|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1052 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1944.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 1 MPKDPTLKKILVIGSGPIVIGQAAEFDYAGTQACQALKEEGLEVVLVNSNPATIMTDTNMADRVYIEPLTAEFITQVIRK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 81 ERPDGLLPTLGGQTGLNLAVELAKQGVLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAG 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 161 ETGYPVIVRPAYTLGGTGGGIAHTEAELREIVDNGLRYSPICQCLIEKSIAGYKEIEYEVMRDANDNCIVVCNMENFDPV 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 241 GVHTGDSIVFAPSQTLSDREYHMLRTSALKIIRSLNIQ-GGCNVQFALDPHSFQYYVIEVNPRVSRSSALASKATGYPIA 319
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 320 RIAAKIAIGYTLDELKNPVTGETYACFEPTLDYVVSKIPRWPFDKFVSANRKLGTQMKATGEVMAIGRTLEESLLKAVRS 399
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 400 LEIGLDHIALPDARQLDDATLRERIRVADDERLFLLGEWFRRGHSLEEAHQLSKIDRFFLHKLERIVKLEQQVAE-AEVL 478
Cdd:PRK05294 401 LEIGVTGLDEDLFEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEnGLPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 479 DVDLLHTAKRMGFTDKTIGRLRNQSEKEIRTLRLAHGLQPVYKIVDTCAAEFEAETPYYYSTYEQEDEVRKSEKKSIIVL 558
Cdd:PRK05294 481 DAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 559 GSGPIRIGQGVEFDYATVHAIWAIRAAGYEAVIINNNPETVSTDFNTSDRLYFEPLYKEDVLNIIEKENPLGVIVQFGGQ 638
Cdd:PRK05294 561 GSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 639 TALNLARDLREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAVTSVEEAAQVAARLGYPVLVRPSYVLGGRAM 718
Cdd:PRK05294 641 TPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 719 EIVYSESELRSYMEVAVQVNPEHPVLIDRYLLGK-ELEVDAICDGEDVLIPGIMEHIERAGVHSGDSIAVYPPQSITPEQ 797
Cdd:PRK05294 721 EIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAiEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 798 KARVIEITTQIAKSLHTKGLINIQFVLFKGDIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIMLGESLQEQGYDNGLCP 877
Cdd:PRK05294 801 IEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLIP 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 878 esKEVAVKVPVFSFAKLRRVDITLGPEMKSTGEVMGRDRDYARAVYKGLLAAGISLPRFGTVVATIGDKEKEEAVSLMRR 957
Cdd:PRK05294 881 --PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDKEEVVELAKR 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 958 FHQLGYKIVCTSGTADILEAASLPVERVHKLREGSPHILDLIRQGKADLVVNTwTRGRTPERDGFRIRREAVENGIACLT 1037
Cdd:PRK05294 959 LLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINT-PTGRQAIRDGFSIRRAALEYKVPYIT 1037
|
1050
....*....|....*
gi 1361143904 1038 SLDTVEALLITLESI 1052
Cdd:PRK05294 1038 TLAGARAAVKAIEAL 1052
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1046 |
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: 1684.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 2 PKDPTLKKILVIGSGPIVIGQAAEFDYAGTQACQALKEEGLEVVLVNSNPATIMTDTNMADRVYIEPLTAEFITQVIRKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 82 RPDGLLPTLGGQTGLNLAVELAKQGVLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAGE 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 162 TGYPVIVRPAYTLGGTGGGIAHTEAELREIVDNGLRYSPICQCLIEKSIAGYKEIEYEVMRDANDNCIVVCNMENFDPVG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 242 VHTGDSIVFAPSQTLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDPHSFQYYVIEVNPRVSRSSALASKATGYPIARI 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 322 AAKIAIGYTLDELKNPVTGETYACFEPTLDYVVSKIPRWPFDKFVSANRKLGTQMKATGEVMAIGRTLEESLLKAVRSLE 401
Cdd:TIGR01369 321 AAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 402 IGLDHIALPDARQLDDATLRERIRVADDERLFLLGEWFRRGHSLEEAHQLSKIDRFFLHKLERIVKLEQQVAE--AEVLD 479
Cdd:TIGR01369 401 IGATGFDLPDREVEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEvkLTDLD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 480 VDLLHTAKRMGFTDKTIGRLRNQSEKEIRTLRLAHGLQPVYKIVDTCAAEFEAETPYYYSTYE-QEDEVRKSEKKSIIVL 558
Cdd:TIGR01369 481 PELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEgERDDVPFTDKKKVLVL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 559 GSGPIRIGQGVEFDYATVHAIWAIRAAGYEAVIINNNPETVSTDFNTSDRLYFEPLYKEDVLNIIEKENPLGVIVQFGGQ 638
Cdd:TIGR01369 561 GSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 639 TALNLARDLREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAVTSVEEAAQVAARLGYPVLVRPSYVLGGRAM 718
Cdd:TIGR01369 641 TPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 719 EIVYSESELRSYMEVAVQVNPEHPVLIDRYL-LGKELEVDAICDGEDVLIPGIMEHIERAGVHSGDSIAVYPPQSITPEQ 797
Cdd:TIGR01369 721 EIVYNEEELRRYLEEAVAVSPEHPVLIDKYLeDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 798 KARVIEITTQIAKSLHTKGLINIQFVLFKGDIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIMLGESLQEQGYdnGLCP 877
Cdd:TIGR01369 801 VDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGV--GKEK 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 878 ESKEVAVKVPVFSFAKLRRVDITLGPEMKSTGEVMGRDRDYARAVYKGLLAAGISLPRFGTVVATIGDKEKEEAVSLMRR 957
Cdd:TIGR01369 879 EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARK 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 958 FHQLGYKIVCTSGTADILEAASLPVERVHKLREGSPHILDLIRQGKADLVVNTWTRGRTPERDGFRIRREAVENGIACLT 1037
Cdd:TIGR01369 959 LAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTSKGAGTATDGYKIRREALDYGVPLIT 1038
|
....*....
gi 1361143904 1038 SLDTVEALL 1046
Cdd:TIGR01369 1039 TLNTAEAFA 1047
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1059 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1582.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 1 MPKDPTLKKILVIGSGPIVIGQAAEFDYAGTQACQALKEEGLEVVLVNSNPATIMTDTNMADRVYIEPLTAEFITQVIRK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 81 ERPDGLLPTLGGQTGLNLAVELAKQGVLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAG 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 161 ETGYPVIVRPAYTLGGTGGGIAHTEAELREIVDNGLRYSPICQCLIEKSIAGYKEIEYEVMRDANDNCIVVCNMENFDPV 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 241 GVHTGDSIVFAPSQTLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDPHSFQYYVIEVNPRVSRSSALASKATGYPIAR 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 321 IAAKIAIGYTLDELKNPVTGETYACFEPTLDYVVSKIPRWPFDKFVSANRKLGTQMKATGEVMAIGRTLEESLLKAVRSL 400
Cdd:PRK12815 321 IAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 401 EIGLDHIALPDA-RQLDDATLRERIRVADDERLFLLGEWFRRGHSLEEAHQLSKIDRFFLHKLERIVKLEQQVAEA-EVL 478
Cdd:PRK12815 401 EIKRNGLSLPIElSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDgLDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 479 DVDLLHTAKRMGFTDKTIGRLRNQSEKEIRTLRLAHGLQPVYKIVDTCAAEFEAETPYYYSTYEQEDEVRKS-EKKSIIV 557
Cdd:PRK12815 481 SADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPSsEKKKVLI 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 558 LGSGPIRIGQGVEFDYATVHAIWAIRAAGYEAVIINNNPETVSTDFNTSDRLYFEPLYKEDVLNIIEKENPLGVIVQFGG 637
Cdd:PRK12815 561 LGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 638 QTALNLARDLREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAVTSVEEAAQVAARLGYPVLVRPSYVLGGRA 717
Cdd:PRK12815 641 QTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQG 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 718 MEIVYSESELRSYMEVAVQvnPEHPVLIDRYLLGKELEVDAICDGEDVLIPGIMEHIERAGVHSGDSIAVYPPQSITPEQ 797
Cdd:PRK12815 721 MAVVYDEPALEAYLAENAS--QLYPILIDQFIDGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQSLSEEQ 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 798 KARVIEITTQIAKSLHTKGLINIQFVLFKGDIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIMLGESLQEQGYDNGLCP 877
Cdd:PRK12815 799 QEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGYPNGLWP 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 878 ESKEVAVKVPVFSFAKLRRVDITLGPEMKSTGEVMGRDRDYARAVYKGLLAAGISLPRFGTVVATIGDKEKEEAVSLMRR 957
Cdd:PRK12815 879 GSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARR 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 958 FHQLGYKIVCTSGTADILEAASLPVERVHKLREGSPHILDlIRQGKADLVVNTWTRGRTPERDGFRIRREAVENGIACLT 1037
Cdd:PRK12815 959 FAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSPSLLE-RIKQHRIVLVVNTSLSDSASEDAIKIRDEALSTHIPVFT 1037
|
1050 1060
....*....|....*....|..
