|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1069 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2221.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 1 MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 81 ERPDAVLPTMGGQTALNCALELERQGVLAEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEALAVAA 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 161 DVGFPCIIRPSFTMGGTGGGIAYNREEFEEICERGLDLSPTNELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAM 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 241 GIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 321 KVAAKLAVGYTLDELMNDITGgRTPASFEPSIDYVVTKIPRFNFEKFVGANDRLTTQMKSVGEVMAIGRTQQESLQKALR 400
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITG-KTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 401 GLEVGATGFDPKvsLDDPEALTKIRRELKDAGAERIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKvIDLG 480
Cdd:PRK05294 400 SLEIGVTGLDED--LFEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEE-LKEN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 481 INGLDADFLRVLKRKGFADARLAKLAGVREAEIRKLRDQYNLHPVYKRVDTCAAEFATDTAYMYSTYEDECEANPSvDRD 560
Cdd:PRK05294 477 GLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPS-DRK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 561 KIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIV 640
Cdd:PRK05294 556 KVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIV 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 641 QYGGQTPLKLARALEAAGVPVIGTSPDAIDRAEDRERFQQAVDRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRPSYVL 720
Cdd:PRK05294 636 QFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVL 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 721 GGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDRFLDDAVEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYT 800
Cdd:PRK05294 716 GGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQT 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 801 LSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKTLAQQGVT 880
Cdd:PRK05294 796 LSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYT 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 881 KEVIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSSSTMKKQGRALLSVREGDKERVVDL 960
Cdd:PRK05294 876 KGLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDKEEVVEL 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 961 AAKLLKFGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTEGRQAIEDSKLIRRSALQYKVHY 1040
Cdd:PRK05294 956 AKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINTPTGRQAIRDGFSIRRAALEYKVPY 1035
|
1050 1060 1070
....*....|....*....|....*....|.
gi 489109057 1041 DTTLNGGFATAMALNADATEK--VTSVQEMH 1069
Cdd:PRK05294 1036 ITTLAGARAAVKAIEALKFGEleVRSLQEYH 1066
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1054 |
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: 1821.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 2 PKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 82 RPDAVLPTMGGQTALNCALELERQGVLAEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEALAVAAD 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 162 VGFPCIIRPSFTMGGTGGGIAYNREEFEEICERGLDLSPTNELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 242 IHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVEtGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 322 VAAKLAVGYTLDELMNDITGgRTPASFEPSIDYVVTKIPRFNFEKFVGANDRLTTQMKSVGEVMAIGRTQQESLQKALRG 401
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTG-TTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 402 LEVGATGFDpkVSLDDPEALTKIRRELKDAGAERIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVIDLGI 481
Cdd:TIGR01369 399 LEIGATGFD--LPDREVEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 482 NGLDADFLRVLKRKGFADARLAKLAGVREAEIRKLRDQYNLHPVYKRVDTCAAEFATDTAYMYSTYEDECEANPSVDRDK 561
Cdd:TIGR01369 477 TDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 562 IMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQ 641
Cdd:TIGR01369 557 VLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 642 YGGQTPLKLARALEAAGVPVIGTSPDAIDRAEDRERFQQAVDRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRPSYVLG 721
Cdd:TIGR01369 637 FGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLG 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 722 GRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDRFLDDAVEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYTL 801
Cdd:TIGR01369 717 GRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 802 SQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKTLAQQGVTK 881
Cdd:TIGR01369 797 SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGK 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 882 EVIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSSSTMKKQGRALLSVREGDKERVVDLA 961
Cdd:TIGR01369 877 EKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLA 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 962 AKLLKFGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTE-GRQAIEDSKLIRRSALQYKVHY 1040
Cdd:TIGR01369 957 RKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTSkGAGTATDGYKIRREALDYGVPL 1036
|
1050
....*....|....
gi 489109057 1041 DTTLNGGFATAMAL 1054
Cdd:TIGR01369 1037 ITTLNTAEAFAEAL 1050
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1071 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1506.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 1 MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 81 ERPDAVLPTMGGQTALNCALELERQGVLAEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEALAVAA 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 161 DVGFPCIIRPSFTMGGTGGGIAYNREEFEEICERGLDLSPTNELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAM 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 241 GIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVeTGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 321 KVAAKLAVGYTLDELMNDITgGRTPASFEPSIDYVVTKIPRFNFEKFVGANDRLTTQMKSVGEVMAIGRTQQESLQKALR 400
Cdd:PRK12815 320 KIAAKLAVGYTLNELKNPVT-GLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 401 GLEVGATGFDPKVSLdDPEALTKIRRELKDAGAERIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVIDLG 480
Cdd:PRK12815 399 SLEIKRNGLSLPIEL-SGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 481 INgLDADFLRVLKRKGFADARLAKLAGVREAEIRKLRDQYNLHPVYKRVDTCAAEFATDTAYMYSTYEDECEANPSVDRD 560
Cdd:PRK12815 478 LD-LSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPSSEKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 561 KIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIV 640
Cdd:PRK12815 557 KVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIV 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 641 QYGGQTPLKLARALEAAGVPVIGTSPDAIDRAEDRERFQQAVDRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRPSYVL 720
Cdd:PRK12815 637 QFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVI 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 721 GGRAMEIVYDEADLRRYFQTAvsVSNDAPVLLDRFLdDAVEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYT 800
Cdd:PRK12815 717 GGQGMAVVYDEPALEAYLAEN--ASQLYPILIDQFI-DGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQS 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 801 LSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKTLAQQGVT 880
Cdd:PRK12815 794 LSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGYP 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 881 KEVIP--PYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSSSTMKKQGRALLSVREGDKERVV 958
Cdd:PRK12815 874 NGLWPgsPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVT 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 959 DLAAKLLKFGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTEGRQAIEDSKLIRRSALQYKV 1038
Cdd:PRK12815 954 KLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSPSLLERIKQHRIVLVVNTSLSDSASEDAIKIRDEALSTHI 1033
|
1050 1060 1070
....*....|....*....|....*....|....*
gi 489109057 1039 HYDTTLNGG--FATAMALNADATEKVTSVQEMHAQ 1071
Cdd:PRK12815 1034 PVFTELETAqaFLQVLESLALTTQPIQELQEKHKQ 1068
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1056 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1502.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 3 KRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 83 PDAVLPTMGGQTALNCALELERQGVLAEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEALAVAADV 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 163 G-FPCIIRPSFTMGGTGGGIAYNREEFEEICERGLDLSPTNELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMG 241
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 242 IHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 322 VAAKLAVGYTLDELMNDITgGRTPASFEPSIDYVVTKIPRFNFEKFVGANDRLTTQMKSVGEVMAIGRTQQESLQKALRG 401
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDIT-LKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRS 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 402 LEVGATGFDPKVSLDDPEALTKIRRELKDAGAERIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVIDLGI 481
Cdd:PLN02735 418 LETGFSGWGCAKVKELDWDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 482 NGLDADFLRVLKRKGFADARLAKLAGVREAEIRKLRDQYNLHPVYKRVDTCAAEFATDTAYMYSTYEDECEANPSvDRDK 561
Cdd:PLN02735 498 SELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPT-NKKK 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 562 IMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQ 641
Cdd:PLN02735 577 VLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQ 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 642 YGGQTPLKLARALE----------AAG---VPVIGTSPDAIDRAEDRERFQQAVDRLKLKQPANATVTAIEQAVEKAKEI 708
Cdd:PLN02735 657 FGGQTPLKLALPIQkyldknpppsASGngnVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRI 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 709 GYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDRFLDDAVEVDVDAICDGE-MVLIGGIMEHIEQAGV 787
Cdd:PLN02735 737 GYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEgNVVIGGIMEHIEQAGV 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 788 HSGDSACSLPAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAA 866
Cdd:PLN02735 817 HSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYAS 896
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 867 RVMAGKTLAQQGVTKEVIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSSSTMKKQGRAL 946
Cdd:PLN02735 897 LVMSGKSLKDLGFTEEVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGTVF 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 947 LSVREGDKERVVDLAAKLLKFGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTEGRQA-IED 1025
Cdd:PLN02735 977 ISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGDMLANGQIQLMVITSSGDALdQKD 1056
|
1050 1060 1070
....*....|....*....|....*....|.
