|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1035 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1805.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 1 MPKDSSLQSILLIGSGPIVIGQAAEFDYSGTQACIALKEEGYRVILVNNNPATIMTDEVHADAVYFEPLTVDAVEAIIAK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 81 ERPDGLLATFGGQTGLNLAFQLHEAGVLEKYGVRLLGTPIEAIKRGEDREAFRALMHELGEPVPESEIVTSVEEAVAFAE 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 161 QIGFPIIIRPAYTLGGTGGGIAENMEQFLALVEKGLNESPIHQCLIERSVAGFKEIEYEVMRDQSNTCITVCNMENVDPV 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 241 GIHTGDSIVVAPSQTLTDEEYQMLRSSAVKIISALGIIGGCNIQFALDPNSKQYYLIEVNPRVSRSSALASKATGYPIAR 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 321 IAAKLAVGYTLAELVNPVTKTTYASFEPALDYVVVKFPRLPFDKFPHADRKLGTQMKATGEVMAIDRNMERAFQKAVQSL 400
Cdd:PRK12815 321 IAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 401 EGKNNGLLLP-ELSVKTNDELKQLLVDKDDRRFFAILELLRRGVAVEAIHEWTKIDRFFLCSFERLVALEKQAAAATLDt 479
Cdd:PRK12815 401 EIKRNGLSLPiELSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLD- 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 480 IEEQTFRFLKEKGCSDAFLAETWGVTELDVRNKRKELGIVPSYKMVDTCAAEFHSETDYYYSTYFGEDERKQPSGKEKVL 559
Cdd:PRK12815 480 LSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPSSEKKKVL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 560 IIGAGPIRIGQGIEFDYSSVHSVFALQKEGYETVMINNNPETVSTDFAVADRLYFEPLTLESVLDVIEAEQIKHVIVQFG 639
Cdd:PRK12815 560 ILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFG 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 640 GQTAINLVKGLEEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMANNAEELAAKAAEIGCPVLLRPSYVIGGR 719
Cdd:PRK12815 640 GQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQ 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 720 GMFIVHSEAQLAALIEQG-ELTYPILIDAYLDGKEAEADIVTDGTDIVLPVIIEHVEKAGVHSGDSYAWLPAQTLTDEEK 798
Cdd:PRK12815 720 GMAVVYDEPALEAYLAENaSQLYPILIDQFIDGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQSLSEEQQ 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 799 AKIIDYAGRIAKKLGFKGIMNIQYVIADGNVYVLEVNPRASRTVPIVSKTTGVPLAQIATKLLLGKSLVDIVDEKARGLA 878
Cdd:PRK12815 800 EKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGYPNGLWPG 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 879 VMPYAVlKYPVFSTHKLPGVDPVVGPEMKSTGEGISIAATKEEAAYKAFYPYLQKKANANEVYVIGNID-----AELEAE 953
Cdd:PRK12815 880 SPFIHV-KMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEdkpevTKLARR 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 954 MTAKQLTIVADVPFSDWVKRDTALA--------------------------VIDLGK--EEGEANKRMTALSRQLLVFTE 1005
Cdd:PRK12815 959 FAQLGFKLLATEGTANWLAEEGITTgvvekvqegspsllerikqhrivlvvNTSLSDsaSEDAIKIRDEALSTHIPVFTE 1038
|
1050 1060 1070
....*....|....*....|....*....|
gi 1215498573 1006 RETLKLFLQALDVDHLDVQPIHGWLEKKKQ 1035
Cdd:PRK12815 1039 LETAQAFLQVLESLALTTQPIQELQEKHKQ 1068
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-927 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1578.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 1 MPKDSSLQSILLIGSGPIVIGQAAEFDYSGTQACIALKEEGYRVILVNNNPATIMTDEVHADAVYFEPLTVDAVEAIIAK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 81 ERPDGLLATFGGQTGLNLAFQLHEAGVLEKYGVRLLGTPIEAIKRGEDREAFRALMHELGEPVPESEIVTSVEEAVAFAE 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 161 QIGFPIIIRPAYTLGGTGGGIAENMEQFLALVEKGLNESPIHQCLIERSVAGFKEIEYEVMRDQSNTCITVCNMENVDPV 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 241 GIHTGDSIVVAPSQTLTDEEYQMLRSSAVKIISALGII-GGCNIQFALDPNSKQYYLIEVNPRVSRSSALASKATGYPIA 319
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 320 RIAAKLAVGYTLAELVNPVTKTTYASFEPALDYVVVKFPRLPFDKFPHADRKLGTQMKATGEVMAIDRNMERAFQKAVQS 399
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 400 LEGKNNGLLLPELSVKTNDELKQLLVDKDDRRFFAILELLRRGVAVEAIHEWTKIDRFFLCSFERLVALEKQAAAATLDT 479
Cdd:PRK05294 401 LEIGVTGLDEDLFEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 480 IEEqTFRFLKEKGCSDAFLAETWGVTELDVRNKRKELGIVPSYKMVDTCAAEFHSETDYYYSTYFGEDErKQPSGKEKVL 559
Cdd:PRK05294 481 DAE-LLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECE-SNPSDRKKVL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 560 IIGAGPIRIGQGIEFDYSSVHSVFALQKEGYETVMINNNPETVSTDFAVADRLYFEPLTLESVLDVIEAEQIKHVIVQFG 639
Cdd:PRK05294 559 VLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 640 GQTAINLVKGLEEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMANNAEELAAKAAEIGCPVLLRPSYVIGGR 719
Cdd:PRK05294 639 GQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGR 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 720 GMFIVHSEAQLAALIE---QGELTYPILIDAYLDGK-EAEADIVTDGTDIVLPVIIEHVEKAGVHSGDSYAWLPAQTLTD 795
Cdd:PRK05294 719 AMEIVYDEEELERYMReavKVSPDHPVLIDKFLEGAiEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQTLSE 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 796 EEKAKIIDYAGRIAKKLGFKGIMNIQYVIADGNVYVLEVNPRASRTVPIVSKTTGVPLAQIATKLLLGKSLVDIvdEKAR 875
Cdd:PRK05294 799 EIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAEL--GYTK 876
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 1215498573 876 GLAVMPYAVlKYPVFSTHKLPGVDPVVGPEMKSTGEGISIAATKEEAAYKAF 927
Cdd:PRK05294 877 GLIPPYVAV-KEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQ 927
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1016 |
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: 1511.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 2 PKDSSLQSILLIGSGPIVIGQAAEFDYSGTQACIALKEEGYRVILVNNNPATIMTDEVHADAVYFEPLTVDAVEAIIAKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 82 RPDGLLATFGGQTGLNLAFQLHEAGVLEKYGVRLLGTPIEAIKRGEDREAFRALMHELGEPVPESEIVTSVEEAVAFAEQ 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 162 IGFPIIIRPAYTLGGTGGGIAENMEQFLALVEKGLNESPIHQCLIERSVAGFKEIEYEVMRDQSNTCITVCNMENVDPVG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 242 IHTGDSIVVAPSQTLTDEEYQMLRSSAVKIISALGIIGGCNIQFALDPNSKQYYLIEVNPRVSRSSALASKATGYPIARI 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 322 AAKLAVGYTLAELVNPVTKTTYASFEPALDYVVVKFPRLPFDKFPHADRKLGTQMKATGEVMAIDRNMERAFQKAVQSLE 401
Cdd:TIGR01369 321 AAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 402 GKNNGLLLPELSVKTNDELKQLLVDKDDRRFFAILELLRRGVAVEAIHEWTKIDRFFLCSFERLVALEKQAAAATLDTIE 481
Cdd:TIGR01369 401 IGATGFDLPDREVEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 482 EQTFRFLKEKGCSDAFLAETWGVTELDVRNKRKELGIVPSYKMVDTCAAEFHSETDYYYSTYFGEDERKQPSGKEKVLII 561
Cdd:TIGR01369 481 PELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 562 GAGPIRIGQGIEFDYSSVHSVFALQKEGYETVMINNNPETVSTDFAVADRLYFEPLTLESVLDVIEAEQIKHVIVQFGGQ 641
Cdd:TIGR01369 561 GSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 642 TAINLVKGLEEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMANNAEELAAKAAEIGCPVLLRPSYVIGGRGM 721
Cdd:TIGR01369 641 TPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 722 FIVHSEAQLAALIEQG---ELTYPILIDAYL-DGKEAEADIVTDGTDIVLPVIIEHVEKAGVHSGDSYAWLPAQTLTDEE 797
Cdd:TIGR01369 721 EIVYNEEELRRYLEEAvavSPEHPVLIDKYLeDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 798 KAKIIDYAGRIAKKLGFKGIMNIQYVIADGNVYVLEVNPRASRTVPIVSKTTGVPLAQIATKLLLGKSLVDIVDEKARGl 877
Cdd:TIGR01369 801 VDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGKEKE- 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 878 avMPYAVLKYPVFSTHKLPGVDPVVGPEMKSTGEGISIAATKEEAAYKAFYPYLQKKANANEVYVIG------------- 944
Cdd:TIGR01369 880 --PKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVrdkdkeelldlar 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 945 -------NIDAELEAEMTAKQLTIVADV---------PFSDWVKRDTALAVIDL---GKEEGEANKRM--TALSRQLLVF 1003
Cdd:TIGR01369 958 klaekgyKLYATEGTAKFLGEAGIKPELvlkvsegrpNILDLIKNGEIELVINTtskGAGTATDGYKIrrEALDYGVPLI 1037
|
1050
....*....|...