gi 1361143904 1038 SLDTVEALLITLESIHMSAEPI 1059
Cdd:PRK12815 1038 ELETAQAFLQVLESLALTTQPI 1059
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
7-1052 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1215.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 7 LKKILVIGSGPIVIGQAAEFDYAGTQACQALKEEGLEVVLVNSNPATIMTDTNMADRVYIEPLTAEFITQVIRKERPDGL 86
Cdd:PLN02735 23 LKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 87 LPTLGGQTGLNLAVELAKQGVLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAGETG-YP 165
Cdd:PLN02735 103 LPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 166 VIVRPAYTLGGTGGGIAHTEAELREIVDNGLRYSPICQCLIEKSIAGYKEIEYEVMRDANDNCIVVCNMENFDPVGVHTG 245
Cdd:PLN02735 183 LIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 246 DSIVFAPSQTLSDREYHMLRTSALKIIRSLNIQ-GGCNVQFALDPHSFQYYVIEVNPRVSRSSALASKATGYPIARIAAK 324
Cdd:PLN02735 263 DSITVAPAQTLTDKEYQRLRDYSVAIIREIGVEcGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAAK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 325 IAIGYTLDELKNPVTGETYACFEPTLDYVVSKIPRWPFDKFVSANRKLGTQMKATGEVMAIGRTLEESLLKAVRSLEIGL 404
Cdd:PLN02735 343 LSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETGF 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 405 DHIALPDARQL--DDATLRERIRVADDERLFLLGEWFRRGHSLEEAHQLSKIDRFFLHKLERIVKLEQQVAEAEV--LDV 480
Cdd:PLN02735 423 SGWGCAKVKELdwDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLseLSK 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 481 DLLHTAKRMGFTDKTIGRLRNQSEKEIRTLRLAHGLQPVYKIVDTCAAEFEAETPYYYSTYEQEDEVRKSEKKSIIVLGS 560
Cdd:PLN02735 503 DDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLILGG 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 561 GPIRIGQGVEFDYATVHAIWAIRAAGYEAVIINNNPETVSTDFNTSDRLYFEPLYKEDVLNIIEKENPLGVIVQFGGQTA 640
Cdd:PLN02735 583 GPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGGQTP 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 641 LNLARDLRE------------EG-IKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAVTSVEEAAQVAARLGYPVLV 707
Cdd:PLN02735 663 LKLALPIQKyldknpppsasgNGnVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYPVVV 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 708 RPSYVLGGRAMEIVYSESELRSYMEVAVQVNPEHPVLIDRYLL-GKELEVDAICDGE-DVLIPGIMEHIERAGVHSGDSI 785
Cdd:PLN02735 743 RPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSdATEIDVDALADSEgNVVIGGIMEHIEQAGVHSGDSA 822
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 786 AVYPPQSITPEQKARVIEITTQIAKSLHTKGLINIQF-VLFKGDIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIMLGE 864
Cdd:PLN02735 823 CSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGK 902
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 865 SLQEQGYDNGLCPesKEVAVKVPVFSFAKLRRVDITLGPEMKSTGEVMGRDRDYARAVYKGLLAAGISLPRFGTVVATIG 944
Cdd:PLN02735 903 SLKDLGFTEEVIP--AHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGTVFISLN 980
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 945 DKEKEEAVSLMRRFHQLGYKIVCTSGTADILEAASLPVERVHKLREGSPHILDLIRQGKADLVVNTWTRGRTPERDGFRI 1024
Cdd:PLN02735 981 DLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGDMLANGQIQLMVITSSGDALDQKDGRQL 1060
|
1050 1060
....*....|....*....|....*...
gi 1361143904 1025 RREAVENGIACLTsldTVEALLITLESI 1052
Cdd:PLN02735 1061 RRMALAYKVPIIT---TVAGALATAQAV 1085
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-560 |
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: 770.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 13 IGSGPIVIGQAAEFDYAGTQACQALKEEGLEVVLVNSNPATIMTDTNMADRVYIEPLTAEFITQVIRKERPDGLLPTLGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 93 QTGLNLAVELAKQGVLEreGVRLLGTDLRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAGETGYPVIVRPAY 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 173 TLGGTGGGIAHTEAELREIVDNGLRYSPICQCLIEKSIAGYKEIEYEVMRDANDNCIVVCNMENFDPVGVHTGDSIVFAP 252
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 253 SQTLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDphSFQYYVIEVNPRVSRSSALASKATGYPIARIAAKIAIGYTLD 332
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 333 ELKNPvTGetyacFEPTLDYVVSKIPRWPFDKFVSANRKLGTQMKATGEVMAIGRTLEESLLKAVRSLEIGLDHIALpDA 412
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVL-LS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 413 RQLDDATLRERIRVADDERLFLLGEWFRRGHSLEEAHQLSKIDRFFLHKLERIVKLEQQVAEaEVLDVDLLHTAKRMGFT 492
Cdd:COG0458 390 LVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEE-IILVINTLLGAKSLGDS 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1361143904 493 DKTIGRLRNQSEKEIRTLRLAHGLQPVYKIVDTCAAEFEAETPYYYSTYEQEDEVRKSEKKSIIVLGS 560
Cdd:COG0458 469 DGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
558-1057 |
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: 741.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 558 LGSGPIRIGQGVEFDYATVHAIWAIRAAGYEAVIINNNPETVSTDFNTSDRLYFEPLYKEDVLNIIEKENPLGVIVQFGG 637
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 638 QTALNLARDLRE----EGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAVTSVEEAAQVAARLGYPVLVRPSYVL 713
Cdd:COG0458 81 QTALNLAVELEEagilEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 714 GGRAMEIVYSESELRSYMEVAVQVNPEHPVLIDRYLLG-KELEVDAICDGED-VLIPGIMEHIERAGVHSGDSIAVYPPQ 791
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGaKEIEVDVVRDGEDnVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 792 SITPEQKARVIEITTQIAKSLHTKGLINIQFVLFKGDIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIMLGESLQEQGY 871
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 872 DNGLCPESKEVAVKVPVFSFAKLRRVDITLGPEMKSTGEVMGRDRDYARAVYKGLLAAGISLPrfGTVVATIG-DKEKEE 950
Cdd:COG0458 321 DTGFEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP--GTVLLSLVaDDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 951 AVSLMRRFHQLGYKIVCTSGTADILEAASLPVERVHKLREGSPHILDLIRQGKADLVVNTWTRGRTPERDGFRIRREAVE 1030
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAKSLGDSDGIIRRALAA 478
|
490 500
....*....|....*....|....*..
gi 1361143904 1031 NGIACLTSLDTVEALLITLESIHMSAE 1057
Cdd:COG0458 479 KVPYVTTLAAAAAAALAIKAVETEAGE 505
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-332 |
6.72e-91 |
|
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: 289.59 E-value: 6.72e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 128 DRDLFRSLMNELNEPVPESVI--VQSVEEAVDFAGETGYPVIVRPAYTLGGTGGGIAHTEAELREIVDNGLRYSPIC--- 202
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAfgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 203 -QCLIEKSIAGYKEIEYEVMRDANDNCIVVCNMENFDPVgvHTGDSIVFAPSQTLSDREYHMLRTSALKIIRSLNIQGGC 281
Cdd:pfam02786 81 pQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1361143904 282 NVQFALDPHSFQYYVIEVNPRVSRSSALASKATGYPIARIAAKIAIGYTLD 332
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
548-926 |
1.55e-68 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 250.08 E-value: 1.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 548 RKSEKKSIIVLGSGPIRIGQGVEFDYATVHAIWAIRAAGYEAVIINNNPETVSTDFNTSDRLYFEPLYKEDVLNIIEKEN 627
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 628 PLGVIVQFGGQTALNLARDLREEGI------KILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAVTSVEEAAQVAARL 701
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGIlekygvELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 702 G-YPVLVRPSYVLGGRAMEIVYSESELRSYMEVAVQVNPEHPVLIDRYLLG-KELEVDAICDGED-VLIPGIMEHIERAG 778
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGwKEYELEVMRDLADnVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 779 VHSGDSIAVYPPQSITPEQKARVIEITTQIAKSLHTK-GLINIQFVL--FKGDIYVLEVNPRASRTVPFLSKVTGIPMAQ 855
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVEcGGSNVQFAVnpVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1361143904 856 VATRIMLGESLQEQGYDNGL-CPESKE-----VAVKVPVFSFAKLRRVDITLGPEMKSTGEVMGRDRDYARAVYKGL 926
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDITLkTPASFEpsidyVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKAL 415
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
420-541 |
3.01e-57 |
|
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: 193.05 E-value: 3.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 420 LRERIRVADDERLFLLGEWFRRGHSLEEAHQLSKIDRFFLHKLERIVKLEQQVAE--AEVLDVDLLHTAKRMGFTDKTIG 497
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKggLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1361143904 498 RLRNQSEKEIRTLRLAHGLQPVYKIVDTCAAEFEAETPYYYSTY 541
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
937-1046 |
1.51e-42 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 150.71 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 937 GTVVATIGDKEKEEAVSLMRRFHQLGYKIVCTSGTADILEAASLPVERVHKLREGSPHILDLIRQGKADLVVNTwTRGRT 1016
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINT-PSGKR 79
|
90 100 110
....*....|....*....|....*....|
gi 1361143904 1017 PERDGFRIRREAVENGIACLTSLDTVEALL 1046
Cdd:cd01424 80 AIRDGFSIRRAALEYKVPYFTTLDTARAAV 109
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
667-866 |
4.02e-38 |
|
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: 141.67 E-value: 4.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 667 DRKKFEKLLNDTKIAQPPGAA--VTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEIVYSESELRSYMEVAVQVNPE---- 740
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 741 HPVLIDRYLLG-KELEVDAICDGED-VLIPGIMEHIERagVHSGDSIAVYPPQSITPEQKARVIEITTQIAKSLHTKGLI 818
Cdd:pfam02786 81 PQVLVEKSLKGpKHIEYQVLRDAHGnCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1361143904 819 NIQFVL--FKGDIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIMLGESL 866
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
422-499 |
1.20e-30 |
|
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: 115.55 E-value: 1.20e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1361143904 422 ERIRVADDERLFLLGEWFRRGHSLEEAHQLSKIDRFFLHKLERIVKLEQQVAEAEV-LDVDLLHTAKRMGFTDKTIGRL 499
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLdLDAELLREAKRLGFSDRQIAKL 79
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
950-1037 |
2.33e-25 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 100.63 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 950 EAVSLMRRFHQLGYKIVCTSGTADILEAASLPVER--VHKLREGSPHILDLIRQGKADLVVNTWT-RGRTPERDGFRIRR 1026
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVVKtlHPKVHGGIPQILDLIKNGEIDLVINTLYpFEAQAHEDGYSIRR 80
|
90
....*....|.