gi 489109057 1026 SKLIRRSALQYKVHYDTTLNGGFATAMALNA 1056
Cdd:PLN02735 1057 GRQLRRMALAYKVPIITTVAGALATAQAVKS 1087
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
565-1067 |
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: 772.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 565 LGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQYGG 644
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 645 QTPLKLARALEAA----GVPVIGTSPDAIDRAEDRERFQQAVDRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRPSYVL 720
Cdd:COG0458 81 QTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 721 GGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDRFLDDAVEVDVDAICDGEM-VLIGGIMEHIEQAGVHSGDSACSLPAY 799
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDnVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 800 TLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKTLAQQGV 879
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 880 TKEVIP--PYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLgsSSTMKKQGRALLS-VREGDKER 956
Cdd:COG0458 321 DTGFEPtlDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALR--SLEIGLPGTVLLSlVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 957 VVDLAAKLLKFGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTEGRQAIEDSKLIRRSALQY 1036
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAKSLGDSDGIIRRALAA 478
|
490 500 510
....*....|....*....|....*....|.
gi 489109057 1037 KVHYDTTLNGGFATAMALNADATEKVTSVQE 1067
Cdd:COG0458 479 KVPYVTTLAAAAAAALAIKAVETEAGEFEEA 509
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-566 |
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: 770.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 13 LGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 93 QTALNCALELERQGVLAefGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEALAVAADVGFPCIIRPSF 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 173 TMGGTGGGIAYNREEFEEICERGLDLSPTNELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMGIHTGDSITVAP 252
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 253 AQTLTDKEYQIMRNASMAVLREIGVEtGGSNVQFAVnpKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTL 332
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVV-GLCNIQFAV--DDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 333 DELMNDiTGgrtpasFEPSIDYVVTKIPRFNFEKFVGANDRLTTQMKSVGEVMAIGRTQQESLQKALRGLEVGATG--FD 410
Cdd:COG0458 316 DELGND-TG------FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 411 PKVSLDDPEALTKIRRELkdagaERIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKvidLGINGLDADFLR 490
Cdd:COG0458 389 SLVADDDKEEALLLARRL-----ARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIE---LEEIILVINTLL 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489109057 491 VLKRKGFADARLAKLAGVREAEIRKLRDQYNLHPVYKRVDTCAAEFATDTAYMYSTYEDECEANPSVDRDKIMVLG 566
Cdd:COG0458 461 GAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-333 |
4.76e-92 |
|
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: 292.67 E-value: 4.76e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 128 DRRRFDIAMKKIGLDTARSGIA--HTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREEFEEICERGLDLSPT---- 201
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 202 NELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMgiHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGG 281
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489109057 282 sNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLD 333
Cdd:pfam02786 159 -TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
538-931 |
4.69e-80 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 284.36 E-value: 4.69e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 538 TDTAYMYSTYEDECEANPSVDRDKIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLY 617
Cdd:PLN02735 2 SLADTVTRAWSAATKAGKRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 618 FEPVTLEDVLEIVRIEKPKGVIVQYGGQTPLKLARA------LEAAGVPVIGTSPDAIDRAEDRERFQQAVDRLKLKQPA 691
Cdd:PLN02735 82 IAPMTPELVEQVIAKERPDALLPTMGGQTALNLAVAlaesgiLEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 692 NATVTAIEQAVEKAKEIG-YPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDRFLDDAVEVDVDAICD- 769
Cdd:PLN02735 162 SGIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 770 GEMVLIGGIMEHIEQAGVHSGDSACSLPAYTLSQEIQDVMRQQVQKLAFELQVR-GLMNVQFAV--KNNEVYLIEVNPRA 846
Cdd:PLN02735 242 ADNVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVEcGGSNVQFAVnpVDGEVMIIEMNPRV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 847 ARTVPFVSKATGVPLAKVAARVMAGKTLAQ--QGVTKEViPPYY--SVKEVV-----LPFNKFPGVDPLLGPEMRSTGEV 917
Cdd:PLN02735 322 SRSSALASKATGFPIAKMAAKLSVGYTLDQipNDITLKT-PASFepSIDYVVtkiprFAFEKFPGSQPILTTQMKSVGEA 400
|
410
....*....|....
gi 489109057 918 MGVGRTFAEAFAKA 931
Cdd:PLN02735 401 MALGRTFQESFQKA 414
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
424-547 |
5.84e-63 |
|
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: 209.23 E-value: 5.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 424 IRRELKDAGAERIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVIDLGINGLDADFLRVLKRKGFADARLA 503
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489109057 504 KLAGVREAEIRKLRDQYNLHPVYKRVDTCAAEFATDTAYMYSTY 547
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
943-1052 |
8.97e-47 |
|
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: 162.65 E-value: 8.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 943 GRALLSVREGDKERVVDLAAKLLKFGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTEGRQA 1022
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKRA 80
|
90 100 110
....*....|....*....|....*....|
gi 489109057 1023 IEDSKLIRRSALQYKVHYDTTLNGGFATAM 1052
Cdd:cd01424 81 IRDGFSIRRAALEYKVPYFTTLDTARAAVE 110
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
674-874 |
2.90e-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: 142.06 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 674 DRERFQQAVDRLKLKQP--ANATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDAP-- 749
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVpgTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 750 --VLLDRFLDDAVEVDVDAICDGE-MVLIGGIMEHIEQagVHSGDSACSLPAYTLSQEIQDVMRQQVQKLAFELQVRGLM 826
Cdd:pfam02786 81 pqVLVEKSLKGPKHIEYQVLRDAHgNCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489109057 827 NVQFAV--KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKTL 874
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
944-1050 |
4.67e-35 |
|
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: 129.17 E-value: 4.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 944 RALLSVREGDKERVVDLAAKLLKFGFELDATHGTAIVLGEAGINPRLVNKVHE-GRPHIQDRIKN-GEYTYIINTTEGRQ 1021
Cdd:cd00532 1 GVFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEdGEPTVDAAIAEkGKFDVVINLRDPRR 80
|
90 100 110
....*....|....*....|....*....|..
gi 489109057 1022 A---IEDSKLIRRSALQYKVHYDTTLNGGFAT 1050
Cdd:cd00532 81 DrctDEDGTALLRLARLYKIPVTTPNATAMFV 112
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
426-505 |
3.49e-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: 114.01 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 426 RELKDAGAERIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVIDLGINgLDADFLRVLKRKGFADARLAKL 505
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLD-LDAELLREAKRLGFSDRQIAKL 79
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
72-329 |
1.05e-26 |
|
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: 110.35 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 72 EVVRKIIEKERPDAVLPTmggqtalnCALELERQGVLAE-FGVTmiGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAH 150
Cdd:COG0439 7 AAAAELARETGIDAVLSE--------SEFAVETAAELAEeLGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 151 TMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREE----FEEICERGLDLSPTNELLIDESLIGwKEYEME-VVRDKN 225
Cdd:COG0439 77 SPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEleaaLAEARAEAKAGSPNGEVLVEEFLEG-REYSVEgLVRDGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 226 dncIIVCSI---ENFDAMGIHTGDsitVAPAQtLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPkNGRLIVIEMNP 302
Cdd:COG0439 156 ---VVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRRGAFHTEFLLTP-DGEPYLIEINA 227
|
250 260
....*....|....*....|....*....
