|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1091 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1971.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 1 MPKRTDIRSILVIGSGPIVIGQACEFDYSGTQACRVLRAEGYRVILVNSNPATIMTDPEFADATYVEPITPGIVEQIIAR 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 81 ERPDALLPTLGGQTALNTAVALHEAGVLERYGVELVGADIAAIQAGENREQFKGIVARvadrygLNAESARSAICHTLAE 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKK------IGLPVPRSGIAHSMEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 161 CLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQLRRIAGAGLDASPTSEVLLEESILGWKEYELEVMRDRADNVVIVCSI 240
Cdd:PRK05294 155 ALEVAEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 241 ENIDPMGVHTGDSVTVAPAMTLTDREYQNMRDVAIAVIREVGVDTGGCNIQFAVDPRTGRMIVIEMNPRVSRSSALASKA 320
Cdd:PRK05294 235 ENIDPMGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 321 TGFPIAKIAAKLAVGYTLDEIPNDITRETPASFEPSLDYVVVKVPRFAFEKFAGADQTLTTHMKSVGEAMAIGRSFPEAL 400
Cdd:PRK05294 315 TGYPIAKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 401 QKALRSLEKKGASF-AWAGDPGDRAELLAACRTPHDGRLRAMMQALRAGATVEELYEATSVDPWFLDQLL-LIDEEARAV 478
Cdd:PRK05294 395 QKALRSLEIGVTGLdEDLFEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEeIVELEEELK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 479 GAADTLTAGVLTRAKRHGFSDAQIAEIRGLPEERVRELRHELGVRPVYNTVDTCAAEFAARTPYLYSTYDEETEVPPGDR 558
Cdd:PRK05294 475 ENGLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 559 RKVIILGSGPNRIGQGIEFDYACVHASFELSAAGYETVMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVVRAEQESgpv 638
Cdd:PRK05294 555 KKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPK--- 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 639 aGVIVQLGGQTPLGLAQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLPAPKHGTAVTVEQAREIAAEIGYPVLVR 718
Cdd:PRK05294 632 -GVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVR 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 719 PSYVLGGAGMAIVYDEETLGAYMARAGAAS-DHPVLVDRFLDEAIEIDVDALYDGEELYLGGVMEHIEEAGIHSGDSACA 797
Cdd:PRK05294 711 PSYVLGGRAMEIVYDEEELERYMREAVKVSpDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACS 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 798 LPPITLGGFDIKRIRAATEAIARGVGVRGLLNVQYAVAAGVLYVLEANPRASRTVPFVSKATAVPLAKAAARVMMGATIA 877
Cdd:PRK05294 791 LPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLA 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 878 GLRA-EGMLPadgdggtlpldAPIAVKEAVLPFNRFHGVDTVLGPEMRSTGEVMGIDEVFGTAYAKSQAGSYGSLPTKGR 956
Cdd:PRK05294 871 ELGYtKGLIP-----------PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGT 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 957 AFVSVANRDKRAMIFPVKALADLGFEILATEGTAEVLRRNGVHAKIVRKQSdgpgpDGEPTIVSRILSGEVDLIVNTPFG 1036
Cdd:PRK05294 940 VFLSVRDRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVH-----EGRPHIVDLIKNGEIDLVINTPTG 1014
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*
gi 1986616510 1037 spgqSGPRLDGYEIRTAAVLRGIPCVTTVQGLGAAVQGIQAVAAGSVGVRSLQEH 1091
Cdd:PRK05294 1015 ----RQAIRDGFSIRRAALEYKVPYITTLAGARAAVKAIEALKFGELEVRSLQEY 1065
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1094 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1527.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 1 MPKRTDIRSILVIGSGPIVIGQACEFDYSGTQACRVLRAEGYRVILVNSNPATIMTDPEFADATYVEPITPGIVEQIIAR 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 81 ERPDALLPTLGGQTALNTAVALHEAGVLERYGVELVGADIAAIQAGENREQFKGIVARvadrygLNAESARSAICHTLAE 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKE------LGEPVPESEIVTSVEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 161 CLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQLRRIAGAGLDASPTSEVLLEESILGWKEYELEVMRDRADNVVIVCSI 240
Cdd:PRK12815 155 ALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 241 ENIDPMGVHTGDSVTVAPAMTLTDREYQNMRDVAIAVIREVGVdTGGCNIQFAVDPRTGRMIVIEMNPRVSRSSALASKA 320
Cdd:PRK12815 235 ENIDPVGIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 321 TGFPIAKIAAKLAVGYTLDEIPNDITRETPASFEPSLDYVVVKVPRFAFEKFAGADQTLTTHMKSVGEAMAIGRSFPEAL 400
Cdd:PRK12815 314 TGYPIAKIAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 401 QKALRSLEKK--GASFAWAGDPGDRAELLAACRTPHDGRLRAMMQALRAGATVEELYEATSVDPWFLDQLL-LIDEEARA 477
Cdd:PRK12815 394 QKALRSLEIKrnGLSLPIELSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEhIVALEKKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 478 VGAADTLTAGVLTRAKRHGFSDAQIAEIRGLPEERVRELRHELGVRPVYNTVDTCAAEFAARTPYLYSTYDEETEV-PPG 556
Cdd:PRK12815 474 AEDGLDLSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAePSS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 557 DRRKVIILGSGPNRIGQGIEFDYACVHASFELSAAGYETVMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVVRAEQesg 636
Cdd:PRK12815 554 EKKKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAEN--- 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 637 pVAGVIVQLGGQTPLGLAQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLPAPKHGTAVTVEQAREIAAEIGYPVL 716
Cdd:PRK12815 631 -IKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVL 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 717 VRPSYVLGGAGMAIVYDEETLGAYMARAgAASDHPVLVDRFLDeAIEIDVDALYDGEELYLGGVMEHIEEAGIHSGDSAC 796
Cdd:PRK12815 710 IRPSYVIGGQGMAVVYDEPALEAYLAEN-ASQLYPILIDQFID-GKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIA 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 797 ALPPITLGGFDIKRIRAATEAIARGVGVRGLLNVQYAVAAGVLYVLEANPRASRTVPFVSKATAVPLAKAAARVMMGATI 876
Cdd:PRK12815 788 VLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSL 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 877 AGLRAEGMLPadgdggtlPLDAPIAVKEAVLPFNRFHGVDTVLGPEMRSTGEVMGIDEVFGTAYAKSQAGSYGSLPTKGR 956
Cdd:PRK12815 868 AELGYPNGLW--------PGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGT 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 957 AFVSVANRDKRAMIFPVKALADLGFEILATEGTAEVLRRNGVHAKIVRKQSDGPgpdgePTIVSRILSGEVDLIVNTPFG 1036
Cdd:PRK12815 940 IFISVRDEDKPEVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGS-----PSLLERIKQHRIVLVVNTSLS 1014
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*...
