|
Name |
Accession |
Description |
Interval |
E-value |
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
2-1177 |
0e+00 |
|
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 274264 [Multi-domain] Cd Length: 1201 Bit Score: 1916.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 2 FTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAAESYLNVDAVIAACKATGAQAVHPG 81
Cdd:TIGR02712 1 FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 82 YGFLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTDLLQSVDEALSAAETVGYPVMLKSTAG 161
Cdd:TIGR02712 81 YGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGTGLLSSLDEALEAAKEIGYPVMLKSTAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 162 GGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVVEET 241
Cdd:TIGR02712 161 GGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 242 PAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDPQREEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGEDV 321
Cdd:TIGR02712 241 PAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 322 L--SGARGLTPKGAAIEMRVYAEMPHADFRPSAGLLTEVVFPDNARVDGWIETGTEVTPFYDPMLAKLIVAAEDRPAAIE 399
Cdd:TIGR02712 321 DfaSLNISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPDDVRVDTWVETGTEVSPEYDPMLAKIIVHGSDREDAIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 400 KLKAALAETSISGIETNLDYLRTIAASELLASAKVATTALRDLAFVPDVVEVLAPGAQSSIQELPGRLGLWHVGVPPSGP 479
Cdd:TIGR02712 401 KLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNSFVYTPPAIEVLSPGAQTTVQDYPGRTGYWDVGVPPSGP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 480 MDERSFRHANRLVGNADVTAALELTVSGPILRFYADQTIALAGARMAMTCDGTQLPHGEPVLIRAGQVLSIGTIEGPGQR 559
Cdd:TIGR02712 481 MDSYSFRLANRIVGNDEGAAGLEITLTGPTLRFHSDAVIAITGAPAPATLDGQPVPQWKPITVKAGSTLSIGKIAGSGCR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 560 AYLAVAGGFAAPVVLGSRATFGLGQFGGNATGTLKTGHVLHFARQVATEPATPAKEPATL----TREWDVGVVYGPHGAP 635
Cdd:TIGR02712 561 TYLAIRGGIDVPDYLGSRSTFTLGQFGGHAGRALKTGDVLHIGEPELHEASIPAPIPAAPippyGSEWRIGVLYGPHGAP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 636 DFFEDNDIETLFSTAYEVHFNSARTGVRLIGPAPVWARHDGGEAGLHPSNLHDNAYAIGAIDFTGDMPIILGPDGPSLGG 715
Cdd:TIGR02712 641 DFFTEEDIEEFFSAEWKVHYNSNRTGVRLIGPKPKWARSDGGEAGLHPSNIHDNVYAIGAIDFTGDMPVILGPDGPSLGG 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 716 FVCPAVIARDEQWKMGQFKPGDRIRFHAVA------------------------RPEDPIAGPAvrrpTEETGSPILGIS 771
Cdd:TIGR02712 721 FVCPAVVAEAELWKVGQLKPGDTVRFVPISedsaralkdaqdvaisnldslsllSLPDSLALPS----YEDPGVLARVPA 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 772 EDGPVSVVYRRQGDDNLLVEYGPMTLDIALRLRVHLLMQAVIEARLPGIVDLTPGIRSLQIHYDGTQLTRRRLLGLLAEI 851
Cdd:TIGR02712 797 DGDSPKVVYRQAGDRYLLVEYGENVLDIALRYRIHLLMEALQKAKLPGIIDLTPGIRSLQIHYDPRVISQSELLEVLVAI 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 852 EATLPAAQEVTVPSRIVHLPLSWNDPDAELAMRKYQELVRPNAPWCPSNIEFIRRINGLPDERAVRDIVFDASYLVLGLG 931
Cdd:TIGR02712 877 EEQLPAAEDLQVPSRIVHLPLSWEDPATLLAVERYMETVRSDAPWCPSNIEFIRRVNGLSSRDDVRDTVFDASYLVLGLG 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 932 DVYLGAPVATPTDPRHRLVTTKYNPARTWTPENAVGIGGAYMCIYGMEGPGGYQLFGRTIQVWNTWRETPAFaRGKPWLL 1011
Cdd:TIGR02712 957 DVYLGAPVATPLDPRHRLLTTKYNPARTWTPENAVGIGGAYMCIYGMEGPGGYQLVGRTIQIWNRYRLGGAF-QDGPWLL 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1012 NFFDQIRFFPVSNQELTEARDAFPHGGYPIRIEETEFSYAAYEKELQANSASIGRFKATQQAAFDAERRRWKEAGLDSFV 1091
Cdd:TIGR02712 1036 RFFDQIRFYPVSEEELLELREEFDNGRFKVRVEETVFDLAEYQRFLADNADSIEAFKERQQGAFEAERARWIASGNADLA 1115
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1092 TDEGTGESPDGDIPDGCFGVASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGD 1171
Cdd:TIGR02712 1116 EEVTEAPEEEADLPEGAEQVESEYAGNFWKVLVEVGDRVEAGQPLVILEAMKMEMPVSAPVAGKVTKILCQPGDMVDAGD 1195
|
....*.
gi 573471879 1172 IIVVLE 1177
Cdd:TIGR02712 1196 IVAVLE 1201
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-456 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 713.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1 MFTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAAESYLNVDAVIAACKATGAQAVHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 81 GYGFLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTD-LLQSVDEALSAAETVGYPVMLKST 159
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDgPVQDAEEALAIAEEIGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 160 AGGGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVVE 239
Cdd:COG4770 161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 240 ETPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDPQReEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGE 319
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADG-NFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 320 DVLSGARGLTPKGAAIEMRVYAEMPHADFRPSAGLLTEVVFP--DNARVDGWIETGTEVTPFYDPMLAKLIVAAEDRPAA 397
Cdd:COG4770 320 PLPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPggPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 573471879 398 IEKLKAALAETSISGIETNLDYLRTIAASELLASAKVATTAL---RDLAFVPDVVEVLAPGA 456
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIereLAELLAAAAPEELALAA 461
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-427 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 576.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1 MFTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAAESYLNVDAVIAACKATGAQAVHP 80
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 81 GYGFLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTD-LLQSVDEALSAAETVGYPVMLKST 159
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDgPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 160 AGGGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVVE 239
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 240 ETPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDPQrEEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGE 319
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKN-GEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 320 DVLSGARGLTPKGAAIEMRVYAEMPHADFRPSAGLLTEVVFPD--NARVDGWIETGTEVTPFYDPMLAKLIVAAEDRPAA 397
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGgpGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399
|
410 420 430
....*....|....*....|....*....|
gi 573471879 398 IEKLKAALAETSISGIETNLDYLRTIAASE 427
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDP 429
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-441 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 546.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1 MFTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAAESYLNVDAVIAACKATGAQAVHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 81 GYGFLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTDL-LQSVDEALSAAETVGYPVMLKST 159
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTnLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 160 AGGGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVVE 239
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 240 ETPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDPQrEEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGE 319
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQ-KNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 320 dVLSGARG-LTPKGAAIEMRVYAEMPHAdFRPSAGLLTEVVFPDN--ARVDGWIETGTEVTPFYDPMLAKLIVAAEDRPA 396
Cdd:PRK06111 320 -KLSFTQDdIKRSGHAIEVRIYAEDPKT-FFPSPGKITDLTLPGGegVRHDHAVENGVTVTPFYDPMIAKLIAHGETREE 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 573471879 397 AIEKLKAALAETSISGIETNLDYLRTIAASELLASAKVATTALRD 441
Cdd:PRK06111 398 AISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-423 |
1.27e-172 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 518.38 E-value: 1.27e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1 MFTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAAESYLNVDAVIAACKATGAQAVHP 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 81 GYGFLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTD-LLQSVDEALSAAETVGYPVMLKST 159
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEeGIEDIEEAKEIAEEIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 160 AGGGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVVE 239
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 240 ETPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDpqREEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGE 319
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 320 DVLSGARGLTPKGAAIEMRVYAEMPHADFRPSAGLLTEVVFPD--NARVDGWIETGTEVTPFYDPMLAKLIVAAEDRPAA 397
Cdd:PRK08654 319 ELSFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGgpGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEA 398
|
410 420
....*....|....*....|....*.
