|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1086 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1898.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 1 MPKRNDINTILLIGSGPIIIGQACEFDYSGTQAIKTLKELGYRVVLINSNPATIMTDPDFADATYIEPITKENILSIIKK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 81 EKVDAILPTMGGQVALNAAMQIYESGLLGK--VKFLGANPEAIKKGEDRQIFKESMKKIGMDLPKSMYAYNYNEALKAID 158
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKygVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 159 EIGFPLMIRSSFTLGGAGSGVVYNLEEFQELAQQALSLSPIGEILIEESLLGWKEYEMEVIRDKFDNCIIVCSIENLDPM 238
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 239 GVHTGDSITIAPALTLTDKEYQAMRNASFEILREIGVDTGGSNVQFAINPENGRMIVIEMNPRVSRSSALASKATGYPIA 318
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 319 KVATLLAVGFSLDEIKNDITG-TPASFEPVIDYIVTKIPRFAFEKFPKADKILGTSMKSVGEVMAIGRTFKESIQKALCS 397
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGkTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 398 LEKNYDGFNEINIK--DKNELVFNIRNANEKRLLYIAEAFREGLNINEIYEYSKIDTWFLNQIKEIIDFEKKIDMDILN- 474
Cdd:PRK05294 401 LEIGVTGLDEDLFEeeSLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPl 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 475 NKNLLRKAKTMGFSDKRIAHLINTkdnlelSQNDIYYARVNQNIITEFHEVDTCSGEFNAITPYYYSSFNV-LELTQSin 553
Cdd:PRK05294 481 DAELLREAKRLGFSDARIAKLLGV------TEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEeCESNPS-- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 554 kkekKEKKVMIIGGGPNRIGQGIEFDYACVQASFALKDMGIKTIMYNCNPETVSTDYDISDVLYFEPIDFEHLRAVIEKE 633
Cdd:PRK05294 553 ----DRKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKE 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 634 KPDGIIVHFGGQTPLKFAKQLSAFGAKIIGTNARVIDLAEDRKKFSEFIVKLGINQPKNGTAYSIEEAILKANEIGYPVL 713
Cdd:PRK05294 629 KPKGVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVL 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 714 VRPSYVLGGRAMRIVHNEEELKLYVKEAVKLSNKSPILIDQFLDNASEFDVDAICDGKNVYVAGIMEHIEEAGIHSGDSA 793
Cdd:PRK05294 709 VRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSA 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 794 CSLPPCNIDEKIQELIIQKTADIALNLGVIGLLNIQFALYQNELYIIEVNPRASRTVPFVSKATGIALAKVATRVMWQGN 873
Cdd:PRK05294 789 CSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKK 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 874 LKEAlnfydkfgivkeknGILRPKKSQRINLKGVVFPFSKLSGSDLELGPEMRSTGEVMGISKDFANSYAKIQIASSNNL 953
Cdd:PRK05294 869 LAEL--------------GYTKGLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRL 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 954 PEKGSIFISLKDEDKKYTKKIASEYSKLGFKLMATSGTYKEIIKNGFECELIYKISEGRPNVEDKLKNGEIELVINTSDE 1033
Cdd:PRK05294 935 PTSGTVFLSVRDRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINTPTG 1014
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 1956323229 1034 NSFKEDTRKIRANIIRFKTPYFTNLRAAFAGAKSIKAIQDKTyLEVKSLQEWL 1086
Cdd:PRK05294 1015 RQAIRDGFSIRRAALEYKVPYITTLAGARAAVKAIEALKFGE-LEVRSLQEYH 1066
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1068 |
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: 1531.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 2 PKRNDINTILLIGSGPIIIGQACEFDYSGTQAIKTLKELGYRVVLINSNPATIMTDPDFADATYIEPITKENILSIIKKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 82 KVDAILPTMGGQVALNAAMQIYESGLLGK--VKFLGANPEAIKKGEDRQIFKESMKKIGMDLPKSMYAYNYNEALKAIDE 159
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKygVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 160 IGFPLMIRSSFTLGGAGSGVVYNLEEFQELAQQALSLSPIGEILIEESLLGWKEYEMEVIRDKFDNCIIVCSIENLDPMG 239
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 240 VHTGDSITIAPALTLTDKEYQAMRNASFEILREIGVDtGGSNVQFAINPENGRMIVIEMNPRVSRSSALASKATGYPIAK 319
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 320 VATLLAVGFSLDEIKNDITG-TPASFEPVIDYIVTKIPRFAFEKFPKADKILGTSMKSVGEVMAIGRTFKESIQKALCSL 398
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTGtTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 399 EKNYDGF--NEINIKDKNELVFNIRNANEKRLLYIAEAFREGLNINEIYEYSKIDTWFLNQIKEIIDFEKKIDMDILN-- 474
Cdd:TIGR01369 400 EIGATGFdlPDREVEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTdl 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 475 NKNLLRKAKTMGFSDKRIAHLINTkdnlelSQNDIYYARVNQNIITEFHEVDTCSGEFNAITPYYYSSFNvlelTQSINK 554
Cdd:TIGR01369 480 DPELLRRAKKLGFSDAQIARLIGV------TEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYE----GERDDV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 555 KEKKEKKVMIIGGGPNRIGQGIEFDYACVQASFALKDMGIKTIMYNCNPETVSTDYDISDVLYFEPIDFEHLRAVIEKEK 634
Cdd:TIGR01369 550 PFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEK 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 635 PDGIIVHFGGQTPLKFAKQLSAFGAKIIGTNARVIDLAEDRKKFSEFIVKLGINQPKNGTAYSIEEAILKANEIGYPVLV 714
Cdd:TIGR01369 630 PEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLV 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 715 RPSYVLGGRAMRIVHNEEELKLYVKEAVKLSNKSPILIDQFLDNASEFDVDAICDGKNVYVAGIMEHIEEAGIHSGDSAC 794
Cdd:TIGR01369 710 RPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTC 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 795 SLPPCNIDEKIQELIIQKTADIALNLGVIGLLNIQFALYQNELYIIEVNPRASRTVPFVSKATGIALAKVATRVMWQGNL 874
Cdd:TIGR01369 790 VLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 875 KEAlnfydkfgivkeknGILRPKKSQRINLKGVVFPFSKLSGSDLELGPEMRSTGEVMGISKDFANSYAKIQIASSNNLP 954
Cdd:TIGR01369 870 EEL--------------GVGKEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIP 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 955 EKGSIFISLKDEDKKYTKKIASEYSKLGFKLMATSGTYKEIIKNGFECELIYKISEGRPNVEDKLKNGEIELVINTSDE- 1033
Cdd:TIGR01369 936 KKGSVLLSVRDKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTSKg 1015
|
1050 1060 1070
....*....|....*....|....*....|....*
gi 1956323229 1034 NSFKEDTRKIRANIIRFKTPYFTNLRAAFAGAKSI 1068
Cdd:TIGR01369 1016 AGTATDGYKIRREALDYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1086 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1321.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 1 MPKRNDINTILLIGSGPIIIGQACEFDYSGTQAIKTLKELGYRVVLINSNPATIMTDPDFADATYIEPITKENILSIIKK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 81 EKVDAILPTMGGQVALNAAMQIYESGLLGK--VKFLGANPEAIKKGEDRQIFKESMKKIGMDLPKSMYAYNYNEALKAID 158
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQygVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 159 EIGFPLMIRSSFTLGGAGSGVVYNLEEFQELAQQALSLSPIGEILIEESLLGWKEYEMEVIRDKFDNCIIVCSIENLDPM 238
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 239 GVHTGDSITIAPALTLTDKEYQAMRNASFEILREIGVdTGGSNVQFAINPENGRMIVIEMNPRVSRSSALASKATGYPIA 318
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 319 KVATLLAVGFSLDEIKNDITG-TPASFEPVIDYIVTKIPRFAFEKFPKADKILGTSMKSVGEVMAIGRTFKESIQKALCS 397
Cdd:PRK12815 320 KIAAKLAVGYTLNELKNPVTGlTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 398 LEK---NYDGFNEINIKDKNELVFNIRNANEKRLLYIAEAFREGLNINEIYEYSKIDTWFLNQIKEIIDFEKKIDMDILN 474
Cdd:PRK12815 400 LEIkrnGLSLPIELSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 475 -NKNLLRKAKTMGFSDKRIAHLINTkdnlelSQNDIYYARVNQNIITEFHEVDTCSGEFNAITPYYYSSFNVleltQSIN 553
Cdd:PRK12815 480 lSADLLRKVKEKGFSDALLAELTGV------TEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFG----ESEA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 554 KKEKKEKKVMIIGGGPNRIGQGIEFDYACVQASFALKDMGIKTIMYNCNPETVSTDYDISDVLYFEPIDFEHLRAVIEKE 633