gi 1986616510 1037 SPGQSgprlDGYEIRTAAVLRGIPCVTTVQGLGAAVQGIQAVAAGSVGVRSLQEHARR 1094
Cdd:PRK12815 1015 DSASE----DAIKIRDEALSTHIPVFTELETAQAFLQVLESLALTTQPIQELQEKHKQ 1068
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1075 |
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: 1523.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 2 PKRTDIRSILVIGSGPIVIGQACEFDYSGTQACRVLRAEGYRVILVNSNPATIMTDPEFADATYVEPITPGIVEQIIARE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 82 RPDALLPTLGGQTALNTAVALHEAGVLERYGVELVGADIAAIQAGENREQFKGIVARvadrygLNAESARSAICHTLAEC 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKE------IGEPVPESEIAHSVEEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 162 LTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQLRRIAGAGLDASPTSEVLLEESILGWKEYELEVMRDRADNVVIVCSIE 241
Cdd:TIGR01369 155 LAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 242 NIDPMGVHTGDSVTVAPAMTLTDREYQNMRDVAIAVIREVGVDtGGCNIQFAVDPRTGRMIVIEMNPRVSRSSALASKAT 321
Cdd:TIGR01369 235 NFDPMGVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 322 GFPIAKIAAKLAVGYTLDEIPNDITRETPASFEPSLDYVVVKVPRFAFEKFAGADQTLTTHMKSVGEAMAIGRSFPEALQ 401
Cdd:TIGR01369 314 GYPIAKVAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 402 KALRSLEKKGASFAWAG-DPGDRAELLAACRTPHDGRLRAMMQALRAGATVEELYEATSVDPWFLDQLL-LID-EEARAV 478
Cdd:TIGR01369 394 KALRSLEIGATGFDLPDrEVEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKnIVDlEEELEE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 479 GAADTLTAGVLTRAKRHGFSDAQIAEIRGLPEERVRELRHELGVRPVYNTVDTCAAEFAARTPYLYSTY-DEETEVPPGD 557
Cdd:TIGR01369 474 VKLTDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYeGERDDVPFTD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 558 RRKVIILGSGPNRIGQGIEFDYACVHASFELSAAGYETVMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVVRAEQesgp 637
Cdd:TIGR01369 554 KKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEK---- 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 638 VAGVIVQLGGQTPLGLAQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLPAPKHGTAVTVEQAREIAAEIGYPVLV 717
Cdd:TIGR01369 630 PEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLV 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 718 RPSYVLGGAGMAIVYDEETLGAYMARAGAAS-DHPVLVDRFLDEAIEIDVDALYDGEELYLGGVMEHIEEAGIHSGDSAC 796
Cdd:TIGR01369 710 RPSYVLGGRAMEIVYNEEELRRYLEEAVAVSpEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTC 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 797 ALPPITLGGFDIKRIRAATEAIARGVGVRGLLNVQYAVAAGVLYVLEANPRASRTVPFVSKATAVPLAKAAARVMMGATI 876
Cdd:TIGR01369 790 VLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 877 AGLraegmlpadgdGGTLPLDAP-IAVKEAVLPFNRFHGVDTVLGPEMRSTGEVMGIDEVFGTAYAKSQAGSYGSLPTKG 955
Cdd:TIGR01369 870 EEL-----------GVGKEKEPKyVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKG 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 956 RAFVSVANRDKRAMIFPVKALADLGFEILATEGTAEVLRRNGVHAKIVRKQSDGPgpdgePTIVSRILSGEVDLIVNTPf 1035
Cdd:TIGR01369 939 SVLLSVRDKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGR-----PNILDLIKNGEIELVINTT- 1012
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|
gi 1986616510 1036 gSPGQsGPRLDGYEIRTAAVLRGIPCVTTVQGLGAAVQGI 1075
Cdd:TIGR01369 1013 -SKGA-GTATDGYKIRREALDYGVPLITTLNTAEAFAEAL 1050
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1090 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1339.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 3 KRTDIRSILVIGSGPIVIGQACEFDYSGTQACRVLRAEGYRVILVNSNPATIMTDPEFADATYVEPITPGIVEQIIARER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 83 PDALLPTLGGQTALNTAVALHEAGVLERYGVELVGADIAAIQAGENREQFKGIVARVadryGLNaeSARSAICHTLAECL 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKI----GLK--TPPSGIATTLDECF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 163 TAADSLG-YPVVVRPSFTMGGAGSGFAHDEEQLRRIAGAGLDASPTSEVLLEESILGWKEYELEVMRDRADNVVIVCSIE 241
Cdd:PLN02735 173 EIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 242 NIDPMGVHTGDSVTVAPAMTLTDREYQNMRDVAIAVIREVGVDTGGCNIQFAVDPRTGRMIVIEMNPRVSRSSALASKAT 321
Cdd:PLN02735 253 NIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKAT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 322 GFPIAKIAAKLAVGYTLDEIPNDITRETPASFEPSLDYVVVKVPRFAFEKFAGADQTLTTHMKSVGEAMAIGRSFPEALQ 401
Cdd:PLN02735 333 GFPIAKMAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 402 KALRSLEKKGASFAWAGD---PGDRAELLAACRTPHDGRLRAMMQALRAGATVEELYEATSVDPWFLDQL--LLIDEEAR 476
Cdd:PLN02735 413 KALRSLETGFSGWGCAKVkelDWDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLkeLVDVEQFL 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 477 AVGAADTLTAGVLTRAKRHGFSDAQIAEIRGLPEERVRELRHELGVRPVYNTVDTCAAEFAARTPYLYSTYDEETEVPPG 556
Cdd:PLN02735 493 KSRSLSELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPT 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 557 DRRKVIILGSGPNRIGQGIEFDYACVHASFELSAAGYETVMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVVRAEQESg 636
Cdd:PLN02735 573 NKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPD- 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 637 pvaGVIVQLGGQTPLGLA----QALKDAGVP---------VVGTSPESIHLAEERGAFGRVLAEAGLPAPKHGTAVTVEQ 703
Cdd:PLN02735 652 ---GIIVQFGGQTPLKLAlpiqKYLDKNPPPsasgngnvkIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEAD 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 704 AREIAAEIGYPVLVRPSYVLGGAGMAIVYDEETLGAYMARAGAAS-DHPVLVDRFLDEAIEIDVDALYDGE-ELYLGGVM 781
Cdd:PLN02735 729 ALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDpERPVLVDKYLSDATEIDVDALADSEgNVVIGGIM 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 782 EHIEEAGIHSGDSACALPPITLGGFDIKRIRAATEAIARGVGVRGLLNVQYAV-AAGVLYVLEANPRASRTVPFVSKATA 860
Cdd:PLN02735 809 EHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRTVPFVSKAIG 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 861 VPLAKAAARVMMGATIAGLR-AEGMLPADgdggtlpldapIAVKEAVLPFNRFHGVDTVLGPEMRSTGEVMGIDEVFGTA 939
Cdd:PLN02735 889 HPLAKYASLVMSGKSLKDLGfTEEVIPAH-----------VSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKA 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 940 YAKSQAGSYGSLPTKGRAFVSVANRDKRAMIFPVKALADLGFEILATEGTAEVLRRNGVHAKIVRKQSdgpgpDGEPTIV 1019
Cdd:PLN02735 958 FAKAQIAAGQRLPLSGTVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLH-----EGRPHAG 1032
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1986616510 1020 SRILSGEVDLIVNTpfgSPGQSGPRLDGYEIRTAAVLRGIPCVTTVQGLGAAVQGIQAVAAGSVGVRSLQE 1090
Cdd:PLN02735 1033 DMLANGQIQLMVIT---SSGDALDQKDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKECPIEMIALQD 1100
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-566 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 730.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 13 IGSGPIVIGQACEFDYSGTQACRVLRAEGYRVILVNSNPATIMTDPEFADATYVEPITPGIVEQIIARERPDALLPTLGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 93 QTALNTAVALHEAGVLEryGVELVGADIAAIQAGENREQFKGIVARvadrygLNAESARSAICHTLAECLTAADSLGYPV 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDK------LGIPQPKSGTATSVEEALAIAEEIGYPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 173 VVRPSFTMGGAGSGFAHDEEQLRRIAGAGLDASPTSEVLLEESILGWKEYELEVMRDRADNVVIVCSIENIDPMGVHTGD 252
Cdd:COG0458 153 IVRPSYVLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 253 SVTVAPAMTLTDREYQNMRDVAIAVIREVGVDtGGCNIQFAVDprTGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKL 332
Cdd:COG0458 233 SICVAPPQTLSDKEYQRLRDATLKIARALGVV-GLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 333 AVGYTLDEIPNDItretpaSFEPSLDYVVVKVPRFAFEKFAGADQTLTTHMKSVGEAMAIGRSFPEALQKALRSLEKKGA 412