gi 1361143904 1027 EAVENGIACLT 1037
Cdd:smart00851 81 AAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
950-1037 |
4.85e-24 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 97.17 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 950 EAVSLMRRFHQLGYKIVCTSGTADILEAASLPV-ERVHKLREGSPH----ILDLIRQGKADLVVNTWTRGRTPERDGFRI 1024
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVtEVVEKTGEGRPGgrvqIGDLIKNGEIDLVINTLYPFKATVHDGYAI 80
|
90
....*....|...
gi 1361143904 1025 RREAVENGIACLT 1037
Cdd:pfam02142 81 RRAAENIDIPGPT 93
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
656-864 |
4.75e-23 |
|
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: 99.95 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 656 GTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEIVYSESELRSYMEVAV 735
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 736 QVN----PEHPVLIDRYLLGKELEVDAICDGEDVLIPGIMEHIeRAGVHSGDSIAVYPPQsITPEQKARVIEITTQIAKS 811
Cdd:COG0439 123 AEAkagsPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKH-QKPPYFVELGHEAPSP-LPEELRAEIGELVARALRA 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1361143904 812 L-HTKGLINIQFVL-FKGDIYVLEVNPRAS--RTVPFLSKVTGIPMAQVATRIMLGE 864
Cdd:COG0439 201 LgYRRGAFHTEFLLtPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGE 257
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
72-304 |
4.86e-22 |
|
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: 96.87 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 72 EFITQVIRKERPDGLLPtlGGQTGLNLAVELAkqgvlEREGVRllGTDLRAITNAEDRDLFRSLMNELNEPVPESVIVQS 151
Cdd:COG0439 7 AAAAELARETGIDAVLS--ESEFAVETAAELA-----EELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 152 VEEAVDFAGETGYPVIVRPAYTLGGTGGGIAHTEAEL----REIVDNGLRYSPICQCLIEKSIAGyKEIEYEVMrdANDN 227
Cdd:COG0439 78 PEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELeaalAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGL--VRDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 228 CIVVCNM---ENFDPVGVHTGDSivfAPSQtLSDREYHMLRTSALKIIRSLNIQ-GGCNVQFALDPHSfQYYVIEVNPRV 303
Cdd:COG0439 155 EVVVCSItrkHQKPPYFVELGHE---APSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDG-EPYLIEINARL 229
|
.
gi 1361143904 304 S 304
Cdd:COG0439 230 G 230
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
9-313 |
8.96e-22 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 98.85 E-value: 8.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 9 KILVIGSGPIVIGqaaefdyagtqACQALKEEGLEVVLVNSNPATIMTDTNMADRVYIEPLTA-------EFITQVIRKE 81
Cdd:COG3919 7 RVVVLGGDINALA-----------VARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGddpeafvDALLELAERH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 82 RPDGLLPTlgGQTGLNLAVELAKQgvLErEGVRLLGTDLRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAGE 161
Cdd:COG3919 76 GPDVLIPT--GDEYVELLSRHRDE--LE-EHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAED 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 162 TGYPVIVRPAYT--------LGGTGGGIAHTEAELREIVDNGLR--YSPICQCLIEK------SIAGYkeieyevmRDAN 225
Cdd:COG3919 151 LGFPVVVKPADSvgydelsfPGKKKVFYVDDREELLALLRRIAAagYELIVQEYIPGddgemrGLTAY--------VDRD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 226 DNCIVVCnmenfdpVG-VHTGDSIVFAPS---QTLSDREyhmLRTSALKIIRSLNIQGGCNVQFALDPHSFQYYVIEVNP 301
Cdd:COG3919 223 GEVVATF-------TGrKLRHYPPAGGNSaarESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINP 292
|
330
....*....|..
gi 1361143904 302 RVSRSSALASKA 313
Cdd:COG3919 293 RFWRSLYLATAA 304
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
612-844 |
8.78e-21 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 94.57 E-value: 8.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 612 EPLYKEDVLNIIEKENPLGVIVqfGGQTALNL---ARD-LREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAA 687
Cdd:PRK12767 54 DPNYIDRLLDICKKEKIDLLIP--LIDPELPLlaqNRDrFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 688 VTSVE--EAAQVAARLGYPVLVRPSYVLGGRAMEIVYSESELRSYMEVavqvNPEhpVLIDRYLLGKELEVDAICDGEDV 765
Cdd:PRK12767 132 PESLEdfKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEY----VPN--LIIQEFIEGQEYTVDVLCDLNGE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 766 LIpgimeHI---ERAGVHSGDSIavyppQSITPEQKaRVIEITTQIAKSLHTKGLINIQFVLFKGDIYVLEVNPRASRTV 842
Cdd:PRK12767 206 VI-----SIvprKRIEVRAGETS-----KGVTVKDP-ELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGY 274
|
..
gi 1361143904 843 PF 844
Cdd:PRK12767 275 PL 276
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
643-866 |
6.28e-16 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 81.95 E-value: 6.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 643 LARDLREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPG--AAVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEI 720
Cdd:PRK08654 91 FAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGteEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 721 VYSESELRSYMEVAVQV------NPEhpVLIDRYLLG-KELEVDAICDGEDVLIpgimehieragvHSGDS--------- 784
Cdd:PRK08654 171 VYSEEELEDAIESTQSIaqsafgDST--VFIEKYLEKpRHIEIQILADKHGNVI------------HLGDRecsiqrrhq 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 785 --IAVYPPQSITPEQKARVIEITTQIAKSLHTKGLINIQFVLFKGDIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIML 862
Cdd:PRK08654 237 klIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAA 316
|
....
gi 1361143904 863 GESL 866
Cdd:PRK08654 317 GEEL 320
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
674-836 |
1.04e-14 |
|
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: 73.89 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 674 LLNDTKIAQPPGAAVTS-------VEEAAQVAARLGYPVLVRPSyVLGGR-AMEIVYSESELRSYMEVAVQVNPEhpVLI 745
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTRadwklnpKEWCAQVEEALGYPVFVKPA-RLGSSvGVSKVESREELQAAIEEAFQYDEK--VLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 746 DRYLLGKELEVdAICDGEDVLIPGIMEHIERAGV------HSGDSIAVYPPQSITPEQKARVIEITTQIAKSLHTKGLIN 819
Cdd:pfam07478 78 EEGIEGREIEC-AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLAR 156
|
170
....*....|....*...
gi 1361143904 820 IQ-FVLFKGDIYVLEVNP 836
Cdd:pfam07478 157 VDfFLTEDGEIVLNEVNT 174
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
680-860 |
1.68e-13 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 72.45 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 680 IAQPPGAAVTSVE--EAAQVAARLGYPVLVRPsyVLGG--RAMEIVYSESELRSYMEVAVQVnpEHPVLIDRYLLGKELE 755
Cdd:COG1181 108 LPTPPYVVLRRGElaDLEAIEEELGLPLFVKP--AREGssVGVSKVKNAEELAAALEEAFKY--DDKVLVEEFIDGREVT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 756 VdAICDGEDVLIPGIMEHIERAGV-------HSGDSIAVYPPQsITPEQKARVIEITTQIAKSLHTKGLINIQFVLFK-G 827
Cdd:COG1181 184 V-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPAR-LPEELEERIQELALKAFRALGCRGYARVDFRLDEdG 261
|
170 180 190
....*....|....*....|....*....|....*...