Cdd:PRK12815 550 EPSSEKKKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAE 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 634 KPDGIIVHFGGQTPLKFAKQLSAFGAKIIGTNARVIDLAEDRKKFSEFIVKLGINQPKNGTAYSIEEAILKANEIGYPVL 713
Cdd:PRK12815 630 NIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVL 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 714 VRPSYVLGGRAMRIVHNEEELKLYVKEAVklSNKSPILIDQFLDnASEFDVDAICDGKNVYVAGIMEHIEEAGIHSGDSA 793
Cdd:PRK12815 710 IRPSYVIGGQGMAVVYDEPALEAYLAENA--SQLYPILIDQFID-GKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSI 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 794 CSLPPCNIDEKIQELIIQKTADIALNLGVIGLLNIQFALYQNELYIIEVNPRASRTVPFVSKATGIALAKVATRVMWQGN 873
Cdd:PRK12815 787 AVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKS 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 874 LKEalnfydkfgiVKEKNGIlrPKKSQRINLKGVVFPFSKLSGSDLELGPEMRSTGEVMGISKDFANSYAKIQIASSNNL 953
Cdd:PRK12815 867 LAE----------LGYPNGL--WPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHI 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 954 PEKGSIFISLKDEDKKYTKKIASEYSKLGFKLMATSGTYKEIIKNGFECELIYKISEGRPNVEDKLKNGEIELVINTSDE 1033
Cdd:PRK12815 935 PSYGTIFISVRDEDKPEVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSPSLLERIKQHRIVLVVNTSLS 1014
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 1956323229 1034 NSFKEDTRKIRANIIRFKTPYFTNLRAAFAGAKSIKAIQdktyLEVKSLQEWL 1086
Cdd:PRK12815 1015 DSASEDAIKIRDEALSTHIPVFTELETAQAFLQVLESLA----LTTQPIQELQ 1063
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1085 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1290.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 3 KRNDINTILLIGSGPIIIGQACEFDYSGTQAIKTLKELGYRVVLINSNPATIMTDPDFADATYIEPITKENILSIIKKEK 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 83 VDAILPTMGGQVALNAAMQIYESGLLGK--VKFLGANPEAIKKGEDRQIFKESMKKIGMDLPKSMYAYNYNEALKAIDEI 160
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKygVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 161 G-FPLMIRSSFTLGGAGSGVVYNLEEFQELAQQALSLSPIGEILIEESLLGWKEYEMEVIRDKFDNCIIVCSIENLDPMG 239
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 240 VHTGDSITIAPALTLTDKEYQAMRNASFEILREIGVDTGGSNVQFAINPENGRMIVIEMNPRVSRSSALASKATGYPIAK 319
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 320 VATLLAVGFSLDEIKNDIT-GTPASFEPVIDYIVTKIPRFAFEKFPKADKILGTSMKSVGEVMAIGRTFKESIQKALCSL 398
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDITlKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 399 EKNYDGFNEINIK----DKNELVFNIRNANEKRLLYIAEAFREGLNINEIYEYSKIDTWFLNQIKEIIDFEKKIDMDILN 474
Cdd:PLN02735 419 ETGFSGWGCAKVKeldwDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLS 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 475 N--KNLLRKAKTMGFSDKRIAHLINTkdnlelSQNDIYYARVNQNIITEFHEVDTCSGEFNAITPYYYSSFNVLELTQSI 552
Cdd:PLN02735 499 ElsKDDFYEVKRRGFSDKQIAFATKS------TEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPT 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 553 NkkekkEKKVMIIGGGPNRIGQGIEFDYACVQASFALKDMGIKTIMYNCNPETVSTDYDISDVLYFEPIDFEHLRAVIEK 632
Cdd:PLN02735 573 N-----KKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDL 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 633 EKPDGIIVHFGGQTPLKFA----------KQLSAFGA---KIIGTNARVIDLAEDRKKFSEFIVKLGINQPKNGTAYSIE 699
Cdd:PLN02735 648 ERPDGIIVQFGGQTPLKLAlpiqkyldknPPPSASGNgnvKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEA 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 700 EAILKANEIGYPVLVRPSYVLGGRAMRIVHNEEELKLYVKEAVKLSNKSPILIDQFLDNASEFDVDAICDGK-NVYVAGI 778
Cdd:PLN02735 728 DALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEgNVVIGGI 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 779 MEHIEEAGIHSGDSACSLPPCNIDEKIQELIIQKTADIALNLGVIGLLNIQFALYQN-ELYIIEVNPRASRTVPFVSKAT 857
Cdd:PLN02735 808 MEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSgEVYIIEANPRASRTVPFVSKAI 887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 858 GIALAKVATRVMWQGNLKEaLNFydkfgivkEKNGILRpkksqRINLKGVVFPFSKLSGSDLELGPEMRSTGEVMGISKD 937
Cdd:PLN02735 888 GHPLAKYASLVMSGKSLKD-LGF--------TEEVIPA-----HVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYE 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 938 FANSYAKIQIASSNNLPEKGSIFISLKDEDKKYTKKIASEYSKLGFKLMATSGTYKEIIKNGFECELIYKISEGRPNVED 1017
Cdd:PLN02735 954 FSKAFAKAQIAAGQRLPLSGTVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGD 1033
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956323229 1018 KLKNGEIELVINTSDENSFKE-DTRKIRANIIRFKTPYFTNLRAAFAGAKSIKAIQDKTyLEVKSLQEW 1085
Cdd:PLN02735 1034 MLANGQIQLMVITSSGDALDQkDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKECP-IEMIALQDF 1101
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-542 |
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: 717.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 13 IGSGPIIIGQACEFDYSGTQAIKTLKELGYRVVLINSNPATIMTDPDFADATYIEPITKENILSIIKKEKVDAILPTMGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 93 QVALNAAMQIYESGLLGKVKFLGANPEAIKKGEDRQIFKESMKKIGMDLPKSMYAYNYNEALKAIDEIGFPLMIRSSFTL 172
Cdd:COG0458 81 QTALNLAVELEEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 173 GGAGSGVVYNLEEFQELAQQALSLSPIGEILIEESLLGWKEYEMEVIRDKFDNCIIVCSIENLDPMGVHTGDSITIAPAL 252
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 253 TLTDKEYQAMRNASFEILREIGVDtGGSNVQFAINpeNGRMIVIEMNPRVSRSSALASKATGYPIAKVATLLAVGFSLDE 332
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVV-GLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 333 IKNDiTGtpasFEPVIDYIVTKIPRFAFEKFPKADKILGTSMKSVGEVMAIGRTFKESIQKALCSLEKNYDG---FNEIN 409
Cdd:COG0458 318 LGND-TG----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvlLSLVA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 410 IKDKNELVFNIRNANekRLLYIAEAFREGLNINEIYEYSKIDTWFLNQIKEIIDFEKKIDMDILNNkNLLRKAKTMGFSD 489
Cdd:COG0458 393 DDDKEEALLLARRLA--RLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVI-NTLLGAKSLGDSD 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1956323229 490 KRIAHLINTKDnlelsqNDIYYARVNQNIITEFHEVDTCSGEFNAITPYYYSS 542
Cdd:COG0458 470 GIIRRALAAKV------PYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYST 516
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
565-1085 |
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: 665.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 565 IGGGPNRIGQGIEFDYACVQASFALKDMGIKTIMYNCNPETVSTDYDISDVLYFEPIDFEHLRAVIEKEKPDGIIVHFGG 644
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 645 QTPLKFAKQLSA----FGAKIIGTNARVIDLAEDRKKFSEFIVKLGINQPKNGTAYSIEEAILKANEIGYPVLVRPSYVL 720
Cdd:COG0458 81 QTALNLAVELEEagilEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 721 GGRAMRIVHNEEELKLYVKEAVKLSNKSPILIDQFLDNASEFDVDAICDGK-NVYVAGIMEHIEEAGIHSGDSACSLPPC 799
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEdNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 800 NIDEKIQELIIQKTADIALNLGVIGLLNIQFALYQNELYIIEVNPRASRTVPFVSKATGIALAKVATRVMWQGNLKEaLN 879
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDE-LG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 880 FYDKFG------IVKEkngilrpkksqrinlkgVVFPFSKLSGSDLELGPEMRSTGEVMGISKDFANSYAKIQIASSNNL 953
Cdd:COG0458 320 NDTGFEptldyvVVKE-----------------PVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 954 PekGSIFISL-KDEDKKYTKKIASEYSKLGFKLMATSGTYKEIIKNGFECELIYKISEGRPNVEDKLKNGEIELVINTSD 1032
Cdd:COG0458 383 P--GTVLLSLvADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLL 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1956323229 1033 ENSFKEDTRKIRANIIRFKTPYFTNLRAAFAGAKSIKAIQDKTyLEVKSLQEW 1085
Cdd:COG0458 461 GAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEA-GEFEEATAY 512