Cdd:COG0458 310 ALGYTLDELGNDT------GFEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 413 SFAWAGDPGDRAELLAACRTPHDGRLRAMMQALRAGATVEELYEATSVDPWFLDQLLLIDEEARAVGaADTLTAGVLTRA 492
Cdd:COG0458 384 GTVLLSLVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELE-EIILVINTLLGA 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1986616510 493 KRHGFSDAQIAEIRGLPEERVRELRHELGVRPVYNTVDTCAAEFAARTPYLYSTYDEETEVPPGDRRKVIILGS 566
Cdd:COG0458 463 KSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
564-1092 |
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: 659.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 564 LGSGPNRIGQGIEFDYACVHASFELSAAGYETVMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVVRAEQesgpVAGVIV 643
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEK----PDGVIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 644 QLGGQTPLGLAQALKDA----GVPVVGTSPESIHLAEERGAFGRVLAEAGLPAPKHGTAVTVEQAREIAAEIGYPVLVRP 719
Cdd:COG0458 77 QFGGQTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 720 SYVLGGAGMAIVYDEETLGAYMARAGAAS-DHPVLVDRFLDEAIEIDVDALYDGE-ELYLGGVMEHIEEAGIHSGDSACA 797
Cdd:COG0458 157 SYVLGGRGMGIVYNEEELEEYLERALKVSpDHPVLIDESLLGAKEIEVDVVRDGEdNVIIVGIMEHIEPAGVHSGDSICV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 798 LPPITLGGFDIKRIRAATEAIARGVGVRGLLNVQYAVAAGVLYVLEANPRASRTVPFVSKATAVPLAKAAARVMMGATIA 877
Cdd:COG0458 237 APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 878 GLR-AEGMLPAdgdggtlpLDaPIAVKEAVLPFNRFHGVDTVLGPEMRSTGEVMGIDEVFGTAYAKSQAGSYGSLPtkGR 956
Cdd:COG0458 317 ELGnDTGFEPT--------LD-YVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP--GT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 957 AFVS-VANRDKRAMIFPVKALADLGFEILATEGTAEVLRRNGVHAKIVRKQSdgpgpDGEPTIVSRILSGEVDLIVNTPF 1035
Cdd:COG0458 386 VLLSlVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLS-----EGRPIIVDEIELEEIILVINTLL 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1986616510 1036 GSPGQSgprlDGYEIRTAAVLRGIPCVTTVQGLGAAVQGIQAVAAGSVGVRSLQEHA 1092
Cdd:COG0458 461 GAKSLG----DSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYY 513
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
129-339 |
1.19e-74 |
|
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: 245.29 E-value: 1.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 129 REQFKGIVARvadrygLNAESARSAIC--HTLAECLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQLRRIAGAGLDASP 206
Cdd:pfam02786 2 KVLFKAAMKE------AGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 207 TS----EVLLEESILGWKEYELEVMRDRADNVVIVCSIENIDPMgvHTGDSVTVAPAMTLTDREYQNMRDVAIAVIREVG 282
Cdd:pfam02786 76 AAfgnpQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1986616510 283 VdTGGCNIQFAVDPRTGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLD 339
Cdd:pfam02786 154 Y-VGAGTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
426-547 |
1.73e-55 |
|
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: 188.04 E-value: 1.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 426 LLAACRTPHDGRLRAMMQALRAGATVEELYEATSVDPWFLDQLL-LIDEEAR-AVGAADTLTAGVLTRAKRHGFSDAQIA 503
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKeIVELEKElKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1986616510 504 EIRGLPEERVRELRHELGVRPVYNTVDTCAAEFAARTPYLYSTY 547
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
955-1073 |
5.81e-38 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 137.61 E-value: 5.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 955 GRAFVSVANRDKRAMIFPVKALADLGFEILATEGTAEVLRRNGVHAKIVRKQSdgpgpDGEPTIVSRILSGEVDLIVNTP 1034
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVS-----EGRPNIVDLIKNGEIQLVINTP 75
|
90 100 110
....*....|....*....|....*....|....*....
gi 1986616510 1035 fgSPGQSgpRLDGYEIRTAAVLRGIPCVTTVQGLGAAVQ 1073
Cdd:cd01424 76 --SGKRA--IRDGFSIRRAALEYKVPYFTTLDTARAAVE 110
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
677-876 |
3.49e-34 |
|
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: 130.50 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 677 ERGAFGRVLAEAGLPAPKhGTAV---TVEQAREIAAEIGYPVLVRPSYVLGGAGMAIVYDEETLGAYMARA-----GAAS 748
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVP-GTAGpveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALAlaeapAAFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 749 DHPVLVDRFLDEAIEIDVDALYD--GEELYLGGvMEHIEEagIHSGDSACALPPITLGGFDIKRIRAATEAIARGVGVRG 826
Cdd:pfam02786 80 NPQVLVEKSLKGPKHIEYQVLRDahGNCITVCN-RECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1986616510 827 LLNVQYAVAA--GVLYVLEANPRASRTVPFVSKATAVPLAKAAARVMMGATI 876
Cdd:pfam02786 157 AGTVEFALDPfsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
431-505 |
5.47e-29 |
|
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: 110.54 E-value: 5.47e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1986616510 431 RTPHDGRLRAMMQALRAGATVEELYEATSVDPWFLDQLL-LIDEEARAVGAADTLTAGVLTRAKRHGFSDAQIAEI 505
Cdd:pfam02787 4 RTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKnIVELEKELKEAGLDLDAELLREAKRLGFSDRQIAKL 79
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
74-335 |
7.58e-24 |
|
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: 102.26 E-value: 7.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 74 VEQIIARERPDALLptlggqtALNTAVALHEAGVLERYGveLVGADIAAIQAGENreqfKGIVARVADRYGLNaeSARSA 153
Cdd:COG0439 9 AAELARETGIDAVL-------SESEFAVETAAELAEELG--LPGPSPEAIRAMRD----KVLMREALAAAGVP--VPGFA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 154 ICHTLAECLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQL----RRIAGAGLDASPTSEVLLEESILGwKEYELEVMRD 229
Cdd:COG0439 74 LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELeaalAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 230 raDNVVIVCSI---ENIDPMGVHTGDsvtVAPAmTLTDREYQNMRDVAIAVIREVGVDTGGCNIQFAVDPRtGRMIVIEM 306
Cdd:COG0439 153 --DGEVVVCSItrkHQKPPYFVELGH---EAPS-PLPEELRAEIGELVARALRALGYRRGAFHTEFLLTPD-GEPYLIEI 225
|
250 260 270
....*....|....*....|....*....|.
gi 1986616510 307 NPRVS--RSSALASKATGFPIAKIAAKLAVG 335
Cdd:COG0439 226 NARLGgeHIPPLTELATGVDLVREQIRLALG 256
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
969-1063 |
8.03e-22 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 91.01 E-value: 8.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 969 MIFPVKALADLGFEILATEGTAEVLRRNGVHAKIVRKQSDGPGPDGEPTIVSRILSGEVDLIVNTPfgSPGQSGPRlDGY 1048
Cdd:pfam02142 2 LVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEGRPGGRVQIGDLIKNGEIDLVINTL--YPFKATVH-DGY 78
|
90
....*....|....*
gi 1986616510 1049 EIRTAAVLRGIPCVT 1063
Cdd:pfam02142 79 AIRRAAENIDIPGPT 93
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
622-873 |
1.37e-21 |
|
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: 95.71 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 622 LEDVLEVVRAEQESGPVAGVIVQLGGQTPLgLAQALKDAGVPvvGTSPESIHLAEERGAFGRVLAEAGLPAPKHGTAVTV 701
Cdd:COG0439 2 IDAIIAAAAELARETGIDAVLSESEFAVET-AAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 702 EQAREIAAEIGYPVLVRPSYVLGGAGMAIVYDEETLGAYMARAGA-----ASDHPVLVDRFLdEAIEIDVDALYDGEELY 776
Cdd:COG0439 79 EEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAeakagSPNGEVLVEEFL-EGREYSVEGLVRDGEVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 777 LGGVMEHIEEA--GIHSGDSAcalpPITLGGFDIKRIRAATEAIARGVGV-RGLLNVQYAV-AAGVLYVLEANPRAS--R 850
Cdd:COG0439 158 VCSITRKHQKPpyFVELGHEA----PSPLPEELRAEIGELVARALRALGYrRGAFHTEFLLtPDGEPYLIEINARLGgeH 233
|
250 260
....*....|....*....|...
