|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1161 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2082.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1 MPKRQDIKSILIIGAGPIVIGQACEFDYSGTQACKALREEGYRVILVNSNPATIMTDPGLADATYVEPITPEVVAKIIAK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 81 ERPDALLPTMGGQTALNTALSLKRMGVLDRYNVEMIGAKPAAIDMAEDRALFREAMARIGLETPRSMLAnatdikdadrk 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIA----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 161 theaersklkaslsgaaldkaldelenqwnlgesdrkqrymsHAMAIAAQAIDHVGLPAIIRPSFTLGGTGGGIAYNRSE 240
Cdd:PRK05294 150 ------------------------------------------HSMEEALEVAEEIGYPVIIRPSFTLGGTGGGIAYNEEE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 241 FFEIVGGGLDASPTTEVLVEESVLGWKEFEMEVVRDKADNCIIICSIENIDPMGVHTGDSITVAPALTLTDKEYQIMRNA 320
Cdd:PRK05294 188 LEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDSITVAPAQTLTDKEYQMLRDA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 321 SIAVLREIGVETGGSNVQFAVNPKDGRLVVIEMNPRVSRSSALASKATGFPIAKVAAKLAIGYTLDELENDITgGATPAS 400
Cdd:PRK05294 268 SIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDEIKNDIT-GKTPAS 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 401 FEPSIDYVVTKIPRFAFEKFPGASPVLTTAMKSVGEVMAIGRTFAESLQKALRGLETGLTGLDEIeipgtEEGEGNRNAI 480
Cdd:PRK05294 347 FEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDED-----LFEEESLEEL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 481 RAAIGTPTPDRLRMVAQALRLGLTAEEVHEGCKIDPWFIAQLKSIVDMEARIREHGLPEDATNLRMLKAMGFSDARLATL 560
Cdd:PRK05294 422 REELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLREAKRLGFSDARIAKL 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 561 TDKRPKEVAELRNSLNVRPVFKRIDTCAAEFASPTAYMYSTYEtpfvgaARSEAQVSDRKKVVILGGGPNRIGQGIEFDY 640
Cdd:PRK05294 502 LGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYE------EECESNPSDRKKVLVLGSGPNRIGQGIEFDY 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 641 CCCHAAFALKDAGYEAIMINCNPETVSTDYDTSDRLYFEPLTAEDVIEILRAEQEngelVGVIVQFGGQTPLKLAEALEK 720
Cdd:PRK05294 576 CCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKP----KGVIVQFGGQTPLKLAKALEA 651
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 721 NGIPILGTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAMQIIHSEGMLQT 800
Cdd:PRK05294 652 AGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELER 731
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 801 YLLDTVpelvpedikqrypndktgqinTLLGKNPLLFDSYLANAIEVDVDCLSDGTDVYVAGIMEHIEEAGIHSGDSACS 880
Cdd:PRK05294 732 YMREAV---------------------KVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACS 790
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 881 LPPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAIKDGTVYVLEVNPRASRTVPFVAKTIGAPIAKIAARVMAGEKLD 960
Cdd:PRK05294 791 LPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLA 870
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 961 AVFAAYGEKPdprklKHIAVKEAVFPFARFPGVDILLGPEMRSTGEVIGLDTDFALAFAKSQLGAGVELPRDGTVFVSVR 1040
Cdd:PRK05294 871 ELGYTKGLIP-----PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVR 945
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1041 DDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLEGRPHIEDAIRNRQVQLVINTTDSNKAISDSKSLR 1120
Cdd:PRK05294 946 DRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINTPTGRQAIRDGFSIR 1025
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|.
gi 494975558 1121 RATLMQKVPYYTTMAGAEAAAMAIKALKAGNLEVRTLQSYF 1161
Cdd:PRK05294 1026 RAALEYKVPYITTLAGARAAVKAIEALKFGELEVRSLQEYH 1066
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1133 |
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: 1568.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 2 PKRQDIKSILIIGAGPIVIGQACEFDYSGTQACKALREEGYRVILVNSNPATIMTDPGLADATYVEPITPEVVAKIIAKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 82 RPDALLPTMGGQTALNTALSLKRMGVLDRYNVEMIGAKPAAIDMAEDRALFREAMARIGLETPRSmlanatdikdadrkt 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 162 heaersklkaslsgaaldkaldelenqwnlgesdrkqrYMSHAMAIAAQAIDHVGLPAIIRPSFTLGGTGGGIAYNRSEF 241
Cdd:TIGR01369 146 --------------------------------------EIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREEL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 242 FEIVGGGLDASPTTEVLVEESVLGWKEFEMEVVRDKADNCIIICSIENIDPMGVHTGDSITVAPALTLTDKEYQIMRNAS 321
Cdd:TIGR01369 188 KEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGDSIVVAPSQTLTDKEYQMLRDAS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 322 IAVLREIGVEtGGSNVQFAVNPKDGRLVVIEMNPRVSRSSALASKATGFPIAKVAAKLAIGYTLDELENDITGGaTPASF 401
Cdd:TIGR01369 268 IKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDELKNPVTGT-TPASF 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 402 EPSIDYVVTKIPRFAFEKFPGASPVLTTAMKSVGEVMAIGRTFAESLQKALRGLETGLTGLDEIEIPGTEEGEGNRnair 481
Cdd:TIGR01369 346 EPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDLPDREVEPDEDLWR---- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 482 aAIGTPTPDRLRMVAQALRLGLTAEEVHEGCKIDPWFIAQLKSIVDMEARIREHGLPE-DATNLRMLKAMGFSDARLATL 560
Cdd:TIGR01369 422 -ALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDlDPELLRRAKKLGFSDAQIARL 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 561 TDKRPKEVAELRNSLNVRPVFKRIDTCAAEFASPTAYMYSTYEtpfvgAARSEAQVSDRKKVVILGGGPNRIGQGIEFDY 640
Cdd:TIGR01369 501 IGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYE-----GERDDVPFTDKKKVLVLGSGPNRIGQGVEFDY 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 641 CCCHAAFALKDAGYEAIMINCNPETVSTDYDTSDRLYFEPLTAEDVIEILRAEQengeLVGVIVQFGGQTPLKLAEALEK 720
Cdd:TIGR01369 576 CCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEK----PEGVIVQFGGQTPLNLAKALEE 651
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 721 NGIPILGTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAMQIIHSEGMLQT 800
Cdd:TIGR01369 652 AGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRR 731
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 801 YLLDTVpELVPEdikqrypndktgqintllgkNPLLFDSYLANAIEVDVDCLSDGTDVYVAGIMEHIEEAGIHSGDSACS 880
Cdd:TIGR01369 732 YLEEAV-AVSPE--------------------HPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCV 790
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 881 LPPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAIKDGTVYVLEVNPRASRTVPFVAKTIGAPIAKIAARVMAGEKLD 960
Cdd:TIGR01369 791 LPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLE 870
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 961 AVfaAYGEKPDPrklKHIAVKEAVFPFARFPGVDILLGPEMRSTGEVIGLDTDFALAFAKSQLGAGVELPRDGTVFVSVR 1040
Cdd:TIGR01369 871 EL--GVGKEKEP---KYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVR 945
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1041 DDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLEGRPHIEDAIRNRQVQLVINTTD-SNKAISDSKSL 1119
Cdd:TIGR01369 946 DKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTSkGAGTATDGYKI 1025
|
1130
....*....|....