gi 573471879 398 IEKLKAALAETSISGIETNLDYLRTI 423
Cdd:PRK08654 399 IARMRRALYEYVIVGVKTNIPFHKAV 424
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-437 |
4.95e-166 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 522.78 E-value: 4.95e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1 MFTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPA-AESYLNVDAVIAACKATGAQAVH 79
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHpVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 80 PGYGFLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTD-LLQSVDEALSAAETVGYPVMLKS 158
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEgPIDDIEEALEFAEEIGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 159 TAGGGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVV 238
Cdd:PRK12999 164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 239 EETPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDPqREEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAG 318
Cdd:PRK12999 244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDA-DGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 319 EDvLSGARG-------LTPKGAAIEMRVYAEMPHADFRPSAGLLTEVVFPDNA--RVD-GWIETGTEVTPFYDPMLAKLI 388
Cdd:PRK12999 323 AT-LHDLEIgipsqedIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFgvRLDgGNAFAGAEITPYYDSLLVKLT 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 573471879 389 VAAEDRPAAIEKLKAALAETSISGIETNLDYLRTIAASELLASAKVATT 437
Cdd:PRK12999 402 AWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTS 450
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
4-439 |
3.55e-165 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 497.74 E-value: 3.55e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 4 KVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAAESYLNVDAVIAACKATGAQAVHPGYG 83
Cdd:PRK12833 7 KVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGYG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 84 FLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTD-LLQSVDEALSAAETVGYPVMLKSTAGG 162
Cdd:PRK12833 87 FLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDgVVASLDAALEVAARIGYPLMIKAAAGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 163 GGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKgGVIALGERDCSLQRRNQKVVEETP 242
Cdd:PRK12833 167 GGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 243 APGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDPQREEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGEDVL 322
Cdd:PRK12833 246 SPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 323 SGARGLTPKGAAIEMRVYAEMPHADFRPSAGLLTEVVFPDNA--RVDGWIETGTEVTPFYDPMLAKLIVAAEDRPAAIEK 400
Cdd:PRK12833 326 FAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPgvRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALAR 405
|
410 420 430
....*....|....*....|....*....|....*....
gi 573471879 401 LKAALAETSISGIETNLDYLRTIAASELLASAKVATTAL 439
Cdd:PRK12833 406 AARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFL 444
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-437 |
3.04e-163 |
|
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: 515.40 E-value: 3.04e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1 MFTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAA-ESYLNVDAVIAACKATGAQAVH 79
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 80 PGYGFLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTD-LLQSVDEALSAAETVGYPVMLKS 158
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEgPVDDLEEALAFAEEIGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 159 TAGGGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVV 238
Cdd:COG1038 163 AAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 239 EETPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDPQrEEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAG 318
Cdd:COG1038 243 EIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDD-GNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 319 EDVLSGARGL------TPKGAAIEMRVYAEMPHADFRPSAGLLTevvfpdnA---------RVD-GWIETGTEVTPFYDP 382
Cdd:COG1038 322 YSLDDPEIGIpsqediRLNGYAIQCRITTEDPANNFMPDTGRIT-------AyrsaggfgiRLDgGNAYTGAVITPYYDS 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 573471879 383 MLAKLIVAAEDRPAAIEKLKAALAETSISGIETNLDYLRTIAASELLASAKVATT 437
Cdd:COG1038 395 LLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTS 449
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-419 |
5.69e-161 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 486.14 E-value: 5.69e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1 MFTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAAESYLNVDAVIAACKATGAQAVHP 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 81 GYGFLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTD-LLQSVDEALSAAETVGYPVMLKST 159
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEgEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 160 AGGGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVVE 239
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 240 ETPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDpQREEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGE 319
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 320 DVLSGARGLTPKGAAIEMRVYAEMPHADFRPSAGLLTEVVFPD--NARVDGWIETGTEVTPFYDPMLAKLIVAAEDRPAA 397
Cdd:PRK05586 320 KLSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGglGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399
|
410 420
....*....|....*....|..
gi 573471879 398 IEKLKAALAETSISGIETNLDY 419
Cdd:PRK05586 400 IQKMKRALGEFIIEGVNTNIDF 421
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-436 |
1.62e-160 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 485.03 E-value: 1.62e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1 MFTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAAESYLNVDAVIAACKATGAQAVHP 80
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 81 GYGFLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTD-LLQSVDEALSAAETVGYPVMLKST 159
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDgLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 160 AGGGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVVE 239
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 240 ETPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDpQREEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGE 319
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLD-KNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 320 DVLSGARGLTPKGAAIEMRVYAEMPHADFRPSAGLLTEVVFPDN--ARVDGWIETGTEVTPFYDPMLAKLIVAAEDRPAA 397
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGpgVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430
....*....|....*....|....*....|....*....
gi 573471879 398 IEKLKAALAETSISGIETNLDYLRTIAASELLASAKVAT 436
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNI 438
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
4-419 |
1.50e-149 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 456.13 E-value: 1.50e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 4 KVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAAESYLNVDAVIAACKATGAQAVHPGYG 83
Cdd:PRK08462 6 RILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGYG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 84 FLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTD-LLQSVDEALSAAETVGYPVMLKSTAGG 162
Cdd:PRK08462 86 FLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDgALKSYEEAKKIAKEIGYPVILKAAAGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 163 GGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVVEETP 242
Cdd:PRK08462 166 GGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 243 APGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDpQREEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGEDVL 322
Cdd:PRK08462 246 AVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 323 SgARGLTPKGAAIEMRVYAEMPHAdFRPSAGLLTEVVFP--DNARVDGWIETGTEVTPFYDPMLAKLIVAAEDRPAAIEK 400
Cdd:PRK08462 325 S-QESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPggRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAK 402
|
410
....*....|....*....
gi 573471879 401 LKAALAETSISGIETNLDY 419
Cdd:PRK08462 403 MKRALKEFKVEGIKTTIPF 421
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-463 |
9.01e-145 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 444.55 E-value: 9.01e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1 MFTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAAeSYLNVDAVIAACKATGAQAVHP 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPLA-GYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 81 GYGFLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTD-LLQSVDEALSAAETVGYPVMLKST 159
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEgNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 160 AGGGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVVE 239
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 240 ETPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDPQrEEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGE 319
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDAD-GEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 320 DVLSGARGLTPKGAAIEMRVYAEMPHADFRPSAGLLTEVVFPD--NARVDGWIETGTEVTPFYDPMLAKLIVAAEDRPAA 397
Cdd:PRK07178 319 PLSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGgpGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 573471879 398 IEKLKAALAETSISGIETNLDYLRTIAASELLASAKVATtalrdlAFVPDVVEVLAPGAQSSIQEL 463
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNT------SFVESHPELTNYSIKRKPEEL 458
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-426 |
3.52e-126 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 396.11 E-value: 3.52e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1 MFTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAaESYLNVDAVIAACKATGAQAVHP 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 81 GYGFLSENIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTDLL--QSVDEALSAAETVGYPVMLKS 158
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLnsESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 159 TAGGGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVV 238
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 239 EETPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDpQREEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAG 318
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD-DYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 319 EDVLSGARGLTPKGAAIEMRVYAEMPHADFRPSAGLLTEvVFP---DNARVDGWIETGTEVTPFYDPMLAKLIVAAEDRP 395
Cdd:PRK08463 319 EILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITE-YYPalgPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYD 397
|
410 420 430
....*....|....*....|....*....|.