gi 1215498573 1004 TERETLKLFLQAL 1016
Cdd:TIGR01369 1038 TTLNTAEAFAEAL 1050
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-915 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1003.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 3 KDSSLQSILLIGSGPIVIGQAAEFDYSGTQACIALKEEGYRVILVNNNPATIMTDEVHADAVYFEPLTVDAVEAIIAKER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 83 PDGLLATFGGQTGLNLAFQLHEAGVLEKYGVRLLGTPIEAIKRGEDREAFRALMHELGEPVPESEIVTSVEEAVAFAEQI 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 163 G-FPIIIRPAYTLGGTGGGIAENMEQFLALVEKGLNESPIHQCLIERSVAGFKEIEYEVMRDQSNTCITVCNMENVDPVG 241
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 242 IHTGDSIVVAPSQTLTDEEYQMLRSSAVKIISALGI-IGGCNIQFALDPNSKQYYLIEVNPRVSRSSALASKATGYPIAR 320
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVeCGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 321 IAAKLAVGYTLAELVNPVTKTTYASFEPALDYVVVKFPRLPFDKFPHADRKLGTQMKATGEVMAIDRNMERAFQKAVQSL 400
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 401 EGKNNGLLLPELSVKTND--ELKQLLVDKDDRRFFAILELLRRGVAVEAIHEWTKIDRFFLCSFERLVALEKQAAAATLD 478
Cdd:PLN02735 419 ETGFSGWGCAKVKELDWDweQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLS 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 479 TIEEQTFRFLKEKGCSDAFLAETWGVTELDVRNKRKELGIVPSYKMVDTCAAEFHSETDYYYSTYFGEDErKQPSGKEKV 558
Cdd:PLN02735 499 ELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECE-SAPTNKKKV 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 559 LIIGAGPIRIGQGIEFDYSSVHSVFALQKEGYETVMINNNPETVSTDFAVADRLYFEPLTLESVLDVIEAEQIKHVIVQF 638
Cdd:PLN02735 578 LILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQF 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 639 GGQTAINLVKGLEEA-------------GVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMANNAEELAAKAAEIG 705
Cdd:PLN02735 658 GGQTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIG 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 706 CPVLLRPSYVIGGRGMFIVHSEAQLAALIE---QGELTYPILIDAYL-DGKEAEADIVTDGT-DIVLPVIIEHVEKAGVH 780
Cdd:PLN02735 738 YPVVVRPSYVLGGRAMEIVYSDDKLKTYLEtavEVDPERPVLVDKYLsDATEIDVDALADSEgNVVIGGIMEHIEQAGVH 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 781 SGDSYAWLPAQTLTDEEKAKIIDYAGRIAKKLGFKGIMNIQY-VIADGNVYVLEVNPRASRTVPIVSKTTGVPLAQIATK 859
Cdd:PLN02735 818 SGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASL 897
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498573 860 LLLGKSLVDIVDEKArglAVMPYAVLKYPVFSTHKLPGVDPVVGPEMKSTGEGISI 915
Cdd:PLN02735 898 VMSGKSLKDLGFTEE---VIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGI 950
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-562 |
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: 776.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 13 IGSGPIVIGQAAEFDYSGTQACIALKEEGYRVILVNNNPATIMTDEVHADAVYFEPLTVDAVEAIIAKERPDGLLATFGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 93 QTGLNLAFQLHEAGVLEkyGVRLLGTPIEAIKRGEDREAFRALMHELGEPVPESEIVTSVEEAVAFAEQIGFPIIIRPAY 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 173 TLGGTGGGIAENMEQFLALVEKGLNESPIHQCLIERSVAGFKEIEYEVMRDQSNTCITVCNMENVDPVGIHTGDSIVVAP 252
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 253 SQTLTDEEYQMLRSSAVKIISALGIIGGCNIQFALDpnSKQYYLIEVNPRVSRSSALASKATGYPIARIAAKLAVGYTLA 332
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 333 ELVNPvTKttyasFEPALDYVVVKFPRLPFDKFPHADRKLGTQMKATGEVMAIDRNMERAFQKAVQSLEGKNNGLLLPEL 412
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 413 sVKTNDELKQLLVDKDDRRFFAILELLRRGVAVEAIHEWTKIDRFFLCSFERLVALEKQAAAATLDTIeeqTFRFLKEKG 492
Cdd:COG0458 391 -VADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVIN---TLLGAKSLG 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 493 CSDAFLAETWGVTELDVRNKRKELGIVPSYKMVDTCAAEFHSETDYYYSTYFGEDERKQPSGKEKVLIIG 562
Cdd:COG0458 467 DSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
561-927 |
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: 540.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 561 IGAGPIRIGQGIEFDYSSVHSVFALQKEGYETVMINNNPETVSTDFAVADRLYFEPLTLESVLDVIEAEQIKHVIVQFGG 640
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 641 QTAINLVKGLEEA----GVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMANNAEELAAKAAEIGCPVLLRPSYVI 716
Cdd:COG0458 81 QTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 717 GGRGMFIVHSEAQLAALIEQG---ELTYPILIDAYLDG-KEAEADIVTDGTD-IVLPVIIEHVEKAGVHSGDSYAWLPAQ 791
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERAlkvSPDHPVLIDESLLGaKEIEVDVVRDGEDnVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 792 TLTDEEKAKIIDYAGRIAKKLGFKGIMNIQYVIADGNVYVLEVNPRASRTVPIVSKTTGVPLAQIATKLLLGKSLVDIvd 871
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDEL-- 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498573 872 EKARGLA-VMPYAVLKYPVFSTHKLPGVDPVVGPEMKSTGEGISIAATKEEAAYKAF 927
Cdd:COG0458 319 GNDTGFEpTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKAL 375
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-331 |
8.37e-97 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 304.61 E-value: 8.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 128 DREAFRALMHELGEPVPESEI--VTSVEEAVAFAEQIGFPIIIRPAYTLGGTGGGIAENMEQFLALVEKGLNESP----I 201
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPaafgN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 202 HQCLIERSVAGFKEIEYEVMRDQSNTCITVCNMENVDPVgiHTGDSIVVAPSQTLTDEEYQMLRSSAVKIISALGIIGGC 281
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498573 282 NIQFALDPNSKQYYLIEVNPRVSRSSALASKATGYPIARIAAKLAVGYTL 331
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
10-396 |
1.14e-82 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 291.30 E-value: 1.14e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 10 ILLIGSGPIVIGQAAEFDYSGTQACIALKEEGYRVILVNNNPATIMTDEVHADAVYFEPLTVDAVEAIIAKERPDGLLAT 89
Cdd:PLN02735 577 VLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQ 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 90 FGGQTGLNLAFQLHEAgvLEKY---------GVRLLGTPIEAIKRGEDREAFRALMHELGEPVPESEIVTSVEEAVAFAE 160
Cdd:PLN02735 657 FGGQTPLKLALPIQKY--LDKNpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 161 QIGFPIIIRPAYTLGGTGGGIAENMEQFLALVEKGLNESPIHQCLIERSVAGFKEIEYEVMRDQSNTCITVCNMENVDPV 240
Cdd:PLN02735 735 RIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVVIGGIMEHIEQA 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 241 GIHTGDSIVVAPSQTLTDEEYQMLRSSAVKIISALGIIGGCNIQFALDPNSkQYYLIEVNPRVSRSSALASKATGYPIAR 320
Cdd:PLN02735 815 GVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSG-EVYIIEANPRASRTVPFVSKAIGHPLAK 893
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498573 321 IAAKLAVGYTLAELvnPVTKttyasfEPALDYVVVKFPRLPFDKFPHADRKLGTQMKATGEVMAIDRNMERAFQKA 396
Cdd:PLN02735 894 YASLVMSGKSLKDL--GFTE------EVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKA 961
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
534-927 |
4.13e-71 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 257.40 E-value: 4.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 534 SETDYYYSTYFGEDERKQPSGKEKVLIIGAGPIRIGQGIEFDYSSVHSVFALQKEGYETVMINNNPETVSTDFAVADRLY 613
Cdd:PLN02735 2 SLADTVTRAWSAATKAGKRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 614 FEPLTLESVLDVIEAEQIKHVIVQFGGQTAINLVKGLEEAG------VPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVP 687
Cdd:PLN02735 82 IAPMTPELVEQVIAKERPDALLPTMGGQTALNLAVALAESGilekygVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 688 GLMANNAEELAAKAAEIG-CPVLLRPSYVIGGRGMFIVHSEAQLAALIEQG---ELTYPILIDAYLDG-KEAEADIVTDG 762
Cdd:PLN02735 162 SGIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGlaaSITSQVLVEKSLLGwKEYELEVMRDL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 763 TD-IVLPVIIEHVEKAGVHSGDSYAWLPAQTLTDEEKAKIIDYAGRIAKKLGFK-GIMNIQYVI--ADGNVYVLEVNPRA 838
Cdd:PLN02735 242 ADnVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVEcGGSNVQFAVnpVDGEVMIIEMNPRV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 839 SRTVPIVSKTTGVPLAQIATKLLLGKSLVDIVDEKARGLAV-----MPYAVLKYPVFSTHKLPGVDPVVGPEMKSTGEGI 913
Cdd:PLN02735 322 SRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDITLKTPAsfepsIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAM 401
|
410
....*....|....