gi 1986616510 851 TVPFVSKATAVPLAKAAARVMMG 873
Cdd:COG0439 234 IPPLTELATGVDLVREQIRLALG 256
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
968-1063 |
3.88e-21 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 88.69 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 968 AMIFPVKALADLGFEILATEGTAEVLRRNG--VHAKIVRKQSdgpgpDGEPTIVSRILSGEVDLIVNTPfgSPGQSGPRL 1045
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGlpVVKTLHPKVH-----GGIPQILDLIKNGEIDLVINTL--YPFEAQAHE 73
|
90
....*....|....*...
gi 1986616510 1046 DGYEIRTAAVLRGIPCVT 1063
Cdd:smart00851 74 DGYSIRRAAENIDIPGPT 91
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
17-335 |
6.24e-17 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 84.21 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 17 PIVIGqaceFDYSGTQACRVLRAEGYRVILVNSNPATIMTDPEFADATYVEP----ITPGIVE---QIIARERPDALLPT 89
Cdd:COG3919 8 VVVLG----GDINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPdpgdDPEAFVDallELAERHGPDVLIPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 90 LGGQTALntaVALHEAgVLERYgVELVGADIAAIQAGENREQFkgivARVADRYGLNAesARSAICHTLAECLTAADSLG 169
Cdd:COG3919 84 GDEYVEL---LSRHRD-ELEEH-YRLPYPDADLLDRLLDKERF----YELAEELGVPV--PKTVVLDSADDLDALAEDLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 170 YPVVVRPS--------FTMGGAGSGFAHDEEQLRRIAGAGLDASPtsEVLLEESILGWKEYE--LEVMRDRADNVVIVCS 239
Cdd:COG3919 153 FPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAGY--ELIVQEYIPGDDGEMrgLTAYVDRDGEVVATFT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 240 IENI--DPMGVhtgdSVTVApAMTLTDREyqnMRDVAIAVIREVGVdTGGCNIQFAVDPRTGRMIVIEMNPRVSRSSALA 317
Cdd:COG3919 231 GRKLrhYPPAG----GNSAA-RESVDDPE---LEEAARRLLEALGY-HGFANVEFKRDPRDGEYKLIEINPRFWRSLYLA 301
|
330
....*....|....*...
gi 1986616510 318 SKAtGFPIAKIAAKLAVG 335
Cdd:COG3919 302 TAA-GVNFPYLLYDDAVG 318
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
651-869 |
5.25e-13 |
|
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: 70.74 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 651 LGLAQALKDAGVPVVGtSPESIHLAEERGAFGRVLAEAGLPAPKhgTAVT--VEQAREIAAEIGYPVLVRPSYVLGGAGM 728
Cdd:COG0189 71 LALLRQLEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIPVPP--TLVTrdPDDLRAFLEELGGPVVLKPLDGSGGRGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 729 AIVYDEETLGAYMARAGAASDHPVLVDRFLDEAIEIDVDALYDGEELYlgGVMEHIEEAG-----IHSGDSA--CALPPi 801
Cdd:COG0189 148 FLVEDEDALESILEALTELGSEPVLVQEFIPEEDGRDIRVLVVGGEPV--AAIRRIPAEGefrtnLARGGRAepVELTD- 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1986616510 802 tlggfdikRIRAATEAIARGVGVrGLLNVQYAVAAGVLYVLEANPRASrtVPFVSKATAVPLAKAAAR 869
Cdd:COG0189 225 --------EERELALRAAPALGL-DFAGVDLIEDDDGPLVLEVNVTPG--FRGLERATGVDIAEAIAD 281
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
622-854 |
7.20e-13 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 71.07 E-value: 7.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 622 LEDVLEVVRAEQesgpVAGVIVqlGGQTPLGL----AQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLPAPKHGT 697
Cdd:PRK12767 58 IDRLLDICKKEK----IDLLIP--LIDPELPLlaqnRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 698 AVTVEQAREI--AAEIGYPVLVRPSYVLGGAGMAIVYDEETLGAYMARAGaasdhPVLVDRFLDEaIEIDVDALYDgeel 775
Cdd:PRK12767 132 PESLEDFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVP-----NLIIQEFIEG-QEYTVDVLCD---- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 776 yLGGVMEHI---EEAGIHSGDSACAlppITlggFDIKRIRAATEAIARGVGVRGLLNVQYAVAAGVLYVLEANPRASRTV 852
Cdd:PRK12767 202 -LNGEVISIvprKRIEVRAGETSKG---VT---VKDPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGY 274
|
..
gi 1986616510 853 PF 854
Cdd:PRK12767 275 PL 276
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
958-1066 |
1.13e-12 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 65.40 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 958 FVSVANRDKRAMIFPVKALADLGFEILATEGTAEVLRRNGVHAKIVRKQSDGPGPDgEPTIVSRILSGEVDLIVNTPfgS 1037
Cdd:cd01423 4 LISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQND-KPSLRELLAEGKIDLVINLP--S 80
|
90 100
....*....|....*....|....*....
gi 1986616510 1038 PGQSGPRLDGYEIRTAAVLRGIPCVTTVQ 1066
Cdd:cd01423 81 NRGKRVLDNDYVMRRAADDFAVPLITNPK 109
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
652-778 |
2.10e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 70.83 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 652 GLAQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLP-APKHGTAV-TVEQAREIAAEIGYPVLVRPSYVLGGAGMA 729
Cdd:PRK06111 90 SFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPvVPGITTNLeDAEEAIAIARQIGYPVMLKASAGGGGIGMQ 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1986616510 730 IVYDEETLGAYMA--RAGAAS---DHPVLVDRFLDEA--IEIDVDALYDGEELYLG 778
Cdd:PRK06111 170 LVETEQELTKAFEsnKKRAANffgNGEMYIEKYIEDPrhIEIQLLADTHGNTVYLW 225
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
654-874 |
3.26e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 70.17 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 654 AQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLPA--PKHGTAVTVEQAREIAAEIGYPVLVRPSYVLGGAGMAIV 731
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTvpGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 732 YDEETLGAYMARA-----GAASDHPVLVDRFLDEAIEIDVDALYDGEELylggvmehieeagIHSGDSACAL-------- 798
Cdd:PRK12833 175 HDAAQLAAELPLAqreaqAAFGDGGVYLERFIARARHIEVQILGDGERV-------------VHLFERECSLqrrrqkil 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 799 ---PPITLGGFDIKRIRAATEAIARGVGVR--GLLNVQYAVAAGVLYVLEANPRASRTVPFVSKATAVPLAKAAARVMMG 873
Cdd:PRK12833 242 eeaPSPSLTPAQRDALCASAVRLARQVGYRgaGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADG 321
|
.