gi 573471879 396 AAIEKLKAALAETSISGIETNLDYLRTIAAS 426
Cdd:PRK08463 398 LAVNKLERALKEFVIDGIRTTIPFLIAITKT 428
|
|
| AHS2 |
smart00797 |
Allophanate hydrolase subunit 2; This domain represents subunit 2 of allophanate hydrolase ... |
471-748 |
2.66e-109 |
|
Allophanate hydrolase subunit 2; This domain represents subunit 2 of allophanate hydrolase (AHS2).
Pssm-ID: 214821 Cd Length: 280 Bit Score: 343.31 E-value: 2.66e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 471 HVGVPPSGPMDERSFRHANRLVGNADVTAALELTVSGPILRFYADQTIALAGARMAMTCDGTQLPHGEPVLIRAGQVLSI 550
Cdd:smart00797 1 HLGVPPSGAMDQLALRLANRLVGNPENAAALEITLGGPTLRFTADAVIALTGADFPATLDGQPVPPWKPFAVRAGQVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 551 GTIEGpGQRAYLAVAGGFAAPVVLGSRATFGLGQFGGNATGTLKTGHVLHFARQVATEPAT---PAKEPATLTREWDVGV 627
Cdd:smart00797 81 GAPKA-GARAYLAVRGGIDVPPVLGSRSTDTRGGFGGFEGRALKAGDVLPLGAAPAAAPAGaalPAALIPDYGKEWVIRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 628 VYGPHgaPDFFEDNDIETLFSTAYEVHFNSARTGVRLIGPAPVWarhdggeagLHPSNLHDNAYAIGAIDFTGD-MPIIL 706
Cdd:smart00797 160 IPGPH--PDFFTEESIERFFSSEWKVTPNSDRMGYRLEGPKLEW---------LHPSNIISEGVAIGAIQVPPDgQPIIL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 573471879 707 GPDGPSLGGFVCPAVIARDEQWKMGQFKPGDRIRFHAVARPE 748
Cdd:smart00797 229 LADRQTTGGYPKIATVISADLWKLAQLRPGDKVRFVPVSLEE 270
|
|
| PxpC |
COG1984 |
5-oxoprolinase subunit C/Allophanate hydrolase subunit 2 [Amino acid transport and metabolism]; ... |
449-743 |
8.00e-106 |
|
5-oxoprolinase subunit C/Allophanate hydrolase subunit 2 [Amino acid transport and metabolism];
Pssm-ID: 441587 Cd Length: 285 Bit Score: 334.37 E-value: 8.00e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 449 VEVLAPGAQSSIQELpGRLGLWHVGVPPSGPMDERSFRHANRLVGNADVTAALELTVSGPILRFYADQTIALAGARMAMT 528
Cdd:COG1984 3 LEVLKPGLLTTVQDL-GRPGYQHLGVPPSGAMDRLALRLANRLVGNPEGAAALEITLGGPTLRFEEDTVIALTGADMPAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 529 CDGTQLPHGEPVLIRAGQVLSIGTIEGpGQRAYLAVAGGFAAPVVLGSRATFGLGQFGGNATGTLKTGHVLHFARQVATE 608
Cdd:COG1984 82 LDGRPVPPWRPVAVKAGDVLTLGAPRA-GARAYLAVAGGIDVPPVLGSRSTDLRAGLGGLEGRALQAGDVLPLGAPAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 609 PATPAKEPATLTREWDVGVVYGPHgaPDFFEDNDIETLFSTAYEVHFNSARTGVRLIGPAPVWArhdggeaglHPSNLHD 688
Cdd:COG1984 161 PGRGLPAELLPGEEVTLRVVPGPQ--DDWFTEEAIERFFSSEWTVTPQSDRMGYRLEGPPLERA---------HPSEILS 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 573471879 689 NAYAIGAIDFTGD-MPIILGPDGPSLGGFVCPAVIARDEQWKMGQFKPGDRIRFHA 743
Cdd:COG1984 230 EGIVPGAIQVPPDgQPIVLLADRQTTGGYPKIATVISADLPRLAQLRPGDTVRFVP 285
|
|
| CT_A_B |
pfam02626 |
Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ... |
472-743 |
7.19e-104 |
|
Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the A and B subdomains of the CT domain. This domain covers the whole length of KipA (kinase A) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.
Pssm-ID: 460627 Cd Length: 264 Bit Score: 328.22 E-value: 7.19e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 472 VGVPPSGPMDERSFRHANRLVGNADVTAALELTVSGPILRFYADQTIALAGARMAMTCDGTQLPHGEPVLIRAGQVLSIG 551
Cdd:pfam02626 1 LGVPPSGAMDPLALRLANRLVGNPEGAAALEITLGGPTLRFHADAVIAVTGADMPATLDGKPVPMWTPVAVKAGDVLSFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 552 TIEGpGQRAYLAVAGGFAAPVVLGSRATFGLGQFGGNATGTLKTGHVLHFARQVATEPAT---PAKEPATLTREWDVGVV 628
Cdd:pfam02626 81 APRG-GLRAYLAVAGGFDVPPVLGSRSTDLLGGLGGHEGRPLRAGDVLPLGPPAAPAPALaplPPAPPPPDTPEWVIRVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 629 YGPHGapDFFEDNDIETLFSTAYEVHFNSARTGVRLIGPApvwarhdggeagLHP---SNLHDNAYAIGAIDF-TGDMPI 704
Cdd:pfam02626 160 PGPQD--DWFTPEALETFFSTEWTVSPNSDRMGYRLDGEA------------LHPargSNILSEGYVPGAIQVpPGGQPI 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 573471879 705 ILGPDGPSLGGFVCPAVIARDEQWKMGQFKPGDRIRFHA 743
Cdd:pfam02626 226 ILLADGQTTGGYPKIATVISADLWKLAQLRPGDKVRFVP 264
|
|
| urea_amlyse_rel |
TIGR00724 |
biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces ... |
449-744 |
2.74e-81 |
|
biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces cerevisiae is a 1835 amino acid protein with an amidase domain, a biotin/lipoyl cofactor attachment domain, a carbamoyl-phosphate synthase L chain-like domain, and uncharacterized regions. It has both urea carboxylase and allophanate hydrolase activities. This model models a domain that represents uncharacterized prokaryotic proteins of about 300 amino acids, regions of prokaryotic urea carboxylase and of the urea carboxylase region of yeast urea amidolyase, and regions of other biotin-containing proteins. [Unknown function, General]
Pssm-ID: 129807 Cd Length: 314 Bit Score: 268.58 E-value: 2.74e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 449 VEVLAPGAQSSIQELpGRLGLWHVGVPPSGPMDERSFRHANRLVGNADVTAALELTVSGPILRFYADQTIALAGARMAMT 528
Cdd:TIGR00724 2 IEILRAGSHTLIQDL-GRVGYRRIGVPHSGAMDAYSLRLANRLVGNPDDTPAIEVTLGGPTIRFHCDVIFAVTGADTDLC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 529 CDGTQL-PHGEPVLIRAGQVLSIGTIEGpGQRAYLAVAGGFAAPVVLGSRATFGLGQFGGNATGTLKTGHVLHFARQVAT 607