gi 1361143904 828 DIYVLEVNP-----RASrTVPFLSKVTGIPMAQVATRI 860
Cdd:COG1181 262 EPYLLEVNTlpgmtPTS-LLPKAAAAAGISYEELIERI 298
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
9-313 |
1.95e-13 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 72.61 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 9 KILVIGSGpivigqaaefdyAGTQACQALKEEGLEVVLVNSNPATIMTDTNMADRVYI-----EPLTAEFITQVIRKERP 83
Cdd:PRK12767 3 NILVTSAG------------RRVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVvpkvtDPNYIDRLLDICKKEKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 84 DGLLPTLGGQTGLnLAVELAKqgvLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEPVPESVIVQSVE--EAVDFAGE 161
Cdd:PRK12767 71 DLLIPLIDPELPL-LAQNRDR---FEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEdfKAALAKGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 162 TGYPVIVRPAYTLGGTGGGIAHTEAELR---EIVDNglrysPICQCLIEksiagYKEIEYEVMRDANDNCIVVCNMENFD 238
Cdd:PRK12767 147 LQFPLFVKPRDGSASIGVFKVNDKEELEfllEYVPN-----LIIQEFIE-----GQEYTVDVLCDLNGEVISIVPRKRIE 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1361143904 239 PVGVHTGDSIVFapsqtlsdrEYHMLRTSALKIIRSLNIQGGCNVQFALDPHsfQYYVIEVNPRVSRSSALASKA 313
Cdd:PRK12767 217 VRAGETSKGVTV---------KDPELFKLAERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFGGGYPLSYMA 280
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
7-303 |
4.25e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 70.01 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 7 LKKILVIGSGPIVIgqaaefdyagtQACQALKEEGLEVVLVNSNPATIMTDTNMADRVY-IEP-------LTAEFITQVI 78
Cdd:PRK08654 2 FKKILIANRGEIAI-----------RVMRACRELGIKTVAVYSEADKNALFVKYADEAYpIGPappsksyLNIERIIDVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 79 RKERPDGLLPTLGGqtgLNLAVELAKQgvLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEPV----PESVivQSVEE 154
Cdd:PRK08654 71 KKAGADAIHPGYGF---LAENPEFAKA--CEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVlpgtEEGI--EDIEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 155 AVDFAGETGYPVIVRPAYTLGGTGGGIAHTEAELREIVDNGLRyspICQ-------CLIEKSIAGYKEIEYEVMRDANDN 227
Cdd:PRK08654 144 AKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQS---IAQsafgdstVFIEKYLEKPRHIEIQILADKHGN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 228 CIvvcnmenfdpvgvHTGDS-----------IVFAPSQTLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDphSFQYYV 296
Cdd:PRK08654 221 VI-------------HLGDRecsiqrrhqklIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS--NGNFYF 285
|
....*..
gi 1361143904 297 IEVNPRV 303
Cdd:PRK08654 286 LEMNTRL 292
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
643-867 |
9.76e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 68.59 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 643 LARDLREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAA--VTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEI 720
Cdd:PRK07178 90 LAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEgnLADLDEALAEAERIGYPVMLKATSGGGGRGIRR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 721 VYSESELRS------------------YMEVAVqVNPEHpvlidryllgkeLEVDAICDGEDVLIpGIMEH---IERagv 779
Cdd:PRK07178 170 CNSREELEQnfprviseatkafgsaevFLEKCI-VNPKH------------IEVQILADSHGNVV-HLFERdcsIQR--- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 780 HSGDSIAVYPPQSITPEQKARVIEITTQIAKSLHTKGLINIQFVLFKGD-IYVLEVNPRASRTVPFLSKVTGIPMAQVAT 858
Cdd:PRK07178 233 RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGeVYFMEMNTRVQVEHTITEEITGIDIVREQI 312
|
....*....
gi 1361143904 859 RIMLGESLQ 867
Cdd:PRK07178 313 RIASGLPLS 321
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
8-301 |
1.98e-11 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 66.28 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 8 KKILVI-GsgpiviGQAAEFD---YAGTQACQALKEEGLEVVLVNSNPATIMTDtnmadrvyiepltaefitqvIRKERP 83
Cdd:COG1181 1 MRVAVLfG------GRSAEREvslKSGRAVAAALDKAGYDVVPIGIDVEDLPAA--------------------LKELKP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 84 DGLLPTLGGQTGLNLAVelakQGVLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAV--DFAGE 161
Cdd:COG1181 55 DVVFPALHGRGGEDGTI----QGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADleAIEEE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 162 TGYPVIVRPAytLGGTGGGI--AHTEAELREIVDNGLRYSPicQCLIEKSIAGyKEIEYEVMRDANDNC-----IVVCNm 234
Cdd:COG1181 131 LGLPLFVKPA--REGSSVGVskVKNAEELAAALEEAFKYDD--KVLVEEFIDG-REVTVGVLGNGGPRAlppieIVPEN- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1361143904 235 ENFD------PvgvhtGDSIVFAPSQtLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDPHSfQYYVIEVNP 301
Cdd:COG1181 205 GFYDyeakytD-----GGTEYICPAR-LPEELEERIQELALKAFRALGCRGYARVDFRLDEDG-EPYLLEVNT 270
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
643-867 |
2.47e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 67.36 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 643 LARDLREEGIKILGTSLEEI----DRAEDRKKFEKLlnDTKIAQPPGAAVTSVEEAAQVAARLGYPVLVRPSYVLGGRAM 718
Cdd:PRK06111 91 FAERCKEEGIVFIGPSADIIakmgSKIEARRAMQAA--GVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGM 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 719 EIVYSESELRSYMEV----AVQV--NPEhpVLIDRYLL-GKELEVDAICDGEDvlipgimeHIeragVHSGDS------- 784
Cdd:PRK06111 169 QLVETEQELTKAFESnkkrAANFfgNGE--MYIEKYIEdPRHIEIQLLADTHG--------NT----VYLWERecsvqrr 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 785 ----IAVYPPQSITPEQKARVIEITTQIAKSLHTKGLINIQFVLFKG-DIYVLEVNPRASRTVPFLSKVTGIPMAQVATR 859
Cdd:PRK06111 235 hqkvIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQkNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLR 314
|
....*...
gi 1361143904 860 IMLGESLQ 867
Cdd:PRK06111 315 IAAGEKLS 322
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
651-866 |
3.46e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 66.70 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 651 GIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGA--AVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEIVYSESELR 728
Cdd:PRK12833 102 GLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSdgVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 729 SYMEVAvQVNPEHP-----VLIDRYLL-GKELEVDAICDGEDVLipgimeHI-ERAGVHSGDSIAVY---PPQSITPEQK 798
Cdd:PRK12833 182 AELPLA-QREAQAAfgdggVYLERFIArARHIEVQILGDGERVV------HLfERECSLQRRRQKILeeaPSPSLTPAQR 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1361143904 799 ARVIEITTQIAKSLHTKGLINIQFvLF---KGDIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIMLGESL 866
Cdd:PRK12833 255 DALCASAVRLARQVGYRGAGTLEY-LFddaRGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPL 324
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
615-875 |
4.93e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 65.72 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 615 YKEDVLNIIEKENPlGVIVQFGGQTALNLA--RDLREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAVTSVE 692
Cdd:COG3919 64 FVDALLELAERHGP-DVLIPTGDEYVELLSrhRDELEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSAD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 693 EAAQVAARLGYPVLVRPSY--------VLGGRAMEIVYSESELRSYMEVAVQvnPEHPVLIDRYL---LGKELEVDAICD 761
Cdd:COG3919 143 DLDALAEDLGFPVVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAA--AGYELIVQEYIpgdDGEMRGLTAYVD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 762 --GEDVLIPG---IMEHIERAGVHSGdSIAVYPPQsitpeqkarVIEITTQIAKSLHTKGLINIQFvlfK-----GDIYV 831
Cdd:COG3919 221 rdGEVVATFTgrkLRHYPPAGGNSAA-RESVDDPE---------LEEAARRLLEALGYHGFANVEF---KrdprdGEYKL 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1361143904 832 LEVNPRASRTVpFLSKVTGIPMAQVATRIMLGESL-QEQGYDNGL 875
Cdd:COG3919 288 IEINPRFWRSL-YLATAAGVNFPYLLYDDAVGRPLePVPAYREGV 331
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
648-866 |
5.94e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 65.89 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 648 REEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGA--AVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEIVYSES 725
Cdd:PRK05586 96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSegEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 726 ELRS------------------YMEVAVQvNPEHpvlIDRYLLGKELE-VDAICDGEDVLIPGIMEHIERAgvhsgdsia 786
Cdd:PRK05586 176 ELIKafntakseakaafgddsmYIEKFIE-NPKH---IEFQILGDNYGnVVHLGERDCSLQRRNQKVLEEA--------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 787 vyPPQSITPEQKARVIEITTQIAKSLHTKGLINIQFVLFK-GDIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIMLGES 865
Cdd:PRK05586 243 --PSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKdGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
.