gi 1215498573 914 SIAATKEEAAYKAF 927
Cdd:PLN02735 402 ALGRTFQESFQKAL 415
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
420-543 |
2.98e-51 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 176.10 E-value: 2.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 420 LKQLLVDKDDRRFFAILELLRRGVAVEAIHEWTKIDRFFLCSFERLVALEKQAAAATLDTIEEQTFRFLKEKGCSDAFLA 499
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1215498573 500 ETWGVTELDVRNKRKELGIVPSYKMVDTCAAEFHSETDYYYSTY 543
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
670-866 |
1.37e-32 |
|
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: 125.88 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 670 DRDRFYQLLEELDIPHVPGLMA--NNAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVHSEAQLAALIEQGELTYP----- 742
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 743 --ILIDAYLDG-KEAEADIVTDGTDIVLPVI-IEHVEKagVHSGDSYAWLPAQTLTDEEKAKIIDYAGRIAKKLGFKGIM 818
Cdd:pfam02786 81 pqVLVEKSLKGpKHIEYQVLRDAHGNCITVCnRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498573 819 NIQYVI--ADGNVYVLEVNPRASRTVPIVSKTTGVPLAQIATKLLLGKSL 866
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
71-328 |
7.61e-31 |
|
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: 122.67 E-value: 7.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 71 VDAVEAIIAKERPDGLLAtfggqtgLNLAFQLHEAGVLEKYGVRllGTPIEAIKRGEDREAFRALMHELGEPVPESEIVT 150
Cdd:COG0439 6 IAAAAELARETGIDAVLS-------ESEFAVETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 151 SVEEAVAFAEQIGFPIIIRPAYTLGGTGGGIAENMEQFLALVEKGLNE----SPIHQCLIERSVAGfKEIEYEVMRDQSN 226
Cdd:COG0439 77 SPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEakagSPNGEVLVEEFLEG-REYSVEGLVRDGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 227 TCIT-VCNMENVDPVGIHTGDsivVAPSQtLTDEEYQMLRSSAVKIISALGII-GGCNIQFALDPNsKQYYLIEVNPRVS 304
Cdd:COG0439 156 VVVCsITRKHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPD-GEPYLIEINARLG 230
|
250 260
....*....|....*....|....*.
gi 1215498573 305 --RSSALASKATGYPIARIAAKLAVG 328
Cdd:COG0439 231 geHIPPLTELATGVDLVREQIRLALG 256
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
17-353 |
3.51e-26 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 111.94 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 17 PIVIGqaaeFDYSGTQACIALKEEGYRVILVNNNPATIMTDEVHADAVYFEPLT-------VDAVEAIIAKERPDGLLAT 89
Cdd:COG3919 8 VVVLG----GDINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPgddpeafVDALLELAERHGPDVLIPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 90 FGGQTglnLAFQLHEAgVLEKYgVRLLGTPIEAIKRGEDREAFRALMHELGEPVPESEIVTSVEEAVAFAEQIGFPIIIR 169
Cdd:COG3919 84 GDEYV---ELLSRHRD-ELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 170 PAYT--------LGGTGGGIAENMEQFLALVEK--GLNESPIHQCLI------ERSVAGFkeieyevmRDQSNTCITVCN 233
Cdd:COG3919 159 PADSvgydelsfPGKKKVFYVDDREELLALLRRiaAAGYELIVQEYIpgddgeMRGLTAY--------VDRDGEVVATFT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 234 MENV--DPVGIHTGDSIVVAPsqtltDEEyqmLRSSAVKIISALGIIGGCNIQFALDPNSKQYYLIEVNPRVSRSSALAS 311
Cdd:COG3919 231 GRKLrhYPPAGGNSAARESVD-----DPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFWRSLYLAT 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1215498573 312 KAtGYPIARIAAKLAVG--YTLAELVNPVTKTTYASFEPALDYV 353
Cdd:COG3919 303 AA-GVNFPYLLYDDAVGrpLEPVPAYREGVLWRVLPGDLLLRYL 345
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
651-864 |
5.90e-22 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 96.48 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 651 EEAGVPllGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMANNAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVHSEAQL 730
Cdd:COG0439 37 EELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 731 AALIEQ-------GELTYPILIDAYLDGKEAEAD-IVTDGTdiVLPVIIEHVEKAGVHSGDSYAWLPAQtLTDEEKAKII 802
Cdd:COG0439 115 EAALAEaraeakaGSPNGEVLVEEFLEGREYSVEgLVRDGE--VVVCSITRKHQKPPYFVELGHEAPSP-LPEELRAEIG 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498573 803 DYAGRIAKKLGFK-GIMNIQYVI-ADGNVYVLEVNPRAS--RTVPIVSKTTGVPLAQIATKLLLGK 864
Cdd:COG0439 192 ELVARALRALGYRrGAFHTEFLLtPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGE 257
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
428-500 |
2.25e-19 |
|
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: 83.19 E-value: 2.25e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498573 428 DDRRFFAILELLRRGVAVEAIHEWTKIDRFFLCSFERLVALEKQAAAATLDtIEEQTFRFLKEKGCSDAFLAE 500
Cdd:pfam02787 7 TDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLD-LDAELLREAKRLGFSDRQIAK 78
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
619-882 |
1.40e-18 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 88.02 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 619 LESVLDVIEAEQIKHVIVqfGGQTAINLV----KGLEEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMANNA 694
Cdd:PRK12767 58 IDRLLDICKKEKIDLLIP--LIDPELPLLaqnrDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 695 --EELAAKAAEIGCPVLLRPSYVIGGRGMFIVHSEAQLAALIEQGEltyPILIDAYLDGKEAEADIVTDGTDIVLPVIIe 772
Cdd:PRK12767 136 edFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVP---NLIIQEFIEGQEYTVDVLCDLNGEVISIVP- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 773 hVEKAGVHSGDSYawlpaQTLTDEEKaKIIDYAGRIAKKLGFKGIMNIQYVIADGNVYVLEVNPRASRTVPiVSKTTGVP 852
Cdd:PRK12767 212 -RKRIEVRAGETS-----KGVTVKDP-ELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYP-LSYMAGAN 283
|
250 260 270
....*....|....*....|....*....|
gi 1215498573 853 LAQIATKLLLGKSLVDIVDEKARGLAVMPY 882
Cdd:PRK12767 284 EPDWIIRNLLGGENEPIIGEYKEGLYMRRY 313
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
557-887 |
7.60e-18 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 86.91 E-value: 7.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 557 KVLIIGAGPIrigqgiefDYSSVHSvfaLQKEGYETVMINNNPETVSTDFAVADRLYFEPLT-------LESVLDVIEAE 629
Cdd:COG3919 7 RVVVLGGDIN--------ALAVARS---LGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPgddpeafVDALLELAERH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 630 QiKHVIVQFGGQTAINLVKGLEE--AGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMANNAEELAAKAAEIGCP 707
Cdd:COG3919 76 G-PDVLIPTGDEYVELLSRHRDEleEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 708 VLLRPSY--------VIGGRGMFIVHSEAQLAALIEQ-GELTYPILIDAYLDGKEAEADIVT-----DGTdiVLPVIIEH 773
Cdd:COG3919 155 VVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRiAAAGYELIVQEYIPGDDGEMRGLTayvdrDGE--VVATFTGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 774 VEKAGVHSGDSYAWLpaQTLTDEEkakIIDYAGRIAKKLGFKGIMNIQYVI--ADGNVYVLEVNPRASRTVPIVSKtTGV 851
Cdd:COG3919 233 KLRHYPPAGGNSAAR--ESVDDPE---LEEAARRLLEALGYHGFANVEFKRdpRDGEYKLIEINPRFWRSLYLATA-AGV 306
|
330 340 350
....*....|....*....|....*....|....*...