Cdd:TIGR00724 81 LNDGQViPQWRPYEVKRGQILSLGRLKS-GMRGYLAVRGGIDVPPVLGSCSTDLRANIGGYEGRPLKAGDVLPLGSNELD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 608 EPATPAKEPATLtrEWDVGVVYGPHGAPDFFEDNDIETLFSTAYEVHFNSARTGVRLIGPAPVWARHDggeaglHPSNLH 687
Cdd:TIGR00724 160 LNEPQGLIPQIP--EWRIEIRVLPGPEYDFFKRESIEAFWRSEWKVSSNSDRMGYRLQGPKLKHARPN------RELLTH 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 573471879 688 DNAYAIGAIDFTGdMPIILGPDGPSLGGFVCPAVIARDEQWKMGQFKPGDRIRFHAV 744
Cdd:TIGR00724 232 GIVYGSIQVPPNG-QPIILMADAQTTGGYPKIAVVIEADLWKVAQVRPGQSIKFVPL 287
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
116-320 |
6.57e-74 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 243.75 E-value: 6.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 116 KHTARELAKASGVPLLPGTD-LLQSVDEALSAAETVGYPVMLKSTAGGGGIGMQLCTDVASLKASFESVQRTARASFGDA 194
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAgPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 195 RVYIERFVAEARHVEVQIFGDGKGGVIALGERDCSLQRRNQKVVEETPAPGLSAETRARLHKAAVDLGRSVSYESAGTVE 274
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 573471879 275 FIYDPQREEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGED 320
Cdd:pfam02786 162 FALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYP 207
|
|
| PxpB |
COG2049 |
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ... |
777-1034 |
1.53e-69 |
|
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism];
Pssm-ID: 441652 Cd Length: 229 Bit Score: 232.34 E-value: 1.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 777 SVVYRRQGDDNLLVEYGPmTLDIALRLRVHLLMQAVIEARLPGIVDLTPGIRSLQIHYDGTQLTRRRLLGLLAEIEATLp 856
Cdd:COG2049 4 AMRILPAGDRALLVEFGD-EIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAEL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 857 aAQEVTVPSRIVHLPLSWNDPdaelamrkyqelvrpnapWCPsNIEFIRRINGLpDERAVRDIVFDASYLVLGLGdVYLG 936
Cdd:COG2049 82 -DAAAEVPSRLVEIPVCYDGE------------------FGP-DLEEVARHNGL-SVEEVIALHTAAEYRVYMLG-FAPG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 937 APVATPTDPRhrLVTTKYNPARTWTPENAVGIGGAYMCIYGMEGPGGYQLFGRT-IQVWNTWREtpafargKPWLLNFFD 1015
Cdd:COG2049 140 FPYLGGLDPR--LATPRRATPRTRVPAGSVGIAGAQTGIYPLESPGGWQLIGRTpLPLFDPDRE-------PPALLRPGD 210
|
250
....*....|....*....
gi 573471879 1016 QIRFFPVSNQELTEARDAF 1034
Cdd:COG2049 211 RVRFVPISEEEFDALRGEV 229
|
|
| AHS1 |
smart00796 |
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ... |
778-1002 |
7.51e-67 |
|
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase (AHS1).
Pssm-ID: 214820 Cd Length: 201 Bit Score: 223.55 E-value: 7.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 778 VVYRRQGDDNLLVEYGPMtLDIALRLRVHLLMQAVIEARLPGIVDLTPGIRSLQIHYDGTQLTRRRLLGLLAEIEAtLPA 857
Cdd:smart00796 1 MRIRPAGDRALLVEFGDE-IDLALNRRVLALARALRAAPLPGVVELVPGYRSLLVHFDPLVIDPAALLARLRALEA-LPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 858 AQEVTVPSRIVHLPLSWNDPdaelamrkyqelvrpnapWCPsNIEFIRRINGLpDERAVRDIVFDASYLVLGLGdVYLGA 937
Cdd:smart00796 79 AEALEVPGRIIEIPVCYGGE------------------FGP-DLEFVARHNGL-SVDEVIRLHSAAEYRVYMLG-FAPGF 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 573471879 938 PVATPTDPRhrLVTTKYNPARTWTPENAVGIGGAYMCIYGMEGPGGYQLFGRT-IQVWNTWRETPA 1002
Cdd:smart00796 138 PYLGGLDPR--LATPRRSTPRTRVPAGSVGIAGAQTGIYPLESPGGWQLIGRTpLPLFDPDREPPA 201
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-109 |
4.25e-55 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 186.54 E-value: 4.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 2 FTKVLIANRGEIAVRVIRTLKRMGIASVAVYSDADRFSMPALTADEAVRLGPAPAAESYLNVDAVIAACKATGAQAVHPG 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 573471879 82 YGFLSENIGFAERLAAEGIAFIGPRPEH 109
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
62-322 |
6.46e-55 |
|
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: 192.01 E-value: 6.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 62 NVDAVIAACKATGAQavHPGYGFLSEN---IGFAERLAAE-GIAfiGPRPEHLSAFGLKHTARELAKASGVPLlPGTDLL 137
Cdd:COG0439 1 DIDAIIAAAAELARE--TGIDAVLSESefaVETAAELAEElGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFALV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 138 QSVDEALSAAETVGYPVMLKSTAGGGGIGMQLCTDVASLKASFESVQRTARASFGDARVYIERFVaEARHVEVQIFGDGk 217
Cdd:COG0439 76 DSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFL-EGREYSVEGLVRD- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 218 GGVIAlgerdCSLQRRNQK---VVE---ETPAPgLSAETRARLHKAAVDLGRSVSY-ESAGTVEFIYDPqREEFYFLEVN 290
Cdd:COG0439 154 GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLTP-DGEPYLIEIN 226
|
250 260 270
....*....|....*....|....*....|....
gi 573471879 291 TRLQVEH--PVTEAVFGIDLVEWMIRQAAGEDVL 322
Cdd:COG0439 227 ARLGGEHipPLTELATGVDLVREQIRLALGEPRI 260
|
|
| CT_C_D |
pfam02682 |
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ... |
780-1003 |
9.38e-45 |
|
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the C and D subdomains of the CT domain. This domain covers the whole length of kipI (kinase A inhibitor) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.