gi 1361143904 866 L 866
Cdd:PRK05586 321 L 321
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
114-303 |
8.82e-11 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 66.32 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 114 RLLGTDLRAITNAEdrdlfrslmnELNEPV-PES-VIVQSVEEAVDFAGETGYPVIVRPAytLGGTGGG--IAHTEAELR 189
Cdd:PRK12999 115 RLLGDKVAARNAAI----------KAGVPViPGSeGPIDDIEEALEFAEEIGYPIMLKAS--AGGGGRGmrIVRSEEELE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 190 EIVDNGLR-----------YspicqclIEKSIAGYKEIEYEVMRDANDNciVV------CNME-NFDPVgvhtgdsIVFA 251
Cdd:PRK12999 183 EAFERAKReakaafgndevY-------LEKYVENPRHIEVQILGDKHGN--VVhlyerdCSVQrRHQKV-------VEIA 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1361143904 252 PSQTLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDPHSfQYYVIEVNPRV 303
Cdd:PRK12999 247 PAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
683-843 |
1.34e-10 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 63.59 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 683 PPGAAVTSVEEAAQVAARLGYPVLVRPsyVLGGR--AMEIVYSESELRSYMEVAVQVNPEhpVLIDRYLLGKELEVdAIC 760
Cdd:PRK01372 114 PPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAFKYDDE--VLVEKYIKGRELTV-AVL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 761 DGEdVLipGIMEhIERAGV--------HSGDSIAVYPPQsITPEQKARVIEITTQIAKSLHTKGLINIQFVL-FKGDIYV 831
Cdd:PRK01372 189 GGK-AL--PVIE-IVPAGEfydyeakyLAGGTQYICPAG-LPAEIEAELQELALKAYRALGCRGWGRVDFMLdEDGKPYL 263
|
170
....*....|..
gi 1361143904 832 LEVNprasrTVP 843
Cdd:PRK01372 264 LEVN-----TQP 270
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
646-855 |
2.74e-10 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 63.40 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 646 DLREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPgaaVTSVEEAAQvaarlgYPVLVRPSYVLGGRAMEIVYSES 725
Cdd:COG2232 91 ERLARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPE---TRFEPPPDP------GPWLVKPIGGAGGWHIRPADSEA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 726 ELRSymevavqvnpehPVLIDRYLLGKELEVDAICDGEDVLIPGIMEHIERAG-----VHSGdsiAVYPPQsITPEQKAR 800
Cdd:COG2232 162 PPAP------------GRYFQRYVEGTPASVLFLADGSDARVLGFNRQLIGPAgerpfRYGG---NIGPLA-LPPALAEE 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1361143904 801 VIEITTQIAKSLHTKGLINIQFVLFKGDIYVLEVNPRASRTVPFLSKVTGIPMAQ 855
Cdd:COG2232 226 MRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFD 280
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-303 |
3.30e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 63.62 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 1 MPKdpTLKKILVIGSGPI---VIGQAAEFDYAGTQACQALKEEGLEVVLVNSnpaTIMTDTNMADRVYIEPltaEFITQV 77
Cdd:PRK12833 1 MPS--RIRKVLVANRGEIavrIIRAARELGMRTVAACSDADRDSLAARMADE---AVHIGPSHAAKSYLNP---AAILAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 78 IRKERPDGLLPTLGGqtgLNLAVELAKQgvLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEP-VPESV-IVQSVEEA 155
Cdd:PRK12833 73 ARQCGADAIHPGYGF---LSENAAFAEA--VEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPtVPGSDgVVASLDAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 156 VDFAGETGYPVIVRPAYTLGGTGGGIAHTEAELReivdnglRYSPICQ-----------CLIEKSIAGYKEIEYEVMRDA 224
Cdd:PRK12833 148 LEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLA-------AELPLAQreaqaafgdggVYLERFIARARHIEVQILGDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 225 NDnciVVCNMENfdPVGVHTGDSIVF--APSQTLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDPHSFQYYVIEVNPR 302
Cdd:PRK12833 221 ER---VVHLFER--ECSLQRRRQKILeeAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTR 295
|
.
gi 1361143904 303 V 303
Cdd:PRK12833 296 I 296
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
35-193 |
8.96e-10 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 61.11 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 35 QALKEEGLEVVLVNsnpatimtdtnmADRVYIEPLTAEFITQVIRKERPDGLLPTlggQTGLNLAVELAKQgvLEREGVR 114
Cdd:COG0189 21 EAAQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPR---IDPPFYGLALLRQ--LEAAGVP 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1361143904 115 LLGtDLRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAGETGYPVIVRPAYTLGGTGGGIAHTEAELREIVD 193
Cdd:COG0189 84 VVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILE 161
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
650-869 |
9.10e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 62.07 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 650 EGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGA--AVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEIVYSESEL 727
Cdd:PRK08462 100 HNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 728 RS------------------YMEVAVQvNPEHpvlidryllgkeLEVDAICDGEDVLIpgimeHI-ER---AGVHSGDSI 785
Cdd:PRK08462 180 ENlylaaesealsafgdgtmYMEKFIN-NPRH------------IEVQILGDKHGNVI-----HVgERdcsLQRRHQKLI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 786 AVYPPQSITPEQKARVIEITTQIAKSLHTKGLINIQFVLFKG-DIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIMLGE 864
Cdd:PRK08462 242 EESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNlDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGE 321
|
....*
gi 1361143904 865 SLQEQ 869
Cdd:PRK08462 322 ELPSQ 326
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
679-837 |
1.11e-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: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 679 KIAQPPGAAVTSVEEAAQVAARLGYPVLVRpSYVLG--GRAMEIVYSESELRSYMEVAVQVnpehPVLIDRYL-LGKELE 755
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVK-ARRGGydGKGQYVVRSEADLPQAWEELGDG----PVIVEEFVpFDRELS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 756 VDAI--CDGEDVLIPgIMEHIERagvhSGDSIAVYPPQSITPEQKARVIEITTQIAKSLHTKGLINIQ-FVLFKGDIYVL 832
Cdd:pfam02222 79 VLVVrsVDGETAFYP-VVETIQE----DGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVElFVTEDGDLLIN 153
|
....*
gi 1361143904 833 EVNPR 837
Cdd:pfam02222 154 ELAPR 158
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
643-870 |
1.26e-09 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 62.46 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 643 LARDLREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPG--AAVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEI 720
Cdd:PRK12999 95 FARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 721 VYSESELRSYMEVAVQV------NPEhpVLIDRYLLG-KELEVDAICDGEdvlipGIMEH---------------IERAg 778
Cdd:PRK12999 175 VRSEEELEEAFERAKREakaafgNDE--VYLEKYVENpRHIEVQILGDKH-----GNVVHlyerdcsvqrrhqkvVEIA- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 779 vhsgdsiavyPPQSITPEQKARVIEITTQIAKSLhtkGLINIQFVLF----KGDIYVLEVNPR--ASRTVPflSKVTGIP 852
Cdd:PRK12999 247 ----------PAPGLSEELRERICEAAVKLARAV---GYVNAGTVEFlvdaDGNFYFIEVNPRiqVEHTVT--EEVTGID 311
|
250
....*....|....*...
gi 1361143904 853 MAQVATRIMLGESLQEQG 870
Cdd:PRK12999 312 IVQSQILIAEGATLHDLE 329
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
149-303 |
1.51e-09 |
|
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: 62.40 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 149 VQSVEEAVDFAGETGYPVIVRPAytLGGTGGG--IAHTEAELREIVDNGLR-----------YspicqclIEKSIAGYKE 215
Cdd:COG1038 141 VDDLEEALAFAEEIGYPVMLKAA--AGGGGRGmrVVRSEEELEEAFESARReakaafgddevF-------LEKYIERPKH 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 216 IEYEVMRDANDNCI---------------VVcnmEnfdpvgvhtgdsivFAPSQTLSDREYHMLRTSALKIIRSLNIQGG 280
Cdd:COG1038 212 IEVQILGDKHGNIVhlferdcsvqrrhqkVV---E--------------IAPAPNLDEELREAICEAAVKLAKAVGYVNA 274
|
170 180
....*....|....*....|...