gi 1986616510 874 A 874
Cdd:PRK12833 322 E 322
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
652-846 |
5.07e-12 |
|
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: 68.21 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 652 GLAQALKD-AGVPVVGTSPESIHLAEERGAFGRVLAEAGLPAPKHG--TAVTVEQAREIAAEIGYPVLVRPsyVLGGA-- 726
Cdd:COG1181 69 GTIQGLLElLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVvlRRGELADLEAIEEELGLPLFVKP--AREGSsv 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 727 GMAIVYDEETLGAYMARAgAASDHPVLVDRFLDeAIEIDVdALYDGEELYLGGVMEHIEEAGI-------HSGDSA---- 795
Cdd:COG1181 147 GVSKVKNAEELAAALEEA-FKYDDKVLVEEFID-GREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEyicp 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1986616510 796 CALPPITlggfdIKRIRAATEAIARGVGVRGllnvqYA------VAAGVLYVLEANP 846
Cdd:COG1181 224 ARLPEEL-----EERIQELALKAFRALGCRG-----YArvdfrlDEDGEPYLLEVNT 270
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
652-778 |
1.42e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 68.09 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 652 GLAQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLPA-PKHGTAVT-VEQAREIAAEIGYPVLVRPSYVLGGAGMA 729
Cdd:PRK08654 90 EFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVlPGTEEGIEdIEEAKEIAEEIGYPVIIKASAGGGGIGMR 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1986616510 730 IVYDEE----TLGAYMARAGAA-SDHPVLVDRFLDEA--IEIDVDALYDGEELYLG 778
Cdd:PRK08654 170 VVYSEEeledAIESTQSIAQSAfGDSTVFIEKYLEKPrhIEIQILADKHGNVIHLG 225
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
83-341 |
2.51e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 67.43 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 83 PDALLPTLGGQTALNTAV-----ALHEAgvlerYGVELVGADIAAIQAgENREQFKGIVARVADRYGLNAESARSAI--- 154
Cdd:PRK07178 53 ADPLAGYLNPRRLVNLAVetgcdALHPG-----YGFLSENAELAEICA-ERGIKFIGPSAEVIRRMGDKTEARRAMIkag 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 155 ----------CHTLAECLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQLR----RIAGAGLDASPTSEVLLEESILGWK 220
Cdd:PRK07178 127 vpvtpgsegnLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEqnfpRVISEATKAFGSAEVFLEKCIVNPK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 221 EYELEVMRDRADNVVIV----CSIENidpmgvHTGDSVTVAPAMTLTDREYQNMRDVAIAVIREVGVDTGGcNIQFAVDp 296
Cdd:PRK07178 207 HIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAG-TVEFLLD- 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1986616510 297 RTGRMIVIEMNPRVSRSSALASKATGFPIAK----IAAKLAVGYTLDEI 341
Cdd:PRK07178 279 ADGEVYFMEMNTRVQVEHTITEEITGIDIVReqirIASGLPLSYKQEDI 327
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
157-408 |
2.18e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 61.20 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 157 TLAECLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQLRR-IAGAGLDASP---TSEVLLEESILGWKEYELEVMRDRAD 232
Cdd:PRK06111 140 DAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKaFESNKKRAANffgNGEMYIEKYIEDPRHIEIQLLADTHG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 233 NVVIV----CSIENidpmgvHTGDSVTVAPAMTLTDREYQNMRDVAIAVIREVGVdTGGCNIQFAVDPRtGRMIVIEMNP 308
Cdd:PRK06111 220 NTVYLwereCSVQR------RHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGY-TNAGTIEFLVDEQ-KNFYFLEMNT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 309 RVSRSSALASKATGFPIA----KIAAKLAVGYTLDEIPND-------ITRETPASFEPS----LDYVVVKVPRFAFEKFA 373
Cdd:PRK06111 292 RLQVEHPVTEEITGIDLVeqqlRIAAGEKLSFTQDDIKRSghaievrIYAEDPKTFFPSpgkiTDLTLPGGEGVRHDHAV 371
|
250 260 270
....*....|....*....|....*....|....*.
gi 1986616510 374 GADQTLTTHMKS-VGEAMAIGRSFPEALQKALRSLE 408
Cdd:PRK06111 372 ENGVTVTPFYDPmIAKLIAHGETREEAISRLHDALE 407
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
956-1067 |
4.11e-09 |
|
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 238297 [Multi-domain] Cd Length: 112 Bit Score: 55.21 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 956 RAFVSVANRDKRAMIFPVKALADLGFEILATEGTAEVLRRNGVHakiVRKQSDGPGpDGEPTIVSRIL-SGEVDLIVNTP 1034
Cdd:cd00532 1 GVFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIP---VRAVSKRHE-DGEPTVDAAIAeKGKFDVVINLR 76
|
90 100 110
....*....|....*....|....*....|....
gi 1986616510 1035 fgSPGQSGPRL-DGYEIRTAAVLRGIPCVTTVQG 1067
Cdd:cd00532 77 --DPRRDRCTDeDGTALLRLARLYKIPVTTPNAT 108
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
683-868 |
1.45e-08 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 57.43 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 683 RVLAEAGLPAPKHGTAVTVEQAREIAAEIGYPVLVRPsyVLGGA--GMAIVYDEETLGAYMARAgAASDHPVLVDRFL-- 758
Cdd:PRK01372 104 LVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELA-FKYDDEVLVEKYIkg 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 759 ---------DEA---IEIDVDA-LYDGEELYLGGVMEHIEEAGihsgdsacaLPPitlggfDI-KRIRAATEAIARGVGV 824
Cdd:PRK01372 181 reltvavlgGKAlpvIEIVPAGeFYDYEAKYLAGGTQYICPAG---------LPA------EIeAELQELALKAYRALGC 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1986616510 825 RGLLNVQYAV-AAGVLYVLEANprasrTVPFVSKATAVPLAKAAA 868
Cdd:PRK01372 246 RGWGRVDFMLdEDGKPYLLEVN-----TQPGMTSHSLVPMAARAA 285
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
661-798 |
2.26e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 57.83 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 661 GVPVVGTSPESIHLAEERGAFGRVLAEAGLPA--PKHGTAVTVEQAREIAAEIGYPVLVRPSYVLGGAGMAIVYDEETL- 737
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVipGSDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLe 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1986616510 738 GAYMARAGAA----SDHPVLVDRFLDEAIEIDVDALYDGEelylGGVmehieeagIHSGDSACAL 798
Cdd:PRK08462 181 NLYLAAESEAlsafGDGTMYMEKFINNPRHIEVQILGDKH----GNV--------IHVGERDCSL 233
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
653-847 |
2.31e-08 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 58.61 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 653 LAQALKDAGVPVVGTSPESIHLaeergaFG-----RVLA-EAGLPAPKhGT---AVTVEQAREIAAEIGYPVLVRPSYVL 723
Cdd:PRK12999 95 FARACAEAGITFIGPTAEVLRL------LGdkvaaRNAAiKAGVPVIP-GSegpIDDIEEALEFAEEIGYPIMLKASAGG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 724 GGAGMAIVYDEETL-GAY-----MARAGAASDHpVLVDRFLDEAIEIDVDALYDGEelylGGVMeH-------------- 783
Cdd:PRK12999 168 GGRGMRIVRSEEELeEAFerakrEAKAAFGNDE-VYLEKYVENPRHIEVQILGDKH----GNVV-Hlyerdcsvqrrhqk 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1986616510 784 -IEEAgihsgdSACALPPITLggfdiKRIRAATEAIARGVGVRGLLNVQYAV-AAGVLYVLEANPR 847
Cdd:PRK12999 242 vVEIA------PAPGLSEELR-----ERICEAAVKLARAVGYVNAGTVEFLVdADGNFYFIEVNPR 296
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
21-308 |
3.33e-08 |
|
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: 56.27 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 21 GQACEFD---YSGTQACRVLRAEGYRVILVNSNPATIMTDpefadatyvepitpgiveqiIARERPDALLPTLGGQTALN 97
Cdd:COG1181 9 GRSAEREvslKSGRAVAAALDKAGYDVVPIGIDVEDLPAA--------------------LKELKPDVVFPALHGRGGED 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 98 TAVAlheaGVLERYGVELVGADIAAIQAGENreqfKGIVARVADRYGLNaeSARSAIC--HTLAECLTAADSLGYPVVVR 175
Cdd:COG1181 69 GTIQ----GLLELLGIPYTGSGVLASALAMD----KALTKRVLAAAGLP--TPPYVVLrrGELADLEAIEEELGLPLFVK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 176 PSFtmggAGSGF----AHDEEQLRR-IAGA-GLDasptSEVLLEESILGwKEYELEVMRDraDNVVIVCSIEnIDPMGV- 248