Pssm-ID: 426925 Cd Length: 201 Bit Score: 160.41 E-value: 9.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 780 YRRQGDDNLLVEYGPmTLDIALRLRVHLLMQAVIEARLPGIVDLTPGIRSLQIHYDGTQLTRRRLLGLLAEIEATLPAAQ 859
Cdd:pfam02682 2 IRPAGDRALLVEFGD-EIDLALNRRVLALAAALRAAPLPGVVEVVPGYRSLLVHYDPLVTDLAALEARLRALLAALEAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 860 EVTvpSRIVHLPLSWNDPDAElamrkyqelvrpnapwcpsNIEFIRRINGLpDERAVRDIVFDASYLVLGLGdVYLGAPV 939
Cdd:pfam02682 81 APG--GRLIEIPVCYDGEFGP-------------------DLAEVAAHNGL-SVEEVIRLHSAAEYRVYFLG-FAPGFPY 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 573471879 940 ATPTDPRhrLVTTKYNPARTWTPENAVGIGGAYMCIYGMEGPGGYQLFGRT-IQVWNTWRETPAF 1003
Cdd:pfam02682 138 LGGLDPR--LAVPRRATPRTRVPAGSVGIAGRQTGIYPLESPGGWQLIGRTpLPLFDPDRDPPAL 200
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-439 |
2.93e-38 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 138.39 E-value: 2.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 336 EMRVYAEMPHADFRPSAGLLTEVVFPD--NARVDGWIETGTEVTPFYDPMLAKLIVAAEDRPAAIEKLKAALAETSISGI 413
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGgpGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*.
gi 573471879 414 ETNLDYLRTIAASELLASAKVATTAL 439
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFL 106
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
336-436 |
7.60e-37 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 134.46 E-value: 7.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 336 EMRVYAEMPHADFRPSAGLLTEVVFPD--NARVDGWIETGTEVTPFYDPMLAKLIVAAEDRPAAIEKLKAALAETSISGI 413
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGgpGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|...
gi 573471879 414 ETNLDYLRTIAASELLASAKVAT 436
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGDVDT 103
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1111-1176 |
3.07e-24 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 96.72 E-value: 3.07e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 573471879 1111 VASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVL 1176
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1111-1178 |
6.25e-17 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 86.73 E-value: 6.25e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 573471879 1111 VASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVLEE 1178
Cdd:PRK12999 1079 VGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1111-1176 |
2.41e-16 |
|
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: 84.75 E-value: 2.41e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 573471879 1111 VASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVL 1176
Cdd:COG1038 1079 IGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1111-1177 |
1.92e-15 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 72.13 E-value: 1.92e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 573471879 1111 VASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVLE 1177
Cdd:PRK08225 4 VYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
3-382 |
3.24e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 75.74 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 3 TKVLIANRGEIAVRVIRTLKRMGIASVAVysDADRFSMPALT--ADEAVRLgPAPAAESYLNVDAVIAACKATGAQAVHP 80
Cdd:COG3919 6 FRVVVLGGDINALAVARSLGEAGVRVIVV--DRDPLGPAARSryVDEVVVV-PDPGDDPEAFVDALLELAERHGPDVLIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 81 GY----GFLSENigfAERLAaEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLlPGTDLLQSVDEALSAAETVGYPVML 156
Cdd:COG3919 83 TGdeyvELLSRH---RDELE-EHYRLPYPDADLLDRLLDKERFYELAEELGVPV-PKTVVLDSADDLDALAEDLGFPVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 157 KSTAG--------GGGIGMQLCTDVASLKASFesvqrtARASFGDARVYIERFVAEARHVEVQIFG--DGKGGVIALGER 226
Cdd:COG3919 158 KPADSvgydelsfPGKKKVFYVDDREELLALL------RRIAAAGYELIVQEYIPGDDGEMRGLTAyvDRDGEVVATFTG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 227 dcslqrrnQKVVEETPAPGLSA----ETRARLHKAAVDLGRSVSYESAGTVEFIYDPQREEFYFLEVNTRLQVEHP-VTE 301
Cdd:COG3919 232 --------RKLRHYPPAGGNSAaresVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFWRSLYlATA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 302 AvfGIDLVEWMIRQAAGEDVlsgarglTPKGAAIEMRVYAEMPHadfrpsaGLLTEVVFPDN--ARVDGWIETGTEVTPF 379
Cdd:COG3919 304 A--GVNFPYLLYDDAVGRPL-------EPVPAYREGVLWRVLPG-------DLLLRYLRDGElrKRLRELLRRGKVVDAV 367
|
...
gi 573471879 380 YDP 382
Cdd:COG3919 368 YAL 370
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1092-1177 |
3.68e-14 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 70.69 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1092 TDEGTGESPDGDIPDGCFGVASAVPGNI-------WKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPG 1164
Cdd:COG0511 44 AAAAPAAAAAAAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENG 123
|
90
....*....|...
gi 573471879 1165 RNVKAGDIIVVLE 1177
Cdd:COG0511 124 QPVEYGQPLFVIE 136
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
1105-1177 |
4.27e-14 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 76.80 E-value: 4.27e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 573471879 1105 PDGCFGVASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVLE 1177
Cdd:PRK09282 519 ASAPGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1119-1176 |
8.75e-14 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 67.24 E-value: 8.75e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 573471879 1119 IWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVL 1176
Cdd:pfam00364 16 VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
99-291 |
2.38e-13 |
|
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: 72.06 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 99 GIAFIGPRPeHLSAFGL-KHTARELAKASGVPLLPGTDLLQS-VDEALSAAETVGYPVMLKSTAGGGGIGMQLCTDVASL 176
Cdd:COG1181 79 GIPYTGSGV-LASALAMdKALTKRVLAAAGLPTPPYVVLRRGeLADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEEL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 177 KASFEsvqrTARAsfGDARVYIERFVaEARHVEVQIFGDGKGGVIALGERD-----CSLQ--RRNQKVVEETPAPgLSAE 249
Cdd:COG1181 158 AAALE----EAFK--YDDKVLVEEFI-DGREVTVGVLGNGGPRALPPIEIVpengfYDYEakYTDGGTEYICPAR-LPEE 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 573471879 250 TRARLHKAAV---------DLGRsvsyesagtVEFIYDPQrEEFYFLEVNT 291
Cdd:COG1181 230 LEERIQELALkafralgcrGYAR---------VDFRLDED-GEPYLLEVNT 270
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
14-331 |
1.28e-12 |
|
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: 72.34 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 14 AVRVIRTLKRMGIASVAVYSDADRFSMPALTADeavRLGPAPAAESYL-------NVDAVIAAckaTGAQAVhpgygfls 86
Cdd:TIGR01369 577 CVHAVLALRELGYETIMINYNPETVSTDYDTSD---RLYFEPLTFEDVmniieleKPEGVIVQ---FGGQTP-------- 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 87 enIGFAERLAAEGIAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGTdLLQSVDEALSAAETVGYPVMLKSTAGGGGIG 166
Cdd:TIGR01369 643 --LNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWK-TATSVEEAVEFASEIGYPVLVRPSYVLGGRA 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 167 MQLCTDVASLKASFEsvqrTARASFGDARVYIERFVAEARHVEVQIFGDGKGGVI-ALGERdcslqrrnqkvVEE----- 240
Cdd:TIGR01369 720 MEIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIpGIMEH-----------IEEagvhs 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 241 ------TPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDpqREEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIR 314
Cdd:TIGR01369 785 gdstcvLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK--DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVR 862
|
330
....*....|....*..