gi 1361143904 281 CNVQFALDPHSfQYYVIEVNPRV 303
Cdd:COG1038 275 GTVEFLVDDDG-NFYFIEVNPRI 296
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
656-865 |
3.27e-09 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 61.02 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 656 GTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEIVYSESELRSYMEVAV 735
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 736 QVNPEHpVLIDRYLLGKELEVDAICDGEDVLIPGIM-EHIERAGvHSGDSIAVYPPQSITPEQKARVIEITTQIAKSLHT 814
Cdd:PRK02186 176 RAGTRA-ALVQAYVEGDEYSVETLTVARGHQVLGITrKHLGPPP-HFVEIGHDFPAPLSAPQRERIVRTVLRALDAVGYA 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1361143904 815 KGLINIQFVLFKGDIYVLEVNPR-ASRTVP-FLSKVTGIPMAQVATRIMLGES 865
Cdd:PRK02186 254 FGPAHTELRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVIDLHLGVA 306
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
113-315 |
4.04e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 60.11 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 113 VRLLGTDLRAITNAEDRDLFRSLMNELNEP-VPESV-IVQSVEEAVDFAGETGYPVIVRPAYTLGGTGGGIAHTEAELRE 190
Cdd:PRK05586 100 IVFIGPDSETIELMGNKSNAREIMIKAGVPvVPGSEgEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 191 IVDNGLRYSPIC----QCLIEKSIAGYKEIEYEVMRDANDNCIVVCNMEnfdpVGVHTGDSIVF--APSQTLSDREYHML 264
Cdd:PRK05586 180 AFNTAKSEAKAAfgddSMYIEKFIENPKHIEFQILGDNYGNVVHLGERD----CSLQRRNQKVLeeAPSPVMTEELRKKM 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1361143904 265 RTSALKIIRSLNIQGGCNVQFALDPHSfQYYVIEVNPRVSRSSALASKATG 315
Cdd:PRK05586 256 GEIAVKAAKAVNYKNAGTIEFLLDKDG-NFYFMEMNTRIQVEHPITEMITG 305
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
945-1041 |
9.62e-09 |
|
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 238297 [Multi-domain] Cd Length: 112 Bit Score: 54.05 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 945 DKEKEEAVSLMRRFHQLGYKIVCTSGTADILEAASLPVERVHKLREGS-PHILDLIR-QGKADLVVNTWTRGRTP--ERD 1020
Cdd:cd00532 8 DHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEDGePTVDAAIAeKGKFDVVINLRDPRRDRctDED 87
|
90 100
....*....|....*....|.
gi 1361143904 1021 GFRIRREAVENGIACLTSLDT 1041
Cdd:cd00532 88 GTALLRLARLYKIPVTTPNAT 108
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
643-837 |
1.06e-08 |
|
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: 59.71 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 643 LARDLREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPG--AAVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEI 720
Cdd:COG1038 94 FARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 721 VYSESELRSYMEVAVQV------NPEhpVLIDRYLLG-KELEVDAICDGEdvlipGIMEH---------------IERAg 778
Cdd:COG1038 174 VRSEEELEEAFESARREakaafgDDE--VFLEKYIERpKHIEVQILGDKH-----GNIVHlferdcsvqrrhqkvVEIA- 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1361143904 779 vhsgdsiavyPPQSITPEQKARVIEITTQIAKSLhtkGLINIQFVLF----KGDIYVLEVNPR 837
Cdd:COG1038 246 ----------PAPNLDEELREAICEAAVKLAKAV---GYVNAGTVEFlvddDGNFYFIEVNPR 295
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
109-303 |
1.46e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 58.50 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 109 EREGVRLLGTDLRAITNAEDRDLFRSLMNELNEP-VP-ESVIVQSVEEAVDFAGETGYPVIVRPAYTLGGTGGGIAHTEA 186
Cdd:PRK06111 96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPvVPgITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 187 ELREIVD-----------NGLRYspicqclIEKSIAGYKEIEYEVMRDANDNCIVV----CNMENfdpvgvHTGDSIVFA 251
Cdd:PRK06111 176 ELTKAFEsnkkraanffgNGEMY-------IEKYIEDPRHIEIQLLADTHGNTVYLwereCSVQR------RHQKVIEEA 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1361143904 252 PSQTLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDPHSfQYYVIEVNPRV 303
Cdd:PRK06111 243 PSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQK-NFYFLEMNTRL 293
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
673-860 |
2.39e-08 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 57.05 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 673 KLLNDTKIAQPPGAAVTSVEEA----AQVAARLGYPVLVRPSyvlggRA-----MEIVYSESELRSYMEVAVQVNPEhpV 743
Cdd:PRK01966 129 RLLAAAGIPVAPYVVLTRGDWEeaslAEIEAKLGLPVFVKPA-----NLgssvgISKVKNEEELAAALDLAFEYDRK--V 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 744 LIDRYLLGKELEVDAICDGEDVLIPGimEHIeragVHSG----------DSIAVYPPQSITPEQKARVIEITTQIAKSLH 813
Cdd:PRK01966 202 LVEQGIKGREIECAVLGNDPKASVPG--EIV----KPDDfydyeakyldGSAELIIPADLSEELTEKIRELAIKAFKALG 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1361143904 814 TKGLINIQFVLFK-GDIYVLEVNprasrTVP-FLS--------KVTGIPMAQVATRI 860
Cdd:PRK01966 276 CSGLARVDFFLTEdGEIYLNEIN-----TMPgFTPismypklwEASGLSYPELIDRL 327
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
700-837 |
3.73e-08 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 53.93 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 700 RLGYPVLVRPSYVLGGRAMEIVYSESELRSYMEvavqvnpehPVLIDRYLLGKELEVDAICDGEDVLI----PGIMEHIE 775
Cdd:pfam02655 29 REEKKYVVKPRDGCGGEGVRKVENGREDEAFIE---------NVLVQEFIEGEPLSVSLLSDGEKALPlsvnRQYIDNGG 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1361143904 776 RAGVHSGDSIavyppQSITPEQKaRVIEITTQIAKSLH-TKGLINIQFVLFKGDIYVLEVNPR 837
Cdd:pfam02655 100 SGFVYAGNVT-----PSRTELKE-EIIELAEEVVECLPgLRGYVGVDLVLKDNEPYVIEVNPR 156
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
942-1037 |
4.13e-08 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 52.69 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 942 TIGDKEKEEAVSLMRRFHQLGYKIVCTSGTADILEAASLPVERVHKLRE----GSPHILDLIRQGKADLVVNTWTRGRTP 1017
Cdd:cd01423 6 SIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEepqnDKPSLRELLAEGKIDLVINLPSNRGKR 85
|
90 100
....*....|....*....|.
gi 1361143904 1018 ERD-GFRIRREAVENGIACLT 1037
Cdd:cd01423 86 VLDnDYVMRRAADDFAVPLIT 106
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
7-315 |
4.25e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 57.03 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 7 LKKILVIGSGPIVIgqaaefdyagtQACQALKEEGLEVVLVNSNPATIMTDTNMADRVYI---EP----LTAEFITQVIR 79
Cdd:PRK07178 2 IKKILIANRGEIAV-----------RIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSigaDPlagyLNPRRLVNLAV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 80 KERPDGLLPTLGGqtgLNLAVELAKqgVLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEPV-PESV-IVQSVEEAVD 157
Cdd:PRK07178 71 ETGCDALHPGYGF---LSENAELAE--ICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVtPGSEgNLADLDEALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 158 FAGETGYPVIVRPayTLGGTGGGI--AHTEAELRE----IVDNGLRYSPICQCLIEKSIAGYKEIEYEVMRDANDNCIVV 231
Cdd:PRK07178 146 EAERIGYPVMLKA--TSGGGGRGIrrCNSREELEQnfprVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 232 ----CNMENfdpvgvHTGDSIVFAPSQTLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDpHSFQYYVIEVNPRVSRSS 307
Cdd:PRK07178 224 ferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLD-ADGEVYFMEMNTRVQVEH 296
|
....*...
gi 1361143904 308 ALASKATG 315
Cdd:PRK07178 297 TITEEITG 304
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
128-303 |
4.47e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 56.73 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 128 DRDLFRSLMNELNEP-VPESV-IVQSVEEAVDFAGETGYPVIVRPayTLGGTGGGI--AHTEAELREIVD---------- 193
Cdd:PRK08591 115 DKVTAKATMKKAGVPvVPGSDgPVDDEEEALAIAKEIGYPVIIKA--TAGGGGRGMrvVRTEAELEKAFSmaraeakaaf 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 194 -NGLRYspicqclIEKSIAGYKEIEYEVMRDANDNCIvvcnmenfdpvgvHTGD---SI------VF--APSQTLSDREY 261
Cdd:PRK08591 193 gNPGVY-------MEKYLENPRHIEIQVLADGHGNAI-------------HLGErdcSLqrrhqkVLeeAPSPAITEELR 252
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1361143904 262 HMLRTSALKIIRSLNIQGGCNVQFALDpHSFQYYVIEVNPRV 303
Cdd:PRK08591 253 RKIGEAAVKAAKAIGYRGAGTIEFLYE-KNGEFYFIEMNTRI 293
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
669-837 |
5.87e-08 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 54.21 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 669 KKFEK-LLNDTKIAQPPGAAVTSVEEAAQVAARLGYPVLV-RPSYVLGGRAMEIVYSESE----LRSYMEVAVQVNPEHP 742
Cdd:pfam01071 3 KSFAKdFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVvKADGLAAGKGVIVASSNEEaikaVDEILEQKKFGEAGET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 743 VLIDRYLLGKELEVDAICDGEDVL-IPGIMEHiERA-----GVHSGDSIAVYPPQSITPEQKARVIE-ITTQIAKSLHT- 814
Cdd:pfam01071 83 VVIEEFLEGEEVSVLAFVDGKTVKpLPPAQDH-KRAgegdtGPNTGGMGAYSPAPVITPELLERIKEtIVEPTVDGLRKe 161
|
170 180
....*....|....*....|....*..
