|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
2-448 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 944.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 2 QFAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSKSYLNIPNIISAALTRNATAIHP 81
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 82 GYGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIKAT 161
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 162 AGGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLLE 241
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 242 EAPSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEK 321
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 322 LQIKQDQVIFRGHSIECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETAI 401
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 488822547 402 KRMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEHLLP 448
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLAL 447
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
3-448 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 893.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 3 FAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSKSYLNIPNIISAALTRNATAIHPG 82
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 83 YGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIKATA 162
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 163 GGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLLEE 242
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 243 APSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEKL 322
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 323 QIKQDQVIFRGHSIECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETAIK 402
Cdd:COG4770 322 PFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 488822547 403 RMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEHLLP 448
Cdd:COG4770 402 RMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAE 447
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
3-446 |
0e+00 |
|
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: 797.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 3 FAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSKSYLNIPNIISAALTRNATAIHPG 82
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 83 YGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIKATA 162
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 163 GGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLLEE 242
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 243 APSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEKL 322
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 323 QIKQDQVIFRGHSIECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETAIK 402
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 488822547 403 RMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEHL 446
Cdd:TIGR00514 402 RMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKL 445
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 749.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 3 FAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSKSYLNIPNIISAALTRNATAIHPG 82
Cdd:PRK08654 2 FKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 83 YGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIKATA 162
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 163 GGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLLEE 242
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 243 APSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKhGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEKL 322
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN-GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 323 QIKQDQVIFRGHSIECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETAIK 402
Cdd:PRK08654 321 SFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 488822547 403 RMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEH 445
Cdd:PRK08654 401 RMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEE 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-446 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 702.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 3 FAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSKSYLNIPNIISAALTRNATAIHPG 82
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 83 YGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIKATA 162
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 163 GGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLLEE 242
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 243 APSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEKL 322
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 323 QIKQDQVIFRGHSIECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETAIK 402
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQ 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 488822547 403 RMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEHL 446
Cdd:PRK05586 402 KMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKL 445
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-445 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 686.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 1 MQFAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPS-SKSYLNIPNIISAALTRNATAI 79
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHpVRAYLDIDEIIRVAKQAGVDAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 80 HPGYGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIK 159
Cdd:PRK12999 83 HPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 160 ATAGGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKL 239
Cdd:PRK12999 163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 240 LEEAPSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQG 319
Cdd:PRK12999 243 VEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 320 EKL------QIKQDQVIFRGHSIECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDS-HVYTDYEIPPYYDSLIGKLIV 392
Cdd:PRK12999 323 ATLhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVKLTA 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 488822547 393 WGENRETAIKRMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEH 445
Cdd:PRK12999 403 WGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDET 455
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
3-446 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 682.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 3 FAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSKSYLNIPNIISAALTRNATAIHPG 82
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 83 YGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIKATA 162
Cdd:PRK06111 82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 163 GGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLLEE 242
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 243 APSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEKL 322
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 323 QIKQDQVIFRGHSIECRINAEDPDhNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETAIK 402
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDPK-TFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAIS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 488822547 403 RMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEHL 446
Cdd:PRK06111 401 RLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQL 444
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-445 |
0e+00 |
|
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: 672.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 1 MQFAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSS-KSYLNIPNIISAALTRNATAI 79
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 80 HPGYGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIK 159
Cdd:COG1038 82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 160 ATAGGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKL 239
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 240 LEEAPSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQG 319
Cdd:COG1038 242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 320 EKL---QI---KQDQVIFRGHSIECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDS-HVYTDYEIPPYYDSLIGKLIV 392
Cdd:COG1038 322 YSLddpEIgipSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGgNAYTGAVITPYYDSLLVKVTA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 488822547 393 WGENRETAIKRMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEH 445
Cdd:COG1038 402 WGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDET 454
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 640.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 1 MQFAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSKSYLNIPNIISAALTRNATAIH 80