gi 494975558 1120 RRATLMQKVPYYTT 1133
Cdd:TIGR01369 1026 RREALDYGVPLITT 1039
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
625-1161 |
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: 722.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 625 LGGGPNRIGQGIEFDYCCCHAAFALKDAGYEAIMINCNPETVSTDYDTSDRLYFEPLTAEDVIEILRAEQENGelvgVIV 704
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDG----VIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 705 QFGGQTPLKLAEALEKN----GIPILGTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGFPLVVRP 780
Cdd:COG0458 77 QFGGQTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 781 SYVLGGRAMQIIHSEGMLQTYLLDTVpelvpedikqrypndktgqinTLLGKNPLLFDSYLANAIEVDVDCLSDGTD-VY 859
Cdd:COG0458 157 SYVLGGRGMGIVYNEEELEEYLERAL---------------------KVSPDHPVLIDESLLGAKEIEVDVVRDGEDnVI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 860 VAGIMEHIEEAGIHSGDSACSLPPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAIKDGTVYVLEVNPRASRTVPFVA 939
Cdd:COG0458 216 IVGIMEHIEPAGVHSGDSICVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFAS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 940 KTIGAPIAKIAARVMAGEKLDAVFAAYGEKPdprKLKHIAVKEAVFPFARFPGVDILLGPEMRSTGEVIGLDTDFALAFA 1019
Cdd:COG0458 296 KATGYPIAKIAAKLALGYTLDELGNDTGFEP---TLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1020 KSQLGAGVELPrdGTVFVS-VRDDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLEGRPHIEDAIRNR 1098
Cdd:COG0458 373 KALRSLEIGLP--GTVLLSlVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELE 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494975558 1099 QVQLVINTTDSNKAISDSKSLRRATLMQKVPYYTTMAGAEAAAMAIKALKAGNLEVRTLQSYF 1161
Cdd:COG0458 451 EIILVINTLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYY 513
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-386 |
2.13e-72 |
|
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: 239.51 E-value: 2.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 128 DRALFREAMARIGLETPRSMlanatdikdadrktheaersklkaslsgAALDKALDElenqwnlgesdrkqrymshAMAI 207
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGT----------------------------AGPVETEEE-------------------ALAA 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 208 AAQaidhVGLPAIIRPSFTLGGTGGGIAYNRSEFFEIVGGGLDASPTT----EVLVEESVLGWKEFEMEVVRDKADNCII 283
Cdd:pfam02786 34 AKE----IGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAfgnpQVLVEKSLKGPKHIEYQVLRDAHGNCIT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 284 ICSIENIDPMgvHTGDSITVAPALTLTDKEYQIMRNASIAVLREIGVETGGsNVQFAVNPKDGRLVVIEMNPRVSRSSAL 363
Cdd:pfam02786 110 VCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG-TVEFALDPFSGEYYFIEMNTRLQVEHAL 186
|
250 260
....*....|....*....|...
gi 494975558 364 ASKATGFPIAKVAAKLAIGYTLD 386
Cdd:pfam02786 187 AEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
480-602 |
2.63e-57 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 193.43 E-value: 2.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 480 IRAAIGTPTPDRLRMVAQALRLGLTAEEVHEGCKIDPWFIAQLKSIVDMEARIREHGLPE-DATNLRMLKAMGFSDARLA 558
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDElDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 494975558 559 TLTDKRPKEVAELRNSLNVRPVFKRIDTCAAEFASPTAYMYSTY 602
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
1033-1133 |
2.57e-46 |
|
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: 161.49 E-value: 2.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1033 GTVFVSVRDDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLEGRPHIEDAIRNRQVQLVINTTDSNKA 1112
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKRA 80
|
90 100
....*....|....*....|.
gi 494975558 1113 ISDSKSLRRATLMQKVPYYTT 1133
Cdd:cd01424 81 IRDGFSIRRAALEYKVPYFTT 101
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1161 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2082.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1 MPKRQDIKSILIIGAGPIVIGQACEFDYSGTQACKALREEGYRVILVNSNPATIMTDPGLADATYVEPITPEVVAKIIAK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 81 ERPDALLPTMGGQTALNTALSLKRMGVLDRYNVEMIGAKPAAIDMAEDRALFREAMARIGLETPRSMLAnatdikdadrk 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIA----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 161 theaersklkaslsgaaldkaldelenqwnlgesdrkqrymsHAMAIAAQAIDHVGLPAIIRPSFTLGGTGGGIAYNRSE 240
Cdd:PRK05294 150 ------------------------------------------HSMEEALEVAEEIGYPVIIRPSFTLGGTGGGIAYNEEE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 241 FFEIVGGGLDASPTTEVLVEESVLGWKEFEMEVVRDKADNCIIICSIENIDPMGVHTGDSITVAPALTLTDKEYQIMRNA 320
Cdd:PRK05294 188 LEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDSITVAPAQTLTDKEYQMLRDA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 321 SIAVLREIGVETGGSNVQFAVNPKDGRLVVIEMNPRVSRSSALASKATGFPIAKVAAKLAIGYTLDELENDITgGATPAS 400
Cdd:PRK05294 268 SIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDEIKNDIT-GKTPAS 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 401 FEPSIDYVVTKIPRFAFEKFPGASPVLTTAMKSVGEVMAIGRTFAESLQKALRGLETGLTGLDEIeipgtEEGEGNRNAI 480
Cdd:PRK05294 347 FEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDED-----LFEEESLEEL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 481 RAAIGTPTPDRLRMVAQALRLGLTAEEVHEGCKIDPWFIAQLKSIVDMEARIREHGLPEDATNLRMLKAMGFSDARLATL 560
Cdd:PRK05294 422 REELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLREAKRLGFSDARIAKL 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 561 TDKRPKEVAELRNSLNVRPVFKRIDTCAAEFASPTAYMYSTYEtpfvgaARSEAQVSDRKKVVILGGGPNRIGQGIEFDY 640
Cdd:PRK05294 502 LGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYE------EECESNPSDRKKVLVLGSGPNRIGQGIEFDY 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 641 CCCHAAFALKDAGYEAIMINCNPETVSTDYDTSDRLYFEPLTAEDVIEILRAEQEngelVGVIVQFGGQTPLKLAEALEK 720
Cdd:PRK05294 576 CCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKP----KGVIVQFGGQTPLKLAKALEA 651
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 721 NGIPILGTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAMQIIHSEGMLQT 800
Cdd:PRK05294 652 AGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELER 731
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 801 YLLDTVpelvpedikqrypndktgqinTLLGKNPLLFDSYLANAIEVDVDCLSDGTDVYVAGIMEHIEEAGIHSGDSACS 880
Cdd:PRK05294 732 YMREAV---------------------KVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACS 790
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 881 LPPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAIKDGTVYVLEVNPRASRTVPFVAKTIGAPIAKIAARVMAGEKLD 960
Cdd:PRK05294 791 LPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLA 870
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 961 AVFAAYGEKPdprklKHIAVKEAVFPFARFPGVDILLGPEMRSTGEVIGLDTDFALAFAKSQLGAGVELPRDGTVFVSVR 1040
Cdd:PRK05294 871 ELGYTKGLIP-----PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVR 945
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1041 DDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLEGRPHIEDAIRNRQVQLVINTTDSNKAISDSKSLR 1120
Cdd:PRK05294 946 DRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINTPTGRQAIRDGFSIR 1025
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|.