gi 489109057 303 RVS--RSSALASKATGFPIAKVAAKLAVG 329
Cdd:COG0439 228 RLGgeHIPPLTELATGVDLVREQIRLALG 256
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
651-872 |
1.72e-26 |
|
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: 109.96 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 651 ARALEAAGVPviGTSPDAIDRAEDRERFQQAVDRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRAMEIVYD 730
Cdd:COG0439 33 AELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 731 EADLRRYFQTAVS----VSNDAPVLLDRFLdDAVEVDVDAICDGEMVLIGGIMEHIeQAGVHSGDSACSLPAyTLSQEIQ 806
Cdd:COG0439 111 EEELEAALAEARAeakaGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRKH-QKPPYFVELGHEAPS-PLPEELR 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 807 DVMRQQVQKLAFELQV-RGLMNVQFAV-KNNEVYLIEVNPRA--ARTVPFVSKATGVPLAKVAARVMAGK 872
Cdd:COG0439 188 AEIGELVARALRALGYrRGAFHTEFLLtPDGEPYLIEINARLggEHIPPLTELATGVDLVREQIRLALGE 257
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
956-1042 |
1.85e-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: 101.01 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 956 RVVDLAAKLLKFGFELDATHGTAIVLGEAGINP--RLVNKVHEGRPHIQDRIKNGEYTYIINTTEG--RQAIEDSKLIRR 1031
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVvkTLHPKVHGGIPQILDLIKNGEIDLVINTLYPfeAQAHEDGYSIRR 80
|
90
....*....|.
gi 489109057 1032 SALQYKVHYDT 1042
Cdd:smart00851 81 AAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
956-1042 |
1.38e-22 |
|
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: 92.94 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 956 RVVDLAAKLLKFGFELDATHGTAIVLGEAGINPR-LVNKVHEGRPH----IQDRIKNGEYTYIINTTEGRQAIE-DSKLI 1029
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTeVVEKTGEGRPGgrvqIGDLIKNGEIDLVINTLYPFKATVhDGYAI 80
|
90
....*....|...
gi 489109057 1030 RRSALQYKVHYDT 1042
Cdd:pfam02142 81 RRAAENIDIPGPT 93
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
623-852 |
1.09e-17 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 85.32 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 623 LEDVLEIVRIEKPKGVIVqyGGQTPLK-LAR---ALEAAGVPVIGTSPDAIDRAEDRERFQQAVDRLKLKQPANATVTAI 698
Cdd:PRK12767 58 IDRLLDICKKEKIDLLIP--LIDPELPlLAQnrdRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 699 EQAVE--KAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAvsvsndAPVLLDRFLDDAvEVDVDAICDGEMVLIG 776
Cdd:PRK12767 136 EDFKAalAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYV------PNLIIQEFIEGQ-EYTVDVLCDLNGEVIS 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489109057 777 GI-MEHIEqagVHSGDSacsLPAYTlsqEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPF 852
Cdd:PRK12767 209 IVpRKRIE---VRAGET---SKGVT---VKDPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
561-884 |
6.36e-17 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 84.21 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 561 KIMVLGGGPNrigqgiefDYCCVHAslaLREDGYETIMVNCNPETVSTDYDTSDRLYFEP-------VTLEDVLEIVRiE 633
Cdd:COG3919 7 RVVVLGGDIN--------ALAVARS---LGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPdpgddpeAFVDALLELAE-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 634 KPKGVIVQYGGQTPLKLARALE--AAGVPVIGTSPDAIDRAEDRERFQQAVDRLKLKQPANATVTAIEQAVEKAKEIGYP 711
Cdd:COG3919 75 HGPDVLIPTGDEYVELLSRHRDelEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 712 LVVRPSY--------VLGGRAMEIVYDEADLRRYFQTAVSvsNDAPVLLDRFL--DDAVEVDVDAICD--GEMVLIGG-- 777
Cdd:COG3919 155 VVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAA--AGYELIVQEYIpgDDGEMRGLTAYVDrdGEVVATFTgr 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 778 -IMEHIEQAGVhsgdsacslPAYTLSQEIQDVMRQqVQKLAFELQVRGLMNVQFAV--KNNEVYLIEVNPRAARTVPFVS 854
Cdd:COG3919 233 kLRHYPPAGGN---------SAARESVDDPELEEA-ARRLLEALGYHGFANVEFKRdpRDGEYKLIEINPRFWRSLYLAT 302
|
330 340 350
....*....|....*....|....*....|
gi 489109057 855 KAtGVPLAKVAARVMAGKTLAQQGVTKEVI 884
Cdd:COG3919 303 AA-GVNFPYLLYDDAVGRPLEPVPAYREGV 331
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
651-877 |
2.37e-16 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 83.27 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 651 ARALEAAGVPVIGTSPDAI----DRAEDRERFQQAvdRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRAME 726
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIrtmgDKARARRTARRA--GVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 727 IVYDEADLRRYFQTAVSVSN----DAPVLLDRFLDDAVEVDVDAICDGEMVliggimehieqagVHSGDSACSL------ 796
Cdd:PRK12833 173 VAHDAAQLAAELPLAQREAQaafgDGGVYLERFIARARHIEVQILGDGERV-------------VHLFERECSLqrrrqk 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 797 -----PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQ--FAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVM 869
Cdd:PRK12833 240 ileeaPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEylFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIA 319
|
250
....*....|
gi 489109057 870 AGKTL--AQQ 877
Cdd:PRK12833 320 DGEPLrfAQG 329
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
9-329 |
2.81e-16 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 81.90 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 9 SILILGAGPIVIGqacefdysgaqACKALREEGYRVILVNSNPATIMT------------DPEMADATYIEpihweVVRK 76
Cdd:COG3919 7 RVVVLGGDINALA-----------VARSLGEAGVRVIVVDRDPLGPAArsryvdevvvvpDPGDDPEAFVD-----ALLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 77 IIEKERPDAVLPTMGGQTALncaleLERQGVLAEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEAL 156
Cdd:COG3919 71 LAERHGPDVLIPTGDEYVEL-----LSRHRDELEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 157 AVAADVGFPCIIRPS--------FTMGGTGGGIAYNREEFEEICERGLDLSptNELLIDESLIGWKEYE--MEVVRDKND 226
Cdd:COG3919 146 ALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAG--YELIVQEYIPGDDGEMrgLTAYVDRDG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 227 NCIIVCSIENF----DAMGIHTGdsITVAPAQTLTDkeyqimrnASMAVLREIGVeTGGSNVQFAVNPKNGRLIVIEMNP 302
Cdd:COG3919 224 EVVATFTGRKLrhypPAGGNSAA--RESVDDPELEE--------AARRLLEALGY-HGFANVEFKRDPRDGEYKLIEINP 292
|
330 340
....*....|....*....|....*..