Cdd:COG1181 139 PAR----EGSSVgvskVKNAEELAAaLEEAfKYD----DKVLVEEFIDG-REVTVGVLGN--GGPRALPPIE-IVPENGf 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1986616510 249 -------HTGDSVTVAPAmTLTDREYQNMRDVAIAVIREVG------VDtggcniqFAVDPrTGRMIVIEMNP 308
Cdd:COG1181 207 ydyeakyTDGGTEYICPA-RLPEELEERIQELALKAFRALGcrgyarVD-------FRLDE-DGEPYLLEVNT 270
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
654-798 |
4.60e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 56.73 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 654 AQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLPA-PKHGTAV-TVEQAREIAAEIGYPVLVRPSYVLGGAGMAIV 731
Cdd:PRK08591 92 AEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVvPGSDGPVdDEEEALAIAKEIGYPVIIKATAGGGGRGMRVV 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1986616510 732 YDEETL--GAYMAR--AGAASDHP-VLVDRFLDEAIEIDVDALYDGEelylGGVmehieeagIHSGDSACAL 798
Cdd:PRK08591 172 RTEAELekAFSMARaeAKAAFGNPgVYMEKYLENPRHIEIQVLADGH----GNA--------IHLGERDCSL 231
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
592-913 |
5.12e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 57.16 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 592 GYETVMVNCNPETvstdYDTSDRLYFEPLTLE--DVLEVVRAEQESGPVAGVIVQLGG--QTPLGLAQALkdaGVPvvGT 667
Cdd:PRK02186 27 GFTPYFLTANRGK----YPFLDAIRVVTISADtsDPDRIHRFVSSLDGVAGIMSSSEYfiEVASEVARRL---GLP--AA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 668 SPESIHLAEERGAFGRVLAEAGLPAPKHGTAVTVEQAREIAAEIGYPVLVRPSYVLGGAGMAIVYDEETLGAYMARAGAA 747
Cdd:PRK02186 98 NTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 748 SDHPVLVDRFLDEAiEIDVDALYDGEELYLGGVMehieeaGIHSGDSACALP-----PITLGGFDIKRIRAATEAIARGV 822
Cdd:PRK02186 178 GTRAALVQAYVEGD-EYSVETLTVARGHQVLGIT------RKHLGPPPHFVEighdfPAPLSAPQRERIVRTVLRALDAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 823 GVR-GLLNVQYAVAAGVLYVLEANPR-ASRTVP-FVSKATAVPLAKAAARVMMG-ATIAGLRAEG------MLPADGD-- 890
Cdd:PRK02186 251 GYAfGPAHTELRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVIDLHLGvAAFADPTAKRygairfVLPARSGvl 330
|
330 340
....*....|....*....|...
gi 1986616510 891 GGTLPLDAPIavkeAVLPFNRFH 913
Cdd:PRK02186 331 RGLLFLPDDI----AARPELRFH 349
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
40-323 |
1.55e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 54.50 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 40 EGYRVILVNSNP-ATIMTdpeFADATYVEP-IT-PGIVE---QIIARERPDALLPtlGGQTALNTAVALHEAgvLERYGV 113
Cdd:PRK12767 24 LKGRVIGADISElAPALY---FADKFYVVPkVTdPNYIDrllDICKKEKIDLLIP--LIDPELPLLAQNRDR--FEEIGV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 114 ELVGADIAAIQAGEN----REQFKGIVARVADRYGLNAESARSAIChtlaecltAADSLGYPVVVRPSFTMGGAGSGFAH 189
Cdd:PRK12767 97 KVLVSSKEVIEICNDkwltYEFLKENGIPTPKSYLPESLEDFKAAL--------AKGELQFPLFVKPRDGSASIGVFKVN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 190 DEEQLRRIagagldASPTSEVLLEESILGwKEYELEVMRDRADNVVIVCSIENIDPMGVHTGDSVTVapamtltdrEYQN 269
Cdd:PRK12767 169 DKEELEFL------LEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIEVRAGETSKGVTV---------KDPE 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1986616510 270 MRDVAIAVIREVGVDtGGCNIQFAVDPrtGRMIVIEMNPRVSRSSALASKAtGF 323
Cdd:PRK12767 233 LFKLAERLAEALGAR-GPLNIQCFVTD--GEPYLFEINPRFGGGYPLSYMA-GA 282
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
654-778 |
1.64e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 55.10 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 654 AQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLP-AP-KHGTAVTVEQAREIAAEIGYPVLVRPSYVLGGAGMAIV 731
Cdd:PRK05586 92 AKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPvVPgSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIV 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1986616510 732 YDEETL--GAYMARAGAAS---DHPVLVDRFLDEAIEIDVDALYD--GEELYLG 778
Cdd:PRK05586 172 RSEEELikAFNTAKSEAKAafgDDSMYIEKFIENPKHIEFQILGDnyGNVVHLG 225
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
156-407 |
5.54e-07 |
|
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: 53.93 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 156 HTLAECLTAADSLGYPVVVRPSftMGGAGSG--FAHDEEQL-------RRIAGA--GLDasptsEVLLEESILGWKEYEL 224
Cdd:COG1038 142 DDLEEALAFAEEIGYPVMLKAA--AGGGGRGmrVVRSEEELeeafesaRREAKAafGDD-----EVFLEKYIERPKHIEV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 225 EVMRDRADNVVIV----CS--------IEnidpmgvhtgdsvtVAPAMTLTDREYQNMRDVAIAVIREVGVDTGGcNIQF 292
Cdd:COG1038 215 QILGDKHGNIVHLferdCSvqrrhqkvVE--------------IAPAPNLDEELREAICEAAVKLAKAVGYVNAG-TVEF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 293 AVDpRTGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDE----IPND-------------ITRETPA-SFE 354
Cdd:COG1038 280 LVD-DDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLDDpeigIPSQedirlngyaiqcrITTEDPAnNFM 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1986616510 355 PslDYVVVKVPRFAF---------EKFAGADQT---------LTTHmksvgeamaiGRSFPEALQKALRSL 407
Cdd:COG1038 359 P--DTGRITAYRSAGgfgirldggNAYTGAVITpyydsllvkVTAW----------GRTFEEAIRKMRRAL 417
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
156-407 |
5.64e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 53.99 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 156 HTLAECLTAADSLGYPVVVRPSftMGGAGSG--FAHDEEQL-------RRIAGAgldASPTSEVLLEESILGWKEYELEV 226
Cdd:PRK12999 143 DDIEEALEFAEEIGYPIMLKAS--AGGGGRGmrIVRSEEELeeaferaKREAKA---AFGNDEVYLEKYVENPRHIEVQI 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 227 MRDRADNVVIV----CS--------IEnidpmgvhtgdsvtVAPAMTLTDREYQNMRDVAIAVIREVGVdTGGCNIQFAV 294
Cdd:PRK12999 218 LGDKHGNVVHLyerdCSvqrrhqkvVE--------------IAPAPGLSEELRERICEAAVKLARAVGY-VNAGTVEFLV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 295 DPRtGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDE----IPND-------------ITRETPA-SFEPs 356
Cdd:PRK12999 283 DAD-GNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLHDleigIPSQedirlrgyaiqcrITTEDPAnNFMP- 360
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1986616510 357 lDYVVVKVPRFAF---------EKFAGAdqTLTTHMKSVGEAM-AIGRSFPEALQKALRSL 407
Cdd:PRK12999 361 -DTGRITAYRSPGgfgvrldggNAFAGA--EITPYYDSLLVKLtAWGRTFEQAVARMRRAL 418
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
653-744 |
7.57e-07 |
|
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: 53.54 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 653 LAQALKDAGVPVVGTSPESIHLaeergaFG-----RVLA-EAGLPA-PKHGTAVT-VEQAREIAAEIGYPVLVRPSYVLG 724
Cdd:COG1038 94 FARACEEAGITFIGPSPEVLEM------LGdkvaaRAAAiEAGVPViPGTEGPVDdLEEALAFAEEIGYPVMLKAAAGGG 167
|
90 100
....*....|....*....|
gi 1986616510 725 GAGMAIVYDEETLGAYMARA 744
Cdd:COG1038 168 GRGMRVVRSEEELEEAFESA 187
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-345 |
8.99e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 52.83 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 1 MPKRtdIRSILVIGSGPIvigqacefdysgtqACRVLRAE---GYRVILVNSN------PA-----TIMTDPEFADATYV 66
Cdd:PRK12833 1 MPSR--IRKVLVANRGEI--------------AVRIIRAArelGMRTVAACSDadrdslAArmadeAVHIGPSHAAKSYL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 67 EPitpgivEQIIARER---PDALLPTLGgqtALNTAVALHEAgvLERYGVELVGADIAAIQagenREQFKGIVARVADRY 143
Cdd:PRK12833 65 NP------AAILAAARqcgADAIHPGYG---FLSENAAFAEA--VEAAGLIFVGPDAQTIR----TMGDKARARRTARRA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 144 GLNAESARSAICHTLAECLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQLRR---IAGAGLDASPTS-EVLLEESILGW 219