gi 494975558 1121 RATLMQKVPYYTTMAGAEAAAMAIKALKAGNLEVRTLQSYF 1161
Cdd:PRK05294 1026 RAALEYKVPYITTLAGARAAVKAIEALKFGELEVRSLQEYH 1066
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1133 |
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: 1568.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 2 PKRQDIKSILIIGAGPIVIGQACEFDYSGTQACKALREEGYRVILVNSNPATIMTDPGLADATYVEPITPEVVAKIIAKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 82 RPDALLPTMGGQTALNTALSLKRMGVLDRYNVEMIGAKPAAIDMAEDRALFREAMARIGLETPRSmlanatdikdadrkt 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 162 heaersklkaslsgaaldkaldelenqwnlgesdrkqrYMSHAMAIAAQAIDHVGLPAIIRPSFTLGGTGGGIAYNRSEF 241
Cdd:TIGR01369 146 --------------------------------------EIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREEL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 242 FEIVGGGLDASPTTEVLVEESVLGWKEFEMEVVRDKADNCIIICSIENIDPMGVHTGDSITVAPALTLTDKEYQIMRNAS 321
Cdd:TIGR01369 188 KEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGDSIVVAPSQTLTDKEYQMLRDAS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 322 IAVLREIGVEtGGSNVQFAVNPKDGRLVVIEMNPRVSRSSALASKATGFPIAKVAAKLAIGYTLDELENDITGGaTPASF 401
Cdd:TIGR01369 268 IKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDELKNPVTGT-TPASF 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 402 EPSIDYVVTKIPRFAFEKFPGASPVLTTAMKSVGEVMAIGRTFAESLQKALRGLETGLTGLDEIEIPGTEEGEGNRnair 481
Cdd:TIGR01369 346 EPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDLPDREVEPDEDLWR---- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 482 aAIGTPTPDRLRMVAQALRLGLTAEEVHEGCKIDPWFIAQLKSIVDMEARIREHGLPE-DATNLRMLKAMGFSDARLATL 560
Cdd:TIGR01369 422 -ALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDlDPELLRRAKKLGFSDAQIARL 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 561 TDKRPKEVAELRNSLNVRPVFKRIDTCAAEFASPTAYMYSTYEtpfvgAARSEAQVSDRKKVVILGGGPNRIGQGIEFDY 640
Cdd:TIGR01369 501 IGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYE-----GERDDVPFTDKKKVLVLGSGPNRIGQGVEFDY 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 641 CCCHAAFALKDAGYEAIMINCNPETVSTDYDTSDRLYFEPLTAEDVIEILRAEQengeLVGVIVQFGGQTPLKLAEALEK 720
Cdd:TIGR01369 576 CCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEK----PEGVIVQFGGQTPLNLAKALEE 651
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 721 NGIPILGTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAMQIIHSEGMLQT 800
Cdd:TIGR01369 652 AGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRR 731
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 801 YLLDTVpELVPEdikqrypndktgqintllgkNPLLFDSYLANAIEVDVDCLSDGTDVYVAGIMEHIEEAGIHSGDSACS 880
Cdd:TIGR01369 732 YLEEAV-AVSPE--------------------HPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCV 790
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 881 LPPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAIKDGTVYVLEVNPRASRTVPFVAKTIGAPIAKIAARVMAGEKLD 960
Cdd:TIGR01369 791 LPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLE 870
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 961 AVfaAYGEKPDPrklKHIAVKEAVFPFARFPGVDILLGPEMRSTGEVIGLDTDFALAFAKSQLGAGVELPRDGTVFVSVR 1040
Cdd:TIGR01369 871 EL--GVGKEKEP---KYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVR 945
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1041 DDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLEGRPHIEDAIRNRQVQLVINTTD-SNKAISDSKSL 1119
Cdd:TIGR01369 946 DKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTSkGAGTATDGYKI 1025
|
1130
....*....|....
gi 494975558 1120 RRATLMQKVPYYTT 1133
Cdd:TIGR01369 1026 RREALDYGVPLITT 1039
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1161 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1448.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 3 KRQDIKSILIIGAGPIVIGQACEFDYSGTQACKALREEGYRVILVNSNPATIMTDPGLADATYVEPITPEVVAKIIAKER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 83 PDALLPTMGGQTALNTALSLKRMGVLDRYNVEMIGAKPAAIDMAEDRALFREAMARIGLETPRSMLANAtdikdadrkth 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATT----------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 163 eaersklkaslsgaaldkaLDElenqwnlgesdrkqrymshAMAIAAQaidhVG-LPAIIRPSFTLGGTGGGIAYNRSEF 241
Cdd:PLN02735 168 -------------------LDE-------------------CFEIAED----IGeFPLIIRPAFTLGGTGGGIAYNKEEF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 242 FEIVGGGLDASPTTEVLVEESVLGWKEFEMEVVRDKADNCIIICSIENIDPMGVHTGDSITVAPALTLTDKEYQIMRNAS 321
Cdd:PLN02735 206 ETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 322 IAVLREIGVETGGSNVQFAVNPKDGRLVVIEMNPRVSRSSALASKATGFPIAKVAAKLAIGYTLDELENDITgGATPASF 401
Cdd:PLN02735 286 VAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDIT-LKTPASF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 402 EPSIDYVVTKIPRFAFEKFPGASPVLTTAMKSVGEVMAIGRTFAESLQKALRGLETGLTGLDeieIPGTEEGEGNRNAIR 481
Cdd:PLN02735 365 EPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETGFSGWG---CAKVKELDWDWEQLK 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 482 AAIGTPTPDRLRMVAQALRLGLTAEEVHEGCKIDPWFIAQLKSIVDMEARIREHGLPE-DATNLRMLKAMGFSDARLATL 560
Cdd:PLN02735 442 YKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLSElSKDDFYEVKRRGFSDKQIAFA 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 561 TDKRPKEVAELRNSLNVRPVFKRIDTCAAEFASPTAYMYSTYEtpfvgaARSEAQVSDRKKVVILGGGPNRIGQGIEFDY 640
Cdd:PLN02735 522 TKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYD------GECESAPTNKKKVLILGGGPNRIGQGIEFDY 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 641 CCCHAAFALKDAGYEAIMINCNPETVSTDYDTSDRLYFEPLTAEDVIEILRAEQENgelvGVIVQFGGQTPLKLA----E 716
Cdd:PLN02735 596 CCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPD----GIIVQFGGQTPLKLAlpiqK 671
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 717 ALEKNGIP---------ILGTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGFPLVVRPSYVLGGR 787
Cdd:PLN02735 672 YLDKNPPPsasgngnvkIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYPVVVRPSYVLGGR 751
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 788 AMQIIHSEGMLQTYLLDTVpELVPEdikqrypndktgqintllgkNPLLFDSYLANAIEVDVDCLSDGT-DVYVAGIMEH 866
Cdd:PLN02735 752 AMEIVYSDDKLKTYLETAV-EVDPE--------------------RPVLVDKYLSDATEIDVDALADSEgNVVIGGIMEH 810
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 867 IEEAGIHSGDSACSLPPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAI-KDGTVYVLEVNPRASRTVPFVAKTIGAP 945
Cdd:PLN02735 811 IEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRTVPFVSKAIGHP 890
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 946 IAKIAARVMAGEKLDAVfaAYGEKPDPRklkHIAVKEAVFPFARFPGVDILLGPEMRSTGEVIGLDTDFALAFAKSQLGA 1025
Cdd:PLN02735 891 LAKYASLVMSGKSLKDL--GFTEEVIPA---HVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAA 965
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1026 GVELPRDGTVFVSVRDDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLEGRPHIEDAIRNRQVQLVIN 1105
Cdd:PLN02735 966 GQRLPLSGTVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGDMLANGQIQLMVI 1045
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*..