gi 1215498573 852 PLAQIATKLLLGKSL--VDIVDEKARGLAVMPYAVLKY 887
Cdd:COG3919 307 NFPYLLYDDAVGRPLepVPAYREGVLWRVLPGDLLLRY 344
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
105-329 |
5.39e-15 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 78.99 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 105 AGVLEKYGVRLLGTPIEAIKRGEDREAFRALMHELGEPV-PESE-IVTSVEEAVAFAEQIGFPIIIRPayTLGGTGGGI- 181
Cdd:PRK07178 91 AEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVtPGSEgNLADLDEALAEAERIGYPVMLKA--TSGGGGRGIr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 182 --------AENMEQFLALVEKGLNESPIhqcLIERSVAGFKEIEYEVMRDQSNTCITV----CNMENvdpvgiHTGDSIV 249
Cdd:PRK07178 169 rcnsreelEQNFPRVISEATKAFGSAEV---FLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 250 VAPSQTLTDEEYQMLRSSAVKIISALGIIGGCNIQFALDPNSkQYYLIEVNPRVSRSSALASKATGYPIA----RIAAKL 325
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADG-EVYFMEMNTRVQVEHTITEEITGIDIVreqiRIASGL 318
|
....
gi 1215498573 326 AVGY 329
Cdd:PRK07178 319 PLSY 322
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
55-332 |
8.12e-14 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 75.18 E-value: 8.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 55 MTDEV------HADAVYFEPltvdavEAIIAKERPDGLLATFGGQTGL--NLAFqlheAGVLEKYGVRLLGTPIEAIKRG 126
Cdd:PRK12833 47 MADEAvhigpsHAAKSYLNP------AAILAAARQCGADAIHPGYGFLseNAAF----AEAVEAAGLIFVGPDAQTIRTM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 127 EDREAFRALMHELGEP-VPESE-IVTSVEEAVAFAEQIGFPIIIRPAYTLGGTGGGIAENMEQFLAlvekglnESPIHQ- 203
Cdd:PRK12833 117 GDKARARRTARRAGVPtVPGSDgVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAA-------ELPLAQr 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 204 ----------CLIERSVAGFKEIEYEVMRDQSNtciTVCNMENVDPVGIHTGDSIVVAPSQTLTDEEYQMLRSSAVKIIS 273
Cdd:PRK12833 190 eaqaafgdggVYLERFIARARHIEVQILGDGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLAR 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498573 274 ALGIIGGCNIQFALDPNSKQYYLIEVNPRVSRSSALASKATGYPIARIAAKLAVGYTLA 332
Cdd:PRK12833 267 QVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-328 |
1.47e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 74.63 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 109 EKYGVRLLGTPIEAIKRGEDREAFRALMHELGEPV-PES-EIVTSVEEAVAFAEQIGFPIIIRPAYTLGGTGGGIAENME 186
Cdd:PRK08654 96 EKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVlPGTeEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 187 QFLALVEKGLN-------ESPIHqclIERSVAGFKEIEYEVMRD-QSNTcitvcnmenvdpvgIHTGDS----------- 247
Cdd:PRK08654 176 ELEDAIESTQSiaqsafgDSTVF---IEKYLEKPRHIEIQILADkHGNV--------------IHLGDRecsiqrrhqkl 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 248 IVVAPSQTLTDEEYQMLRSSAVKIISALGIIGGCNIQFALDpnSKQYYLIEVNPRVSRSSALASKATGYPIARIAAKLAV 327
Cdd:PRK08654 239 IEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAA 316
|
.
gi 1215498573 328 G 328
Cdd:PRK08654 317 G 317
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
112-303 |
1.94e-13 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 75.17 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 112 GVRLLGTPIEAIKRGEDREAFRALMHELGEPV-PESEI-VTSVEEAVAFAEQIGFPIIIRPAytLGGTGGG--IAENMEQ 187
Cdd:PRK12999 103 GITFIGPTAEVLRLLGDKVAARNAAIKAGVPViPGSEGpIDDIEEALEFAEEIGYPIMLKAS--AGGGGRGmrIVRSEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 188 FLALVEKGLNE------SPihQCLIERSVAGFKEIEYEVMRDQSNtcitvcnmeNVdpVGIHTGD-SI------VV--AP 252
Cdd:PRK12999 181 LEEAFERAKREakaafgND--EVYLEKYVENPRHIEVQILGDKHG---------NV--VHLYERDcSVqrrhqkVVeiAP 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498573 253 SQTLTDEEYQMLRSSAVKIISALGIIGGCNIQFALDPNSkQYYLIEVNPRV 303
Cdd:PRK12999 248 APGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
652-856 |
3.11e-13 |
|
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: 72.64 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 652 EAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMANNAEElaakaaeigCPVLLRPSYVIGGRGMFIVHSEAQLA 731
Cdd:COG2232 94 ARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPETRFEPPPDP---------GPWLVKPIGGAGGWHIRPADSEAPPA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 732 AlieqgeltyPILIDAYLDGKEAEADIVTDGTDIVLpviiehvekAGVH------SGDS-YAW----LPAqTLTDEEKAK 800
Cdd:COG2232 165 P---------GRYFQRYVEGTPASVLFLADGSDARV---------LGFNrqligpAGERpFRYggniGPL-ALPPALAEE 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498573 801 IIDYAGRIAKKLGFKGIMNIQYVIADGNVYVLEVNPRASRTVPIVSKTTGVPLAQI 856
Cdd:COG2232 226 MRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDA 281
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
105-303 |
2.06e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 70.60 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 105 AGVLEKYGVRLLGTPIEAIKRGEDREAFRALMHELGEP-VPESE-IVTSVEEAVAFAEQIGFPIIIRPayTLGGTGGGI- 181
Cdd:PRK08591 92 AEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPvVPGSDgPVDDEEEALAIAKEIGYPVIIKA--TAGGGGRGMr 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 182 -AENMEQFLALVEKGLNES------PihQCLIERSVAGFKEIEYEVMRDQSNtcitvcnmeNVdpvgIHTGD---SI--- 248
Cdd:PRK08591 170 vVRTEAELEKAFSMARAEAkaafgnP--GVYMEKYLENPRHIEIQVLADGHG---------NA----IHLGErdcSLqrr 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 249 ---VV--APSQTLTDEEYQMLRSSAVKIISALGIIGGCNIQFALDPNsKQYYLIEVNPRV 303
Cdd:PRK08591 235 hqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKN-GEFYFIEMNTRI 293
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
107-331 |
1.40e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 67.85 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 107 VLEKYGVRLLGTPIEAIKRGEDREAFRALMHELGEPV-PESE-IVTSVEEAVAFAEQIGFPIIIRPAYTLGGTGGGIAEN 184
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPViPGSDgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 185 MEQ----FLALVEKGLNESPIHQCLIERSVAGFKEIEYEVMRDQSNTCITV----CNMENvdpvgiHTGDSIVVAPSQTL 256
Cdd:PRK08462 176 ESDlenlYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498573 257 TDEEYQMLRSSAVKIISALGIIGGCNIQFALDPNSKqYYLIEVNPRVSRSSALASKATGYPIARIAAKLAVGYTL 331
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLD-FYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
133-303 |
1.97e-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: 68.57 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 133 RALMHELGEPV-PESEI-VTSVEEAVAFAEQIGFPIIIRPAytLGGTGGG--IAENMEQFLALVEKGLNESP----IHQC 204
Cdd:COG1038 123 RAAAIEAGVPViPGTEGpVDDLEEALAFAEEIGYPVMLKAA--AGGGGRGmrVVRSEEELEEAFESARREAKaafgDDEV 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 205 LIERSVAGFKEIEYEVMRDQSNtcitvcnmeNVdpVGIHTGD-SI------VV--APSQTLTDEEYQMLRSSAVKIISAL 275
Cdd:COG1038 201 FLEKYIERPKHIEVQILGDKHG---------NI--VHLFERDcSVqrrhqkVVeiAPAPNLDEELREAICEAAVKLAKAV 269
|
170 180
....*....|....*....|....*...
