DYNRFYFMEMNTRIQV 295
|
170 180 190
....*....|....*....|....*....|....
gi 86450127 643 SSALASKATGYPLA----YVAAKLCLAIPLPDIK 672
Cdd:PRK08463 296 EHGVTEEITGIDLIvrqiRIAAGEILDLEQSDIK 329
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
986-1094 |
7.20e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 43.82 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 986 KVLGTSPESIDSAENRFKFSRMLDRKG--ILQPRWKELTNLKSAIEFCDEVGYPCLVRPSYVLSGAAMNVAYSNQDLETY 1063
Cdd:PRK08654 101 VFIGPSSDVIEAMGSKINAKKLMKKAGvpVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDA 180
|
90 100 110
....*....|....*....|....*....|....*
gi 86450127 1064 LNAASFVSK----EHPVVISKFLTEAKEIDVDAVA 1094
Cdd:PRK08654 181 IESTQSIAQsafgDSTVFIEKYLEKPRHIEIQILA 215
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
991-1169 |
8.21e-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: 42.72 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 991 SPESIDSAENRFKFSRMLDRKGILQPRWKELTNLKSAIEFCDEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASFV 1070
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1071 SKEHPV-VISKFLTEAKEIDVDAVAADGEIL-CMA--VSEHVEnAGVHSGDATLVTPPQDINAETLVKIKGIVRDLAALL 1146
Cdd:TIGR00768 159 NGPQNLfLVQEYIKKPGGRDIRVFVVGDEVVaAIYriTSGHWR-SNLARGGKAEPCSLTEEIEELAIKAAKALGLDVAGV 237
|
170 180
....*....|....*....|...
gi 86450127 1147 DvtgpfnmqLIAKNNELKVIECN 1169
Cdd:TIGR00768 238 D--------LLESEDGLLVNEVN 252
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1011-1150 |
1.34e-03 |
|
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: 41.53 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 1011 KGILQPRWKELTNLKSAiEFCDEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAsfVSKEHPVVISKFLtEAKEIDV 1090
Cdd:pfam07478 13 VTFTRADWKLNPKEWCA-QVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEA--FQYDEKVLVEEGI-EGREIEC 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450127 1091 dAVAADGEILCMAVSEHVENAGV------HSGDATLVTPPQDINAETLVKIKGIVRDLAALLDVTG 1150
Cdd:pfam07478 89 -AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRG 153
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
469-554 |
1.68e-03 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 42.03 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450127 469 KIFAERV-AQIGEKVAPSEAV----YSVKEALDAATKLGYPVMARAAfslgGLGSGF----ANNEKELQELAQQAFAHSN 539
Cdd:PRK01966 124 KILTKRLlAAAGIPVAPYVVLtrgdWEEASLAEIEAKLGLPVFVKPA----NLGSSVgiskVKNEEELAAALDLAFEYDR 199
|
90
....*....|....*
gi 86450127 540 QLIVDKSLRGwKEVE 554
Cdd:PRK01966 200 KVLVEQGIKG-REIE 213
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
605-679 |
3.65e-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: 38.75 E-value: 3.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450127 605 AIKVIRHFGIVGECNIQYALNpeSEEYYIIEVNARLsrSSALA-SKATGYPLAYVAAKLCLAIPLPDIKNSVTGVT 679
Cdd:pfam15632 53 ARRLAEAFGLDGLFNVQFRYD--GDGPKLLEINPRM--SGGIGySCLAGVNLPYLALKLLLGLETPDPVEPRLGLR 124
|
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