gi 489109057 303 RVSRSSALASKAtGFPIAKVAAKLAVG 329
Cdd:COG3919 293 RFWRSLYLATAA-GVNFPYLLYDDAVG 318
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
10-314 |
8.46e-16 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 79.93 E-value: 8.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 10 ILILGAGpivigqacefdySGAQACKALREE--GYRVILV---NSNPATIMTD-----PEMADATYIEPIHwevvrKIIE 79
Cdd:PRK12767 4 ILVTSAG------------RRVQLVKALKKSllKGRVIGAdisELAPALYFADkfyvvPKVTDPNYIDRLL-----DICK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 80 KERPDAVLPTMGGQTALNCAlELERqgvLAEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEALAV- 158
Cdd:PRK12767 67 KEKIDLLIPLIDPELPLLAQ-NRDR---FEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAAl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 159 -AADVGFPCIIRPSFTMGGTGGGIAYNREEFEEICERGLDlsptneLLIDESLIGwKEYEMEVVRDKNDNCIIVCSIENF 237
Cdd:PRK12767 143 aKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPN------LIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRI 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489109057 238 DAMGIHTGDSITVapaqtltdkEYQIMRNASMAVLREIGvETGGSNVQFAVNpkNGRLIVIEMNPRVSRSSALASKA 314
Cdd:PRK12767 216 EVRAGETSKGVTV---------KDPELFKLAERLAEALG-ARGPLNIQCFVT--DGEPYLFEINPRFGGGYPLSYMA 280
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
649-874 |
2.95e-14 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 76.38 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 649 KLARALEAAGVPVIGTSPDAIDRAEDRERFQQAVdrLKLKQP----ANATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRA 724
Cdd:PRK08591 90 DFAEICEDSGFTFIGPSAETIRLMGDKVTAKATM--KKAGVPvvpgSDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 725 MEIVYDEADLRRYFQTA-----VSVSNDApVLLDRFLDDAVEVDVDAICDGEmvliGGImehieqagVHSGDSACSL--- 796
Cdd:PRK08591 168 MRVVRTEAELEKAFSMAraeakAAFGNPG-VYMEKYLENPRHIEIQVLADGH----GNA--------IHLGERDCSLqrr 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 797 --------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAAR 867
Cdd:PRK08591 235 hqkvleeaPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYeKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIR 314
|
....*..
gi 489109057 868 VMAGKTL 874
Cdd:PRK08591 315 IAAGEPL 321
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
650-875 |
3.13e-14 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 76.22 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 650 LARALEAAGVPVIGTSPDAI----DRAEDRERFQQAvdrlklKQP----ANATVTAIEQAVEKAKEIGYPLVVRPSYVLG 721
Cdd:PRK06111 91 FAERCKEEGIVFIGPSADIIakmgSKIEARRAMQAA------GVPvvpgITTNLEDAEEAIAIARQIGYPVMLKASAGGG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 722 GRAMEIVYDEADLRRYF----QTAVSVSNDAPVLLDRFLDDAVEVDVDAICDGEmvliggimEHIeqagVHSGDSACSL- 796
Cdd:PRK06111 165 GIGMQLVETEQELTKAFesnkKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTH--------GNT----VYLWERECSVq 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 797 ----------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNE-VYLIEVNPRAARTVPFVSKATGVPLAKVA 865
Cdd:PRK06111 233 rrhqkvieeaPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQ 312
|
250
....*....|
gi 489109057 866 ARVMAGKTLA 875
Cdd:PRK06111 313 LRIAAGEKLS 322
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
649-880 |
9.75e-14 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 75.02 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 649 KLARALEAAGVPVIGTSPDAIDRAEDRerfqqaVDRLKLKQPANATV--------TAIEQAVEKAKEIGYPLVVRPSYVL 720
Cdd:PRK08654 90 EFAKACEKAGIVFIGPSSDVIEAMGSK------INAKKLMKKAGVPVlpgteegiEDIEEAKEIAEEIGYPVIIKASAGG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 721 GGRAMEIVYDEADLRRYFQTAVSVSN----DAPVLLDRFLDDAVEVDVDAICDGEmvliGGImehieqagVHSGDSACSL 796
Cdd:PRK08654 164 GGIGMRVVYSEEELEDAIESTQSIAQsafgDSTVFIEKYLEKPRHIEIQILADKH----GNV--------IHLGDRECSI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 797 -----------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVA 865
Cdd:PRK08654 232 qrrhqklieeaPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQ 311
|
250
....*....|....*..
gi 489109057 866 ARVMAGKTLA--QQGVT 880
Cdd:PRK08654 312 IKIAAGEELSfkQEDIT 328
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
625-879 |
1.84e-13 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 75.17 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 625 DVLEIVRIEKPKGVIVQYGGQTPL----KLARALEAAGVPVIGTSPDAIDRAEDRerfqqaVDRLKLKQPANATV----- 695
Cdd:PRK12999 66 DIDEIIRVAKQAGVDAIHPGYGFLsenpEFARACAEAGITFIGPTAEVLRLLGDK------VAARNAAIKAGVPVipgse 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 696 ---TAIEQAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVS-----NDApVLLDRFLDDAVEVDVDAI 767
Cdd:PRK12999 140 gpiDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAkaafgNDE-VYLEKYVENPRHIEVQIL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 768 CDGEmvliGGImehieqagVHSGDSACSL-----------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNN 835
Cdd:PRK12999 219 GDKH----GNV--------VHLYERDCSVqrrhqkvveiaPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVdADG 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489109057 836 EVYLIEVNPR--AARTVpfVSKATGVPLAKVAARVMAGKTLAQQGV 879
Cdd:PRK12999 287 NFYFIEVNPRiqVEHTV--TEEVTGIDIVQSQILIAEGATLHDLEI 330
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
112-340 |
2.12e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 73.86 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 112 GVTMIGATADAIDKAEDRRRFDIAMKKIGLDT--ARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREEFE 189
Cdd:PRK08654 99 GIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVlpGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 190 EICERGLDLSPTN----ELLIDESLIGWKEYEMEVVRDKNDNCIIV----CSIENFdamgiHTgDSITVAPAQTLTDKEY 261
Cdd:PRK08654 179 DAIESTQSIAQSAfgdsTVFIEKYLEKPRHIEIQILADKHGNVIHLgdreCSIQRR-----HQ-KLIEEAPSPIMTPELR 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489109057 262 QIMRNASMAVLREIGVETGGSnVQFAVNpkNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELMNDIT 340
Cdd:PRK08654 253 ERMGEAAVKAAKAINYENAGT-VEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSFKQEDIT 328
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
649-875 |
5.16e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 72.44 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 649 KLARALEAAGVPVIGTSPDAID----RAEDRERFQQAvdRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRA 724
Cdd:PRK05586 90 KFAKMCKECNIVFIGPDSETIElmgnKSNAREIMIKA--GVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 725 MEIVYDEADLRRYFQTAVSVS----NDAPVLLDRFLDDAVEVDVDAICDGemvlIGGImehieqagVHSGDSACSL---- 796
Cdd:PRK05586 168 IRIVRSEEELIKAFNTAKSEAkaafGDDSMYIEKFIENPKHIEFQILGDN----YGNV--------VHLGERDCSLqrrn 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 797 -------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARV 868
Cdd:PRK05586 236 qkvleeaPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKI 315
|
....*..
gi 489109057 869 MAGKTLA 875
Cdd:PRK05586 316 AYGEKLS 322
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
614-872 |
3.55e-12 |
|
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: 68.43 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 614 DRLYFEPVTLEDVLEIVRIEKPKGVIVQYGG-QTPLKLARALEAAGVPVIGtSPDAIDRAEDRERFQQAVDRLKLKQPAN 692
Cdd:COG0189 36 DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPpFYGLALLRQLEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIPVPPT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 693 ATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDaPVLLDRFLDDAVEVDVDAIC-DGE 771
Cdd:COG0189 115 LVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSE-PVLVQEFIPEEDGRDIRVLVvGGE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 772 MVligGIMEHIEQAG-----VHSGDSACslpAYTLSQEiqdvMRQQVQKLA--FELQVRGlmnVQFAVKNNEVYLIEVNP 844
Cdd:COG0189 194 PV---AAIRRIPAEGefrtnLARGGRAE---PVELTDE----ERELALRAApaLGLDFAG---VDLIEDDDGPLVLEVNV 260
|
250 260
....*....|....*....|....*...