gi 494975558 1106 TTDSNKA-ISDSKSLRRATLMQKVPYYTTMAGAEAAAMAIKALKAGNLEVRTLQSYF 1161
Cdd:PLN02735 1046 TSSGDALdQKDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKECPIEMIALQDFF 1102
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1160 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1428.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1 MPKRQDIKSILIIGAGPIVIGQACEFDYSGTQACKALREEGYRVILVNSNPATIMTDPGLADATYVEPITPEVVAKIIAK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 81 ERPDALLPTMGGQTALNTALSLKRMGVLDRYNVEMIGAKPAAIDMAEDRALFREAMARIGLETPRSMLANatdikdadrK 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVT---------S 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 161 THEAERsklkaslsgaaldkaldelenqwnlgesdrkqrymshamaIAaqaiDHVGLPAIIRPSFTLGGTGGGIAYNRSE 240
Cdd:PRK12815 152 VEEALA----------------------------------------FA----EKIGFPIIVRPAYTLGGTGGGIAENLEE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 241 FFEIVGGGLDASPTTEVLVEESVLGWKEFEMEVVRDKADNCIIICSIENIDPMGVHTGDSITVAPALTLTDKEYQIMRNA 320
Cdd:PRK12815 188 LEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDSIVVAPSQTLTDDEYQMLRSA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 321 SIAVLREIGVeTGGSNVQFAVNPKDGRLVVIEMNPRVSRSSALASKATGFPIAKVAAKLAIGYTLDELENDITgGATPAS 400
Cdd:PRK12815 268 SLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAVGYTLNELKNPVT-GLTYAS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 401 FEPSIDYVVTKIPRFAFEKFPGASPVLTTAMKSVGEVMAIGRTFAESLQKALRGLETGLTGLDEIeipgTEEGEGNRNAI 480
Cdd:PRK12815 346 FEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGLSLP----IELSGKSDEEL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 481 RAAIGTPTPDRLRMVAQALRLGLTAEEVHEGCKIDPWFIAQLKSIVDMEARIREHGLPEDATNLRMLKAMGFSDARLATL 560
Cdd:PRK12815 422 LQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLDLSADLLRKVKEKGFSDALLAEL 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 561 TDKRPKEVAELRNSLNVRPVFKRIDTCAAEFASPTAYMYSTYETpfvgaaRSEAQVS-DRKKVVILGGGPNRIGQGIEFD 639
Cdd:PRK12815 502 TGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFG------ESEAEPSsEKKKVLILGSGPIRIGQGIEFD 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 640 YCCCHAAFALKDAGYEAIMINCNPETVSTDYDTSDRLYFEPLTAEDVIEIlrAEQENGElvGVIVQFGGQTPLKLAEALE 719
Cdd:PRK12815 576 YSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNV--AEAENIK--GVIVQFGGQTAINLAKGLE 651
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 720 KNGIPILGTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAMQIIHSEGMLQ 799
Cdd:PRK12815 652 EAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALE 731
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 800 TYLldtvpelvPEDIKQRYpndktgqintllgknPLLFDSYLaNAIEVDVDCLSDGTDVYVAGIMEHIEEAGIHSGDSAC 879
Cdd:PRK12815 732 AYL--------AENASQLY---------------PILIDQFI-DGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIA 787
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 880 SLPPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAIKDGTVYVLEVNPRASRTVPFVAKTIGAPIAKIAARVMAGEKL 959
Cdd:PRK12815 788 VLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSL 867
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 960 DAVFAAYGEKPDPrklKHIAVKEAVFPFARFPGVDILLGPEMRSTGEVIGLDTDFALAFAKSQLGAGVELPRDGTVFVSV 1039
Cdd:PRK12815 868 AELGYPNGLWPGS---PFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISV 944
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1040 RDDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLEGRPHIEDAIRNRQVQLVINTTDSNKAISDSKSL 1119
Cdd:PRK12815 945 RDEDKPEVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSPSLLERIKQHRIVLVVNTSLSDSASEDAIKI 1024
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|.
gi 494975558 1120 RRATLMQKVPYYTTMAGAEAAAMAIKALKAGNLEVRTLQSY 1160
Cdd:PRK12815 1025 RDEALSTHIPVFTELETAQAFLQVLESLALTTQPIQELQEK 1065
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
625-1161 |
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: 722.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 625 LGGGPNRIGQGIEFDYCCCHAAFALKDAGYEAIMINCNPETVSTDYDTSDRLYFEPLTAEDVIEILRAEQENGelvgVIV 704
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDG----VIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 705 QFGGQTPLKLAEALEKN----GIPILGTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGFPLVVRP 780
Cdd:COG0458 77 QFGGQTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 781 SYVLGGRAMQIIHSEGMLQTYLLDTVpelvpedikqrypndktgqinTLLGKNPLLFDSYLANAIEVDVDCLSDGTD-VY 859
Cdd:COG0458 157 SYVLGGRGMGIVYNEEELEEYLERAL---------------------KVSPDHPVLIDESLLGAKEIEVDVVRDGEDnVI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 860 VAGIMEHIEEAGIHSGDSACSLPPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAIKDGTVYVLEVNPRASRTVPFVA 939
Cdd:COG0458 216 IVGIMEHIEPAGVHSGDSICVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFAS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 940 KTIGAPIAKIAARVMAGEKLDAVFAAYGEKPdprKLKHIAVKEAVFPFARFPGVDILLGPEMRSTGEVIGLDTDFALAFA 1019
Cdd:COG0458 296 KATGYPIAKIAAKLALGYTLDELGNDTGFEP---TLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1020 KSQLGAGVELPrdGTVFVS-VRDDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLEGRPHIEDAIRNR 1098
Cdd:COG0458 373 KALRSLEIGLP--GTVLLSlVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELE 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494975558 1099 QVQLVINTTDSNKAISDSKSLRRATLMQKVPYYTTMAGAEAAAMAIKALKAGNLEVRTLQSYF 1161
Cdd:COG0458 451 EIILVINTLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYY 513
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-627 |
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: 715.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 13 IGAGPIVIGQACEFDYSGTQACKALREEGYRVILVNSNPATIMTDPGLADATYVEPITPEVVAKIIAKERPDALLPTMGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 93 QTALNTALSLKRMGVLDryNVEMIGAKPAAIDMAEDRALFREAMARIGLETPRSMLANAtdikdadrktheaersklkas 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATS--------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 173 lsgaaldkaLDElenqwnlgesdrkqrymshAMAIAaqaiDHVGLPAIIRPSFTLGGTGGGIAYNRSEFFEIVGGGLDAS 252
Cdd:COG0458 138 ---------VEE-------------------ALAIA----EEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLERALKVS 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 253 PTTEVLVEESVLGWKEFEMEVVRDKADNCIIICSIENIDPMGVHTGDSITVAPALTLTDKEYQIMRNASIAVLREIGVEt 332
Cdd:COG0458 186 PDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQTLSDKEYQRLRDATLKIARALGVV- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 333 GGSNVQFAVnpKDGRLVVIEMNPRVSRSSALASKATGFPIAKVAAKLAIGYTLDELENDiTGgatpasFEPSIDYVVTKI 412
Cdd:COG0458 265 GLCNIQFAV--DDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGND-TG------FEPTLDYVVVKE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 413 PRFAFEKFPGASPVLTTAMKSVGEVMAIGRTFAESLQKALRGLETGLTG--LDEIEIPGTEEgegnrnaiRAAIGTPTPD 490
Cdd:COG0458 336 PVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSLVADDDKE--------EALLLARRLA 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 491 RLRMVAQALRLGLTAEEVHEGCKIDPWFIAQLKSIVDMEARIREHGLpeDATNLRMLKAMGFSDARLATLTDKRPKEVAE 570
Cdd:COG0458 408 RLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIIL--VINTLLGAKSLGDSDGIIRRALAAKVPYVTT 485
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 494975558 571 LRNSLNVRPVFKRIDTCAAEFASPTAYMYSTYETpfvgaaRSEAQVSDRKKVVILGG 627
Cdd:COG0458 486 LAAAAAAALAIKAVETEAGEFEEATAYYYSTYEY------ENESEETEEPKVVVIGS 536
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-386 |
2.13e-72 |
|
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: 239.51 E-value: 2.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 128 DRALFREAMARIGLETPRSMlanatdikdadrktheaersklkaslsgAALDKALDElenqwnlgesdrkqrymshAMAI 207
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGT----------------------------AGPVETEEE-------------------ALAA 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 208 AAQaidhVGLPAIIRPSFTLGGTGGGIAYNRSEFFEIVGGGLDASPTT----EVLVEESVLGWKEFEMEVVRDKADNCII 283
Cdd:pfam02786 34 AKE----IGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAfgnpQVLVEKSLKGPKHIEYQVLRDAHGNCIT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 284 ICSIENIDPMgvHTGDSITVAPALTLTDKEYQIMRNASIAVLREIGVETGGsNVQFAVNPKDGRLVVIEMNPRVSRSSAL 363
Cdd:pfam02786 110 VCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG-TVEFALDPFSGEYYFIEMNTRLQVEHAL 186
|
250 260
....*....|....*....|...