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 81 PGYGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIKA 160
Cdd:PRK08462 82 PGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 161 TAGGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLL 240
Cdd:PRK08462 162 AAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 241 EEAPSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGE 320
Cdd:PRK08462 242 EESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 321 KLqIKQDQVIFRGHSIECRINAEDPDhNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETA 400
Cdd:PRK08462 322 EL-PSQESIKLKGHAIECRITAEDPK-KFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 488822547 401 IKRMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEH 445
Cdd:PRK08462 400 IAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 620.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 3 FAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSkSYLNIPNIISAALTRNATAIHPG 82
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPLA-GYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 83 YGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIKATA 162
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 163 GGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLLEE 242
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 243 APSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEKL 322
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 323 QIKQDQVIFRGHSIECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETAIK 402
Cdd:PRK07178 321 SYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALD 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 488822547 403 RMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEH 445
Cdd:PRK07178 401 RGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESH 443
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
5-443 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 589.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 5 KILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSKSYLNIPNIISAALTRNATAIHPGYG 84
Cdd:PRK12833 7 KVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGYG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 85 FLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIKATAGG 164
Cdd:PRK12833 87 FLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 165 GGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHgNVIHLGERDCSIQRRHQKLLEEAP 244
Cdd:PRK12833 167 GGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 245 SPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKH-GNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEKLQ 323
Cdd:PRK12833 246 SPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDArGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 324 IKQDQVIFRGHSIECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETAIKR 403
Cdd:PRK12833 326 FAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALAR 405
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 488822547 404 MKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQ 443
Cdd:PRK12833 406 AARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
3-442 |
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: 538.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 3 FAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSKSYLNIPNIISAALTRNATAIHPG 82
Cdd:TIGR02712 1 FDTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 83 YGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGgLITSEAEAKRIADDIGYPVLIKATA 162
Cdd:TIGR02712 81 YGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGTG-LLSSLDEALEAAKEIGYPVMLKSTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 163 GGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLLEE 242
Cdd:TIGR02712 160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 243 APSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKH-GNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEK 321
Cdd:TIGR02712 240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEArDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 322 L---QIKQDQVIfRGHSIECRINAEDPDHNFRPHPGKISGYLPPGgpGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRE 398
Cdd:TIGR02712 320 PdfaSLNISLTP-RGAAIEARVYAENPAKNFQPSPGLLTDVQFPD--DVRVDTWVETGTEVSPEYDPMLAKIIVHGSDRE 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 488822547 399 TAIKRMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFI 442
Cdd:TIGR02712 397 DAILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTL 440
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
5-445 |
0e+00 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 535.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 5 KILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSK---SYLNIPNIISAALTRNATAIHP 81
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLGpieAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 82 GYGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIKAT 161
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 162 AGGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLLE 241
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 242 EAPSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEK 321
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 322 LQIK------QDQVIFRGHSIECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDS-HVYTDYEIPPYYDSLIGKLIVWG 394
Cdd:TIGR01235 321 LPTPqlgvpnQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGgNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 488822547 395 ENRETAIKRMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEH 445
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTT 451
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
2-446 |
0e+00 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 527.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 2 QFAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSsKSYLNIPNIISAALTRNATAIHP 81
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPI-KGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 82 GYGFLAENARFAEICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGSGGLITSEAEA-KRIADDIGYPVLIKA 160
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEiKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 161 TAGGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLL 240
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 241 EEAPSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGE 320
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 321 KLQIKQDQVIFRGHSIECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETA 400
Cdd:PRK08463 320 ILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 488822547 401 IKRMKRALRECAITGVPTTIDFHRKILETPAFLAGDVYTNFIQEHL 446
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHM 445
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
116-322 |
2.38e-101 |
|
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: 301.15 E-value: 2.38e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 116 DKSTAKKTMQKAGVPTIPGSGGLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGNMLKAAQGEAEAAFGN 195
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 196 SGVYLEKFIECPRHIEFQILADSHGNVIHLGERDCSIQRRHQKLLEEAPSPFLTPHLRSKMGNAAVKAAKSINYVGVGTV 275
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488822547 276 EFLVD-KHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEKL 322
Cdd:pfam02786 161 EFALDpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
63-321 |
9.51e-78 |
|
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: 242.47 E-value: 9.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 63 NIPNIISAALtrnatAIHPGYGF---LAENAR----FAEICADHQLTfiGPSPSAILAMGDKSTAKKTMQKAGVPTiPGS 135
Cdd:COG0439 1 DIDAIIAAAA-----ELARETGIdavLSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 136 GgLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGNMLKAAQGEAEAAFGNSGVYLEKFIECpRHIEFQIL 215
Cdd:COG0439 73 A-LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 216 ADsHGNVIHlgerdCSIQRRHQK------LLEEAPSPfLTPHLRSKMGNAAVKAAKSINYV-GVGTVEFLVDKHGNFYFM 288
Cdd:COG0439 151 VR-DGEVVV-----CSITRKHQKppyfveLGHEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDGEPYLI 223
|
250 260 270
....*....|....*....|....*....|....*
gi 488822547 289 EMNTRIQVEH--PVTEMITGIDLIREQILVAQGEK 321
Cdd:COG0439 224 EINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
337-442 |
4.80e-64 |
|
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: 201.49 E-value: 4.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 337 ECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETAIKRMKRALRECAITGV 416
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*.