gi 489109057 845 RAArtVPFVSKATGVPLAKVAARVMAGK 872
Cdd:COG0189 261 TPG--FRGLERATGVDIAEAIADYLEAR 286
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
112-404 |
5.66e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 69.29 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 112 GVTMIGATADAI----DKAEDRRrfdiAMKKIGL------DTARSGIahtmEEALAVAADVGFPCIIRPSFTMGGTGGGI 181
Cdd:PRK06111 99 GIVFIGPSADIIakmgSKIEARR----AMQAAGVpvvpgiTTNLEDA----EEAIAIARQIGYPVMLKASAGGGGIGMQL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 182 AYNREE----FEEICERGLDLSPTNELLIDESLIGWKEYEMEVVRDKNDNCIIV----CSIENfdamgiHTGDSITVAPA 253
Cdd:PRK06111 171 VETEQEltkaFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLwereCSVQR------RHQKVIEEAPS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 254 QTLTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNpKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLD 333
Cdd:PRK06111 245 PFLDEETRKAMGERAVQAAKAIGYTNAGT-IEFLVD-EQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 334 ELMNDITG----------GRTPASFEPS----IDYVVTKIPRFNFEKFVGANDRLTTQMKS-VGEVMAIGRTQQESLQK- 397
Cdd:PRK06111 323 FTQDDIKRsghaievriyAEDPKTFFPSpgkiTDLTLPGGEGVRHDHAVENGVTVTPFYDPmIAKLIAHGETREEAISRl 402
|
....*....
gi 489109057 398 --ALRGLEV 404
Cdd:PRK06111 403 hdALEELKV 411
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
625-845 |
1.27e-11 |
|
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: 68.95 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 625 DVLEIVRIEKPKGVIVQYGGQTPL----KLARALEAAGVPVIGTSPDAIDRAED----RERFQQA-VDRLklkqPANAT- 694
Cdd:COG1038 65 DIEEIIRVAKEKGVDAIHPGYGFLsenpEFARACEEAGITFIGPSPEVLEMLGDkvaaRAAAIEAgVPVI----PGTEGp 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 695 VTAIEQAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVS-----NDApVLLDRFLDDA--VEVDVDAI 767
Cdd:COG1038 141 VDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAkaafgDDE-VFLEKYIERPkhIEVQILGD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 768 CDGEMVliggimeHIeqagvHSGDsaCSL-----------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNN 835
Cdd:COG1038 220 KHGNIV-------HL-----FERD--CSVqrrhqkvveiaPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDDG 285
|
250
....*....|
gi 489109057 836 EVYLIEVNPR 845
Cdd:COG1038 286 NFYFIEVNPR 295
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-339 |
1.08e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 65.12 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 109 AEFGVTMIGATADAI----DKAEDRRrfdiAMKKIGLDT--ARSGIAHTMEEALAVAADVGFPCIIRPsfTMGGTGGGI- 181
Cdd:PRK07178 95 AERGIKFIGPSAEVIrrmgDKTEARR----AMIKAGVPVtpGSEGNLADLDEALAEAERIGYPVMLKA--TSGGGGRGIr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 182 -AYNREEFEEICERGLDLSP----TNELLIDESLIGWKEYEMEVVRDKNDNCIIV----CSIENfdamgiHTGDSITVAP 252
Cdd:PRK07178 169 rCNSREELEQNFPRVISEATkafgSAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 253 AQTLTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNpKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTL 332
Cdd:PRK07178 243 SPQLTPEQRAYIGDLAVRAAKAVGYENAGT-VEFLLD-ADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
....*..
gi 489109057 333 DELMNDI 339
Cdd:PRK07178 321 SYKQEDI 327
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
618-863 |
2.66e-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: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 618 FEPVTLED-VLEIVRIEKPKGVIvqYGG---QTPLKLARAleAAGVPVIGTSPDAIDRAEDRERFQQAVDRLKLKQPAna 693
Cdd:COG2232 56 FDLEDLPAaLLELAAADDPDGLV--YGSgfeNFPELLERL--ARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPE-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 694 TVTAIEQAvekakeiGYPLVVRPSYVLGGRAMEIVYDEADLR--RYFQ-----TAVSVSndapvlldrFLddavevdvda 766
Cdd:COG2232 130 TRFEPPPD-------PGPWLVKPIGGAGGWHIRPADSEAPPApgRYFQryvegTPASVL---------FL---------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 767 iCDGEMVLIGGIME-HIEQAGVH----SGdsaCSLPaYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIE 841
Cdd:COG2232 184 -ADGSDARVLGFNRqLIGPAGERpfryGG---NIGP-LALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLE 258
|
250 260
....*....|....*....|..
gi 489109057 842 VNPRAARTVPFVSKATGVPLAK 863
Cdd:COG2232 259 VNPRPQASLDLYEDATGGNLFD 280
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
21-339 |
3.06e-10 |
|
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: 62.82 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 21 GQACEFD---YSGAQACKALREEGYRVILVNSNPATIMTDpemadatyiepihwevvrkiIEKERPDAVLPTMGGQTALN 97
Cdd:COG1181 9 GRSAEREvslKSGRAVAAALDKAGYDVVPIGIDVEDLPAA--------------------LKELKPDVVFPALHGRGGED 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 98 CALelerQGVLAEFGVTMIG----ATADAIDKaedrrrfdIAMKKI----GLDTARSGI--AHTMEEALAVAADVGFPCI 167
Cdd:COG1181 69 GTI----QGLLELLGIPYTGsgvlASALAMDK--------ALTKRVlaaaGLPTPPYVVlrRGELADLEAIEEELGLPLF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 168 IRPSftMGGTGGGI--AYNREEFEEICERGLDLSPtnELLIDESLIGwKEYEMEVVrdKNDNCIIVCSIE--------NF 237
Cdd:COG1181 137 VKPA--REGSSVGVskVKNAEELAAALEEAFKYDD--KVLVEEFIDG-REVTVGVL--GNGGPRALPPIEivpengfyDY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 238 DAMGIhTGDSITVAPAQtLTDKEYQIMRNASMAVLREIGVEtGGSNVQFAVNPkNGRLIVIEMN--PRVSRSSalaskat 315
Cdd:COG1181 210 EAKYT-DGGTEYICPAR-LPEELEERIQELALKAFRALGCR-GYARVDFRLDE-DGEPYLLEVNtlPGMTPTS------- 278
|
330 340
....*....|....*....|....