Cdd:PRK12833 130 GVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpLAQREAQAAFGDgGVYLERFIARA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 220 KEYELEVMRDRADNVVIV---CSIENidpmgvHTGDSVTVAPAMTLTDREYQNMRDVAIAVIREVGVDTGGcNIQFAVDP 296
Cdd:PRK12833 210 RHIEVQILGDGERVVHLFereCSLQR------RRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAG-TLEYLFDD 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1986616510 297 RTGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDEIPNDI 345
Cdd:PRK12833 283 ARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRFAQGDI 331
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
160-346 |
9.35e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 52.68 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 160 ECLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQL-------RRIAGAgldASPTSEVLLEESILGWKEYELEVMRDRAD 232
Cdd:PRK08654 143 EAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELedaiestQSIAQS---AFGDSTVFIEKYLEKPRHIEIQILADKHG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 233 NVVIV----CSIENIDPMGVHTGDSvtvaPAMTLTDREyqNMRDVAIAVIREVGVDTGGcNIQFAVDprTGRMIVIEMNP 308
Cdd:PRK08654 220 NVIHLgdreCSIQRRHQKLIEEAPS----PIMTPELRE--RMGEAAVKAAKAINYENAG-TVEFLYS--NGNFYFLEMNT 290
|
170 180 190
....*....|....*....|....*....|....*...
gi 1986616510 309 RVSRSSALASKATGFPIAKIAAKLAVGYTLDEIPNDIT 346
Cdd:PRK08654 291 RLQVEHPITEMVTGIDIVKEQIKIAAGEELSFKQEDIT 328
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
156-345 |
1.75e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 51.64 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 156 HTLAECLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQL-RRIAGAGLDASPT---SEVLLEESILGWKEYELEVMRDRA 231
Cdd:PRK05586 139 ENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELiKAFNTAKSEAKAAfgdDSMYIEKFIENPKHIEFQILGDNY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 232 DNVVIV----CSIENidpmgvHTGDSVTVAPAMTLTDREYQNMRDVAIAVIREVGVDTGGcNIQFAVDpRTGRMIVIEMN 307
Cdd:PRK05586 219 GNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAG-TIEFLLD-KDGNFYFMEMN 290
|
170 180 190
....*....|....*....|....*....|....*...
gi 1986616510 308 PRVSRSSALASKATGFPIAKIAAKLAVGYTLDEIPNDI 345
Cdd:PRK05586 291 TRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQEDI 328
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
156-345 |
2.65e-06 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 51.35 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 156 HTLAECLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQL-------RRIAGAGLDaspTSEVLLEESILGWKEYELEVMR 228
Cdd:PRK08463 139 ESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLenafescKREALAYFN---NDEVFMEKYVVNPRHIEFQILG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 229 DRADNVVIV----CSIENidpmgvHTGDSVTVAPAMTLTDREYQNMRDVAIAVIREVGVDTGGcNIQFAVDPRTgRMIVI 304
Cdd:PRK08463 216 DNYGNIIHLcerdCSIQR------RHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAG-TIEFLLDDYN-RFYFM 287
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1986616510 305 EMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDEIPNDI 345
Cdd:PRK08463 288 EMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQSDI 328
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
156-356 |
7.82e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 49.74 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 156 HTLAECLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQLRRIAGA----GLDASPTSEVLLEESILGWKEYELEVMRDRA 231
Cdd:PRK08462 141 KSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAaeseALSAFGDGTMYMEKFINNPRHIEVQILGDKH 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 232 DNVVIV----CSIENidpmgvHTGDSVTVAPAMTLTDREYQNMRDVAIAVIREVGVDTGGcNIQFAVDpRTGRMIVIEMN 307
Cdd:PRK08462 221 GNVIHVgerdCSLQR------RHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAG-TFEFLLD-SNLDFYFMEMN 292
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1986616510 308 PRVSRSSALASKATGFPIAKIAAKLAVGYTLDE----------IPNDITRETPASFEPS 356
Cdd:PRK08462 293 TRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSqesiklkghaIECRITAEDPKKFYPS 351
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
61-216 |
1.17e-05 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 48.98 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 61 ADATYVEPIT-PGIVEQIIARERPDALLPTLggqTALNTAvALHEagvLERYGVELV-GADIAAIQAgeNREqfkGIVAR 138
Cdd:PRK09288 53 AHRSHVIDMLdGDALRAVIEREKPDYIVPEI---EAIATD-ALVE---LEKEGFNVVpTARATRLTM--NRE---GIRRL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 139 VADRYGLNaeSARSAICHTLAECLTAADSLGYPVVVRPsfTMG--GAGSGFAHDEEQLRR-----IAGAGLDAsptSEVL 211
Cdd:PRK09288 121 AAEELGLP--TSPYRFADSLEELRAAVEEIGYPCVVKP--VMSssGKGQSVVRSPEDIEKaweyaQEGGRGGA---GRVI 193
|
....*
gi 1986616510 212 LEESI 216
Cdd:PRK09288 194 VEEFI 198
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
660-866 |
1.20e-05 |
|
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: 48.76 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 660 AGVPVVGTSPESIHLAEERGAFGRVLAEAGLPAPKhgTAVTVEQAreiaaeiGYPVLVRPSYVLGGAGMAIVYDEETLGA 739
Cdd:COG2232 95 RRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPE--TRFEPPPD-------PGPWLVKPIGGAGGWHIRPADSEAPPAP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 740 ymaragaasdhpvlvDRFLDEAIE---IDVDALYDGEELYLGGVMEHIEEAGIHSGDSAC-ALPPITLGGFDIKRIRAAT 815
Cdd:COG2232 166 ---------------GRYFQRYVEgtpASVLFLADGSDARVLGFNRQLIGPAGERPFRYGgNIGPLALPPALAEEMRAIA 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1986616510 816 EAIARGVGVRGLLNVQYAVAAGVLYVLEANPRASRTVPFVSKATAVPLAKA 866
Cdd:COG2232 231 EALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDA 281
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
651-775 |
1.62e-05 |
|
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: 47.73 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 651 LGLAQALKDAGVPVVgTSPESIHLAEERGAFGRVLAEAGLPAPKHGTAVTVEQAREIAAEIGYPVLVRPSYVLGGAGMAI 730
Cdd:TIGR00768 63 LAVLRYLESLGVPVI-NSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSL 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1986616510 731 VYDEETLGAYMA--RAGAASDHPVLVDRFLDEAIEIDVDALYDGEEL 775
Cdd:TIGR00768 142 ARDRQAAESLLEhfEQLNGPQNLFLVQEYIKKPGGRDIRVFVVGDEV 188
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
683-758 |
3.36e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 47.84 E-value: 3.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1986616510 683 RVLAEAGLPAPKHGTAVTVEQAREIAAEIGYPVLVRPSYVLGGAGMAI-VYDEETLGAYMARAGAASDHpVLVDRFL 758
Cdd:PRK14016 220 RLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESSD-VIVERYI 295
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
683-847 |
5.87e-05 |
|
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: 44.68 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 683 RVLAEAGLPAPKHGTAvtveqarEIAAEIGYPVLVRPsyVLGGAGMAIVYDEEtlgaymARAGAASDHPVLVDRFLdEAI 762
Cdd:pfam02655 9 KALKNAGVPTPETLQA-------EELLREEKKYVVKP--RDGCGGEGVRKVEN------GREDEAFIENVLVQEFI-EGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 763 EIDVDALYDGEELYLGGV-MEHIEEAGIHSGDSACALP-PITLGGfdiKRIRAATEAIARGVGVRGLLNVQYAVAAGVLY 840
Cdd:pfam02655 73 PLSVSLLSDGEKALPLSVnRQYIDNGGSGFVYAGNVTPsRTELKE---EIIELAEEVVECLPGLRGYVGVDLVLKDNEPY 149
|
....*..