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
126-331 |
4.80e-81 |
|
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: 263.01 E-value: 4.80e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 126 DRQIFKESMKKIGMDLPKSMYAYNYN--EALKAIDEIGFPLMIRSSFTLGGAGSGVVYNLEEFQELAQQALSLSP----I 199
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETeeEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPaafgN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 200 GEILIEESLLGWKEYEMEVIRDKFDNCIIVCSIENLDPMgvHTGDSITIAPALTLTDKEYQAMRNASFEILREIGVdTGG 279
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGY-VGA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956323229 280 SNVQFAINPENGRMIVIEMNPRVSRSSALASKATGYPIAKVATLLAVGFSLD 331
Cdd:pfam02786 158 GTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
420-543 |
1.15e-44 |
|
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: 157.23 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 420 IRNANEKRLLYIAEAFREGLNINEIYEYSKIDTWFLNQIKEIIDFEKKIDMDILN--NKNLLRKAKTMGFSDKRIAHLIN 497
Cdd:smart01096 5 LRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDelDADLLRKAKRLGFSDRQIAKLLG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1956323229 498 TkdnlelSQNDIYYARVNQNIITEFHEVDTCSGEFNAITPYYYSSF 543
Cdd:smart01096 85 V------TEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
957-1066 |
1.66e-39 |
|
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: 141.85 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 957 GSIFISLKDEDKKYTKKIASEYSKLGFKLMATSGTYKEIIKNGFECELIYKISEGRPNVEDKLKNGEIELVINTSDENSF 1036
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKRA 80
|
90 100 110
....*....|....*....|....*....|
gi 1956323229 1037 KEDTRKIRANIIRFKTPYFTNLRAAFAGAK 1066
Cdd:cd01424 81 IRDGFSIRRAALEYKVPYFTTLDTARAAVE 110
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
674-868 |
1.96e-35 |
|
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: 133.97 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 674 DRKKFSEFIVKLGINQPKN--GTAYSIEEAILKANEIGYPVLVRPSYVLGGRAMRIVHNEEELKLYVKEAVKLSNKSP-- 749
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 750 --ILIDQFLDNASEFDVDAICDGK-NVYVAGIMEHIEEagIHSGDSACSLPPCNIDEKIQELIIQKTADIALNLGVIGLL 826
Cdd:pfam02786 81 pqVLVEKSLKGPKHIEYQVLRDAHgNCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956323229 827 NIQFAL--YQNELYIIEVNPRASRTVPFVSKATGIALAKVATRV 868
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKI 202
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
420-495 |
4.69e-30 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 113.63 E-value: 4.69e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956323229 420 IRNANEKRLLYIAEAFREGLNINEIYEYSKIDTWFLNQIKEIIDFEKKI-DMDILNNKNLLRKAKTMGFSDKRIAHL 495
Cdd:pfam02787 3 LRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELkEAGLDLDAELLREAKRLGFSDRQIAKL 79
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
77-327 |
1.21e-25 |
|
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: 107.65 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 77 IIKKEKVDAILPTMGGQVALnAAMQIYESGLLGkvkflgANPEAIKKGEDRQIFKESMKKIGMDLPKSMYAYNYNEALKA 156
Cdd:COG0439 12 LARETGIDAVLSESEFAVET-AAELAEELGLPG------PSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 157 IDEIGFPLMIRSSFtlGGAGSGV--VYNLEEFQELAQQALS----LSPIGEILIEESLLGwKEYEMEVIRdkFDNCIIVC 230
Cdd:COG0439 85 AEEIGYPVVVKPAD--GAGSRGVrvVRDEEELEAALAEARAeakaGSPNGEVLVEEFLEG-REYSVEGLV--RDGEVVVC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 231 SI---ENLDPMGVHTGDsitIAPALtLTDKEYQAMRNASFEILREIGVDTGGSNVQFAINPeNGRMIVIEMNPRVS--RS 305
Cdd:COG0439 160 SItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRRGAFHTEFLLTP-DGEPYLIEINARLGgeHI 234
|
250 260
....*....|....*....|..
gi 1956323229 306 SALASKATGYPIAKVATLLAVG 327
Cdd:COG0439 235 PPLTELATGVDLVREQIRLALG 256
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
624-869 |
1.11e-22 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 98.79 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 624 EHLRAVIEKEKPDGIIVHFGGQTPLkFAKQLSAFGakIIGTNARVIDLAEDRKKFSEFIVKLGINQPKNGTAYSIEEAIL 703
Cdd:COG0439 7 AAAAELARETGIDAVLSESEFAVET-AAELAEELG--LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 704 KANEIGYPVLVRPSYVLGGRAMRIVHNEEEL----KLYVKEAVKLSNKSPILIDQFLDNAsEFDVDAICDGKNVYVAGIM 779
Cdd:COG0439 84 FAEEIGYPVVVKPADGAGSRGVRVVRDEEELeaalAEARAEAKAGSPNGEVLVEEFLEGR-EYSVEGLVRDGEVVVCSIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 780 EHIEEA--GIHSGDSAcslpPCNIDEKIQELIIQKTADIALNLGVI-GLLNIQFaLY--QNELYIIEVNPRAS--RTVPF 852
Cdd:COG0439 163 RKHQKPpyFVELGHEA----PSPLPEELRAEIGELVARALRALGYRrGAFHTEF-LLtpDGEPYLIEINARLGgeHIPPL 237
|
250
....*....|....*..
gi 1956323229 853 VSKATGIALAKVATRVM 869
Cdd:COG0439 238 TELATGVDLVREQIRLA 254
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
624-852 |
3.59e-21 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 95.72 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 624 EHLRAVIEKEKPDGIIVhfGGQTPLKF-AKQLSAF---GAKIIGTNARVIDLAEDRKKFSEFIVKLGINQPKNGTAYSIE 699
Cdd:PRK12767 59 DRLLDICKKEKIDLLIP--LIDPELPLlAQNRDRFeeiGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 700 --EAILKANEIGYPVLVRPSYVLGGRAMRIVHNEEELKLYVKEAVKLsnkspiLIDQFLDnASEFDVDAICDGKNVYVAG 777
Cdd:PRK12767 137 dfKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPNL------IIQEFIE-GQEYTVDVLCDLNGEVISI 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956323229 778 I-MEHIEeagIHSG--DSACSLPpcniDEKIQELIIqktaDIALNLGVIGLLNIQFALYQNELYIIEVNPRASRTVPF 852
Cdd:PRK12767 210 VpRKRIE---VRAGetSKGVTVK----DPELFKLAE----RLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
974-1056 |
4.34e-20 |
|
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: 85.99 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 974 IASEYSKLGFKLMATSGTYKEIIKNGFE--CELIYKISEGRPNVEDKLKNGEIELVINTSD--ENSFKEDTRKIRANIIR 1049
Cdd:smart00851 5 FAKRLAELGFELLATGGTAKFLREAGLPvvKTLHPKVHGGIPQILDLIKNGEIDLVINTLYpfEAQAHEDGYSIRRAAEN 84
|
....*..
gi 1956323229 1050 FKTPYFT 1056
Cdd:smart00851 85 IDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
974-1056 |
8.10e-17 |
|
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: 76.37 E-value: 8.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 974 IASEYSKLGFKLMATSGTYKEIIKNGFEC-ELIYKISEGRPN----VEDKLKNGEIELVINTSDENSFKE-DTRKIRANI 1047
Cdd:pfam02142 5 LAKALVELGFELLATGGTAKFLREAGIPVtEVVEKTGEGRPGgrvqIGDLIKNGEIDLVINTLYPFKATVhDGYAIRRAA 84
|
....*....
gi 1956323229 1048 IRFKTPYFT 1056
Cdd:pfam02142 85 ENIDIPGPT 93
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
38-338 |
4.33e-14 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 76.18 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 38 KELGYRVVLINSNPATIMTDPDFAD-ATYIEP-------ITKENILSIIKKEKVDAILPTMGGqVALNA--AMQIYESGl 107
Cdd:PRK08654 22 RELGIKTVAVYSEADKNALFVKYADeAYPIGPappsksyLNIERIIDVAKKAGADAIHPGYGF-LAENPefAKACEKAG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 108 lgkVKFLGANPEAIKKGEDRQIFKESMKKIGMD-LPKSMYAY-NYNEALKAIDEIGFPLMIRSSFTLGGAGSGVVYNLEE 185
Cdd:PRK08654 100 ---IVFIGPSSDVIEAMGSKINAKKLMKKAGVPvLPGTEEGIeDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 186 FQE-------LAQQALSLSpigEILIEESLLGWKEYEMEVIRDKFDNCIIV----CSI----ENLdpmgvhtgdsITIAP 250
Cdd:PRK08654 177 LEDaiestqsIAQSAFGDS---TVFIEKYLEKPRHIEIQILADKHGNVIHLgdreCSIqrrhQKL----------IEEAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 251 ALTLTDKEYQAMRNASFEILREIGVDTGGSnVQFAInpENGRMIVIEMNPRVSRSSALASKATGYPIAKVATLLAVGFSL 330
Cdd:PRK08654 244 SPIMTPELRERMGEAAVKAAKAINYENAGT-VEFLY--SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
....*...