gi 489109057 316 GFPIAkvAAklAVGYTLDELMNDI 339
Cdd:COG1181 279 LLPKA--AA--AAGISYEELIERI 298
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
60-190 |
1.84e-09 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 60.92 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 60 MADAtyiepihwEVVRKIIEKERPDAVLPTMggqTALNCA--LELERQGvlaeFGVTmigATADAIDKAEDR---RRFdi 134
Cdd:PRK09288 61 MLDG--------DALRAVIEREKPDYIVPEI---EAIATDalVELEKEG----FNVV---PTARATRLTMNRegiRRL-- 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489109057 135 AMKKIGLDTARSGIAHTMEEALAVAADVGFPCIIRPsfTMGGTGGG--IAYNREEFEE 190
Cdd:PRK09288 121 AAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKP--VMSSSGKGqsVVRSPEDIEK 176
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
658-877 |
3.09e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 60.53 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 658 GVPVIGTSPDAIDRAEDRERFQQAVDR--LKLKQPANATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLR 735
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRagVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 736 RYF----QTAVSVSNDAPVLLDRFLDDAVEVDVDAICDGEmvliGGImehieqagVHSGDSACSL-----------PAYT 800
Cdd:PRK08462 181 NLYlaaeSEALSAFGDGTMYMEKFINNPRHIEVQILGDKH----GNV--------IHVGERDCSLqrrhqklieesPAVV 248
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489109057 801 LSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKTLAQQ 877
Cdd:PRK08462 249 LDEKTRERLHETAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQ 326
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
635-862 |
6.03e-09 |
|
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: 58.51 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 635 PKGVIVQYGgqtpLKLARALEAAGVPVIgTSPDAIDRAEDRERFQQAVDRLKLKQPANATVTAIEQAVEKAKEIGYPLVV 714
Cdd:TIGR00768 54 VRIVSMFRG----LAVLRYLESLGVPVI-NSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 715 RPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDAPV-LLDRFLDDAVEVDVDAICDGEMVLigGIMEHIE----QAGVHS 789
Cdd:TIGR00768 129 KPVFGSWGRGVSLARDRQAAESLLEHFEQLNGPQNLfLVQEYIKKPGGRDIRVFVVGDEVV--AAIYRITsghwRSNLAR 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489109057 790 GDSACSLPaytLSQEIQDVMRQQVQklAFELQVRGlmnVQFAVKNNEVYLIEVNPraarTVPF--VSKATGVPLA 862
Cdd:TIGR00768 207 GGKAEPCS---LTEEIEELAIKAAK--ALGLDVAG---VDLLESEDGLLVNEVNA----NPEFknSVKTTGVNIA 269
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
654-844 |
6.13e-09 |
|
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: 58.58 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 654 LEAAGVPVIGTSPDAIDRAEDRERFQQAVDRLKLKQPANATVTAIEQAV--EKAKEIGYPLVVRPsyVLGG--RAMEIVY 729
Cdd:COG1181 75 LELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADleAIEEELGLPLFVKP--AREGssVGVSKVK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 730 DEADLRRYFQTAVSvsNDAPVLLDRFLDdAVEVDVdAICDGEMVLIGGIMEHIEQAGV-------HSGDSACSLPAyTLS 802
Cdd:COG1181 153 NAEELAAALEEAFK--YDDKVLVEEFID-GREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA-RLP 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489109057 803 QEIQDVMRQQVQKlAFE-LQVRGLMNVQFAV-KNNEVYLIEVNP 844
Cdd:COG1181 228 EELEERIQELALK-AFRaLGCRGYARVDFRLdEDGEPYLLEVNT 270
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
109-304 |
2.05e-08 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 58.61 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 109 AEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARS--GIAHTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNRE 186
Cdd:PRK12999 100 AEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 187 EFEEICER---------GLDlsptnELLIDESLIGWKEYEMEVVRDKNDNciIV------CS--------IEnfdamgih 243
Cdd:PRK12999 180 ELEEAFERakreakaafGND-----EVYLEKYVENPRHIEVQILGDKHGN--VVhlyerdCSvqrrhqkvVE-------- 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489109057 244 tgdsitVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNPkNGRLIVIEMNPRV 304
Cdd:PRK12999 245 ------IAPAPGLSEELRERICEAAVKLARAVGYVNAGT-VEFLVDA-DGNFYFIEVNPRI 297
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
109-339 |
2.88e-08 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 57.52 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 109 AEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTArSGI----AHTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYN 184
Cdd:PRK08463 95 EDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIV-PGTeklnSESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 185 REEFE---EICER-GLDLSPTNELLIDESLIGWKEYEMEVVRDKNDNCIIV----CSIENfdamgiHTGDSITVAPAQTL 256
Cdd:PRK08463 174 EEDLEnafESCKReALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLcerdCSIQR------RHQKVIEIAPCPSI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 257 TDKEYQIMRNASMAVLREIGVETGGSnVQFAVNPKNgRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELM 336
Cdd:PRK08463 248 SDNLRKTMGVTAVAAAKAVGYTNAGT-IEFLLDDYN-RFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQ 325
|
...
gi 489109057 337 NDI 339
Cdd:PRK08463 326 SDI 328
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
108-190 |
1.11e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 55.58 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 108 LAEFGVTMIGATADAI----DKAEDRRrfdiAMKKIGLDT--ARSGIAHTMEEALAVAADVGFPCIIRPsfTMGGTGGGI 181
Cdd:PRK08591 95 CEDSGFTFIGPSAETIrlmgDKVTAKA----TMKKAGVPVvpGSDGPVDDEEEALAIAKEIGYPVIIKA--TAGGGGRGM 168
|
90
....*....|.
gi 489109057 182 --AYNREEFEE 190
Cdd:PRK08591 169 rvVRTEAELEK 179
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
110-339 |
3.42e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 53.95 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 110 EFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDT--ARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREE 187
Cdd:PRK05586 97 ECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVvpGSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 188 FEEICERGLDLSPTN----ELLIDESLIGWKEYEMEVVRDKNDNCIIV----CSIENFDAMGIHTgdsitvAPAQTLTDK 259
Cdd:PRK05586 177 LIKAFNTAKSEAKAAfgddSMYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQRRNQKVLEE------APSPVMTEE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 260 EYQIMRNASMAVLREIGVETGGSnVQFAVNpKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELMNDI 339
Cdd:PRK05586 251 LRKKMGEIAVKAAKAVNYKNAGT-IEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQEDI 328
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
651-912 |
4.55e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 54.08 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 651 ARALEAAGVPviGTSPDAIDRAEDRERFQQAVDRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRAMEIVYD 730
Cdd:PRK02186 86 SEVARRLGLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCAS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 731 EADLRRYFQTAVSVSNDApVLLDRFLDDAvEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYTLS---QEIQD 807
Cdd:PRK02186 164 VAEAAAHCAALRRAGTRA-ALVQAYVEGD-EYSVETLTVARGHQVLGITRKHLGPPPHFVEIGHDFPAPLSApqrERIVR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 808 VMRQQVQKLAFELqvrGLMNVQFAVKNNEVYLIEVNPR-AARTVP-FVSKATGVPLAKVAARVMAGK------TLAQQGV 879
Cdd:PRK02186 242 TVLRALDAVGYAF---GPAHTELRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVIDLHLGVaafadpTAKRYGA 318
|
250 260 270
....*....|....*....|....*....|...
gi 489109057 880 TKEVIPPyysvKEVVLPFNKFPGVDPLLGPEMR 912
Cdd:PRK02186 319 IRFVLPA----RSGVLRGLLFLPDDIAARPELR 347
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
650-875 |
7.39e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 53.18 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 650 LARALEAAGVPVIGTSPDAIDRAEDRERFQQAVdrLKLKQP----ANATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRAM 725
Cdd:PRK07178 90 LAEICAERGIKFIGPSAEVIRRMGDKTEARRAM--IKAGVPvtpgSEGNLADLDEALAEAERIGYPVMLKATSGGGGRGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 726 EIVYDEADLRRYFQTAVSVSN----DAPVLLDRFLDDAVEVDVDAICDGEmvliGGImehieqagVHSGDSACSL----- 796
Cdd:PRK07178 168 RRCNSREELEQNFPRVISEATkafgSAEVFLEKCIVNPKHIEVQILADSH----GNV--------VHLFERDCSIqrrnq 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 797 ------PAYTLSQEiqdvMRQQVQKLAfelqVR-----GLMN---VQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPL 861
Cdd:PRK07178 236 klieiaPSPQLTPE----QRAYIGDLA----VRaakavGYENagtVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDI 307
|
250
....*....|....