gi 1215498573 276 GIIGGCNIQFALDPNsKQYYLIEVNPRV 303
Cdd:COG1038 270 GYVNAGTVEFLVDDD-GNFYFIEVNPRI 296
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
105-332 |
7.78e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 65.50 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 105 AGVLEKYGVRLLGTPIEAIKRGEDREAFRALMHELGEP-VPESE-IVTSVEEAVAFAEQIGFPIIIRPAYTLGGTGGGIA 182
Cdd:PRK05586 92 AKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPvVPGSEgEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 183 ENMEQFLALVEKGLNESPIH----QCLIERSVAGFKEIEYEVMRDqsntcitvcNMENVdpvgIHTGDS----------- 247
Cdd:PRK05586 172 RSEEELIKAFNTAKSEAKAAfgddSMYIEKFIENPKHIEFQILGD---------NYGNV----VHLGERdcslqrrnqkv 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 248 IVVAPSQTLTDEEYQMLRSSAVKIISALGIIGGCNIQFALDPNSkQYYLIEVNPRVSRSSALASKATGYPIARIAAKLAV 327
Cdd:PRK05586 239 LEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDG-NFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAY 317
|
....*
gi 1215498573 328 GYTLA 332
Cdd:PRK05586 318 GEKLS 322
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
109-334 |
1.16e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 65.05 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 109 EKYGVRLLGTPIEAIKRGEDREAFRALMHELGEP-VP-ESEIVTSVEEAVAFAEQIGFPIIIRPAYTLGGTGGGIAENME 186
Cdd:PRK06111 96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPvVPgITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 187 QFLALVEkgLNESPIHQCL------IERSVAGFKEIEYEVMRDQSNTCITVCNMEnvdpVGIHTGDSIVV--APSQTLTD 258
Cdd:PRK06111 176 ELTKAFE--SNKKRAANFFgngemyIEKYIEDPRHIEIQLLADTHGNTVYLWERE----CSVQRRHQKVIeeAPSPFLDE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 259 EEYQMLRSSAVKIISALGIIGGCNIQFALDpNSKQYYLIEVNPRVSRSSALASKATGYPIA----RIAAKLAVGYTLAEL 334
Cdd:PRK06111 250 ETRKAMGERAVQAAKAIGYTNAGTIEFLVD-EQKNFYFLEMNTRLQVEHPVTEEITGIDLVeqqlRIAAGEKLSFTQDDI 328
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
30-313 |
3.20e-10 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 62.98 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 30 GTQACIALKEE--GYRVILVNNNP-ATIMTDevhADAVYF-----EPLTVDAVEAIIAKERPDGLLATFggQTGLNLAFQ 101
Cdd:PRK12767 12 RVQLVKALKKSllKGRVIGADISElAPALYF---ADKFYVvpkvtDPNYIDRLLDICKKEKIDLLIPLI--DPELPLLAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 102 LHEAgvLEKYGVRLLGTPIEAIKRGEDREAFRALMHELGEPVPESEIVTSVE--EAVAFAEQIGFPIIIRPAYTLGGTGG 179
Cdd:PRK12767 87 NRDR--FEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEdfKAALAKGELQFPLFVKPRDGSASIGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 180 GIAENMEQFLALVEKGLNesPIHQCLIErsvagfkEIEY--EVMRDQSNTCITVCNMENVDPVGIHTGDSIVVapsqtlt 257
Cdd:PRK12767 165 FKVNDKEELEFLLEYVPN--LIIQEFIE-------GQEYtvDVLCDLNGEVISIVPRKRIEVRAGETSKGVTV------- 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498573 258 deEYQMLRSSAVKIISALGIIGGCNIQFALDPNskQYYLIEVNPRVSRSSALASKA 313
Cdd:PRK12767 229 --KDPELFKLAERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFGGGYPLSYMA 280
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
677-861 |
3.52e-10 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 60.79 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 677 LLEELDIPHVPGLM-------ANNAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVHSEAQL-AALIEQGELTYPILIDAY 748
Cdd:pfam07478 1 LLKAAGLPVVPFVTftradwkLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELqAAIEEAFQYDEKVLVEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 749 LDGKEAEADIVTDGTDIVLPViIEHVEKAGVH-------SGDSYAWLPAQtLTDEEKAKIIDYAGRIAKKLGFKGIMNIQ 821
Cdd:pfam07478 81 IEGREIECAVLGNEDPEVSPV-GEIVPSGGFYdyeakyiDDSAQIVVPAD-LEEEQEEQIQELALKAYKALGCRGLARVD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1215498573 822 -YVIADGNVYVLEVNPRASRT----VPIVSKTTGVPLAQIATKLL 861
Cdd:pfam07478 159 fFLTEDGEIVLNEVNTIPGFTsismFPKLAAAAGVSFPDLVDQLI 203
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
108-326 |
6.90e-10 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 61.50 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 108 LEKYGVRLLGTPiEAIKRGEDREAFRALMHELGEPVPESEIVTSVEEAVAFAEQIGFPIIIRPAYTLGGTGGGIAENMEQ 187
Cdd:COG0189 77 LEAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 188 FLALVEKgLNESPIHQCLIERSVAGFKEIEY--EVMRDQSNTCITVCNMENVDPVGIHTGDSIVVAPsqtLTDEEYQMlr 265
Cdd:COG0189 156 LESILEA-LTELGSEPVLVQEFIPEEDGRDIrvLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVE---LTDEEREL-- 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498573 266 ssAVKIISALGI-IGGcnIQFALDPNskQYYLIEVNPrvsrSSALA--SKATGYPIA-RIAAKLA 326
Cdd:COG0189 230 --ALRAAPALGLdFAG--VDLIEDDD--GPLVLEVNV----TPGFRglERATGVDIAeAIADYLE 284
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
670-854 |
8.13e-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: 61.28 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 670 DRDRFYQLLEELDIPHVPGLMAN--NAEELAAKAAEIGCPVLLRPSYviGG--RGMFIVHSEAQLAALIEQgELTY--PI 743
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKPAR--EGssVGVSKVKNAEELAAALEE-AFKYddKV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 744 LIDAYLDGKEAEADIVTDGTDIVLPViIEHVEKAGV-------HSGDSYAWLPAQtLTDEEKAKIIDYAGRIAKKLGFKG 816
Cdd:COG1181 172 LVEEFIDGREVTVGVLGNGGPRALPP-IEIVPENGFydyeakyTDGGTEYICPAR-LPEELEERIQELALKAFRALGCRG 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1215498573 817 ------IMNiqyviADGNVYVLEVNprasrTVPIVSKTTGVPLA 854
Cdd:COG1181 250 yarvdfRLD-----EDGEPYLLEVN-----TLPGMTPTSLLPKA 283
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
105-323 |
4.58e-09 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 60.21 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 105 AGVLEKYGVRLLGTPIEAIKRGEDREAFRALMHELGEP-VPESEIVT--SVEEAVAFAEQIGFPIIIRPAYtlGGTGGGI 181
Cdd:PRK08463 91 AKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPiVPGTEKLNseSMEEIKIFARKIGYPVILKASG--GGGGRGI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 182 -----AENMEQ-FLALVEKGLNESPIHQCLIERSVAGFKEIEYEVMRDQSNTCITVCnmENVDPVGIHTGDSIVVAPSQT 255
Cdd:PRK08463 169 rvvhkEEDLENaFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLC--ERDCSIQRRHQKVIEIAPCPS 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498573 256 LTDEEYQMLRSSAVKIISALGIIGGCNIQFALDPNSKqYYLIEVNPRVSRSSALASKATGYPIA----RIAA 323
Cdd:PRK08463 247 ISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNR-FYFMEMNTRIQVEHGVTEEITGIDLIvrqiRIAA 317
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
651-866 |
5.77e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 59.73 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 651 EEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMA--NNAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVHSEA 728
Cdd:PRK05586 96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGeiENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 729 QlaalieqgeltypiLIDAYLDGK-EAEADIVTDgtDIVLPVIIE---HVE------KAG--VHSGDSYAWL-------- 788
Cdd:PRK05586 176 E--------------LIKAFNTAKsEAKAAFGDD--SMYIEKFIEnpkHIEfqilgdNYGnvVHLGERDCSLqrrnqkvl 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 789 ---PAQTLTDEEKAKIIDYAGRIAKKLGFKGIMNIQYVI-ADGNVYVLEVNPRASRTVPIVSKTTGVPLAQIATKLLLGK 864
Cdd:PRK05586 240 eeaPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
..
gi 1215498573 865 SL 866
Cdd:PRK05586 320 KL 321
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
557-866 |
7.91e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 59.27 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 557 KVLIIGAGPI--RIgqgiefdyssvhsVFALQKEGYETVMINNNPETVSTDFAVADRLYF--EPLTLESVLDVieaEQIK 632
Cdd:PRK06111 4 KVLIANRGEIavRI-------------IRTCQKLGIRTVAIYSEADRDALHVKMADEAYLigGPRVQESYLNL---EKII 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 633 HVIVQFGGQtAINLVKGL-----------EEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMAN--NAEELAA 699
Cdd:PRK06111 68 EIAKKTGAE-AIHPGYGLlsenasfaercKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNleDAEEAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 700 KAAEIGCPVLLRPSYVIGGRGMFIVHSEAQLAALIEqgeltypilidayLDGKEAeADIVTDGTdIVLPVIIE---HVE- 775
Cdd:PRK06111 147 IARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFE-------------SNKKRA-ANFFGNGE-MYIEKYIEdprHIEi 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 776 --KAGVHSGDSYAW----------------LPAQTLTDEEKAKIIDYAGRIAKKLGFKGIMNIQYVIADG-NVYVLEVNP 836
Cdd:PRK06111 212 qlLADTHGNTVYLWerecsvqrrhqkvieeAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQkNFYFLEMNT 291
|
330 340 350
....*....|....*....|....*....|
gi 1215498573 837 RASRTVPIVSKTTGVPLAQIATKLLLGKSL 866
Cdd:PRK06111 292 RLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
575-836 |
7.97e-09 |
|
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: 58.03 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 575 DYSSVHSVFALQKEGYETVMINnnpetvstdfavADRLYFEPLTLESVLDVIEAEQIKHVIVQFGG-QTAINLVKGLEEA 653
Cdd:COG0189 13 KDSTKALIEAAQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPRIDPpFYGLALLRQLEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 654 GVPLLGvTYDMIDQLEDRDRFYQLLEELDIPHVPGLMANNAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVHSEAQLAAL 733
Cdd:COG0189 81 GVPVVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 734 IEQGELTY--PILIDAYLDgKEAEADI---VTDGTdiVLPVII----EHVEKAGVHSGDSYAwlpAQTLTDEEkakiIDY 804
Cdd:COG0189 160 LEALTELGsePVLVQEFIP-EEDGRDIrvlVVGGE--PVAAIRripaEGEFRTNLARGGRAE---PVELTDEE----REL 229
|
250 260 270
....*....|....*....|....*....|....*..