gi 1956323229 331 DEIKNDIT 338
Cdd:PRK08654 321 SFKQEDIT 328
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
17-327 |
1.55e-12 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 70.73 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 17 PIIIGqaceFDYSGTQAIKTLKELGYRVVLINSNPATIMTDPDFADATYIEPITK-------ENILSIIKKEKVDAILPT 89
Cdd:COG3919 8 VVVLG----GDINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGddpeafvDALLELAERHGPDVLIPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 90 MGGQVALNAAmqiYESGLLGKVKFLGANPEAIKKGEDRQIFKESMKKIGMDLPKSMYAYNYNEALKAIDEIGFPLMI--- 166
Cdd:COG3919 84 GDEYVELLSR---HRDELEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVkpa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 167 -----RSSFTLGGAGSGVVYNLEEFQELAQQALSLSpiGEILIEESLLGWKEYE--MEVIRDKFDNCIIVCSIEnldpmg 239
Cdd:COG3919 161 dsvgyDELSFPGKKKVFYVDDREELLALLRRIAAAG--YELIVQEYIPGDDGEMrgLTAYVDRDGEVVATFTGR------ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 240 VHTGDSITIAPALTLTDKEYQAMRNASFEILREIGVdTGGSNVQFAINPENGRMIVIEMNPRVSRSSALASKAtGYPIAK 319
Cdd:COG3919 233 KLRHYPPAGGNSAARESVDDPELEEAARRLLEALGY-HGFANVEFKRDPRDGEYKLIEINPRFWRSLYLATAA-GVNFPY 310
|
....*...
gi 1956323229 320 VATLLAVG 327
Cdd:COG3919 311 LLYDDAVG 318
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
649-845 |
2.42e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 70.60 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 649 KFAKQLSAFGAKIIGTNARVIDLAEDRKKFSEFIVKLGInqP----KNGTAYSIEEAILKANEIGYPVLVRPSYVLGGRA 724
Cdd:PRK08591 90 DFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGV--PvvpgSDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 725 MRIVHNEEELKLYVK----EAVKLSNKSPILIDQFLDNASEFDVDAICDGK-NVyvagimehieeagIHSGDSACSL--- 796
Cdd:PRK08591 168 MRVVRTEAELEKAFSmaraEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHgNA-------------IHLGERDCSLqrr 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956323229 797 --------PPCNIDEKIQELIIQKTADIALNLGVIGLLNIQFaLYQ--NELYIIEVNPR 845
Cdd:PRK08591 235 hqkvleeaPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LYEknGEFYFIEMNTR 292
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
958-1061 |
3.81e-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: 64.24 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 958 SIFISLKDEDKKYTKKIASEYSKLGFKLMATSGTYKEIIKNGFECELIYKISE----GRPNVEDKLKNGEIELVINTSDE 1033
Cdd:cd01423 2 GILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEepqnDKPSLRELLAEGKIDLVINLPSN 81
|
90 100 110
....*....|....*....|....*....|
gi 1956323229 1034 NSFKEDTR--KIRANIIRFKTPYFTNLRAA 1061
Cdd:cd01423 82 RGKRVLDNdyVMRRAADDFAVPLITNPKCA 111
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
34-337 |
7.04e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 68.90 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 34 IKTLKELGYRVVLINSNpatimTDPD-----FADATY-IEP-------ITKENILSIIKKEKVDAILPTMGgQVALNA-- 98
Cdd:PRK06111 18 IRTCQKLGIRTVAIYSE-----ADRDalhvkMADEAYlIGGprvqesyLNLEKIIEIAKKTGAEAIHPGYG-LLSENAsf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 99 AMQIYESGLLgkvkFLGANPEAIKKGEDRQIFKESMKKIGMD-LPKSMYAY-NYNEALKAIDEIGFPLMIRSSFTLGGAG 176
Cdd:PRK06111 92 AERCKEEGIV----FIGPSADIIAKMGSKIEARRAMQAAGVPvVPGITTNLeDAEEAIAIARQIGYPVMLKASAGGGGIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 177 SGVVYNLEEF-------QELAQQALSlspIGEILIEESLLGWKEYEMEVIRDKFDNCIIV----CSIENldpmgvHTGDS 245
Cdd:PRK06111 168 MQLVETEQELtkafesnKKRAANFFG---NGEMYIEKYIEDPRHIEIQLLADTHGNTVYLwereCSVQR------RHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 246 ITIAPALTLTDKEYQAMRNASFEILREIGVdTGGSNVQFAINpENGRMIVIEMNPRVSRSSALASKATGYPIAKVATLLA 325
Cdd:PRK06111 239 IEEAPSPFLDEETRKAMGERAVQAAKAIGY-TNAGTIEFLVD-EQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIA 316
|
330
....*....|..
gi 1956323229 326 VGFSLDEIKNDI 337
Cdd:PRK06111 317 AGEKLSFTQDDI 328
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
650-868 |
7.68e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 69.01 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 650 FAKQLSAFGAKIIGTNARVI----DLAEDRKKFSEFIVKLGINQPknGTAYSIEEAILKANEIGYPVLVRPSYVLGGRAM 725
Cdd:PRK12833 94 FAEAVEAAGLIFVGPDAQTIrtmgDKARARRTARRAGVPTVPGSD--GVVASLDAALEVAARIGYPLMIKAAAGGGGRGI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 726 RIVHNEEELK----LYVKEAVKLSNKSPILIDQFLDNASEFDVDAICDGKNVyvagimehieeagIHSGDSACSL----- 796
Cdd:PRK12833 172 RVAHDAAQLAaelpLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGERV-------------VHLFERECSLqrrrq 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 797 ------PPCNIDEKIQELIIQKTADIALNLGV--IGLLNIQFALYQNELYIIEVNPRASRTVPFVSKATGIALAKVATRV 868
Cdd:PRK12833 239 kileeaPSPSLTPAQRDALCASAVRLARQVGYrgAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRI 318
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
697-871 |
8.46e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 68.90 E-value: 8.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 697 SIEEAILKANEIGYPVLVRPSYVLGGRAMRIVHNEEELK----LYVKEAVKLSNKSPILIDQFLDNASEFDVDAICDGKn 772
Cdd:PRK06111 140 DAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTkafeSNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTH- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 773 vyvagimEHIeeagIHSGDSACSL-----------PPCNIDEKIQELIIQKTADIALNLGVIGLLNIQFaLYQNE--LYI 839
Cdd:PRK06111 219 -------GNT----VYLWERECSVqrrhqkvieeaPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQknFYF 286
|
170 180 190
....*....|....*....|....*....|..
gi 1956323229 840 IEVNPRASRTVPFVSKATGIALakvatrVMWQ 871
Cdd:PRK06111 287 LEMNTRLQVEHPVTEEITGIDL------VEQQ 312
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
32-302 |
1.75e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 67.85 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 32 QAIKTLKELGYRVVLINSNPATIMTDPDFADATYI--EPITKE---NILSIIKKEKV---DAILPTMGgqvALNAAMQIY 103
Cdd:PRK08462 18 RAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICigGAKSSEsylNIPAIISAAEIfeaDAIFPGYG---FLSENQNFV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 104 ESGLLGKVKFLGANPEAIKKGEDRQIFKESMKKIGMD-LPKSMYAY-NYNEALKAIDEIGFPLMIRSSFTLGGAGSGVVY 181
Cdd:PRK08462 95 EICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPvIPGSDGALkSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 182 NLEEFQEL----AQQALSLSPIGEILIEESLLGWKEYEMEVIRDKFDNCIIV----CSIENldpmgvHTGDSITIAPALT 253
Cdd:PRK08462 175 DESDLENLylaaESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1956323229 254 LTDKEYQAMRNASFEILREIGVDTGGSnVQFAINpENGRMIVIEMNPRV 302
Cdd:PRK08462 249 LDEKTRERLHETAIKAAKAIGYEGAGT-FEFLLD-SNLDFYFMEMNTRL 295
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
631-862 |
2.15e-11 |
|
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: 65.83 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 631 EKEKPDGIIVHF-GGQTPLKFAKQLSAFGAKIIGTnARVIDLAEDRKKFSEFIVKLGINQPKNGTAYSIEEAILKANEIG 709
Cdd:TIGR00768 45 ALAELDVVIVRIvSMFRGLAVLRYLESLGVPVINS-SDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 710 YPVLVRPSYVLGGRAMRIVHNEEELK--LYVKEAVKLSNKSpILIDQFLDNASEFDVDAICDGKNVyVAGIMEHIEE--- 784
Cdd:TIGR00768 124 FPVVLKPVFGSWGRGVSLARDRQAAEslLEHFEQLNGPQNL-FLVQEYIKKPGGRDIRVFVVGDEV-VAAIYRITSGhwr 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 785 AGIHSGDSAcslPPCNIDEKIQELIIQKTAdiALNLGVIGllnIQFALYQNELYIIEVNPrasrTVPF--VSKATGIALA 862
Cdd:TIGR00768 202 SNLARGGKA---EPCSLTEEIEELAIKAAK--ALGLDVAG---VDLLESEDGLLVNEVNA----NPEFknSVKTTGVNIA 269
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
72-302 |
3.46e-11 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 67.86 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 72 ENILSIIKKEKVDAILPtmG-GQVALNA--AMQIYESGLlgkvKFLGANPEAIKKGEDRQIFKESMKKIGM-------DL 141
Cdd:PRK12999 68 DEIIRVAKQAGVDAIHP--GyGFLSENPefARACAEAGI----TFIGPTAEVLRLLGDKVAARNAAIKAGVpvipgseGP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 142 PKSMyaynyNEALKAIDEIGFPLMIRSSftLGGAGSG--VVYNLEEFQELAQQALSLSP----IGEILIEESLLGWKEYE 215
Cdd:PRK12999 142 IDDI-----EEALEFAEEIGYPIMLKAS--AGGGGRGmrIVRSEEELEEAFERAKREAKaafgNDEVYLEKYVENPRHIE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 216 MEVIRDKFDNciIV------CS--------IEnldpmgvhtgdsitIAPALTLTDKEYQAMRNASFEILREIGVDTGGSn 281
Cdd:PRK12999 215 VQILGDKHGN--VVhlyerdCSvqrrhqkvVE--------------IAPAPGLSEELRERICEAAVKLARAVGYVNAGT- 277
|
250 260
....*....|....*....|.