gi 494975558 364 ASKATGFPIAKVAAKLAIGYTLD 386
Cdd:pfam02786 187 AEKATGYDLAKEAAKIALGYPLP 209
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
600-1021 |
1.16e-58 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 220.81 E-value: 1.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 600 STYETPFVGAARSEAQVSDRKKVVILGGGPNRIGQGIEFDYCCCHAAFALKDAGYEAIMINCNPETVSTDYDTSDRLYFE 679
Cdd:PLN02735 4 ADTVTRAWSAATKAGKRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 680 PLTAEDVIEILRAEQENgelvGVIVQFGGQTPLKLAEA------LEKNGIPILGTAPDAIDLAEDRDRFQKLLMKLDLNQ 753
Cdd:PLN02735 84 PMTPELVEQVIAKERPD----ALLPTMGGQTALNLAVAlaesgiLEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 754 PNNGIAYSVEQARLVASEIG-FPLVVRPSYVLGGRAMQIIHSEGMLQTYlldtvpelvpedIKQRYPNDKTGQIntLLGK 832
Cdd:PLN02735 160 PPSGIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETI------------CKAGLAASITSQV--LVEK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 833 NPLLFDSYlanAIEVDVDcLSDgtDVYVAGIMEHIEEAGIHSGDSACSLPPRTLSPAMIDELERQAKAMAKALNV--GGl 910
Cdd:PLN02735 226 SLLGWKEY---ELEVMRD-LAD--NVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVecGG- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 911 MNVQFAI--KDGTVYVLEVNPRASRTVPFVAKTIGAPIAKIAARVMAGEKLDAVfaaygekPDPRKLK----------HI 978
Cdd:PLN02735 299 SNVQFAVnpVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTLDQI-------PNDITLKtpasfepsidYV 371
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 494975558 979 AVKEAVFPFARFPGVDILLGPEMRSTGEVIGLDTDFALAFAKS 1021
Cdd:PLN02735 372 VTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKA 414
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
480-602 |
2.63e-57 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 193.43 E-value: 2.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 480 IRAAIGTPTPDRLRMVAQALRLGLTAEEVHEGCKIDPWFIAQLKSIVDMEARIREHGLPE-DATNLRMLKAMGFSDARLA 558
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDElDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 494975558 559 TLTDKRPKEVAELRNSLNVRPVFKRIDTCAAEFASPTAYMYSTY 602
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
1033-1133 |
2.57e-46 |
|
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: 161.49 E-value: 2.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1033 GTVFVSVRDDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLEGRPHIEDAIRNRQVQLVINTTDSNKA 1112
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKRA 80
|
90 100
....*....|....*....|.
gi 494975558 1113 ISDSKSLRRATLMQKVPYYTT 1133
Cdd:cd01424 81 IRDGFSIRRAALEYKVPYFTT 101
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
482-560 |
6.19e-32 |
|
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: 119.02 E-value: 6.19e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494975558 482 AAIGTPTPDRLRMVAQALRLGLTAEEVHEGCKIDPWFIAQLKSIVDMEARIREHGLPEDATNLRMLKAMGFSDARLATL 560
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDAELLREAKRLGFSDRQIAKL 79
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
738-960 |
2.52e-26 |
|
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: 107.78 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 738 DRDRFQKLLMKLDLNQPNNGIAY--SVEQARLVASEIGFPLVVRPSYVLGGRAMQIIHSEgmlqtyllDTVPELVPEdik 815
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNE--------EELAELFAL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 816 qrypndKTGQINTLLGKNPLLFDSYLANAIEVDVDCLSDGTD-VYVAGIMEHIEEagIHSGDSACSLPPRTLSPAMIDEL 894
Cdd:pfam02786 70 ------ALAEAPAAFGNPQVLVEKSLKGPKHIEYQVLRDAHGnCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQML 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494975558 895 ERQAKAMAKALNVGGLMNVQFAI--KDGTVYVLEVNPRASRTVPFVAKTIGAPIAKIAARVMAGEKLD 960
Cdd:pfam02786 142 REAAVKIARHLGYVGAGTVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1046-1132 |
6.70e-25 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 99.47 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1046 RVLPAIRMLTELGFKVLATGGTQRYLAEQGIA--ATKINKVLEGRPHIEDAIRNRQVQLVINTTDSNKAIS--DSKSLRR 1121
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPvvKTLHPKVHGGIPQILDLIKNGEIDLVINTLYPFEAQAheDGYSIRR 80
|
90
....*....|.
gi 494975558 1122 ATLMQKVPYYT 1132
Cdd:smart00851 81 AAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1046-1132 |
1.93e-24 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 98.33 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1046 RVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATK-INKVLEGRPH----IEDAIRNRQVQLVINTTDSNKA-ISDSKSL 1119
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEvVEKTGEGRPGgrvqIGDLIKNGEIDLVINTLYPFKAtVHDGYAI 80
|
90
....*....|...
gi 494975558 1120 RRATLMQKVPYYT 1132
Cdd:pfam02142 81 RRAAENIDIPGPT 93
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
713-958 |
2.09e-18 |
|
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: 86.46 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 713 KLAEALeknGIPilGTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAMQII 792
Cdd:COG0439 34 ELAEEL---GLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 793 HSEGMLQTYLLDTVPELVPEDIKQRYpndktgqintllgknplLFDSYLANaIEVDVDCLSDGTDVYVAGIMEHIEEA-- 870
Cdd:COG0439 109 RDEEELEAALAEARAEAKAGSPNGEV-----------------LVEEFLEG-REYSVEGLVRDGEVVVCSITRKHQKPpy 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 871 GIHSGDSAcslpPRTLSPAMIDELERQAKAMAKALNVG-GLMNVQFAI-KDGTVYVLEVNPRAS--RTVPFVAKTIGAPI 946
Cdd:COG0439 171 FVELGHEA----PSPLPEELRAEIGELVARALRALGYRrGAFHTEFLLtPDGEPYLIEINARLGgeHIPPLTELATGVDL 246
|
250
....*....|..
gi 494975558 947 AKIAARVMAGEK 958
Cdd:COG0439 247 VREQIRLALGEP 258
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
72-382 |
2.36e-17 |
|
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: 83.38 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 72 EVVAKIIAKERPDALLPTmGGQTALNTALSLKRMGVldrynvemIGAKPAAIDMAEDRALFREAMARIGLETPRSMLana 151
Cdd:COG0439 7 AAAAELARETGIDAVLSE-SEFAVETAAELAEELGL--------PGPSPEAIRAMRDKVLMREALAAAGVPVPGFAL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 152 tdIKDADRktheaersklkaslsgaaldkaldelenqwnlgesdrkqrymshamaiAAQAIDHVGLPAIIRPSFTLGGTG 231
Cdd:COG0439 75 --VDSPEE------------------------------------------------ALAFAEEIGYPVVVKPADGAGSRG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 232 GGIAYNRSE----FFEIVGGGLDASPTTEVLVEESVLGwKEFEME-VVRDKAdncIIICSI---ENIDPMGVHTGDsitV 303
Cdd:COG0439 105 VRVVRDEEEleaaLAEARAEAKAGSPNGEVLVEEFLEG-REYSVEgLVRDGE---VVVCSItrkHQKPPYFVELGH---E 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 304 APALtLTDKEYQIMRNASIAVLREIGVETGGSNVQFAVNPkDGRLVVIEMNPRVS--RSSALASKATGFPIAKVAAKLAI 381
Cdd:COG0439 178 APSP-LPEELRAEIGELVARALRALGYRRGAFHTEFLLTP-DGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLAL 255
|
.