gi 1361143904 815 ----KGLINIQFVLFKGDIYVLEVNPR 837
Cdd:pfam01071 162 gipfKGVLYAGLMLTKDGPKVLEFNCR 188
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
572-855 |
8.84e-08 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 54.95 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 572 DYATVHAIWAIRAAGYEAVIINnnPETVSTDFNTSDRLY-FEPLYKEDVlnIIEKENPLgvivqfggQTALNLARDLREE 650
Cdd:COG0189 13 KDSTKALIEAAQRRGHEVEVID--PDDLTLDLGRAPELYrGEDLSEFDA--VLPRIDPP--------FYGLALLRQLEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 651 GIKILGtSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEIVYSESELRSY 730
Cdd:COG0189 81 GVPVVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 731 MEvAVQVNPEHPVLIDRYLlGKELEVD---AICDGEdvLIPGIM----EHIERAGVHSGDSIAVYPpqsITPEqkarVIE 803
Cdd:COG0189 160 LE-ALTELGSEPVLVQEFI-PEEDGRDirvLVVGGE--PVAAIRripaEGEFRTNLARGGRAEPVE---LTDE----ERE 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1361143904 804 ITTQIAKSLhtKGLIN-IQFVLFKGDIYVLEVNPRASrtVPFLSKVTGIPMAQ 855
Cdd:COG0189 229 LALRAAPAL--GLDFAgVDLIEDDDGPLVLEVNVTPG--FRGLERATGVDIAE 277
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
684-869 |
1.52e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 55.19 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 684 PGA--AVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEIVYSESELRSYMEVAVQV------NPEhpVLIDRYLLG-KEL 754
Cdd:PRK08591 132 PGSdgPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEakaafgNPG--VYMEKYLENpRHI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 755 EVDAICDGedvlipgimehiERAGVHSGD---SI----------AvyPPQSITPEQKARVIEITTQIAKSLHTKGLINIQ 821
Cdd:PRK08591 210 EIQVLADG------------HGNAIHLGErdcSLqrrhqkvleeA--PSPAITEELRRKIGEAAVKAAKAIGYRGAGTIE 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1361143904 822 FVL-FKGDIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIMLGESL---QEQ 869
Cdd:PRK08591 276 FLYeKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsikQED 327
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
32-300 |
7.93e-07 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 52.04 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 32 QAC-QALKEEGLEVVLVNsnpatimtdtnmadrvyieplTAEFITQVIRKERPDGLLPTLGGQTGLNLAVelakQGVLER 110
Cdd:PRK01372 26 AAVlAALREAGYDAHPID---------------------PGEDIAAQLKELGFDRVFNALHGRGGEDGTI----QGLLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 111 EGVRLLGTDLRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAGETGYPVIVRPAytLGGTGGGIA--HTEAEL 188
Cdd:PRK01372 81 LGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPA--REGSSVGVSkvKEEDEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 189 REIVDNGLRYSPicQCLIEKSIAGykeIEYEVmrdandnCIV------VCNMEnfdPVGV--------HTGDSIVFAPSQ 254
Cdd:PRK01372 159 QAALELAFKYDD--EVLVEKYIKG---RELTV-------AVLggkalpVIEIV---PAGEfydyeakyLAGGTQYICPAG 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1361143904 255 tLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDPHSfQYYVIEVN 300
Cdd:PRK01372 224 -LPAEIEAELQELALKAYRALGCRGWGRVDFMLDEDG-KPYLLEVN 267
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
148-301 |
1.24e-06 |
|
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: 50.39 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 148 IVQSVEEAVdfagetGYPVIVRPAytLGGTGGGI--AHTEAELREIVDNGLRYSPicQCLIEKSIAGyKEIEYEVMrdAN 225
Cdd:pfam07478 27 WCAQVEEAL------GYPVFVKPA--RLGSSVGVskVESREELQAAIEEAFQYDE--KVLVEEGIEG-REIECAVL--GN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 226 DNCIVVcnmenfdPVGVHTGDSIVF------APSQT-------LSDREYHMLRTSALKIIRSLNIQGGCNVQFALDPhSF 292
Cdd:pfam07478 94 EDPEVS-------PVGEIVPSGGFYdyeakyIDDSAqivvpadLEEEQEEQIQELALKAYKALGCRGLARVDFFLTE-DG 165
|
....*....
gi 1361143904 293 QYYVIEVNP 301
Cdd:pfam07478 166 EIVLNEVNT 174
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
748-868 |
2.69e-06 |
|
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: 47.61 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 748 YLLGKELEVDAICDGEDVLIPgimehIERAGVHSGDsiavyppQSItpEQKARVIEITTQIAKSLHTKGLINIQFVLFKG 827
Cdd:pfam15632 10 YLPGPEYSVDCLAGHGELIAA-----VPRRKGDGGI-------QTL--EDDPELIEAARRLAEAFGLDGLFNVQFRYDGD 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1361143904 828 DIYVLEVNPRASRTVPfLSKVTGIPMAQVATRIMLGESLQE 868
Cdd:pfam15632 76 GPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGLETPD 115
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
126-212 |
8.36e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 49.77 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 126 AEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAGETGYPVIVRPAYtlGGTGGGIA---HTEAELREIVDNGLRYSPic 202
Cdd:PRK14016 212 ACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLD--GNHGRGVTvniTTREEIEAAYAVASKESS-- 287
|
90
....*....|
gi 1361143904 203 QCLIEKSIAG 212
Cdd:PRK14016 288 DVIVERYIPG 297
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
673-753 |
2.30e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 48.61 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 673 KLLNDTKIAQPPGAAVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEI-VYSESELRSYMEVAVQVNPEhpVLIDRYLLG 751
Cdd:PRK14016 220 RLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESSD--VIVERYIPG 297
|
..
gi 1361143904 752 KE 753
Cdd:PRK14016 298 KD 299
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
697-835 |
4.82e-05 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 46.75 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 697 VAARLGYPVLVRPSYVLGGRAMEIVYSESELRSYMEVAVQVnpEHPVLIDRYLLGKELEVDAICDGE-DVLIPG------ 769
Cdd:PRK14570 166 IKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKY--DLTVVIEKFIEAREIECSVIGNEQiKIFTPGeivvqd 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 770 --IMEHIERAGVHSGDSIAVYPPQSITPEQKARVIEITTQIAKSLHTKGLINIQFVLFK--GDIYVLEVN 835
Cdd:PRK14570 244 fiFYDYDAKYSTIPGNSIVFNIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKdtGLIYLNEIN 313
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
701-864 |
8.67e-05 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 45.97 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 701 LGYPVLVRPSYVLGGRAMEIVYSESELRSYMEVAVQVNPEhpVLIDRYLLGKELEVDAICDGEDVLIPGIMEHieRAGVH 780
Cdd:PRK14571 124 LGYPCVVKPRREGSSIGVFICESDEEFQHALKEDLPRYGS--VIVQEYIPGREMTVSILETEKGFEVLPILEL--RPKRR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 781 SGDSIAVYP--------PQSITPEQKARVIEITTQIAKSLHTKGLINIQFVLFKGDIYVLEVNprasrTVPFLSKVTGIP 852
Cdd:PRK14571 200 FYDYVAKYTkgetefilPAPLNPEEERLVKETALKAFVEAGCRGFGRVDGIFSDGRFYFLEIN-----TVPGLTELSDLP 274
|
170
....*....|..