gi 1956323229 282 VQFAINpENGRMIVIEMNPRV 302
Cdd:PRK12999 278 VEFLVD-ADGNFYFIEVNPRI 297
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
54-337 |
6.55e-11 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 65.99 E-value: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 54 IMTDPD-------FADATYI---EPIT----KENILSIIKKEKVDAILPTMGGqVALNA--AMQIYESGLLgkvkFLGAN 117
Cdd:PRK08463 31 IYTEPDreclhvkIADEAYRigtDPIKgyldVKRIVEIAKACGADAIHPGYGF-LSENYefAKAVEDAGII----FIGPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 118 PEAIKKGEDRQIFKESMKKIGMDLPKSMYAYNyNEALKAIDE----IGFPLMIRSSFTLGGAGSGVVYNLEE----FQEL 189
Cdd:PRK08463 106 SEVIRKMGNKNIARYLMKKNGIPIVPGTEKLN-SESMEEIKIfarkIGYPVILKASGGGGGRGIRVVHKEEDlenaFESC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 190 AQQALSLSPIGEILIEESLLGWKEYEMEVIRDKFDNCIIV----CSIENldpmgvHTGDSITIAPALTLTDKEYQAMRNA 265
Cdd:PRK08463 185 KREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLcerdCSIQR------RHQKVIEIAPCPSISDNLRKTMGVT 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956323229 266 SFEILREIGVDTGGSnVQFAINpENGRMIVIEMNPRVSRSSALASKATGYPIAKVATLLAVGFSLDEIKNDI 337
Cdd:PRK08463 259 AVAAAKAVGYTNAGT-IEFLLD-DYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQSDI 328
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
650-845 |
9.78e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 65.15 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 650 FAKQLSAFGAKIIGTNARVIDLAEDRKKFSEFIVKLGInqP----KNGTAYSIEEAILKANEIGYPVLVRPSYVLGGRAM 725
Cdd:PRK08462 93 FVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGV--PvipgSDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGM 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 726 RIVHNEEEL-KLYV---KEAVKLSNKSPILIDQFLDNASEFDVDAICDGK-NVyvagimehieeagIHSGDSACSL---- 796
Cdd:PRK08462 171 RVVEDESDLeNLYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILGDKHgNV-------------IHVGERDCSLqrrh 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956323229 797 -------PPCNIDEKIQELIIQKTADIALNLGVIGLLNIQFALYQN-ELYIIEVNPR 845
Cdd:PRK08462 238 qklieesPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNlDFYFMEMNTR 294
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
111-337 |
1.84e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 64.74 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 111 VKFLGANPEAIKKGEDRQIFKESMKKIGMDL-PKSMYAY-NYNEALKAIDEIGFPLMIRSsfTLGGAGSGV--------- 179
Cdd:PRK07178 99 IKFIGPSAEVIRRMGDKTEARRAMIKAGVPVtPGSEGNLaDLDEALAEAERIGYPVMLKA--TSGGGGRGIrrcnsreel 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 180 VYNLEEFQELAQQALSLSpigEILIEESLLGWKEYEMEVIRDKFDNCIIV----CSIENldpmgvHTGDSITIAPALTLT 255
Cdd:PRK07178 177 EQNFPRVISEATKAFGSA---EVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQLT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 256 DKEYQAMRNASFEILREIGVDTGGSnVQFAINpENGRMIVIEMNPRVSRSSALASKATGYPIAKVATLLAVGFSLDEIKN 335
Cdd:PRK07178 248 PEQRAYIGDLAVRAAKAVGYENAGT-VEFLLD-ADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSYKQE 325
|
..
gi 1956323229 336 DI 337
Cdd:PRK07178 326 DI 327
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
649-870 |
2.56e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 64.23 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 649 KFAKQLSAFGAKIIGTNARVIDLAEDRKKFSEFIVKLGInqP----KNGTAYSIEEAILKANEIGYPVLVRPSYVLGGRA 724
Cdd:PRK08654 90 EFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGV--PvlpgTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 725 MRIVHNEEELKLYVKEAVKLSNK----SPILIDQFLDNASEFDVDAICDGK-NVyvagimehieeagIHSGDSACSlppc 799
Cdd:PRK08654 168 MRVVYSEEELEDAIESTQSIAQSafgdSTVFIEKYLEKPRHIEIQILADKHgNV-------------IHLGDRECS---- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 800 nIDEKIQELI------------IQKTADIALNLG-VIGLLN---IQFaLYQN-ELYIIEVNPRASRTVPFVSKATGIALA 862
Cdd:PRK08654 231 -IQRRHQKLIeeapspimtpelRERMGEAAVKAAkAINYENagtVEF-LYSNgNFYFLEMNTRLQVEHPITEMVTGIDIV 308
|
....*...
gi 1956323229 863 KVATRVMW 870
Cdd:PRK08654 309 KEQIKIAA 316
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-337 |
2.59e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 64.01 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 1 MPKRndINTILLIGSGPIIIgqacefdysgtQAIKTLKELGYRVVL------INSNPA-----TIMTDPDFADATYIEPi 69
Cdd:PRK12833 1 MPSR--IRKVLVANRGEIAV-----------RIIRAARELGMRTVAacsdadRDSLAArmadeAVHIGPSHAAKSYLNP- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 70 tkENILSIIKKEKVDAILPTMGGqVALNAAM--QIYESGLLgkvkFLGANPEAIKKGEDRQIFKESMKKIGMD-LPKSMY 146
Cdd:PRK12833 67 --AAILAAARQCGADAIHPGYGF-LSENAAFaeAVEAAGLI----FVGPDAQTIRTMGDKARARRTARRAGVPtVPGSDG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 147 A-YNYNEALKAIDEIGFPLMIRSSFTLGGAGSGVVYNLEEFQE---LAQ-QALSLSPIGEILIEESLLGWKEYEMEVIRD 221
Cdd:PRK12833 140 VvASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpLAQrEAQAAFGDGGVYLERFIARARHIEVQILGD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 222 KFDNCIIV---CSIENldpmgvHTGDSITIAPALTLTDKEYQAMRNASFEILREIGVDTGGSnVQFAINPENGRMIVIEM 298
Cdd:PRK12833 220 GERVVHLFereCSLQR------RRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGT-LEYLFDDARGEFYFIEM 292
|
330 340 350
....*....|....*....|....*....|....*....
gi 1956323229 299 NPRVSRSSALASKATGYPIAKVATLLAVGFSLDEIKNDI 337
Cdd:PRK12833 293 NTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRFAQGDI 331
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
649-863 |
2.77e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 63.96 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 649 KFAKQLSAFGAKIIGTNARVIDLAEDRKKFSEFIVKLG--INQPKNGTAYSIEEAILKANEIGYPVLVRPSYVLGGRAMR 726
Cdd:PRK05586 90 KFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGvpVVPGSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 727 IVHNEEEL----KLYVKEAVKLSNKSPILIDQFLDNASEFDVDAICDG-KNVyvagimehieeagIHSGDSACSL----- 796
Cdd:PRK05586 170 IVRSEEELikafNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNyGNV-------------VHLGERDCSLqrrnq 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956323229 797 -----PPCNI-DEKIQELI--IQKTADIALNLGVIGllNIQFAL-YQNELYIIEVNPRASRTVPFVSKATGIALAK 863
Cdd:PRK05586 237 kvleeAPSPVmTEELRKKMgeIAVKAAKAVNYKNAG--TIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVK 310
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
672-845 |
4.42e-10 |
|
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: 59.32 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 672 AEDRKKFSEFIVKLGINQPKNGTAYSIEEAilkaneiGYPVLVRPSYVLGGRAMRIVHNEEELKLYVkeavklsnkSPIL 751
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTPETLQAEELLRE-------EKKYVVKPRDGCGGEGVRKVENGREDEAFI---------ENVL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 752 IDQFLDnASEFDVDAICDGKNVYVAGI-MEHIEEAGIHSGDSACSLP-PCNIDEKIQELIIQKTADIAlnlGVIGLLNIQ 829
Cdd:pfam02655 65 VQEFIE-GEPLSVSLLSDGEKALPLSVnRQYIDNGGSGFVYAGNVTPsRTELKEEIIELAEEVVECLP---GLRGYVGVD 140
|
170
....*....|....*.