gi 573471879 315 QAAGEDVLSGARGLTPK 331
Cdd:TIGR01369 863 VMLGKKLEELGVGKEKE 879
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
1111-1176 |
3.35e-12 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 70.73 E-value: 3.35e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 573471879 1111 VASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVL 1176
Cdd:PRK14040 527 VTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
34-343 |
3.37e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 69.14 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 34 DADRFSmPALT-ADEAVRLgPAPAAESYLnvDAVIAACKATGAQAVHPGY----GFLSENigfAERLAAEGIAFIGPRPE 108
Cdd:PRK12767 32 DISELA-PALYfADKFYVV-PKVTDPNYI--DRLLDICKKEKIDLLIPLIdpelPLLAQN---RDRFEEIGVKVLVSSKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 109 HLSAFGLKHTARELAKASGVPL----LPGTdlLQSVDEALSAAEtVGYPVMLKSTAGGGGIGMQLCTDVASLKASFESVq 184
Cdd:PRK12767 105 VIEICNDKWLTYEFLKENGIPTpksyLPES--LEDFKAALAKGE-LQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYV- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 185 rtarasfgdARVYIERFVaEARHVEVQIFGDGKGGVIalgerdCSLQRRNQKVVeetpapglSAET-------RARLHKA 257
Cdd:PRK12767 181 ---------PNLIIQEFI-EGQEYTVDVLCDLNGEVI------SIVPRKRIEVR--------AGETskgvtvkDPELFKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 258 AVDLGRSVSYESAGTVEFIYDPQreEFYFLEVNTRLQVEHPVTeAVFGIDLVEWMIRQAAGEDVLSGARGLTPKgaaIEM 337
Cdd:PRK12767 237 AERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFGGGYPLS-YMAGANEPDWIIRNLLGGENEPIIGEYKEG---LYM 310
|
....*.
gi 573471879 338 RVYAEM 343
Cdd:PRK12767 311 RRYDEV 316
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
16-314 |
1.36e-11 |
|
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: 66.89 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 16 RVIRTLKRMGIAsvAVYSDADRFSMPALTADEAVRLGPAPAaesylnVDAVIAACkatgaqaVHPGYGFlseniGFAERL 95
Cdd:COG0189 18 ALIEAAQRRGHE--VEVIDPDDLTLDLGRAPELYRGEDLSE------FDAVLPRI-------DPPFYGL-----ALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 96 AAEGIAFIgPRPEHLSAFGLKHTARELAKASGVPLlPGTDLLQSVDEALSAAETVGYPVMLKSTAGGGGIGMQLCTDVAS 175
Cdd:COG0189 78 EAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPV-PPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 176 LKASFESVQRTarasfGDARVYIERFVAEARHVEVQIFG-DGKggVIAlgerdcSLQRRNQKvvEET---PAPGLSAETR 251
Cdd:COG0189 156 LESILEALTEL-----GSEPVLVQEFIPEEDGRDIRVLVvGGE--PVA------AIRRIPAE--GEFrtnLARGGRAEPV 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 573471879 252 ---ARLHKAAVDLGRSVSYESAGtVEFIYDPQReeFYFLEVNTRLQVEHpvTEAVFGIDLVEWMIR 314
Cdd:COG0189 221 eltDEERELALRAAPALGLDFAG-VDLIEDDDG--PLVLEVNVTPGFRG--LERATGVDIAEAIAD 281
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
20-340 |
3.89e-11 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 67.69 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 20 TLKRMGIASVAVYSDADRFSMPALTADeavRLGPAPaaesyLNVDAVIAACKATGAQAVHPGYGFLSEnIGFAERLAAEG 99
Cdd:PRK12815 584 ALKKEGYETIMINNNPETVSTDYDTAD---RLYFEP-----LTLEDVLNVAEAENIKGVIVQFGGQTA-INLAKGLEEAG 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 100 IAFIGPRPEHLSAFGLKHTARELAKASGVPLLPGtDLLQSVDEALSAAETVGYPVMLKSTAGGGGIGMQLCTDVASLKAS 179
Cdd:PRK12815 655 LTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG-LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAY 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 180 FEsvqrtaRASFGDARVYIERFVaEARHVEVQIFGDGK----GGVIalgERdcslqrrnqkvVEET-----------PAP 244
Cdd:PRK12815 734 LA------ENASQLYPILIDQFI-DGKEYEVDAISDGEdvtiPGII---EH-----------IEQAgvhsgdsiavlPPQ 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 245 GLSAETRARLHKAAVDLGRSVSYESAGTVEFIYdpQREEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAG----ED 320
Cdd:PRK12815 793 SLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL--ANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGkslaEL 870
|
330 340
....*....|....*....|
gi 573471879 321 VLSGARGLTPKGAAIEMRVY 340
Cdd:PRK12815 871 GYPNGLWPGSPFIHVKMPVF 890
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1094-1171 |
2.29e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 56.74 E-value: 2.29e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 573471879 1094 EGTGESPDGDIPDGCFGVASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGD 1171
Cdd:PRK06549 47 QVEAQAPQPAAAAGADAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGD 124
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
128-291 |
2.93e-09 |
|
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: 58.10 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 128 VPLLPGTDLLQSVDEALSAAETVGYPVMLKSTAGGGGIGMQLCTDVASLKASFEsvqrtaRASFGDARVYIERFVaEARH 207
Cdd:pfam07478 13 VTFTRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIE------EAFQYDEKVLVEEGI-EGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 208 VEVQIFGDGKGGVIALGER--DCSLQRRNQKVVEET-----PApGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDPQ 280
Cdd:pfam07478 86 IECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALGCRGLARVDFFLTED 164
|
170
....*....|.
gi 573471879 281 rEEFYFLEVNT 291
Cdd:pfam07478 165 -GEIVLNEVNT 174
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
119-292 |
3.96e-09 |
|
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: 60.66 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 119 ARELAKA---SGVPLLpGTD---------------LLQ-------------SVDEALSAAETVGYPVMLKSTAGGGGIGM 167
Cdd:COG0458 87 AVELEEAgilEGVKIL-GTSpdaidlaedrelfkeLLDklgipqpksgtatSVEEALAIAEEIGYPVIVRPSYVLGGRGM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 168 QLCTDVASLKasfESVQRTARASfGDARVYIERFVAEARHVEVQIFGDGKGGVIALgerdCSLQrrNqkvVEE------- 240
Cdd:COG0458 166 GIVYNEEELE---EYLERALKVS-PDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPagvhsgd 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 573471879 241 ----TPAPGLSAETRARLHKAAVDLGRSVSYESAGTVEFIYDpqREEFYFLEVNTR 292
Cdd:COG0458 233 sicvAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPR 286
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
119-320 |
9.44e-09 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 58.20 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 119 ARELAKASGVPLLPGTdLLQSVDEALSAAETVGYPVMLKSTAGGGGIGMQLCTDVASLKASFEsvqrtaRASFGDARVYI 198
Cdd:PRK01372 102 TKLVWQAAGLPTPPWI-VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALE------LAFKYDDEVLV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 199 ERFVaEARHVEVQIFGDGKGGVIALG------------ERDCSlqrrnQKVVeetPApGLSAETRARLHKAAVDLGRSVS 266
Cdd:PRK01372 175 EKYI-KGRELTVAVLGGKALPVIEIVpagefydyeakyLAGGT-----QYIC---PA-GLPAEIEAELQELALKAYRALG 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 573471879 267 YESAGTVEFIYDPQREeFYFLEVNTrlqveHP-------VTEA--VFGID---LVEWMIRQAAGED 320
Cdd:PRK01372 245 CRGWGRVDFMLDEDGK-PYLLEVNT-----QPgmtshslVPMAarAAGISfseLVDRILEDALCDR 304
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
119-365 |
2.24e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 58.71 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 119 ARELAKAsGVPLlPGTDLLQSVDEALSAAETVGYPVMLKSTAGGGGIGMQLCTDVASLKASFESVQRTarasfGDARVYI 198
Cdd:PRK02186 112 ARTLRDH-GIDV-PRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRA-----GTRAALV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 199 ERFVaEARHVEVQIFGDGKG----GVIA--LGERDCSLQrrnqkVVEETPAPgLSAETRARLHKAAVDLGRSVSYEsagt 272
Cdd:PRK02186 185 QAYV-EGDEYSVETLTVARGhqvlGITRkhLGPPPHFVE-----IGHDFPAP-LSAPQRERIVRTVLRALDAVGYA---- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 273 vefiYDPQREEF-------YFLEVNTRLQVEH-PVT-EAVFGIDLVEWMIRQAAGEdvlSGARGLTPKG-AAIEMRVyae 342
Cdd:PRK02186 254 ----FGPAHTELrvrgdtvVIIEINPRLAGGMiPVLlEEAFGVDLLDHVIDLHLGV---AAFADPTAKRyGAIRFVL--- 323
|
250 260
....*....|....*....|...