gi 489109057 862 AKVAARVMAGKTLA 875
Cdd:PRK07178 308 VREQIRIASGLPLS 321
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
672-845 |
2.00e-06 |
|
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: 48.92 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 672 AEDRERFQQAVDRLKLKQPANATVtaieqavEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQtavsvsndaPVL 751
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTPETLQA-------EELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIE---------NVL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 752 LDRFLDdAVEVDVDAICDGEMVLIGGI-MEHIEQAGVHSGDSACSLPA-YTLSQEIQDVMRQQVQKLAfelQVRGLMNVQ 829
Cdd:pfam02655 65 VQEFIE-GEPLSVSLLSDGEKALPLSVnRQYIDNGGSGFVYAGNVTPSrTELKEEIIELAEEVVECLP---GLRGYVGVD 140
|
170
....*....|....*.
gi 489109057 830 FAVKNNEVYLIEVNPR 845
Cdd:pfam02655 141 LVLKDNEPYVIEVNPR 156
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
35-194 |
3.24e-06 |
|
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: 50.32 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 35 KALREEGYRVILVNsnpatimtdpemADATYIEPIHWEVVRKIIEKERPDAVLPTmggQTALNCALELERQgvLAEFGVT 114
Cdd:COG0189 21 EAAQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPR---IDPPFYGLALLRQ--LEAAGVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 115 MIGaTADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREEFEEICER 194
Cdd:COG0189 84 VVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEA 162
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
162-303 |
5.90e-06 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 47.28 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 162 VGFPCIIRPSFTMGGTGGGIAYNREEFEEICERGL-DLSPTNEL-----------LIdESLIGWKEYEMEVVRDKNDNCI 229
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIReEIEQWKEMypeavvdggsfLV-EEYIEGEEFAVDAYFDENGEPV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489109057 230 IVCSIENFDAMGIHTGDSITVAPAQTLTDKEYQIMrNASMAVLREIGVETGGSNVQFAVNpKNGRLIVIEMNPR 303
Cdd:pfam13535 80 ILNILKHDFASSEDVSDRIYVTSASIIRETQAAFT-EFLKRINALLGLKNFPVHIELRVD-EDGQIIPIEVNPL 151
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
109-304 |
8.48e-06 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 50.08 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 109 AEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARS--GIAHTMEEALAVAADVGFPCIIRPSftMGGTGGG--IAYN 184
Cdd:COG1038 99 EEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAA--AGGGGRGmrVVRS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 185 REEFEEICER---------GLDlsptnELLIDESLIGWKEYEMEVVRDKNDNciIV------CS--------IEnfdamg 241
Cdd:COG1038 177 EEELEEAFESarreakaafGDD-----EVFLEKYIERPKHIEVQILGDKHGN--IVhlferdCSvqrrhqkvVE------ 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489109057 242 ihtgdsitVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNpKNGRLIVIEMNPRV 304
Cdd:COG1038 244 --------IAPAPNLDEELREAICEAAVKLAKAVGYVNAGT-VEFLVD-DDGNFYFIEVNPRI 296
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
651-912 |
9.19e-06 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 49.43 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 651 ARALEAAGVPVIGTSPDAIDRAEDRE--RFQQAVDRLKL---KQPANATvtAIEQAVEKAKEIGYPLVVRPSYVLGGRAM 725
Cdd:PRK08463 91 AKAVEDAGIIFIGPKSEVIRKMGNKNiaRYLMKKNGIPIvpgTEKLNSE--SMEEIKIFARKIGYPVILKASGGGGGRGI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 726 EIVYDEADLRRYFQT----AVSVSNDAPVLLDRFLDDAVEVDVDAICDGemvlIGGImehieqagVHSGDSACSL----- 796
Cdd:PRK08463 169 RVVHKEEDLENAFESckreALAYFNNDEVFMEKYVVNPRHIEFQILGDN----YGNI--------IHLCERDCSIqrrhq 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 797 ------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVM 869
Cdd:PRK08463 237 kvieiaPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIA 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489109057 870 AGKTL-------AQQGVTKEVIPPYYSVKEVVLPF-NKFPGVDPLLGPEMR 912
Cdd:PRK08463 317 AGEILdleqsdiKPRGFAIEARITAENVWKNFIPSpGKITEYYPALGPSVR 367
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
944-1006 |
1.33e-05 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 48.93 E-value: 1.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489109057 944 RALLSVreGDKERVVDLAAKLLKFGFELDATHGTAIVLGEAGINprlVNKVHE--GRPHIQD-RIK 1006
Cdd:PRK00881 6 RALISV--SDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIP---VTEVSDvtGFPEILDgRVK 66
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
944-1006 |
3.45e-05 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 47.71 E-value: 3.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489109057 944 RALLSVreGDKERVVDLAAKLLKFGFELDATHGTAIVLGEAGINprlVNKVHE--GRPHIQD-RIK 1006
Cdd:COG0138 5 RALISV--SDKTGLVEFARALVELGVEIISTGGTAKALREAGIP---VTEVSEvtGFPEILDgRVK 65
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-190 |
6.11e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 46.67 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 1 MPKRtdIKSILILGAGPIVIgqacefdysgaQACKALREEGYRVILVNSN------PA-----TIMTDPEMADATYIEPi 69
Cdd:PRK12833 1 MPSR--IRKVLVANRGEIAV-----------RIIRAARELGMRTVAACSDadrdslAArmadeAVHIGPSHAAKSYLNP- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 70 hwEVVRKIIEKERPDAVLPTMGGqTALNCALElerQGVLAEfGVTMIGATADAI----DKAEDRRrfdiAMKKIGLDT-- 143
Cdd:PRK12833 67 --AAILAAARQCGADAIHPGYGF-LSENAAFA---EAVEAA-GLIFVGPDAQTIrtmgDKARARR----TARRAGVPTvp 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489109057 144 ARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREEFEE 190
Cdd:PRK12833 136 GSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAA 182
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
653-845 |
6.71e-05 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 46.67 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 653 ALEAAGVPVIgtsPDAidRAE----DRERFQQ-AVDRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRPsyVLG--GRAM 725
Cdd:PRK09288 93 ELEKEGFNVV---PTA--RATrltmNREGIRRlAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKP--VMSssGKGQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 726 EIVYDEADLRRYFQTAVSVS--NDAPVLLDRFLDDAVEVDVDAIC--DGEMVLIGGImEHIEQagvhSGDSACSL-PAyT 800
Cdd:PRK09288 166 SVVRSPEDIEKAWEYAQEGGrgGAGRVIVEEFIDFDYEITLLTVRavDGGTHFCAPI-GHRQE----DGDYRESWqPQ-P 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489109057 801 LSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPR 845
Cdd:PRK09288 240 MSPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVYFSEVSPR 284
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
683-845 |
9.71e-05 |
|
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: 44.17 E-value: 9.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 683 DRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRpSYVLG--GRAMEIVYDEADLrryfQTAVSVSNDAPVLLDRFLDDAV 760
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVK-ARRGGydGKGQYVVRSEADL----PQAWEELGDGPVIVEEFVPFDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 761 EVDVDAI--CDGEMVlIGGIMEHIEQAGVhsgdsaCSL---PAyTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNN 835
Cdd:pfam02222 76 ELSVLVVrsVDGETA-FYPVVETIQEDGI------CRLsvaPA-RVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTED 147
|
170
....*....|.