gi 1215498573 805 AGRIAKKLGfkgimnIQYV-----IADGNVYVLEVNP 836
Cdd:COG0189 230 ALRAAPALG------LDFAgvdliEDDDGPLVLEVNV 260
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
669-837 |
9.56e-09 |
|
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: 55.47 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 669 EDRDRFYQLLEELDIPhVPglmannAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVHSEAQLAALIEqgeltyPILIDAY 748
Cdd:pfam02655 2 SDKLKTYKALKNAGVP-TP------ETLQAEELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIE------NVLVQEF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 749 LDGKEAEADIVTDGTDiVLPV-----IIEHVEKAGVHSGDSyawLPAQTltdEEKAKIIDYAGRIAKKL-GFKGIMNIQY 822
Cdd:pfam02655 69 IEGEPLSVSLLSDGEK-ALPLsvnrqYIDNGGSGFVYAGNV---TPSRT---ELKEEIIELAEEVVECLpGLRGYVGVDL 141
|
170
....*....|....*
gi 1215498573 823 VIADGNVYVLEVNPR 837
Cdd:pfam02655 142 VLKDNEPYVIEVNPR 156
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
791-871 |
1.09e-08 |
|
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: 54.54 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 791 QTLTDEEKAkiIDYAGRIAKKLGFKGIMNIQYVIADGNVYVLEVNPRASRTVPIvSKTTGVPLAQIATKLLLGKSLVDIV 870
Cdd:pfam15632 41 QTLEDDPEL--IEAARRLAEAFGLDGLFNVQFRYDGDGPKLLEINPRMSGGIGY-SCLAGVNLPYLALKLLLGLETPDPV 117
|
.
gi 1215498573 871 D 871
Cdd:pfam15632 118 E 118
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
651-837 |
4.16e-08 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 57.46 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 651 EEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPG--LMANNAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVHSEA 728
Cdd:PRK12999 100 AEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 729 QLAalieqgeltypiliDAYLDGK-EAEADIvtdGTDIVlpviieHVEKAGVHS--------GDSYAWL----------- 788
Cdd:PRK12999 180 ELE--------------EAFERAKrEAKAAF---GNDEV------YLEKYVENPrhievqilGDKHGNVvhlyerdcsvq 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 789 ----------PAQTLTDEEKAKIIDYAGRIAKKLGFKGIMNIQY-VIADGNVYVLEVNPR 837
Cdd:PRK12999 237 rrhqkvveiaPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFlVDADGNFYFIEVNPR 296
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
21-336 |
2.24e-07 |
|
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: 53.96 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 21 GQAAEFD---YSGTQACIALKEEGYRVILVNNNPATIMTDEVHADavyfepltVDAVeaiiakerpdgLLATFGGQtGLN 97
Cdd:COG1181 9 GRSAEREvslKSGRAVAAALDKAGYDVVPIGIDVEDLPAALKELK--------PDVV-----------FPALHGRG-GED 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 98 LAFQlheaGVLEKYGVRLLGTPIEAIKRGEDREAFRALMHELGEPVPESEIVTSVEEAV--AFAEQIGFPIIIRPAytLG 175
Cdd:COG1181 69 GTIQ----GLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADleAIEEELGLPLFVKPA--RE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 176 GTGGGI--AENMEQFLALVEKGLNESpiHQCLIERSVAGfKEIEYEVMRDQSNTCITVcnMENVDPVGI-------HTGD 246
Cdd:COG1181 143 GSSVGVskVKNAEELAAALEEAFKYD--DKVLVEEFIDG-REVTVGVLGNGGPRALPP--IEIVPENGFydyeakyTDGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 247 SIVVAPSQtLTDEEYQMLRSSAVKIISALGIIGGCNIQFALDPNsKQYYLIEVN--PRVSRSSalaskatGYPIAriAAk 324
Cdd:COG1181 218 TEYICPAR-LPEELEERIQELALKAFRALGCRGYARVDFRLDED-GEPYLLEVNtlPGMTPTS-------LLPKA--AA- 285
|
330
....*....|..
gi 1215498573 325 lAVGYTLAELVN 336
Cdd:COG1181 286 -AAGISYEELIE 296
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
651-879 |
5.16e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 53.57 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 651 EEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMAN--NAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVHSEA 728
Cdd:PRK07178 95 AERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNlaDLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSRE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 729 QLaalieqgELTYPILIdayldgKEAE-----ADIVTDGTdIVLPVIIEhVEKAGVHSGDSYAWL--------------- 788
Cdd:PRK07178 175 EL-------EQNFPRVI------SEATkafgsAEVFLEKC-IVNPKHIE-VQILADSHGNVVHLFerdcsiqrrnqklie 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 789 --PAQTLTDEEKAKIIDYAGRIAKKLGFKGIMNIQYVI-ADGNVYVLEVNPRASRTVPIVSKTTGVPLAQIATKLLLGKS 865
Cdd:PRK07178 240 iaPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
250
....*....|....*
gi 1215498573 866 L-VDIVDEKARGLAV 879
Cdd:PRK07178 320 LsYKQEDIQHRGFAL 334
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
651-855 |
7.48e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 52.83 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 651 EEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGL--MANNAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVHSEA 728
Cdd:PRK12833 99 EAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSdgVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 729 QLAAL--IEQGELTypiliDAYLDG-----------KEAEADIVTDGTDIVlpviieHV---------------EKAgvh 780
Cdd:PRK12833 179 QLAAElpLAQREAQ-----AAFGDGgvylerfiaraRHIEVQILGDGERVV------HLferecslqrrrqkilEEA--- 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498573 781 sgdsyawlPAQTLTDEEKAKIIDYAGRIAKKLGFKGIMNIQYVIAD--GNVYVLEVNPRASRTVPIVSKTTGVPLAQ 855
Cdd:PRK12833 245 --------PSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQVEHPVTEAITGIDLVQ 313
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
108-326 |
1.09e-06 |
|
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: 51.58 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 108 LEKYGVRLLGTPIeAIKRGEDREAFRALMHELGEPVPESEIVTSVEEAVAFAEQIGFPIIIRPAYTLGGTGGGIAENMEQ 187
Cdd:TIGR00768 69 LESLGVPVINSSD-AILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 188 FLALVE--KGLNESPIH---QCLIERSvaGFKEIEYEVMRDQSNTCITVCNMENVDpVGIHTGDSIVVAPsqtLTDEEYQ 262
Cdd:TIGR00768 148 AESLLEhfEQLNGPQNLflvQEYIKKP--GGRDIRVFVVGDEVVAAIYRITSGHWR-SNLARGGKAEPCS---LTEEIEE 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498573 263 MlrssAVKIISALGiIGGCNIQFALDPNSkqYYLIEVNPRVSRSSalASKATGYPIARIAAKLA 326
Cdd:TIGR00768 222 L----AIKAAKALG-LDVAGVDLLESEDG--LLVNEVNANPEFKN--SVKTTGVNIAGKLLDYI 276
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
128-170 |
1.32e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 52.47 E-value: 1.32e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1215498573 128 DREAFRALMHELGEPVPESEIVTSVEEAVAFAEQIGFPIIIRP 170
Cdd:PRK14016 214 DKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKP 256
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
670-843 |
1.38e-06 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 51.27 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 670 DRDRFYQLLEELDIPHVPGLMANNAEELAAKAAEIGCPVLLRP----SYViggrGMFIVHSEAQLAALIEQgELTYP--I 743
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKParegSSV----GVSKVKEEDELQAALEL-AFKYDdeV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 744 LIDAYLDGKEAEADIVtDGTdiVLPVI-IEHVEK-----AGVHSGDSYAWLPAQtLTDEEKAKIIDYAGRIAKKLGFKGI 817
Cdd:PRK01372 173 LVEKYIKGRELTVAVL-GGK--ALPVIeIVPAGEfydyeAKYLAGGTQYICPAG-LPAEIEAELQELALKAYRALGCRGW 248
|
170 180
....*....|....*....|....*..