gi 494975558 382 G 382
Cdd:COG0439 256 G 256
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
1035-1133 |
3.35e-15 |
|
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: 72.93 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1035 VFVSVRDDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLE-GRPHIEDAIRNR-QVQLVINTTD---S 1109
Cdd:cd00532 2 VFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEdGEPTVDAAIAEKgKFDVVINLRDprrD 81
|
90 100
....*....|....*....|....
gi 494975558 1110 NKAISDSKSLRRATLMQKVPYYTT 1133
Cdd:cd00532 82 RCTDEDGTALLRLARLYKIPVTTP 105
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
713-960 |
4.25e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 73.09 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 713 KLAEALEKNGIPILGTAPDAIDLAEDRDRFQKLLMKLD---LNQPNNGIAySVEQARLVASEIGFPLVVRPSYVLGGRAM 789
Cdd:PRK08654 90 EFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGvpvLPGTEEGIE-DIEEAKEIAEEIGYPVIIKASAGGGGIGM 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 790 QIIHSEGMLQTYLLDTvpelvpEDIKQRYPNDKTGQIntllgknpllfDSYLANAIEVDVDCLSDgtdvyvagimehieE 869
Cdd:PRK08654 169 RVVYSEEELEDAIEST------QSIAQSAFGDSTVFI-----------EKYLEKPRHIEIQILAD--------------K 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 870 AG--IHSGDSACSLPPR-------TLSPAMIDELERQ----AKAMAKALNVGGLMNVQFAIKDGTVYVLEVNPRASRTVP 936
Cdd:PRK08654 218 HGnvIHLGDRECSIQRRhqklieeAPSPIMTPELRERmgeaAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHP 297
|
250 260
....*....|....*....|....
gi 494975558 937 FVAKTIGAPIAKIAARVMAGEKLD 960
Cdd:PRK08654 298 ITEMVTGIDIVKEQIKIAAGEELS 321
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1035-1132 |
7.50e-11 |
|
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: 60.39 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 1035 VFVSVRDDDKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKVLE----GRPHIEDAIRNRQVQLVINTTDSN 1110
Cdd:cd01423 3 ILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEepqnDKPSLRELLAEGKIDLVINLPSNR 82
|
90 100
....*....|....*....|....
gi 494975558 1111 KAISDSK--SLRRATLMQKVPYYT 1132
Cdd:cd01423 83 GKRVLDNdyVMRRAADDFAVPLIT 106
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
684-937 |
8.62e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 64.91 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 684 EDVIEILRAEQengelVGVIVQfGGQTPLKL----AEALEKNGIPILGTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIA 759
Cdd:PRK12767 59 DRLLDICKKEK-----IDLLIP-LIDPELPLlaqnRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 760 YSVEQ--ARLVASEIGFPLVVRPSYVLGGRAMQIIHSEGMLQTYLldtvpELVPEDIKQRYPNDKtgqintllgknpllf 837
Cdd:PRK12767 133 ESLEDfkAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLL-----EYVPNLIIQEFIEGQ--------------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 838 dsylanaiEVDVDCLSDGTDVYVAGI-MEHIEeagIHSGDSacslpprtlSPAMI---DELERQAKAMAKALNVGGLMNV 913
Cdd:PRK12767 193 --------EYTVDVLCDLNGEVISIVpRKRIE---VRAGET---------SKGVTvkdPELFKLAERLAEALGARGPLNI 252
|
250 260
....*....|....*....|....
gi 494975558 914 QFAIKDGTVYVLEVNPRASRTVPF 937
Cdd:PRK12767 253 QCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
621-1016 |
1.36e-10 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 64.56 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 621 KVVILGGGPNrigqgiefDYCCCHAafaLKDAGYEAIMINCNPETVSTDYDTSDRLYFEPLTAED---VIEILRAEQENG 697
Cdd:COG3919 7 RVVVLGGDIN--------ALAVARS---LGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGDDpeaFVDALLELAERH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 698 ElVGVIVQFGGQTPLKLA---EALEKNgIPILGTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGF 774
Cdd:COG3919 76 G-PDVLIPTGDEYVELLSrhrDELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 775 PLVVRPSYvlgGRAMQIIHSEGMLQTYLLDTVPELVpEDIKQRYPNDktgqintllgkNPLLFDSYL--ANAIEVDVDCL 852
Cdd:COG3919 154 PVVVKPAD---SVGYDELSFPGKKKVFYVDDREELL-ALLRRIAAAG-----------YELIVQEYIpgDDGEMRGLTAY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 853 SDGT-DVYVAGIMEHIEEAGIHSGDSACslpprtLSPAMIDELERQAKAMAKALNVGGLMNVQFAI--KDGTVYVLEVNP 929
Cdd:COG3919 219 VDRDgEVVATFTGRKLRHYPPAGGNSAA------RESVDDPELEEAARRLLEALGYHGFANVEFKRdpRDGEYKLIEINP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 930 RASRTVPFVAKTiGAPIAKIAARVMAGEKLDAVFAaygekPDPRKLKHIAVKEAVFPFARFPGVDILLGPEMRSTGEVig 1009
Cdd:COG3919 293 RFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPA-----YREGVLWRVLPGDLLLRYLRDGELRKRLRELLRRGKVV-- 364
|
....*..
gi 494975558 1010 lDTDFAL 1016
Cdd:COG3919 365 -DAVYAL 370
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
713-960 |
3.38e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 60.50 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 713 KLAEALEKNGIPILGTAPDAIDLAEDRDRFQKLLMKLDLnqP----NNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRA 788
Cdd:PRK05586 90 KFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGV--PvvpgSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 789 MQIIHSEgmlqtylldtvpelvpEDIKQRYPNDKTgQINTLLGKNPLLFDSYLANAIEVDVDCLSDGtdvyvagiMEHIe 868
Cdd:PRK05586 168 IRIVRSE----------------EELIKAFNTAKS-EAKAAFGDDSMYIEKFIENPKHIEFQILGDN--------YGNV- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 869 eagIHSGDSACSLPPR-------TLSPAMIDELERQ----AKAMAKALNVGGLMNVQFAI-KDGTVYVLEVNPRASRTVP 936
Cdd:PRK05586 222 ---VHLGERDCSLQRRnqkvleeAPSPVMTEELRKKmgeiAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHP 298
|
250 260
....*....|....*....|....
gi 494975558 937 FVAKTIGAPIAKIAARVMAGEKLD 960
Cdd:PRK05586 299 ITEMITGVDLVKEQIKIAYGEKLS 322
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
714-959 |
1.72e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 58.50 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 714 LAEALEKNGIPILGTAPDAIDLAEDrdrfqKLLMKLDLNQ--------PNNGIAySVEQARLVASEIGFPLVVRPSYVLG 785
Cdd:PRK06111 91 FAERCKEEGIVFIGPSADIIAKMGS-----KIEARRAMQAagvpvvpgITTNLE-DAEEAIAIARQIGYPVMLKASAGGG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 786 GRAMQIIHSEGMLQTYLldtvpelvpEDIKQRYPNdktgqintLLGKNPLLFDSYLANA--IEVDVDCLSDGTDVYVagi 863
Cdd:PRK06111 165 GIGMQLVETEQELTKAF---------ESNKKRAAN--------FFGNGEMYIEKYIEDPrhIEIQLLADTHGNTVYL--- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 864 mehieeagihsGDSACSL-----------PPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAI-KDGTVYVLEVNPRA 931
Cdd:PRK06111 225 -----------WERECSVqrrhqkvieeaPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVdEQKNFYFLEMNTRL 293
|
250 260
....*....|....*....|....*...