gi 1956323229 830 FALYQNELYIIEVNPR 845
Cdd:pfam02655 141 LVLKDNEPYVIEVNPR 156
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
588-863 |
5.79e-10 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 61.50 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 588 ALKDMGIKTIMYNcnPETVSTDYDISDVLYfEPIDFEHLRAVIEKEKPDgiivHFGgqtpLKFAKQLSAFGAKIIGtNAR 667
Cdd:COG0189 22 AAQRRGHEVEVID--PDDLTLDLGRAPELY-RGEDLSEFDAVLPRIDPP----FYG----LALLRQLEAAGVPVVN-DPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 668 VIDLAEDRKKFSEFIVKLGINQPKNGTAYSIEEAILKANEIGYPVLVRPSYVLGGRAMRIVHNEEELKLYVkEAVKLSNK 747
Cdd:COG0189 90 AIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESIL-EALTELGS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 748 SPILIDQFLDNASEFDVDAIC-DGKNVY-VAGIMEHIEEAG-IHSGDSACslpPCNIDEKIQELIIqKTADiALNLGVIG 824
Cdd:COG0189 169 EPVLVQEFIPEEDGRDIRVLVvGGEPVAaIRRIPAEGEFRTnLARGGRAE---PVELTDEERELAL-RAAP-ALGLDFAG 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 1956323229 825 llnIQFALYQNELYIIEVNPRASrtVPFVSKATGIALAK 863
Cdd:COG0189 244 ---VDLIEDDDGPLVLEVNVTPG--FRGLERATGVDIAE 277
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
618-863 |
9.10e-10 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 61.86 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 618 FEPIDFEH-LRAVIEKEKPDGIIvhFGG---QTPLKFAkqLSAFGAKIIGTNARVIDLAEDRKKFSEFIVKLGINQPkng 693
Cdd:COG2232 56 FDLEDLPAaLLELAAADDPDGLV--YGSgfeNFPELLE--RLARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHP--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 694 taysieEAILKANEIGYPVLVRPSYVLGGRAMRIVHNEEELKlyvkeavklsnkSPILIDQFLD--NASefdVDAICDGK 771
Cdd:COG2232 129 ------ETRFEPPPDPGPWLVKPIGGAGGWHIRPADSEAPPA------------PGRYFQRYVEgtPAS---VLFLADGS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 772 NVYVAGIME-HIEEAG----IHSGdsacSLPPCNIDEKIQELIIQKTADIALNLGVIGLLNIQFALYQNELYIIEVNPRA 846
Cdd:COG2232 188 DARVLGFNRqLIGPAGerpfRYGG----NIGPLALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRP 263
|
250
....*....|....*..
gi 1956323229 847 SRTVPFVSKATGIALAK 863
Cdd:COG2232 264 QASLDLYEDATGGNLFD 280
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
72-302 |
3.20e-09 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 61.25 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 72 ENILSIIKKEKVDAILPtmG-GQVALNA--AMQIYESGLlgkvKFLGANPEAIKKGEDRQIFKESMKKIGM-------DL 141
Cdd:COG1038 67 EEIIRVAKEKGVDAIHP--GyGFLSENPefARACEEAGI----TFIGPSPEVLEMLGDKVAARAAAIEAGVpvipgteGP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 142 PKSMyaynyNEALKAIDEIGFPLMIRSSftLGGAGSG--VVYNLEEFQELAQQALS--LSPIG--EILIEESLLGWKEYE 215
Cdd:COG1038 141 VDDL-----EEALAFAEEIGYPVMLKAA--AGGGGRGmrVVRSEEELEEAFESARReaKAAFGddEVFLEKYIERPKHIE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 216 MEVIRDKFDNciIV------CS--------IEnldpmgvhtgdsitIAPALTLTDKEYQAMRNASFEILREIGVDTGGSn 281
Cdd:COG1038 214 VQILGDKHGN--IVhlferdCSvqrrhqkvVE--------------IAPAPNLDEELREAICEAAVKLAKAVGYVNAGT- 276
|
250 260
....*....|....*....|.
gi 1956323229 282 VQFAINpENGRMIVIEMNPRV 302
Cdd:COG1038 277 VEFLVD-DDGNFYFIEVNPRI 296
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
73-302 |
5.25e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 59.82 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 73 NILSIIKKEKVDAILPtmG-GQVALNA--AMQIYESGLlgkvKFLGANPEAIKKGEDRQIFKESMKKIGMDL-PKSMYA- 147
Cdd:PRK08591 65 AIISAAEITGADAIHP--GyGFLSENAdfAEICEDSGF----TFIGPSAETIRLMGDKVTAKATMKKAGVPVvPGSDGPv 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 148 YNYNEALKAIDEIGFPLMIRSsfTLGGAGSG--VVYNLEEFQELAQQALS--LSPIG--EILIEESLLGWKEYEMEVIRD 221
Cdd:PRK08591 139 DDEEEALAIAKEIGYPVIIKA--TAGGGGRGmrVVRTEAELEKAFSMARAeaKAAFGnpGVYMEKYLENPRHIEIQVLAD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 222 KFDNCIIV----CSI---------EnldpmgvhtgdsitiAPALTLTDKEYQAMRNASFEILREIGVdTGGSNVQFaINP 288
Cdd:PRK08591 217 GHGNAIHLgerdCSLqrrhqkvleE---------------APSPAITEELRRKIGEAAVKAAKAIGY-RGAGTIEF-LYE 279
|
250
....*....|....
gi 1956323229 289 ENGRMIVIEMNPRV 302
Cdd:PRK08591 280 KNGEFYFIEMNTRI 293
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
30-312 |
1.80e-08 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 57.59 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 30 GTQAIKTLKE--LGYRVvlinsnpatIMTDPD-------FADATYIEP-ITKEN----ILSIIKKEKVDAILPTMGGQVA 95
Cdd:PRK12767 12 RVQLVKALKKslLKGRV---------IGADISelapalyFADKFYVVPkVTDPNyidrLLDICKKEKIDLLIPLIDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 96 LNAAMQ--IYESGllgkVKFLGANPEAIKKGEDRQIFKESMKKIGMDLPKSmYAYNYNEALKAID---EIGFPLMIRSSF 170
Cdd:PRK12767 83 LLAQNRdrFEEIG----VKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKS-YLPESLEDFKAALakgELQFPLFVKPRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 171 TLGGAGSGVVYNLEEFQELAQQALslspigEILIEESLLGwKEYEMEVIRDKFDNCIivcSIENLDPMGVHTGDSITiap 250
Cdd:PRK12767 158 GSASIGVFKVNDKEELEFLLEYVP------NLIIQEFIEG-QEYTVDVLCDLNGEVI---SIVPRKRIEVRAGETSK--- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956323229 251 ALTLTDKEYQAMRNASFEILREIGVdtggSNVQFAINpeNGRMIVIEMNPRVSRSSALASKA 312
Cdd:PRK12767 225 GVTVKDPELFKLAERLAEALGARGP----LNIQCFVT--DGEPYLFEINPRFGGGYPLSYMA 280
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
111-337 |
2.45e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 57.80 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 111 VKFLGANPEAIKKGEDRQIFKESMKKIGMDL-PKSMYAYNYNE-ALKAIDEIGFPLMIRSSFTLGGAGSGVVYNLEEFQE 188
Cdd:PRK05586 100 IVFIGPDSETIELMGNKSNAREIMIKAGVPVvPGSEGEIENEEeALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 189 LAQQALSLSPI----GEILIEESLLGWKEYEMEVIRDKFDNCIIV----CSIENldpmgvHTGDSITIAPALTLTDKEYQ 260
Cdd:PRK05586 180 AFNTAKSEAKAafgdDSMYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEELRK 253
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956323229 261 AMRNASFEILREIGVDTGGSnVQFAINpENGRMIVIEMNPRVSRSSALASKATGYPIAKVATLLAVGFSLDEIKNDI 337
Cdd:PRK05586 254 KMGEIAVKAAKAVNYKNAGT-IEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQEDI 328
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
684-845 |
3.19e-08 |
|
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: 54.18 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 684 KLGINQPKNGTAYSIEEAILKANEIGYPVLVRpSYVLG--GRAMRIVHNEEELklyvKEAVKLSNKSPILIDQFLDnase 761
Cdd:pfam02222 2 KLGLPTPRFMAAESLEELIEAGQELGYPCVVK-ARRGGydGKGQYVVRSEADL----PQAWEELGDGPVIVEEFVP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 762 FDVDAIC------DGKnVYVAGIMEHIEEAGIhsgdsaC--SLPPCNIDEKIQELIIQKTADIALNLGVIGLLNIQ-FAL 832
Cdd:pfam02222 73 FDRELSVlvvrsvDGE-TAFYPVVETIQEDGI------CrlSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVElFVT 145
|
170
....*....|...