gi 488822547 417 PTTIDFHRKILETPAFLAGDVYTNFI 442
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
337-444 |
2.48e-63 |
|
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: 199.64 E-value: 2.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 337 ECRINAEDPDHNFRPHPGKISGYLPPGGPGVRMDSHVYTDYEIPPYYDSLIGKLIVWGENRETAIKRMKRALRECAITGV 416
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*...
gi 488822547 417 PTTIDFHRKILETPAFLAGDVYTNFIQE 444
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
3-110 |
6.80e-62 |
|
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: 196.17 E-value: 6.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 3 FAKILIANRGEIALRILHSCEELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSKSYLNIPNIISAALTRNATAIHPG 82
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 488822547 83 YGFLAENARFAEICADHQLTFIGPSPSA 110
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
98-323 |
4.83e-20 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 93.11 E-value: 4.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 98 DHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGsgGLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADE 177
Cdd:PRK12815 652 EAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPA 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 178 LGNMLkaaqgeAEAAFGNSGVYLEKFIECprhIEFQILADSHGNVIHLG---ErdcsiqrrHqklLEEA----------- 243
Cdd:PRK12815 730 LEAYL------AENASQLYPILIDQFIDG---KEYEVDAISDGEDVTIPgiiE--------H---IEQAgvhsgdsiavl 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 244 PSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVdKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEKLQ 323
Cdd:PRK12815 790 PPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLA 868
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
104-293 |
4.24e-19 |
|
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: 89.55 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 104 IGPSPSAILAMGDKSTAKKTMQKAGVPTIPGsgGLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGNMLK 183
Cdd:COG0458 102 LGTSPDAIDLAEDRELFKELLDKLGIPQPKS--GTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 184 aaqgEAEAAFGNSGVYLEKFIECPRHIEFQILADSHGNV-------------IHLGERDCSiqrrhqklleeAPSPFLTP 250
Cdd:COG0458 180 ----RALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNViivgimehiepagVHSGDSICV-----------APPQTLSD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488822547 251 HLRSKMGNAAVKAAKSINYVGVGTVEFLVDKhGNFYFMEMNTR 293
Cdd:COG0458 245 KEYQRLRDATLKIARALGVVGLCNIQFAVDD-GRVYVIEVNPR 286
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
97-323 |
5.91e-19 |
|
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: 90.06 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 97 ADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGsgGLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSAD 176
Cdd:TIGR01369 650 EEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 177 ELGNMLKaaqgEAEAAFGNSGVYLEKFIECPRHIEFQILADsHGNV-------------IHLGERDCSIqrrhqklleea 243
Cdd:TIGR01369 728 ELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVlipgimehieeagVHSGDSTCVL----------- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 244 PSPFLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVdKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEKLQ 323
Cdd:TIGR01369 792 PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV-KDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLE 870
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
106-290 |
3.20e-17 |
|
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: 82.43 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 106 PSPSAILAMGDKSTAKKTMQKAGVPTIPGSggLITSEAEAKRIADDIGYPVLIKATAGG-GGRGMRLVKSADELGnmlka 184
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAPFA--AVDSLEDLEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADLE----- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 185 aqgEAEAAFGNSGVYLEKFIECPRhiEFQILA--DSHGNVIH--LGErdcSIQRRHQklLEE--APSPfLTPHLRSKMGN 258
Cdd:COG0026 152 ---AAWAALGGGPCILEEFVPFER--ELSVIVarSPDGEVATypVVE---NVHRNGI--LDEsiAPAR-ISEALAAEAEE 220
|
170 180 190
....*....|....*....|....*....|..