gi 494975558 932 SRTVPFVAKTIGAPIAKIAARVMAGEKL 959
Cdd:PRK06111 294 QVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
17-382 |
2.21e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 57.63 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 17 PIVIGqaceFDYSGTQACKALREEGYRVILVNSNPATIMT------------DPGLADATYVEpitpeVVAKIIAKERPD 84
Cdd:COG3919 8 VVVLG----GDINALAVARSLGEAGVRVIVVDRDPLGPAArsryvdevvvvpDPGDDPEAFVD-----ALLELAERHGPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 85 ALLPTMGGQTALntaLSLKRMGVLDRYNVEMIGAkpAAIDMAEDRALFREAMARIGLETPRSMLANATDikDADRkthea 164
Cdd:COG3919 79 VLIPTGDEYVEL---LSRHRDELEEHYRLPYPDA--DLLDRLLDKERFYELAEELGVPVPKTVVLDSAD--DLDA----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 165 ersklkaslsgaaldkaldelenqwnlgesdrkqrymshamaiaaqAIDHVGLPAIIRPS--------FTLGGTGGGIAY 236
Cdd:COG3919 147 ----------------------------------------------LAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVD 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 237 NRSEFFEIVGGGLDASptTEVLVEESVLGWKEfEMEVV---RDKADNCIIICSIENI--DPMGVHTGDSITVAPaltltD 311
Cdd:COG3919 181 DREELLALLRRIAAAG--YELIVQEYIPGDDG-EMRGLtayVDRDGEVVATFTGRKLrhYPPAGGNSAARESVD-----D 252
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494975558 312 KEyqiMRNASIAVLREIGVeTGGSNVQFAVNPKDGRLVVIEMNPRVSRSSALASKAtGFPIAKVAAKLAIG 382
Cdd:COG3919 253 PE---LEEAARRLLEALGY-HGFANVEFKRDPRDGEYKLIEINPRFWRSLYLATAA-GVNFPYLLYDDAVG 318
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
648-929 |
2.05e-07 |
|
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: 53.79 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 648 ALKDAGYEAIMINcnPETVSTDYDTSDRLY-FEPLTAEDVIeILRAEQENgelvgvivqfggqTPLKLAEALEKNGIPIL 726
Cdd:COG0189 22 AAQRRGHEVEVID--PDDLTLDLGRAPELYrGEDLSEFDAV-LPRIDPPF-------------YGLALLRQLEAAGVPVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 727 GTaPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAMQIIHSEGMLQTYLldtv 806
Cdd:COG0189 86 ND-PEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESIL---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 807 pelvpedikqrypndktgQINTLLGKNPLLFDSYLANAIEVDVDCL-SDGTDVY-VAGIMEHIEEAG-IHSGDSACslpP 883
Cdd:COG0189 161 ------------------EALTELGSEPVLVQEFIPEEDGRDIRVLvVGGEPVAaIRRIPAEGEFRTnLARGGRAE---P 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 494975558 884 RTLSPAMIDELERQAKAMakALNVGGlmnVQFAIKDGTVYVLEVNP 929
Cdd:COG0189 220 VELTDEERELALRAAPAL--GLDFAG---VDLIEDDDGPLVLEVNV 260
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
715-960 |
9.07e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 52.83 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 715 AEALEKNGIPILGTAPDAIDLAEDRDRFQKLLMKLdlNQP----NNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAMQ 790
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRA--GVPtvpgSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 791 IIHSEGMLQTYLldtvpelvpeDIKQRypndktgQINTLLGKNPLLFDSYLANAIEVDVDCLSDGTDVyvagimehieea 870
Cdd:PRK12833 173 VAHDAAQLAAEL----------PLAQR-------EAQAAFGDGGVYLERFIARARHIEVQILGDGERV------------ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 871 gIHSGDSACSL-----------PPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAIKD--GTVYVLEVNPRASRTVPF 937
Cdd:PRK12833 224 -VHLFERECSLqrrrqkileeaPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQVEHPV 302
|
250 260
....*....|....*....|...
gi 494975558 938 VAKTIGAPIAKIAARVMAGEKLD 960
Cdd:PRK12833 303 TEAITGIDLVQEMLRIADGEPLR 325
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
644-930 |
2.44e-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: 51.07 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 644 HAAFALKDAGYEAIMINCnpetvSTDYDTSD------RLYFEPL--TAEDVIEILRAEQENGELVGVIVQFGGQTPLKLA 715
Cdd:COG2232 16 ALAQSARRAGYRVYAVDL-----FADLDTRAlaerwvRLDAESCgfDLEDLPAALLELAAADDPDGLVYGSGFENFPELL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 716 EALEKnGIPILGTAPDAIDLAEDRDRFQKLLMKLDLNQPnngiaysveQARLVASEIGFPLVVRPSYVLGGRAMQIIHSE 795
Cdd:COG2232 91 ERLAR-RLPLLGNPPEVVRRVKDPLRFFALLDELGIPHP---------ETRFEPPPDPGPWLVKPIGGAGGWHIRPADSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 796 gmlqtylldtvPELVPEDIKQRYpndktgqintllgknpllfdsylanaIE---VDVDCLSDGTDVYVAGIMEHIEEAGI 872
Cdd:COG2232 161 -----------APPAPGRYFQRY--------------------------VEgtpASVLFLADGSDARVLGFNRQLIGPAG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 494975558 873 HSGDSAC-SLPPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAIKDGTVYVLEVNPR 930
Cdd:COG2232 204 ERPFRYGgNIGPLALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPR 262
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
201-392 |
3.31e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 50.87 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 201 MSHAMAIAAQaidhVGLPAIIRPsfTLGGTGGGI------AYNRSEFFEIVGGGLDASPTTEVLVEESVLGWKEFEMEVV 274
Cdd:PRK07178 140 LDEALAEAER----IGYPVMLKA--TSGGGGRGIrrcnsrEELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQIL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 275 RDKADNCIII----CSIENidpmgvHTGDSITVAPALTLTDKEYQIMRNASIAVLREIGVETGGSnVQFAVNpKDGRLVV 350
Cdd:PRK07178 214 ADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGT-VEFLLD-ADGEVYF 285
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494975558 351 IEMNPRVSRSSALASKATGFPIAKVAAKLAIGYTLDELENDI 392
Cdd:PRK07178 286 MEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSYKQEDI 327
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
834-962 |
5.97e-06 |
|
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.