gi 1956323229 833 YQNELYIIEVNPR 845
Cdd:pfam02222 146 EDGDLLINELAPR 158
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
562-865 |
4.02e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 56.86 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 562 VMIIGGGPNrigqgiefDYACVQAsfaLKDMGIKTIMYNCNPETVSTDYDISDVLY------FEPIDF-EHLRAVIEKEK 634
Cdd:COG3919 8 VVVLGGDIN--------ALAVARS---LGEAGVRVIVVDRDPLGPAARSRYVDEVVvvpdpgDDPEAFvDALLELAERHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 635 PDGII-VHFGGQTPL-KFAKQLSAfGAKIIGTNARVIDLAEDRKKFSEFIVKLGINQPKNGTAYSIEEAILKANEIGYPV 712
Cdd:COG3919 77 PDVLIpTGDEYVELLsRHRDELEE-HYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 713 LVRPSY--------VLGGRAMRIVHNEEELKLYVKEAVKLSNksPILIDQFL--DNASEFDVDAICDGK-NVYVAGIMEH 781
Cdd:COG3919 156 VVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAAAGY--ELIVQEYIpgDDGEMRGLTAYVDRDgEVVATFTGRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 782 IEEAGIHSGDSAcslppCNIDEKIQELiIQKTADIALNLGVIGLLNIQFaLYQ---NELYIIEVNPRASRTVPFVSKAtG 858
Cdd:COG3919 234 LRHYPPAGGNSA-----ARESVDDPEL-EEAARRLLEALGYHGFANVEF-KRDprdGEYKLIEINPRFWRSLYLATAA-G 305
|
....*..
gi 1956323229 859 IALAKVA 865
Cdd:COG3919 306 VNFPYLL 312
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
650-845 |
4.07e-08 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 57.84 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 650 FAKQLSAFGAKIIGTNARVIDLAEDRKKFSEFIVKLGInqP----KNGTAYSIEEAILKANEIGYPVLVRPSYVLGGRAM 725
Cdd:PRK12999 95 FARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGV--PvipgSEGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 726 RIVHNEEELKLYVKEAVKLSNKS----PILIDQFLDNASEFDVDAICDGK-NVYvagimeHIEEAgihsgDsaCSL---- 796
Cdd:PRK12999 173 RIVRSEEELEEAFERAKREAKAAfgndEVYLEKYVENPRHIEVQILGDKHgNVV------HLYER-----D--CSVqrrh 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956323229 797 -------PPCNIDEKIQELIIQKTADIALNLGVIGLLNIQFALYQN-ELYIIEVNPR 845
Cdd:PRK12999 240 qkvveiaPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADgNFYFIEVNPR 296
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
622-845 |
8.04e-08 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 55.91 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 622 DFEHLRAVIEKEKPDGIIvhfggqtPLKFA------KQLSAFGAKIIgTNARVIDLAEDRKKFSEFIVK-LGINQPKNGT 694
Cdd:PRK09288 63 DGDALRAVIEREKPDYIV-------PEIEAiatdalVELEKEGFNVV-PTARATRLTMNREGIRRLAAEeLGLPTSPYRF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 695 AYSIEEAILKANEIGYPVLVRPsyVLG--GRAMRIVHNEEELKLYVKEAVKLS--NKSPILIDQFLDNASEFDVDAIC-- 768
Cdd:PRK09288 135 ADSLEELRAAVEEIGYPCVVKP--VMSssGKGQSVVRSPEDIEKAWEYAQEGGrgGAGRVIVEEFIDFDYEITLLTVRav 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 769 DGKNVYVAGImEHIEEagihSGDSACSLPPCNIDEKiqelIIQKTADIAL----NLGVIGLLNIQFALYQNELYIIEVNP 844
Cdd:PRK09288 213 DGGTHFCAPI-GHRQE----DGDYRESWQPQPMSPA----ALEEAQEIAKkvtdALGGRGLFGVELFVKGDEVYFSEVSP 283
|
.
gi 1956323229 845 R 845
Cdd:PRK09288 284 R 284
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
663-872 |
8.74e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 56.39 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 663 GTNARVIDLAEDRKKFSEFIVKLGINQPKNGTAYSIEEAILKANEIGYPVLVRPSYVLGGRAMRIVHNEEELkLYVKEAV 742
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEA-AAHCAAL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 743 KLSNKSPILIDQFLDNAsEFDVDAICDGKNVYVAGIMehieeaGIHSGDSACSLP-----PCNIDEKIQELIIqKTADIA 817
Cdd:PRK02186 175 RRAGTRAALVQAYVEGD-EYSVETLTVARGHQVLGIT------RKHLGPPPHFVEighdfPAPLSAPQRERIV-RTVLRA 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956323229 818 LN-LGV-IGLLNIQFALYQNELYIIEVNPR-ASRTVP-FVSKATGIALAKVATRvMWQG 872
Cdd:PRK02186 247 LDaVGYaFGPAHTELRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVID-LHLG 304
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
697-734 |
1.66e-07 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 55.02 E-value: 1.66e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1956323229 697 SIEEAILKANEIGYPVLVRPSYVLGGRAMRIVHNEEEL 734
Cdd:COG4770 140 DAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEEL 177
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
707-844 |
2.06e-07 |
|
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: 52.70 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 707 EIGYPVLVRPSyVLGGR-AMRIVHNEEELKLYVKEAVKLSNKspILIDQFLdNASEFDVdAICDGKNVYVAGIMEHIEEA 785
Cdd:pfam07478 34 ALGYPVFVKPA-RLGSSvGVSKVESREELQAAIEEAFQYDEK--VLVEEGI-EGREIEC-AVLGNEDPEVSPVGEIVPSG 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956323229 786 GI------HSGDSACSLPPCNIDEKIQELiIQKTADIAL-NLGVIGLLNIQFAL-YQNELYIIEVNP 844
Cdd:pfam07478 109 GFydyeakYIDDSAQIVVPADLEEEQEEQ-IQELALKAYkALGCRGLARVDFFLtEDGEIVLNEVNT 174
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
697-741 |
2.72e-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: 55.09 E-value: 2.72e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1956323229 697 SIEEAILKANEIGYPVLVRPSYVLGGRAMRIVHNEEELKLYVKEA 741
Cdd:COG1038 143 DLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESA 187
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
650-868 |
4.59e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 53.57 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 650 FAKQLSAFGAKIIGTNARVIDLAEDRKKFSEFIVKLGInqP----KNGTAYSIEEAILKANEIGYPVLVRPSYVLGGRAM 725
Cdd:PRK07178 90 LAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGV--PvtpgSEGNLADLDEALAEAERIGYPVMLKATSGGGGRGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 726 RIVHNEEELK----LYVKEAVKLSNKSPILIDQFLDNASEFDVDAICDGK-NVyvagimehieeagIHSGDSACSlppcn 800
Cdd:PRK07178 168 RRCNSREELEqnfpRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHgNV-------------VHLFERDCS----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 801 IDEKIQELI--------IQKTADIALNLGV-----IGLLN---IQFAL-YQNELYIIEVNPRASRTVPFVSKATGIALAK 863
Cdd:PRK07178 230 IQRRNQKLIeiapspqlTPEQRAYIGDLAVraakaVGYENagtVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVR 309
|
....*
gi 1956323229 864 VATRV 868
Cdd:PRK07178 310 EQIRI 314
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
686-844 |
5.02e-06 |
|
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: 49.72 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 686 GINQPKNGTAYSIEEAILKANE--IGYPVLVRPsyVLGG--RAMRIVHNEEELKLYVKEAVKLSNKspILIDQFLDnASE 761
Cdd:COG1181 107 GLPTPPYVVLRRGELADLEAIEeeLGLPLFVKP--AREGssVGVSKVKNAEELAAALEEAFKYDDK--VLVEEFID-GRE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 762 FDVdAICDGKNVYVAGIMEHIEEAGI-------HSGDSA--CslpPCNIDEKIQELIiqktADIALN----LGVIGLLNI 828
Cdd:COG1181 182 VTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEyiC---PARLPEELEERI----QELALKafraLGCRGYARV 253
|
170
....*....|....*..