gi 573471879 343 mphadfRPSAGLLTEVVFPDNAR 365
Cdd:PRK02186 324 ------PARSGVLRGLLFLPDDI 340
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1111-1176 |
7.64e-08 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 50.58 E-value: 7.64e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 573471879 1111 VASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVL 1176
Cdd:PRK05889 5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
1124-1178 |
7.97e-08 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 50.78 E-value: 7.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 573471879 1124 VEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVLEE 1178
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1113-1176 |
2.94e-07 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 48.91 E-value: 2.94e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 573471879 1113 SAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVL 1176
Cdd:COG0508 13 SMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
99-291 |
4.33e-07 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 53.20 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 99 GIAFIGPRPEHlSAFGL-KHTARELAKASGVP------LLPGTDLLQSVDEalsAAETVGYPVMLKSTAGGGGIGMQLCT 171
Cdd:PRK01966 107 GIPYVGCGVLA-SALSMdKILTKRLLAAAGIPvapyvvLTRGDWEEASLAE---IEAKLGLPVFVKPANLGSSVGISKVK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 172 DVASLKASFEsvqrtarASFG-DARVYIERFVaEARHVEVQIFG-DGKGGVIalGERDCS----------LqrrNQKVVE 239
Cdd:PRK01966 183 NEEELAAALD-------LAFEyDRKVLVEQGI-KGREIECAVLGnDPKASVP--GEIVKPddfydyeakyL---DGSAEL 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 573471879 240 ETPAPgLSAETRARLHKAAVDLgrsvsYESAGT-----VEFIYDPQrEEFYFLEVNT 291
Cdd:PRK01966 250 IIPAD-LSEELTEKIRELAIKA-----FKALGCsglarVDFFLTED-GEIYLNEINT 299
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
120-293 |
8.90e-07 |
|
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: 53.46 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 120 RELAKASGVPLlPGTDLLQSVDEALSAAETVGYPVMLKS--TAGGGGIGmqLCTDVASLKasfESVQRTARASFGDaRVY 197
Cdd:TIGR01369 132 REAMKEIGEPV-PESEIAHSVEEALAAAKEIGYPVIVRPafTLGGTGGG--IAYNREELK---EIAERALSASPIN-QVL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 198 IERFVAEARHVEVQIFGDGKGGVIALgerdCSLQrrN----------QKVVeeTPAPGLSAETRARLHKAAVDLGRSVSY 267
Cdd:TIGR01369 205 VEKSLAGWKEIEYEVMRDSNDNCITV----CNME--NfdpmgvhtgdSIVV--APSQTLTDKEYQMLRDASIKIIRELGI 276
|
170 180
....*....|....*....|....*.
gi 573471879 268 ESAGTVEFIYDPQREEFYFLEVNTRL 293
Cdd:TIGR01369 277 EGGCNVQFALNPDSGRYYVIEVNPRV 302
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
117-225 |
2.35e-06 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 49.78 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 117 HTARELAKASGVPLLPgTDLLQSVDEALSAAETVGYPVMLKSTAGG-------GGIGMQLcTDVASLKASFESVQRTARA 189
Cdd:pfam13549 13 PEAKALLAAYGIPVVP-TRLARSPEEAVAAAEEIGYPVVLKIVSPDilhksdvGGVRLNL-RSAEAVRAAYEEILERVRR 90
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 573471879 190 SFGDAR---VYIERFVAEARHVEVQIFGDGK-GGVIALGE 225
Cdd:pfam13549 91 YRPDARiegVLVQPMAPGGRELIVGVTRDPQfGPVIMFGL 130
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1117-1176 |
2.61e-06 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 46.28 E-value: 2.61e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 1117 GNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVL 1176
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
28-407 |
1.03e-05 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 49.15 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 28 SVAVYSDADrfsMPALtADEAVRLGPAPAAESYLNV-DAVIAACKATGAQAVHPGYGFlsENigFAERLA--AEGIAFIG 104
Cdd:COG2232 30 AVDLFADLD---TRAL-AERWVRLDAESCGFDLEDLpAALLELAAADDPDGLVYGSGF--EN--FPELLErlARRLPLLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 105 PRPEHLSAFGLKHTARELAKASGVPllpgtdllqsVDEALSAAETVGYPVMLKSTAGGGGIGmqlctdvaslkasfesVQ 184
Cdd:COG2232 102 NPPEVVRRVKDPLRFFALLDELGIP----------HPETRFEPPPDPGPWLVKPIGGAGGWH----------------IR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 185 RTARASFGDARVYIERFVaEARHVEVQIFGDGKgGVIALGerdcslqrRNQKVVEETPAPG-----------LSAETRAR 253
Cdd:COG2232 156 PADSEAPPAPGRYFQRYV-EGTPASVLFLADGS-DARVLG--------FNRQLIGPAGERPfryggnigplaLPPALAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 254 LHKAAVDLGR------SVSyesagtVEFIYDPqrEEFYFLEVNTRLQVEHPVTEAVFGIDLVEWMIRQAAGEdvLSGARG 327
Cdd:COG2232 226 MRAIAEALVAalglvgLNG------VDFILDG--DGPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRGE--LPEVPR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 328 LTPKGAAIEMRVYAemPHAdfrpsagllteVVFPDNARVDGWI----ETGTEVTPfYDPmLAKLIVAAEDRPAAIEKLKA 403
Cdd:COG2232 296 PKPRRVAAKAILYA--PRD-----------LTIPDDLSWPPWVadipAPGTRIEK-GEP-VCTVLAEGPTAEAARALLER 360
|
....