Pssm-ID: 434824 [Multi-domain] Cd Length: 131 Bit Score: 46.84 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 834 PLLFDSYLANAiEVDVDCLSDGTDVYVAgimehieeagihsgdsacslPPRTLSPAMIDELERQ------AKAMAKALNV 907
Cdd:pfam15632 4 PLLVMEYLPGP-EYSVDCLAGHGELIAA--------------------VPRRKGDGGIQTLEDDpelieaARRLAEAFGL 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 494975558 908 GGLMNVQFAIKDGTVYVLEVNPRASRTVPFVAKTiGAPIAKIAARVMAGEKLDAV 962
Cdd:pfam15632 63 DGLFNVQFRYDGDGPKLLEINPRMSGGIGYSCLA-GVNLPYLALKLLLGLETPDP 116
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
10-367 |
6.52e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 49.50 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 10 ILIIGAGpivigqacefdySGTQACKALREE--GYRVILVNSNPatimTDPGL--ADATYVEP-ITP----EVVAKIIAK 80
Cdd:PRK12767 4 ILVTSAG------------RRVQLVKALKKSllKGRVIGADISE----LAPALyfADKFYVVPkVTDpnyiDRLLDICKK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 81 ERPDALLPtmGGQTALNTaLS-----LKRMGVLdrynveMIGAKPAAIDMAEDRALFREAMARIGLETPRSMLANATDik 155
Cdd:PRK12767 68 EKIDLLIP--LIDPELPL-LAqnrdrFEEIGVK------VLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLE-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 156 dadrktheaersklkaslsgaaldkaldelenqwnlgesdrkqrymshaMAIAAQAIDHVGLPAIIRPSFTLGGTGGGIA 235
Cdd:PRK12767 137 -------------------------------------------------DFKAALAKGELQFPLFVKPRDGSASIGVFKV 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 236 YNRSE---FFEIVgggldasptTEVLVEESVLGwKEFEMEVVRDKADNCIIICSIENIDPMGVHTGDSITVapaltltdk 312
Cdd:PRK12767 168 NDKEElefLLEYV---------PNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIEVRAGETSKGVTV--------- 228
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 494975558 313 EYQIMRNASIAVLREIGvETGGSNVQFAVNpkDGRLVVIEMNPRVSRSSALASKA 367
Cdd:PRK12767 229 KDPELFKLAERLAEALG-ARGPLNIQCFVT--DGEPYLFEINPRFGGGYPLSYMA 280
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
712-788 |
8.31e-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: 48.88 E-value: 8.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494975558 712 LKLAEALEKNGIPILgTAPDAIDLAEDRDRFQKLLMKLDLNQPNNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRA 788
Cdd:TIGR00768 63 LAVLRYLESLGVPVI-NSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRG 138
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
715-959 |
2.78e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 48.20 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 715 AEALEKNGIPILGTAPDAIDLAEDRDRFQKLLMK--LDLNQPNNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAMQII 792
Cdd:PRK08462 94 VEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRagVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 793 HSEgmlqtylldtvpelvpEDIKQRYPNDKTGQInTLLGKNPLLFDSYLANAIEVDVDCLSDgtdvyvagimEHieEAGI 872
Cdd:PRK08462 174 EDE----------------SDLENLYLAAESEAL-SAFGDGTMYMEKFINNPRHIEVQILGD----------KH--GNVI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 873 HSGDSACSLPPRTL-----SPAMI-DELERQ-----AKAMAKALNVGGLMNVQFAI-KDGTVYVLEVNPRASRTVPFVAK 940
Cdd:PRK08462 225 HVGERDCSLQRRHQklieeSPAVVlDEKTRErlhetAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTRLQVEHTVSEM 304
|
250
....*....|....*....
gi 494975558 941 TIGAPIAKIAARVMAGEKL 959
Cdd:PRK08462 305 VSGLDLIEWMIKIAEGEEL 323
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
1043-1088 |
5.47e-05 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 47.01 E-value: 5.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 494975558 1043 DKPRVLPAIRMLTELGFKVLATGGTQRYLAEQGIAATKINKV------LEGR 1088
Cdd:PRK00881 13 DKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVtgfpeiLDGR 64
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
713-795 |
1.20e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 45.95 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 713 KLAEALEKNGIPILGTAPDAIDLAEDRDRFQKLLMKLDLnqP----NNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRA 788
Cdd:PRK08591 90 DFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGV--PvvpgSDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRG 167
|
....*..
gi 494975558 789 MQIIHSE 795
Cdd:PRK08591 168 MRVVRTE 174
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
714-795 |
2.17e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 45.51 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 714 LAEALEKNGIPILGTAPDAIDLAEDRDRFQKLLMKLDLnqP----NNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAM 789
Cdd:PRK12999 95 FARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGV--PvipgSEGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGM 172
|
....*.
gi 494975558 790 QIIHSE 795
Cdd:PRK12999 173 RIVRSE 178
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
716-930 |
3.65e-04 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 44.36 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 716 EALEKNGIPILGTApDAIDLAEDRDRFQKLLMKlDLNQPNNGIAY--SVEQARLVASEIGFPLVVRPsyvlggramqIIH 793
Cdd:PRK09288 92 VELEKEGFNVVPTA-RATRLTMNREGIRRLAAE-ELGLPTSPYRFadSLEELRAAVEEIGYPCVVKP----------VMS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 794 SEGMLQtYLLDTvpelvPEDIKQRYPNDKTGQintllgknpllfdsyLANAIEV------DVD--------CLSDGTDVY 859
Cdd:PRK09288 160 SSGKGQ-SVVRS-----PEDIEKAWEYAQEGG---------------RGGAGRViveefiDFDyeitlltvRAVDGGTHF 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494975558 860 VAGImEHIEEagihSGDSACSLPPRTLSPAMIDELERQAKAMAKALNVGGLMNVQFAIKDGTVYVLEVNPR 930
Cdd:PRK09288 219 CAPI-GHRQE----DGDYRESWQPQPMSPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVYFSEVSPR 284
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
301-392 |
6.32e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 43.97 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 301 ITVAPALTLTDKEYQIMRNASIAVLREIGVETGGSnVQFAVNPkDGRLVVIEMNPRVSRSSALASKATGFPIakVAAKLA 380
Cdd:PRK12999 243 VEIAPAPGLSEELRERICEAAVKLARAVGYVNAGT-VEFLVDA-DGNFYFIEVNPRIQVEHTVTEEVTGIDI--VQSQIL 318
|
90
....*....|....
gi 494975558 381 I--GYTLDELENDI 392
Cdd:PRK12999 319 IaeGATLHDLEIGI 332
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
845-930 |
1.78e-03 |
|
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: 40.45 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 845 IEVDVDCLSDGTDVYVAGI-MEHIEEAGIHSGDSACSLPPRT-LSPAMIDELERqakAMAKALNVGGLMNVQFAIKDGTV 922
Cdd:pfam02655 72 EPLSVSLLSDGEKALPLSVnRQYIDNGGSGFVYAGNVTPSRTeLKEEIIELAEE---VVECLPGLRGYVGVDLVLKDNEP 148
|
....*...
gi 494975558 923 YVLEVNPR 930
Cdd:pfam02655 149 YVIEVNPR 156
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
21-355 |
4.61e-03 |
|
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: 40.47 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 21 GQACEFD---YSGTQACKALREEGYRVILVNSNPATIMTDpgladatyvepitpevvakiIAKERPDALLPTMGGQTALN 97
Cdd:COG1181 9 GRSAEREvslKSGRAVAAALDKAGYDVVPIGIDVEDLPAA--------------------LKELKPDVVFPALHGRGGED 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 98 TALSlkrmGVLDRYNVEMIGAKPAAIDMAEDRALFREAMARIGLETPRSMLANATDIKDADRKTHEaersklkaslsgaa 177
Cdd:COG1181 69 GTIQ----GLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEE-------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 178 ldkaldelenqwnlgesdrkqrymshamaiaaqaidhVGLPAIIRPSFtlGGTGGGI--AYNRSEFFEIVGGGLDASPtt 255
Cdd:COG1181 131 -------------------------------------LGLPLFVKPAR--EGSSVGVskVKNAEELAAALEEAFKYDD-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 256 EVLVEESVLGwKEFEMEVVRDkaDNCIIICSIEnIDPMGV--------HTGDSITVAPAlTLTDKEYQIMRNASIAVLRE 327
Cdd:COG1181 170 KVLVEEFIDG-REVTVGVLGN--GGPRALPPIE-IVPENGfydyeakyTDGGTEYICPA-RLPEELEERIQELALKAFRA 244
|
330 340
....*....|....*....|....*...
gi 494975558 328 IGVEtGGSNVQFAVNPkDGRLVVIEMNP 355
Cdd:COG1181 245 LGCR-GYARVDFRLDE-DGEPYLLEVNT 270
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
714-795 |
8.47e-03 |
|
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: 40.45 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494975558 714 LAEALEKNGIPILGTAPDAIDLAEDRDRFQKLLMKLDLnqP----NNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAM 789
Cdd:COG1038 94 FARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGV--PvipgTEGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGM 171
|
....*.
gi 494975558 790 QIIHSE 795
Cdd:COG1038 172 RVVRSE 177
|
|
| |