gi 489109057 836 -EVYLIEVNPR 845
Cdd:pfam02222 148 gDLLINELAPR 158
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
29-301 |
1.04e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 45.49 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 29 SGAQACKALREEGYRVILVnsnpatimtDPEMADATyiepihwevvrkIIEKERPDAVLptmggqTALN-------CAle 101
Cdd:PRK01372 24 SGAAVLAALREAGYDAHPI---------DPGEDIAA------------QLKELGFDRVF------NALHgrggedgTI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 102 lerQGVLAEFGVTMIG----ATADAIDKAedrrRFDIAMKKIGLDTARSGIAHTMEEALAVAADVGFPCIIRPSftmggT 177
Cdd:PRK01372 75 ---QGLLELLGIPYTGsgvlASALAMDKL----RTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPA-----R 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 178 GG---GIA--YNREEFEEICERGLDLSptNELLIDESLIGwKEYEMEVVRDKndnciIVCSIE--------NFDAMGIhT 244
Cdd:PRK01372 143 EGssvGVSkvKEEDELQAALELAFKYD--DEVLVEKYIKG-RELTVAVLGGK-----ALPVIEivpagefyDYEAKYL-A 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 489109057 245 GDSITVAPAQtLTDKEYQIMRNASMAVLREIGVEtGGSNVQFAVNpKNGRLIVIEMN 301
Cdd:PRK01372 214 GGTQYICPAG-LPAEIEAELQELALKAYRALGCR-GWGRVDFMLD-EDGKPYLLEVN 267
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
117-305 |
1.89e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 45.61 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 117 GATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREEFEEICERGL 196
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 197 DlSPTNELLIdESLIGWKEYEMEVVRDkNDNCIIVCSIENFDAMGIHTGDSITVAPAQTLTDKEYQIMRNASMAvLREIG 276
Cdd:PRK02186 176 R-AGTRAALV-QAYVEGDEYSVETLTV-ARGHQVLGITRKHLGPPPHFVEIGHDFPAPLSAPQRERIVRTVLRA-LDAVG 251
|
170 180
....*....|....*....|....*....
gi 489109057 277 VETGGSNVQFAVnpKNGRLIVIEMNPRVS 305
Cdd:PRK02186 252 YAFGPAHTELRV--RGDTVVIIEINPRLA 278
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
654-756 |
2.42e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.15 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 654 LEAAGVPVigtspdaidraedrerfqqavdrlklkqPANATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRAMEI-VYDEA 732
Cdd:PRK14016 222 LAAAGVPV----------------------------PEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTRE 273
|
90 100
....*....|....*....|....
gi 489109057 733 DLRRYFQTAVSVSNDapVLLDRFL 756
Cdd:PRK14016 274 EIEAAYAVASKESSD--VIVERYI 295
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
112-332 |
2.60e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 44.74 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 112 GVTMIGATADAIDKAEDRRRFDIAMKKIGLDT--ARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREEFE 189
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVipGSDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 190 EicergLDLSPTNELL---------IDESLIGWKEYEMEVVRDKNDNCIIV----CSIENfdamgiHTGDSITVAPAQTL 256
Cdd:PRK08462 181 N-----LYLAAESEALsafgdgtmyMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489109057 257 TDKEYQIMRNASMAVLREIGVETGGSnVQFAVNpKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTL 332
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGT-FEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
690-850 |
9.38e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 42.41 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 690 PANATVTAIEQAVEKAKEIGYPLVVRPsyVLGGR--AMEIVYDEADLRRYFQTAVSVsnDAPVLLDRFLdDAVEVDVdAI 767
Cdd:PRK01372 114 PPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAFKY--DDEVLVEKYI-KGRELTV-AV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 768 CDGEMVligGIMEhIEQAGV--------HSGDSACSLPAYtLSQEIQdvmrQQVQKLAFE----LQVRGLMNVQFAVKN- 834
Cdd:PRK01372 188 LGGKAL---PVIE-IVPAGEfydyeakyLAGGTQYICPAG-LPAEIE----AELQELALKayraLGCRGWGRVDFMLDEd 258
|
170 180
....*....|....*....|....*..
gi 489109057 835 NEVYLIEVN-----------PRAARTV 850
Cdd:PRK01372 259 GKPYLLEVNtqpgmtshslvPMAARAA 285
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
946-1015 |
1.63e-03 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 39.21 E-value: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489109057 946 LLSVREGDKERVVDLAAKLLKFGFELDATHGTAIVLGEAGINPRLVNKVHE----GRPHIQDRIKNGEYTYIIN 1015
Cdd:cd01423 4 LISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEepqnDKPSLRELLAEGKIDLVIN 77
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
137-304 |
1.81e-03 |
|
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: 40.31 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 137 KKIGLDTARSGIAHTMEEALAVAADVGFPCIIRPSfTMGGTGGGIAYNREEfeeicergLDLSPTNELLIDESLI--GWK 214
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKAR-RGGYDGKGQYVVRSE--------ADLPQAWEELGDGPVIveEFV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 215 EYEME----VVRDKNDNCIIVCSIENFDAMGIHTgdsITVAPAQTLTDKE---YQIMRNAsMAVLREIGVetggsnvqFA 287
Cdd:pfam02222 72 PFDRElsvlVVRSVDGETAFYPVVETIQEDGICR---LSVAPARVPQAIQaeaQDIAKRL-VDELGGVGV--------FG 139
|
170 180
....*....|....*....|
gi 489109057 288 VN---PKNGRLIVIEMNPRV 304
Cdd:pfam02222 140 VElfvTEDGDLLINELAPRP 159
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
120-304 |
1.94e-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: 41.60 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 120 ADAIDKAEDR---RRFdiaMKKIGLDTARSGIAHTMEEALAVAADVGFPCIIRPSfTMG--GTGGGIAYNREEFEEICEr 194
Cdd:COG0026 81 PEALEIAQDRlleKAF---LAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTR-RGGydGKGQVVIKSAADLEAAWA- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 195 GLDLSPtnelLIDESLIgwkEYEME----VVRDKNDNCIIVCSIENfdamgIHTgDSI---TVAPAQtLTDKEYQIMRNA 267
Cdd:COG0026 156 ALGGGP----CILEEFV---PFERElsviVARSPDGEVATYPVVEN-----VHR-NGIldeSIAPAR-ISEALAAEAEEI 221
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489109057 268 SMAVLREIGVeTGgsnVqFAVN---PKNGRLIVIEMNPRV 304
Cdd:COG0026 222 AKRIAEALDY-VG---V-LAVEffvTKDGELLVNEIAPRP 256
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
8-157 |
5.00e-03 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 40.00 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109057 8 KSILILGAGPivIGQACefdysgAQACKALreeGYRVILVNSNPATImtdpEMA-DATYIEPIH-----WEVVRKIIEKE 81
Cdd:cd05188 136 DTVLVLGAGG--VGLLA------AQLAKAA---GARVIVTDRSDEKL----ELAkELGADHVIDykeedLEEELRLTGGG 200
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489109057 82 RPDAVLPTMGGQTALNCALE-LERQGVLAEFGVTMIGATADAIdkaedrrrFDIAMKKIGLDTARSGIAHTMEEALA 157
Cdd:cd05188 201 GADVVIDAVGGPETLAQALRlLRPGGRIVVVGGTSGGPPLDDL--------RRLLFKELTIIGSTGGTREDFEEALD 269
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
814-886 |
5.62e-03 |
|
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.
Pssm-ID: 434824 [Multi-domain] Cd Length: 131 Bit Score: 37.98 E-value: 5.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489109057 814 QKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPfVSKATGVPLAKVAARvmagktLAQQGVTKEVIPP 886
Cdd:pfam15632 54 RRLAEAFGLDGLFNVQFRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALK------LLLGLETPDPVEP 119
|
|
| |