gi 1215498573 818 MNIQYVI-ADGNVYVLEVNprasrTVP 843
Cdd:PRK01372 249 GRVDFMLdEDGKPYLLEVN-----TQP 270
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
704-874 |
1.69e-06 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 50.98 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 704 IGCPVLLRPSYVIGGRGMFIVHSEAQLA-ALIEQGELTYPILIDAYLDGKEAEADIV-TDGTDIVLPVIIEHVEK----- 776
Cdd:PRK14571 124 LGYPCVVKPRREGSSIGVFICESDEEFQhALKEDLPRYGSVIVQEYIPGREMTVSILeTEKGFEVLPILELRPKRrfydy 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 777 -AGVHSGDSYAWLPAQtLTDEEKAKIIDYAGRIAKKLGFKGIMNIQYVIADGNVYVLEVNprasrTVPIVSKTTGVPLAQ 855
Cdd:PRK14571 204 vAKYTKGETEFILPAP-LNPEEERLVKETALKAFVEAGCRGFGRVDGIFSDGRFYFLEIN-----TVPGLTELSDLPASA 277
|
170
....*....|....*....
gi 1215498573 856 IATKLLLgKSLVDIVDEKA 874
Cdd:PRK14571 278 KAGGIEF-EELVDIIIKSA 295
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
648-879 |
3.54e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 50.75 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 648 KGLEEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMA--NNAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVH 725
Cdd:PRK08654 93 KACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEgiEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVY 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 726 SEAQLAALIEQ---------GELTypILIDAYLDG-KEAEADIVTDGTDIVlpviiehvekagVHSGDSYAWL------- 788
Cdd:PRK08654 173 SEEELEDAIEStqsiaqsafGDST--VFIEKYLEKpRHIEIQILADKHGNV------------IHLGDRECSIqrrhqkl 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 789 ----PAQTLTDEEKAKIIDYAGRIAKKLGFKGIMNIQYVIADGNVYVLEVNPRASRTVPIVSKTTGVPLAQIATKLLLGK 864
Cdd:PRK08654 239 ieeaPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGE 318
|
250
....*....|....*.
gi 1215498573 865 SL-VDIVDEKARGLAV 879
Cdd:PRK08654 319 ELsFKQEDITIRGHAI 334
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
54-315 |
8.69e-06 |
|
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: 49.15 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 54 IMTDEVHADAVYFEPltvdAVEAIIAKERPDGLLATfggqTGLNlafqlHEAGVLE--KYGVRLLGTPIEAIKRGEDREA 131
Cdd:COG2232 49 LDAESCGFDLEDLPA----ALLELAAADDPDGLVYG----SGFE-----NFPELLErlARRLPLLGNPPEVVRRVKDPLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 132 FRALMHELGEPVPEseivTSVEeavafAEQIGFPIIIRPAYTLGGTGGGIAENMeqflALVEKGlnespihqCLIERSVA 211
Cdd:COG2232 116 FFALLDELGIPHPE----TRFE-----PPPDPGPWLVKPIGGAGGWHIRPADSE----APPAPG--------RYFQRYVE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 212 GfkeieyevmRDQSNTCItvCNMENVDPVGIH---TGDSI--------VVAPsQTLTDEEYQMLRSSAVKIISALGIIGG 280
Cdd:COG2232 175 G---------TPASVLFL--ADGSDARVLGFNrqlIGPAGerpfryggNIGP-LALPPALAEEMRAIAEALVAALGLVGL 242
|
250 260 270
....*....|....*....|....*....|....*
gi 1215498573 281 CNIQFALDPNskQYYLIEVNPRVSRSSALASKATG 315
Cdd:COG2232 243 NGVDFILDGD--GPYVLEVNPRPQASLDLYEDATG 275
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
651-837 |
1.22e-05 |
|
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: 49.69 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 651 EEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGLMA--NNAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVHSEA 728
Cdd:COG1038 99 EEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGpvDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 729 QLAalieqgeltypiliDAYLDGK-EAEADIvtdGTDIvlpVIIE-------HVE------KAG--VHsgdsyawL---- 788
Cdd:COG1038 179 ELE--------------EAFESARrEAKAAF---GDDE---VFLEkyierpkHIEvqilgdKHGniVH-------Lferd 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498573 789 --------------PAQTLTDEEKAKIIDYAGRIAKKLGFKGIMNIQY-VIADGNVYVLEVNPR 837
Cdd:COG1038 232 csvqrrhqkvveiaPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFlVDDDGNFYFIEVNPR 295
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
128-300 |
1.27e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 48.18 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 128 DREAFRALMHELGEPVPESEIVTSVEEAVAFAEQIGFPIIIRPAytLGGTGGG--IAENMEQFLALVEKGLNESPihQCL 205
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPA--REGSSVGvsKVKEEDELQAALELAFKYDD--EVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 206 IERSVAGfkeIEYevmrdqsnTCiTVCNMENVDPVGI-------------HTGDSIVVAPSQtLTDEEYQMLRSSAVKII 272
Cdd:PRK01372 174 VEKYIKG---REL--------TV-AVLGGKALPVIEIvpagefydyeakyLAGGTQYICPAG-LPAEIEAELQELALKAY 240
|
170 180
....*....|....*....|....*...
gi 1215498573 273 SALGIIGGCNIQFALDpNSKQYYLIEVN 300
Cdd:PRK01372 241 RALGCRGWGRVDFMLD-EDGKPYLLEVN 267
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
707-924 |
1.31e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 49.46 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 707 PVLLRPSYVIGGRGMFIVHSEAQLAALIE--QGELTYPILIDAYLDGKEAEADIVTDGTDI-VLPVIIEHVEKAG--VHS 781
Cdd:PRK02186 144 PVVVKPRMGSGSVGVRLCASVAEAAAHCAalRRAGTRAALVQAYVEGDEYSVETLTVARGHqVLGITRKHLGPPPhfVEI 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 782 GDSYawlPAQtLTDEEKAKIIDYAGRIAKKLGFK-GIMNIQYVIADGNVYVLEVNPR-ASRTVPI-VSKTTGVPLAQIAT 858
Cdd:PRK02186 224 GHDF---PAP-LSAPQRERIVRTVLRALDAVGYAfGPAHTELRVRGDTVVIIEINPRlAGGMIPVlLEEAFGVDLLDHVI 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498573 859 KLLLGKSlvDIVDEKARGLAVMPYAV------LKYPVFSTHKLPGVDPVVGPEMKSTGEGISIAAT-KEEAAY 924
Cdd:PRK02186 300 DLHLGVA--AFADPTAKRYGAIRFVLparsgvLRGLLFLPDDIAARPELRFHPLKQPGDALRLEGDfRDRIAA 370
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
650-856 |
3.29e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 47.49 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 650 LEEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPG---LMANnAEELAAKAAEIGCPVLLRPSYVIGGRGMFIVHS 726
Cdd:PRK08591 95 CEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGsdgPVDD-EEEALAIAKEIGYPVIIKATAGGGGRGMRVVRT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 727 EAQLAALIEQGEltypilidayldgKEAEADIVTDGtdivlpVIIE-------HVE------KAG--VHSGDSYAWL--- 788
Cdd:PRK08591 174 EAELEKAFSMAR-------------AEAKAAFGNPG------VYMEkylenprHIEiqvladGHGnaIHLGERDCSLqrr 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498573 789 --------PAQTLTDEEKAKIIDYAGRIAKKLGFKGIMNIQYVI-ADGNVYVLEVNPRASRTVPIVSKTTGVPL--AQI 856
Cdd:PRK08591 235 hqkvleeaPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYeKNGEFYFIEMNTRIQVEHPVTEMITGVDLvkEQI 313
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
135-301 |
9.67e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 44.61 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 135 LMHELGEPVPESEIVTS-------VEEAVAFAEQIGFPIIIRPAytLGGTGGGI--AENMEQFLALVEKGLNESpiHQCL 205
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTRadwklnpKEWCAQVEEALGYPVFVKPA--RLGSSVGVskVESREELQAAIEEAFQYD--EKVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 206 IERSVAGfKEIEYEVMRDQSNTCITVcnMENVDPVGIH-------TGDSIVVAPSQtLTDEEYQMLRSSAVKIISALGII 278
Cdd:pfam07478 77 VEEGIEG-REIECAVLGNEDPEVSPV--GEIVPSGGFYdyeakyiDDSAQIVVPAD-LEEEQEEQIQELALKAYKALGCR 152
|
170 180
....*....|....*....|...
gi 1215498573 279 GGCNIQFALDPnSKQYYLIEVNP 301
Cdd:pfam07478 153 GLARVDFFLTE-DGEIVLNEVNT 174
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
671-837 |
1.00e-04 |
|
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: 45.84 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 671 RDRFYQ--LLEELDIPHVPGLMANNAEELAAKAAEIGCPVLLRPS---YviGGRGMFIVHSEAQLAALIEQGELTyPILI 745
Cdd:COG0026 88 QDRLLEkaFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggY--DGKGQVVIKSAADLEAAWAALGGG-PCIL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 746 DAYLD-GKEAEAdIVT---DGTDIVLPVIiEHVEKAGV-HSgdSYAwlPAQtLTDEEKAKIIDYAGRIAKKLGFKGIMNI 820
Cdd:COG0026 165 EEFVPfERELSV-IVArspDGEVATYPVV-ENVHRNGIlDE--SIA--PAR-ISEALAAEAEEIAKRIAEALDYVGVLAV 237
|
170
....*....|....*...