gi 573471879 404 ALAE 407
Cdd:COG2232 361 RAEE 364
|
|
| TIGR00370 |
TIGR00370 |
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved] |
784-1019 |
3.40e-05 |
|
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
Pssm-ID: 129467 Cd Length: 202 Bit Score: 46.00 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 784 GDDNLLVEYGPmTLDIALRLRVHLLMQAVIEarLPGIVDLTPGIRSLQIHYDgtqlTRRRLLGLLAEIEATLPAAQEVTV 863
Cdd:TIGR00370 2 GESAVVIRLGP-PINEQVQGIVWAAAAYLEE--QPGFVECIPGMNNLTVFYD----MYEVYKHLPQRLSSPWEEVKDYEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 864 PSRIVHLPLSWNDPDAElamrkyqelvrpnapwcpsNIEFIRRINGLPDERAVrDIVFDASYLVLGLGDV----YLGAPv 939
Cdd:TIGR00370 75 NRRIIEIPVCYGGEFGP-------------------DLEEVAKINQLSPEEVI-DIHSNGEYVVYMLGFQpgfpYLGGL- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 940 atptdpRHRLVTTKYNPARTWTPENAVGIGGAYMCIYGMEGPGGYQLFGRTIQVWNTWRETPafargkPWLLNFFDQIRF 1019
Cdd:TIGR00370 134 ------PERLHTPRRASPRPSVPAGSVGIGGLQTGVYPISTPGGWQLIGKTPLALFDPQENP------PTLLRAGDIVKF 201
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
89-292 |
4.77e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 47.78 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 89 IGFAERLAAEGIAFIGPRPEHLsafglkHTA--RELAKAsgvpLLPGTDLLQ-------SVDEALSAAETVGYPVMLKST 159
Cdd:PRK05294 643 LKLAKALEAAGVPILGTSPDAI------DLAedRERFSK----LLEKLGIPQppngtatSVEEALEVAEEIGYPVLVRPS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 160 AGGGGIGMQLCTDVASLKasfESVQRTARASfGDARVYIERFVAEARHVEVQIFGDGKGGVIAlG-----ER------D- 227
Cdd:PRK05294 713 YVLGGRAMEIVYDEEELE---RYMREAVKVS-PDHPVLIDKFLEGAIEVDVDAICDGEDVLIG-GimehiEEagvhsgDs 787
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 573471879 228 -CSLqrrnqkvveetPAPGLSAETRARLHKAAVDLGRSVsyesaGT-----VEFIYdpQREEFYFLEVNTR 292
Cdd:PRK05294 788 aCSL-----------PPQTLSEEIIEEIREYTKKLALEL-----NVvglmnVQFAV--KDDEVYVIEVNPR 840
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1111-1176 |
1.02e-04 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 43.70 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 573471879 1111 VASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVL 1176
Cdd:PRK05641 87 VTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
1111-1177 |
1.72e-04 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 45.87 E-value: 1.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 573471879 1111 VASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVLE 1177
Cdd:PRK14042 528 ITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
117-206 |
2.14e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 45.50 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 117 HTARELAKASGVPLLPgTDLLQSVDEALSAAETVGYPVMLK---------STAGGGGIGMQlctDVASLKASFESVQRTA 187
Cdd:COG1042 491 AEAKALLAAYGIPVVP-TRLARSAEEAVAAAEEIGYPVVLKivspdilhkSDVGGVRLNLR---DAEAVRAAFEEILARV 566
|
90 100
....*....|....*....|..
gi 573471879 188 RASFGDAR---VYIERFVAEAR 206
Cdd:COG1042 567 RAARPDARidgVLVQPMVPGGV 588
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
116-217 |
2.97e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.15 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 116 KHTARELAKASGVPLlPGTDLLQSVDEALSAAETVGYPVMLKSTAG--GGGIGMQLcTDVASLKASFEsvqrtARASFGD 193
Cdd:PRK14016 215 KELTKRLLAAAGVPV-PEGRVVTSAEDAWEAAEEIGYPVVVKPLDGnhGRGVTVNI-TTREEIEAAYA-----VASKESS 287
|
90 100 110
....*....|....*....|....*....|....*....
gi 573471879 194 ArVYIERF---------------VAEARHVEVQIFGDGK 217
Cdd:PRK14016 288 D-VIVERYipgkdhrllvvggklVAAARREPPHVIGDGK 325
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1104-1177 |
7.26e-04 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 43.71 E-value: 7.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 573471879 1104 IPDgcfgVASAVPGNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVLE 1177
Cdd:TIGR01348 121 VPD----IGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1117-1177 |
1.69e-03 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 42.55 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 573471879 1117 GNIWKLLVEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVLE 1177
Cdd:TIGR01348 14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
122-314 |
2.44e-03 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 40.56 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 122 LAKAsGVPLlPGTDLLQSVDEALSAAETVG--YPVMLKSTAGGGGIGMQLCTDVASLKASFESVqrtarasfgDARVYIE 199
Cdd:pfam08443 11 LAKH-GIGP-PNTRLAWYPEDAEQFIEQIKrqFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSAT---------NEQILVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 200 RFVAEARHVEVQIFGDGkGGVIAlgerdcSLQRRNQKvveetpapglsAETRARLHKAAV-------DLGRSVSYESAGT 272
Cdd:pfam08443 80 EFIAEANNEDIRCLVVG-DQVVG------ALHRQSNE-----------GDFRSNLHRGGVgekyqlsQEETELAIKAAQA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 573471879 273 VEFIYD-----PQREEFYFLEVNTRLQVEhpVTEAVFGIDLVEWMIR 314
Cdd:pfam08443 142 MQLDVAgvdllRQKRGLLVCEVNSSPGLE--GIEKTLGINIAIKIIA 186
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
116-291 |
4.59e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 40.66 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 116 KHTARELAKASGVPLLPGTDL-----LQSVDEALSAAETVGYPVMLKSTAGGGGIGMQLCTDVASLKASFESVQRTaras 190
Cdd:PRK14572 131 KTRANQIFLQSGQKVAPFFELeklkyLNSPRKTLLKLESLGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFES---- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 191 fgDARVYIERFVAearHVEVQI-----FGDGKGGVIAL--------GE-RDCSLQRRNQKVVEETPAPgLSAETRARLHK 256
Cdd:PRK14572 207 --DSKVMSQSFLS---GTEVSCgvlerYRGGKRNPIALpateivpgGEfFDFESKYKQGGSEEITPAR-ISDQEMKRVQE 280
|
170 180 190
....*....|....*....|....*....|....*
gi 573471879 257 AAVDLGRSVSYESAGTVEFIYdpQREEFYFLEVNT 291
Cdd:PRK14572 281 LAIRAHESLGCKGYSRTDFII--VDGEPHILETNT 313
|
|
| BCCP |
TIGR00531 |
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify ... |
1124-1177 |
8.63e-03 |
|
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify biotin carboxyl carrier protein as a peptide of acetyl-CoA carboxylase. Scoring below the trusted cutoff is a related protein encoded in a region associated with polyketide synthesis in the prokaryote Saccharopolyspora hirsuta, and a reported chloroplast-encoded biotin carboxyl carrier protein that may be highly derived from the last common ancestral sequence. Scoring below the noise cutoff are biotin carboxyl carrier domains of other enzymes such as pyruvate carboxylase.The gene name is accB or fabE. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273123 [Multi-domain] Cd Length: 155 Bit Score: 38.28 E-value: 8.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 573471879 1124 VEPGASVAAGDTLAIIESMKMEINVTAHAAGRVRDLRAGPGRNVKAGDIIVVLE 1177
Cdd:TIGR00531 102 VEVGDKVNKGQTVCIVEAMKMMNEIEAEKAGTVVAILVENGQPVEYGEPLIVIE 155
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
138-224 |
9.37e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 40.15 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573471879 138 QSVDEALSAAETVGYPVMLKSTAGGGGIGMQLCTDVASLKASFEsvqrTARASFGDARVYIERFVAEARHVEVQIFGDGK 217
Cdd:PLN02735 724 RSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLE----TAVEVDPERPVLVDKYLSDATEIDVDALADSE 799
|
....*..
gi 573471879 218 GGVIALG 224
Cdd:PLN02735 800 GNVVIGG 806
|
|
| |