gi 1956323229 829 QFALY-QNELYIIEVNP 844
Cdd:COG1181 254 DFRLDeDGEPYLLEVNT 270
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
650-861 |
9.25e-06 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 49.43 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 650 FAKQLSAFGAKIIGTNARVIDLAEDRKKFSEFIVKLGI-----NQPKNgtAYSIEEAILKANEIGYPVLVRPSYVLGGRA 724
Cdd:PRK08463 90 FAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIpivpgTEKLN--SESMEEIKIFARKIGYPVILKASGGGGGRG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 725 MRIVHNEEELKLYV----KEAVKLSNKSPILIDQFLDNASEFDVDAICDG-KNVyvagimehieeagIHSGDSACS---- 795
Cdd:PRK08463 168 IRVVHKEEDLENAFesckREALAYFNNDEVFMEKYVVNPRHIEFQILGDNyGNI-------------IHLCERDCSiqrr 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956323229 796 ------LPPC-NIDEKIQELIIQKTADIALNLGVIGLLNIQFALYQ-NELYIIEVNPRASRTVPFVSKATGIAL 861
Cdd:PRK08463 235 hqkvieIAPCpSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDyNRFYFMEMNTRIQVEHGVTEEITGIDL 308
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
749-865 |
9.57e-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: 46.07 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 749 PILIDQFLDNAsEFDVDAICDGKNVYVAgimehieeagihsgdsacsLPPCNIDEKIQEL-----IIQKTADIALNLGVI 823
Cdd:pfam15632 4 PLLVMEYLPGP-EYSVDCLAGHGELIAA-------------------VPRRKGDGGIQTLeddpeLIEAARRLAEAFGLD 63
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1956323229 824 GLLNIQFALYQNELYIIEVNPRASRTVPfVSKATGIALAKVA 865
Cdd:pfam15632 64 GLFNVQFRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLA 104
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
590-845 |
1.86e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 48.15 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 590 KDMGIKTIMY----NCnP------ETVSTDYD----------ISDVLYFEP--IDFEHLRAvIEKEKPdgiiVHfggqtP 647
Cdd:COG0026 11 KRLGYRVHVLdpdpDS-PaaqvadEHIVADYDdeealrefaeRCDVVTFEFenVPAEALEA-LEAEVP----VR-----P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 648 lkfakqlsafgakiigtNARVIDLAEDR---KkfsEFIVKLGINQPKNGTAYSIEEAILKANEIGYPVLVRPS---YvlG 721
Cdd:COG0026 80 -----------------GPEALEIAQDRlleK---AFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggY--D 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 722 GRAMRIVHNEEELklyvKEAVKLSNKSPILIDQFLDNASE---------------FDVdaicdGKNVYVAGIMEHieeag 786
Cdd:COG0026 138 GKGQVVIKSAADL----EAAWAALGGGPCILEEFVPFERElsvivarspdgevatYPV-----VENVHRNGILDE----- 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 787 ihsgdsacSLPPCNIDEKIQELIIQKTADIALNLGVIGLLNIQ-FALYQNELYIIEVNPR 845
Cdd:COG0026 204 --------SIAPARISEALAAEAEEIAKRIAEALDYVGVLAVEfFVTKDGELLVNEIAPR 255
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
685-851 |
2.89e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 44.33 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 685 LGINQPKNGTAYSIEEAILKANEIGYPVLVRPsyVLGGR--AMRIVHNEEELKLYVKEAVKLSNKspILIDQFLDNAsEF 762
Cdd:PRK01372 109 AGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAFKYDDE--VLVEKYIKGR-EL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 763 DVdAICDGKnvyVAGIMEhIE--------EAGIHSGDSA--CslpPCNIDEKIQeliiQKTADIALN----LGVIGLLNI 828
Cdd:PRK01372 184 TV-AVLGGK---ALPVIE-IVpagefydyEAKYLAGGTQyiC---PAGLPAEIE----AELQELALKayraLGCRGWGRV 251
|
170 180
....*....|....*....|....
gi 1956323229 829 QFAL-YQNELYIIEVNprasrTVP 851
Cdd:PRK01372 252 DFMLdEDGKPYLLEVN-----TQP 270
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
126-299 |
2.20e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 41.58 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 126 DRQIFKESMKKIGMDLPKSMYaynYNEALKAIDEIGFPLMIRSSftlGGAGSGVVYNLEEFQELAQQALSLSPIGEILIE 205
Cdd:PRK14569 98 DKMISKEILMHHRMPTPMAKF---LTDKLVAEDEISFPVAVKPS---SGGSSIATFKVKSIQELKHAYEEASKYGEVMIE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 206 ESLLGwKEYEMEVIRDK-FDNCIIVCSIENLDPMGVHTGDSITIAPALTLTDKEYQaMRNASFEILREIGVdTGGSNVQF 284
Cdd:PRK14569 172 QWVTG-KEITVAIVNDEvYSSVWIEPQNEFYDYESKYSGKSIYHSPSGLCEQKELE-VRQLAKKAYDLLGC-SGHARVDF 248
|
170
....*....|....*
gi 1956323229 285 aINPENGRMIVIEMN 299
Cdd:PRK14569 249 -IYDDRGNFYIMEIN 262
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
686-809 |
4.01e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 41.30 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 686 GINQPKNGTAYSIEEAILKANEIGYPVLVRPSYVLGGRAMRI-VHNEEELKLYVKEAVKLSNKspILIDQFLDnASEFDV 764
Cdd:PRK14016 226 GVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESSD--VIVERYIP-GKDHRL 302
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1956323229 765 dAICDGKNVYVA-GIMEHIEEAGIHSgdsacslppcnidekIQELI 809
Cdd:PRK14016 303 -LVVGGKLVAAArREPPHVIGDGKHT---------------IRELI 332
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
81-300 |
5.09e-03 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 40.96 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 81 EKVDAILPTMGGQVALNAAMQIYESgLLGKvKFLGANPEAIKKGEDRQIFKESMKKIGMD----LPKSMYAYNYNEAL-- 154
Cdd:PRK14573 525 AKVDVVLPILHGPFGEDGTMQGFLE-IIGK-PYTGPSLAFSAIAMDKVLTKRFASDVGVPvvpyQPLTLAGWKREPELcl 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 155 -KAIDEIGFPLMIRSSFTLGGAGSGVVYNLEEFQELAQQALSLSpiGEILIEESLLGWKEYEMEVIRDKfDNCIIVCS-- 231
Cdd:PRK14573 603 aHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYD--TDVFVEESRLGSREIEVSCLGDG-SSAYVIAGph 679
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956323229 232 --------IENLDPMGVHTGDSITIAPALTLTDKEYQAMRNASFEILREIgVDTGGSNVQFAINPEnGRMIVIEMNP 300
Cdd:PRK14573 680 errgsggfIDYQEKYGLSGKSSAQIVFDLDLSKESQEQVLELAERIYRLL-QGKGSCRIDFFLDEE-GNFWLSEMNP 754
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
27-206 |
5.69e-03 |
|
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: 39.92 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 27 DYSGTQAIKTLKELGYRVVLINsnpatimtdpdfADATYIEPITKENILSIIKKEKVDAILPTMGGQVALNAAMQIYESG 106
Cdd:COG0189 13 KDSTKALIEAAQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPRIDPPFYGLALLRQLEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 107 llgKVKFLGaNPEAIKKGEDRQIFKESMKKIGMDLPKSMYAYNYNEALKAIDEIGFPLMIRSSFTLGGAGSGVVYNLEEF 186
Cdd:COG0189 81 ---GVPVVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDAL 156
|
170 180
....*....|....*....|
gi 1956323229 187 QELAQQALSLSPiGEILIEE 206
Cdd:COG0189 157 ESILEALTELGS-EPVLVQE 175
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
131-269 |
7.77e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 38.78 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 131 KESMKKIGMDLPKSMYAYNYNEALKAIDEIG-FPLMIRSSFTLGGAGSG----VVYNLEEFQELAQQALSLS-------- 197
Cdd:pfam08442 8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGgKVYVVKAQVLAGGRGKAggvkLAKSPEEAKEVAKEMLGKNlvtkqtgp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 198 ---PIGEILIEESLLGWKEYEMEVIRDKFDNCI-IVCSIE---NLDPMGVHTGDSI---TIAPALTLTDkeYQAmRNASF 267
Cdd:pfam08442 88 dgqPVNKVLVEEALDIKKEYYLSIVLDRASKGPvIIASTEggvDIEEVAAKNPEKIhkfPIDPLKGLTP--YQA-REIAF 164
|
..
gi 1956323229 268 EI 269
Cdd:pfam08442 165 KL 166
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
131-210 |
8.47e-03 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 38.80 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956323229 131 KESMKKIGmdLPKSMYAY--NYNEALKAIDEIGFP-LMIRSSFTLGGAGSGVVYNLEEFQELAQQALSLSPIGE----IL 203
Cdd:pfam01071 7 KDFMKRYG--IPTAEYETftDPEEAKSYIQEAGFPaIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEagetVV 84
|
....*..
gi 1956323229 204 IEESLLG 210
Cdd:pfam01071 85 IEEFLEG 91
|
|
| |