gi 1215498573 821 Q-YVIADGNVYVLEVNPR 837
Cdd:COG0026 238 EfFVTKDGELLVNEIAPR 255
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
133-165 |
2.45e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 45.12 E-value: 2.45e-04
10 20 30
....*....|....*....|....*....|...
gi 1215498573 133 RALMHELGEPVPESEIVTSVEEAVAFAEQIGFP 165
Cdd:COG1042 494 KALLAAYGIPVVPTRLARSAEEAVAAAEEIGYP 526
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
134-300 |
2.69e-04 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 43.26 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 134 ALMHELGEPVPESEIVTSVEEAVAFAEQIG--FPIIIRPAYTLGGTGGGIAENmEQFLALVEKGLNESPIHQCLIERsvA 211
Cdd:pfam08443 9 QLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrqFPVIVKSIYGSQGIGVFLAED-EQKLRQTLSATNEQILVQEFIAE--A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 212 GFKEIEYEVMRDQsntciTVCNMENVDPVG-----IHTGDsivVAPSQTLTDEEYQMlrssAVKIISALGI-IGGCNIQf 285
Cdd:pfam08443 86 NNEDIRCLVVGDQ-----VVGALHRQSNEGdfrsnLHRGG---VGEKYQLSQEETEL----AIKAAQAMQLdVAGVDLL- 152
|
170
....*....|....*
gi 1215498573 286 aldPNSKQYYLIEVN 300
Cdd:pfam08443 153 ---RQKRGLLVCEVN 164
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
648-879 |
3.12e-04 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 44.42 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 648 KGLEEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPG---LMANNAEELAAKAAEIGCPVLLRPSYVIGGRGMFIV 724
Cdd:PRK08463 92 KAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGtekLNSESMEEIKIFARKIGYPVILKASGGGGGRGIRVV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 725 HSEAQLAALIEQGEltypilidayldgKEAEADIVTDgtDIVLPVIIE---HVEKAGVhsGDSYAWL------------- 788
Cdd:PRK08463 172 HKEEDLENAFESCK-------------REALAYFNND--EVFMEKYVVnprHIEFQIL--GDNYGNIihlcerdcsiqrr 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 789 --------PAQTLTDEEKAKIIDYAGRIAKKLGFKGIMNIQYVIADGN-VYVLEVNPRASRTVPIVSKTTGVPLAQIATK 859
Cdd:PRK08463 235 hqkvieiaPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNrFYFMEMNTRIQVEHGVTEEITGIDLIVRQIR 314
|
250 260
....*....|....*....|.
gi 1215498573 860 LLLGKSL-VDIVDEKARGLAV 879
Cdd:PRK08463 315 IAAGEILdLEQSDIKPRGFAI 335
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
671-837 |
3.81e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.99 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 671 RDRFYQ--LLEELDIPHVPGLMANNAEELAAKAAEIGCPVLL---RPSYviGGRGMFIVHSEAQLAALIEQGELTyPILI 745
Cdd:PRK06019 99 QDRLTEkqFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLktrRGGY--DGKGQWVIRSAEDLEAAWALLGSV-PCIL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 746 DAYLDgKEAEADIV----TDGTDIVLPViIEHVEKAGV-HSgdSYAwlPAQtLTDEEKAKIIDYAGRIAKKLGFKGIMNI 820
Cdd:PRK06019 176 EEFVP-FEREVSVIvargRDGEVVFYPL-VENVHRNGIlRT--SIA--PAR-ISAELQAQAEEIASRIAEELDYVGVLAV 248
|
170
....*....|....*...
gi 1215498573 821 Q-YVIADGNVYVLEVNPR 837
Cdd:PRK06019 249 EfFVTGDGELLVNEIAPR 266
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
119-279 |
6.37e-04 |
|
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: 43.14 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 119 PIEAIKRGEDREAFRALMHELGEPVPESEIVTSVEEAVAFAEQIGFPIIIRPAyTLG--GTGGGIAENMEQFLALVEkGL 196
Cdd:COG0026 80 GPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTR-RGGydGKGQVVIKSAADLEAAWA-AL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 197 NESPihqCLIErsvaGFKEIEYE----VMRDQSNTCIT--VCNMENVDpvGI-HTgdsiVVAPSQtLTDEEYQMLRSSAV 269
Cdd:COG0026 158 GGGP---CILE----EFVPFERElsviVARSPDGEVATypVVENVHRN--GIlDE----SIAPAR-ISEALAAEAEEIAK 223
|
170
....*....|
gi 1215498573 270 KIISALGIIG 279
Cdd:COG0026 224 RIAEALDYVG 233
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
645-879 |
1.25e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 42.42 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 645 NLVKGLEEAGVPLLGVTYDMIDQLEDRDRFYQLLEELDIPHVPGL--MANNAEELAAKAAEIGCPVLLRPSYVIGGRGMF 722
Cdd:PRK08462 92 NFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 723 IVHSEAQlaalieqgeltypiLIDAYLdGKEAEA-DIVTDGTdIVLPVIIE---HVE------KAG--VHSGDSYAWL-- 788
Cdd:PRK08462 172 VVEDESD--------------LENLYL-AAESEAlSAFGDGT-MYMEKFINnprHIEvqilgdKHGnvIHVGERDCSLqr 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 789 ---------PAQTLTDEEKAKIIDYAGRIAKKLGFKGIMNIQYVI-ADGNVYVLEVNPRASRTVPIVSKTTGVPLAQIAT 858
Cdd:PRK08462 236 rhqklieesPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMI 315
|
250 260
....*....|....*....|.
gi 1215498573 859 KLLLGKSLVDIVDEKARGLAV 879
Cdd:PRK08462 316 KIAEGEELPSQESIKLKGHAI 336
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
133-270 |
1.55e-03 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 40.73 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 133 RALMHELGEPVPESEIVTSVEEAVAFAEQIGFPII-IRPAYTLGGTGGGIAENMEQFLALV----EKGLNESPIHQCLIE 207
Cdd:pfam01071 7 KDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIvVKADGLAAGKGVIVASSNEEAIKAVdeilEQKKFGEAGETVVIE 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498573 208 RSVAGFkeieyEVmrdqsnTCITVCNMENVDPV--------------GIHTGDSIVVAPSQTLTDEEYQMLRSSAVK 270
Cdd:pfam01071 87 EFLEGE-----EV------SVLAFVDGKTVKPLppaqdhkragegdtGPNTGGMGAYSPAPVITPELLERIKETIVE 152
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
130-166 |
3.17e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 40.15 E-value: 3.17e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1215498573 130 EAFRALMHeLGEPVPESEIVTSVEEAVAFAEQIGFPI 166
Cdd:pfam13549 14 EAKALLAA-YGIPVVPTRLARSPEEAVAAAEEIGYPV 49
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
138-303 |
5.59e-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: 38.77 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 138 ELGEPVPESEIVTSVEEAVAFAEQIGFPIIIRpAYTLGGTGGGI-----AENMEQFLALVEKGlnespihQCLIErsvaG 212
Cdd:pfam02222 2 KLGLPTPRFMAAESLEELIEAGQELGYPCVVK-ARRGGYDGKGQyvvrsEADLPQAWEELGDG-------PVIVE----E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 213 FKEIEYEVmrdqsnTCITVCNMENV----DPVGIHTGDSI---VVAP---SQTLTDEEYQMLRssavKIISALGIIGGCN 282
Cdd:pfam02222 70 FVPFDREL------SVLVVRSVDGEtafyPVVETIQEDGIcrlSVAParvPQAIQAEAQDIAK----RLVDELGGVGVFG 139
|
170 180
....*....|....*....|.
gi 1215498573 283 IQFALDPNSkQYYLIEVNPRV 303
Cdd:pfam02222 140 VELFVTEDG-DLLINELAPRP 159
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
704-837 |
7.65e-03 |
|
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: 38.42 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498573 704 IGCPVLLRPSYVIGGRGMFIVHSEAQLAALIEQGE-------LTYP--------ILIDAYLDGKE--AEADIVTDGTdiv 766
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIReeieqwkEMYPeavvdggsFLVEEYIEGEEfaVDAYFDENGE--- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498573 767 lPVIIEHVEKAGVHSGDS----YaWLPAQtLTDEEKAKIIDYAGRIAKKLGFK-GIMNIQY-VIADGNVYVLEVNPR 837
Cdd:pfam13535 78 -PVILNILKHDFASSEDVsdriY-VTSAS-IIRETQAAFTEFLKRINALLGLKnFPVHIELrVDEDGQIIPIEVNPL 151
|
|
| |