gi 1986616510 841 VLEANPR 847
Cdd:pfam02655 150 VIEVNPR 156
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
66-327 |
7.16e-05 |
|
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: 46.09 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 66 VEPITPGIVEQIIARERP----------DALLPTlggQTALNTAVALHEAgvLERYGVELVGaDIAAIQAGENreqfKGI 135
Cdd:COG0189 30 VEVIDPDDLTLDLGRAPElyrgedlsefDAVLPR---IDPPFYGLALLRQ--LEAAGVPVVN-DPEAIRRARD----KLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 136 VARVADRYGLNAesARSAICHTLAECLTAADSLGYPVVVRPSFTMGGAGSGFAHDEEQLRRIAgAGLDASPTSEVLLEES 215
Cdd:COG0189 100 TLQLLARAGIPV--PPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESIL-EALTELGSEPVLVQEF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 216 ILGWKEYELEVMrdradnVV---IVCSIeNIDPMG------VHTGDSVTvapAMTLTDREyqnmRDVAIAVIREVGVDTG 286
Cdd:COG0189 177 IPEEDGRDIRVL------VVggePVAAI-RRIPAEgefrtnLARGGRAE---PVELTDEE----RELALRAAPALGLDFA 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1986616510 287 GcnIQFAVDPrtGRMIVIEMNPrvsrSSALA--SKATGFPIAK 327
Cdd:COG0189 243 G--VDLIEDD--DGPLVLEVNV----TPGFRglERATGVDIAE 277
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
684-846 |
1.18e-04 |
|
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: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 684 VLAEAGLPAPKHgtaVTVEQA----------REIAAEIGYPVLVRPSyVLGGA-GMAIVYDEETLGAYMARAGaASDHPV 752
Cdd:pfam07478 1 LLKAAGLPVVPF---VTFTRAdwklnpkewcAQVEEALGYPVFVKPA-RLGSSvGVSKVESREELQAAIEEAF-QYDEKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 753 LVDRFLdEAIEIDVdALYDGEELYLGGVMEHIEEAGI------HSGDSACALPPITLGGFDIKRIRAATEAIARGVGVRG 826
Cdd:pfam07478 76 LVEEGI-EGREIEC-AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRG 153
|
170 180
....*....|....*....|.
gi 1986616510 827 LLNVQYAV-AAGVLYVLEANP 846
Cdd:pfam07478 154 LARVDFFLtEDGEIVLNEVNT 174
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
653-737 |
4.88e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 43.94 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 653 LAQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLPAP--KHGTAVTVEQAREIAAEIGYPVLVRPSYVLGGAGMAI 730
Cdd:PRK07178 90 LAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTpgSEGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRR 169
|
....*..
gi 1986616510 731 VYDEETL 737
Cdd:PRK07178 170 CNSREEL 176
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
642-773 |
5.07e-04 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 43.96 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 642 IVQLGGQTPL--GLAQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLPAPKHGTAVTVEQAREIAAEIGYPVLVRP 719
Cdd:PLN02257 65 LVVVGPEAPLvaGLADDLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKA 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1986616510 720 SYVLGGAGMAIVYDEETlgAYMA--------RAGAASDHpVLVDRFLDEAiEIDVDALYDGE 773
Cdd:PLN02257 145 DGLAAGKGVVVAMTLEE--AYEAvdsmlvkgAFGSAGSE-VVVEEFLDGE-EASFFALVDGE 202
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
956-998 |
7.32e-04 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 43.48 E-value: 7.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1986616510 956 RAFVSVAnrDKRAMIFPVKALADLGFEILATEGTAEVLRRNGV 998
Cdd:COG0138 5 RALISVS--DKTGLVEFARALVELGVEIISTGGTAKALREAGI 45
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
654-737 |
1.12e-03 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 42.88 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 654 AQALKDAGVPVVGTSPESIHLAEERGAFGRVLAEAGLP-APkhGT----AVTVEQAREIAAEIGYPVLVRPSYVLGGAGM 728
Cdd:PRK08463 91 AKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPiVP--GTeklnSESMEEIKIFARKIGYPVILKASGGGGGRGI 168
|
....*....
gi 1986616510 729 AIVYDEETL 737
Cdd:PRK08463 169 RVVHKEEDL 177
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
683-717 |
1.20e-03 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 42.35 E-value: 1.20e-03
10 20 30
....*....|....*....|....*....|....*
gi 1986616510 683 RVLAEAGLPAPKHGTAVTVEQAREIAAEIGYPVLV 717
Cdd:COG0045 10 ELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVV 44
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
956-998 |
1.78e-03 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 42.38 E-value: 1.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1986616510 956 RAFVSVAnrDKRAMIFPVKALADLGFEILATEGTAEVLRRNGV 998
Cdd:PRK00881 6 RALISVS--DKTGIVEFAKALVELGVEILSTGGTAKLLAEAGI 46
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
145-310 |
7.07e-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: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 145 LNAESARSAICHTLAECLTAADSLGYPVVVRPSfTMG--GAGSGFAHDEEQLrRIAGAGLDASPtseVLLEESILgwKEY 222
Cdd:pfam02222 3 LGLPTPRFMAAESLEELIEAGQELGYPCVVKAR-RGGydGKGQYVVRSEADL-PQAWEELGDGP---VIVEEFVP--FDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986616510 223 ELEVMRDRADNVVIVC--SIENIDpmgvHTGDSVT-VAPAmTLTDREYQNMRDVAIAVIREVgvdtGGCNIqFAVD---P 296
Cdd:pfam02222 76 ELSVLVVRSVDGETAFypVVETIQ----EDGICRLsVAPA-RVPQAIQAEAQDIAKRLVDEL----GGVGV-FGVElfvT 145
|
170
....*....|....
gi 1986616510 297 RTGRMIVIEMNPRV 310
Cdd:pfam02222 146 EDGDLLINELAPRP 159
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
674-715 |
8.55e-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: 39.00 E-value: 8.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1986616510 674 LAEERGAFG-----RVLAEAGLPAPKHGTAVTVEQAREIAAEIGYPV 715
Cdd:pfam13549 3 LAEGRTVLTepeakALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPV 49
|
|
| |