gi 1361143904 853 MAQVATRIMLGE 864
Cdd:PRK14571 275 ASAKAGGIEFEE 286
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
107-303 |
1.39e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 45.51 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 107 VLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEPV-PESV-IVQSVEEAVDFAGETGYPVIVRPAYTLGGTGGGIAHT 184
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPViPGSDgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 185 EAELREI-----------VDNGLRYspicqclIEKSIAGYKEIEYEVMRDANDNCIVV----CNMENfdpvgvHTGDSIV 249
Cdd:PRK08462 176 ESDLENLylaaesealsaFGDGTMY-------MEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIE 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1361143904 250 FAPSQTLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDpHSFQYYVIEVNPRV 303
Cdd:PRK08462 243 ESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRL 295
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
647-837 |
1.58e-04 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 45.39 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 647 LREEGIKILGTSleeidRA----EDRKKFEK-LLNDTKIAQPPGAAVTSVEEAAQVAARLGYPVLVRPSYVLGGRAMEIV 721
Cdd:COG0151 82 FRAAGIPVFGPS-----KAaaqlEGSKAFAKeFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 722 YSESE----LRSYMEVAVQVNPEHPVLIDRYLLGKELEVDAICDGEDVLI-PGIMEHiERAGvhSGD---------SIAv 787
Cdd:COG0151 157 ETLEEalaaVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPlPTAQDH-KRAG--DGDtgpntggmgAYS- 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1361143904 788 yPPQSITPEQKARVI-EITTQIAKSLHT-----KGLINIQFVLFKGDIYVLEVNPR 837
Cdd:COG0151 233 -PAPVVTEELLEKIMeEIIEPTVAGMAAegipyRGVLYAGLMITADGPKVLEFNVR 287
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
616-846 |
3.30e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 43.90 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 616 KEDVLNIIEKeNPLGVIVQFGGQTALN--LARDLREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAVTSVEE 693
Cdd:PRK14569 46 KELVAKLLEL-KPDKCFVALHGEDGENgrVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPTPMAKFLTDKLV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 694 AAQvaaRLGYPVLVRPSYvlGGRAMEI--VYSESELRSYMEvavQVNPEHPVLIDRYLLGKELEVdAICDGE---DVLIP 768
Cdd:PRK14569 125 AED---EISFPVAVKPSS--GGSSIATfkVKSIQELKHAYE---EASKYGEVMIEQWVTGKEITV-AIVNDEvysSVWIE 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1361143904 769 GIMEHIERAGVHSGDSIaVYPPQSITPEQKARVIEITTQIAKSLHTKGLINIQFVLF-KGDIYVLEVNPRASRTVPFLS 846
Cdd:PRK14569 196 PQNEFYDYESKYSGKSI-YHSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDdRGNFYIMEINSSPGMTDNSLS 273
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
84-300 |
4.98e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 43.67 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 84 DGLLPTLGGQTGLNLAVelakQGVLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEP-VP------ESVIVQSVEEAV 156
Cdd:PRK14570 89 DVVFPIVHGRTGEDGAI----QGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPlVPfigfrkYDYFLDKEGIKK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 157 DFAGETGYPVIVRPAYTLGGTGGGIAHTEAELREIVDNGLRYSpiCQCLIEKSIAGyKEIEYEVMrdANDNC-------I 229
Cdd:PRK14570 165 DIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYD--LTVVIEKFIEA-REIECSVI--GNEQIkiftpgeI 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1361143904 230 VVCNMENFD---PVGVHTGDSIVFAPSQTLSDREYHMLRTSALKIIRSLNIQGGCNVQFALDPHSFQYYVIEVN 300
Cdd:PRK14570 240 VVQDFIFYDydaKYSTIPGNSIVFNIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKDTGLIYLNEIN 313
|
|
| cya_phycin_syn |
TIGR02068 |
cyanophycin synthetase; Cyanophycin is an insoluble storage polymer for carbon, nitrogen, and ... |
126-190 |
7.71e-04 |
|
cyanophycin synthetase; Cyanophycin is an insoluble storage polymer for carbon, nitrogen, and energy, found in most Cyanobacteria. The polymer has a backbone of L-aspartic acid, with most Asp side chain carboxyl groups attached to L-arginine. The polymer is made by this enzyme, cyanophycin synthetase, and degraded by cyanophycinase. Heterologously expressed cyanophycin synthetase in E. coli produces a closely related, water-soluble polymer with some Arg replaced by Lys. It is unclear whether enzymes that produce soluble cyanophycin-like polymers in vivo in non-Cyanobacterial species should be designated as cyanophycin synthetase itself or as a related enzyme. This model makes the designation as cyanophycin synthetase. Cyanophycin synthesis is analogous to polyhydroxyalkanoic acid (PHA) biosynthesis, except that PHA polymers lack nitrogen and may be made under nitrogen-limiting conditions. [Cellular processes, Biosynthesis of natural products]
Pssm-ID: 273950 [Multi-domain] Cd Length: 864 Bit Score: 43.62 E-value: 7.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1361143904 126 AEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAGETGYPVIVRPaytLGGTGGGIAHTEAELRE 190
Cdd:TIGR02068 211 ACDKDLTKEILSDAGVPVPEGTVVQSAEDAWEAAQDLGYPVVIKP---YDGNHGRGVTINILTRD 272
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
2-170 |
7.92e-04 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 43.20 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 2 PKDPTLKKILVIGSG----PIVIgqaaefdyagtqACQALkeeGLEVVLVNS--N-PAtimtdtnM--ADRVY-IEPLTA 71
Cdd:PRK09288 7 PLSPSATRVMLLGSGelgkEVAI------------EAQRL---GVEVIAVDRyaNaPA-------MqvAHRSHvIDMLDG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 72 EFITQVIRKERPDGLLPTLGGqtglnLAVE-LAKqgvLEREGVRLLGTdLRAITNAEDRDLFRSLM-NELNEPVPESVIV 149
Cdd:PRK09288 65 DALRAVIEREKPDYIVPEIEA-----IATDaLVE---LEKEGFNVVPT-ARATRLTMNREGIRRLAaEELGLPTSPYRFA 135
|
170 180
....*....|....*....|.
gi 1361143904 150 QSVEEAVDFAGETGYPVIVRP 170
Cdd:PRK09288 136 DSLEELRAAVEEIGYPCVVKP 156
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
644-867 |
1.08e-03 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 42.88 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 644 ARDLREEGIKILGTSLEEIDRAEDRKKFEKLLNDTKIAQPPGAAV---TSVEEAAQVAARLGYPVLVRPSYVLGGRAMEI 720
Cdd:PRK08463 91 AKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlnsESMEEIKIFARKIGYPVILKASGGGGGRGIRV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 721 VYSESELRSYMEV----AVQVNPEHPVLIDRYLLG-KELEVDAICDGEDVLIpGIMEH---IERAgvHSgDSIAVYPPQS 792
Cdd:PRK08463 171 VHKEEDLENAFESckreALAYFNNDEVFMEKYVVNpRHIEFQILGDNYGNII-HLCERdcsIQRR--HQ-KVIEIAPCPS 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1361143904 793 ITPEQKARVIEITTQIAKSLHTKGLINIQFVLFK-GDIYVLEVNPRASRTVPFLSKVTGIPMAQVATRIMLGESLQ 867
Cdd:PRK08463 247 ISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDyNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILD 322
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
121-279 |
1.22e-03 |
|
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: 42.37 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 121 RAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAGETGYPVIVRPAyTLG--GTGGGIAHTEAELREIVDnGLRY 198
Cdd:COG0026 82 EALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTR-RGGydGKGQVVIKSAADLEAAWA-ALGG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 199 SPicqCLIEKSIAgykeIEYE----VMRDANDNciVVCnmenFDPV-GVHTgDSI---VFAPSQtLSDREYHMLRTSALK 270
Cdd:COG0026 160 GP---CILEEFVP----FERElsviVARSPDGE--VAT----YPVVeNVHR-NGIldeSIAPAR-ISEALAAEAEEIAKR 224
|
....*....
gi 1361143904 271 IIRSLNIQG 279
Cdd:COG0026 225 IAEALDYVG 233
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
105-217 |
1.45e-03 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 42.03 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 105 QGVLEREGVRLLGTDLRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEA----VDFAGETGYPVIVRPAytlggTGG- 179
Cdd:PRK01966 100 QGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLTRGDWEeaslAEIEAKLGLPVFVKPA-----NLGs 174
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1361143904 180 --GI--AHTEAELREIVDNGLRYSPicQCLIEKSIAGyKEIE 217
Cdd:PRK01966 175 svGIskVKNEEELAAALDLAFEYDR--KVLVEQGIKG-REIE 213
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
928-997 |
2.74e-03 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 41.70 E-value: 2.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 928 AAGISLPRFGTVVATIGDKEKEEAVSLMRRFHQLGYKIVCTSGTADILEAASLPVERVHKLrEGSPHILD 997
Cdd:PLN02891 12 AQPQSSPSSGKKQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEEL-TNFPEMLD 80
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
952-997 |
3.42e-03 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 41.23 E-value: 3.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1361143904 952 VSLMRRFHQLGYKIVCTSGTADILEAASLPVERVHKLrEGSPHILD 997
Cdd:PRK00881 18 VEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDV-TGFPEILD 62
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
120-276 |
4.63e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 40.52 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 120 LRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAGETGYPVIVRpAYTLG--GTGGGIAHTEAELREIVDNgLR 197
Cdd:PRK06019 92 PDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLK-TRRGGydGKGQWVIRSAEDLEAAWAL-LG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 198 YSPicqCLIEKSIAgykeIEYE----VMRDANDNCIVvcnmenFDPV------GV-HTgdSIVFAP-SQTLSDREYHMlr 265
Cdd:PRK06019 170 SVP---CILEEFVP----FEREvsviVARGRDGEVVF------YPLVenvhrnGIlRT--SIAPARiSAELQAQAEEI-- 232
|
170
....*....|.
gi 1361143904 266 tsALKIIRSLN 276
Cdd:PRK06019 233 --ASRIAEELD 241
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
108-209 |
7.26e-03 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 39.64 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143904 108 LEREGVRLLGTDlRAITNAEDRDLFRSLMNELNEPVPESVIVQSVEEAVDFAGETGYPVIVRPAYTLGGTGGGIAHTEAE 187
Cdd:TIGR00768 69 LESLGVPVINSS-DAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQA 147
|
90 100
....*....|....*....|....*..
gi 1361143904 188 LREIVD-----NGLRYSPICQCLIEKS 209
Cdd:TIGR00768 148 AESLLEhfeqlNGPQNLFLVQEYIKKP 174
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
129-194 |
9.04e-03 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 39.69 E-value: 9.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1361143904 129 RDLFRslmnELNEPVPESVIVQSVEEAVDFAGE-TGYPVIVRPAYTLGGTG--GGI--AHTEAELREIVDN 194
Cdd:PRK00696 9 KELFA----KYGVPVPRGIVATTPEEAVEAAEElGGGVWVVKAQVHAGGRGkaGGVklAKSPEEAREFAKQ 75
|
|
| |