gi 488822547 259 AAVKAAKSINYVGVGTVEFLVDKHGNFYFMEM 290
Cdd:COG0026 221 IAKRIAEALDYVGVLAVEFFVTKDGELLVNEI 252
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
15-294 |
1.10e-16 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 81.51 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 15 ALRILHsceELGIRTVAVHSTIDRHALHVQLADESVCIGPPPSSksylniPNIISAALTRNATAIHPGY---------GF 85
Cdd:COG3919 20 VARSLG---EAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGDD------PEAFVDALLELAERHGPDVliptgdeyvEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 86 LAEN-ARFAEicadhQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPtIPGSGgLITSEAEAKRIADDIGYPVLIKATAG- 163
Cdd:COG3919 91 LSRHrDELEE-----HYRLPYPDADLLDRLLDKERFYELAEELGVP-VPKTV-VLDSADDLDALAEDLGFPVVVKPADSv 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 164 -------GGGRGMRLVKSADELGNMLKAAqgeAEAAFGnsgVYLEKFIECPRHIE--FQILADSHGNVIHLGErdcsiqr 234
Cdd:COG3919 164 gydelsfPGKKKVFYVDDREELLALLRRI---AAAGYE---LIVQEYIPGDDGEMrgLTAYVDRDGEVVATFT------- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488822547 235 rHQKLLEeAPSPFLTPHLRSKMGNAAVKAA-----KSINYVGVGTVEFLVD-KHGNFYFMEMNTRI 294
Cdd:COG3919 231 -GRKLRH-YPPAGGNSAARESVDDPELEEAarrllEALGYHGFANVEFKRDpRDGEYKLIEINPRF 294
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
109-292 |
1.65e-16 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 79.77 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 109 SAiLAMgDKSTAKKTMQKAGVPTIPGSggLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGNMLKAAqge 188
Cdd:PRK01372 93 SA-LAM-DKLRTKLVWQAAGLPTPPWI--VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELA--- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 189 aeAAFGNSgVYLEKFIECPrhiEFQiladshgnVIHLGERD---CSIQRRHQ------KLLEEA-----PSPfLTPHLRS 254
Cdd:PRK01372 166 --FKYDDE-VLVEKYIKGR---ELT--------VAVLGGKAlpvIEIVPAGEfydyeaKYLAGGtqyicPAG-LPAEIEA 230
|
170 180 190
....*....|....*....|....*....|....*...
gi 488822547 255 KMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNT 292
Cdd:PRK01372 231 ELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
105-292 |
1.87e-15 |
|
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: 76.68 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 105 GPSPSAiLAMgDKSTAKKTMQKAGVPTIPGSggLITSE--AEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGNML 182
Cdd:COG1181 86 GVLASA-LAM-DKALTKRVLAAAGLPTPPYV--VLRRGelADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAAL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 183 KAAqgeaeAAFGNSgVYLEKFIEcPRHIEFQILADSHGNVIHLGErdcsIQRRH------QKLLEEA-----PSPfLTPH 251
Cdd:COG1181 162 EEA-----FKYDDK-VLVEEFID-GREVTVGVLGNGGPRALPPIE----IVPENgfydyeAKYTDGGteyicPAR-LPEE 229
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488822547 252 LRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNT 292
Cdd:COG1181 230 LEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
106-290 |
4.77e-15 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 76.34 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 106 PSPSAILAMGDKSTAKKTMQKAGVPTIPGSggLITSEAEAKRIADDIGYPVLIKATAGG-GGRGMRLVKSADELGnmlka 184
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFA--VVDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLE----- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 185 aqgEAEAAFGNSGVYLEKFIECPRhiEFQILA--DSHGNVIH--LGErdcSIQRRHQKLLEEAPSPfLTPHLRSKMGNAA 260
Cdd:PRK06019 163 ---AAWALLGSVPCILEEFVPFER--EVSVIVarGRDGEVVFypLVE---NVHRNGILRTSIAPAR-ISAELQAQAEEIA 233
|
170 180 190
....*....|....*....|....*....|
gi 488822547 261 VKAAKSINYVGVGTVEFLVDKHGNFYFMEM 290
Cdd:PRK06019 234 SRIAEELDYVGVLAVEFFVTGDGELLVNEI 263
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
105-323 |
1.09e-13 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 73.66 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 105 GPSPSAILAMGDKSTAKKTMQKAGVPTIPGsgGLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGNMLK- 183
Cdd:PLN02735 691 GTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLEt 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 184 AAQGEAEAAfgnsgVYLEKFIECPRHIEFQILADSHGNV-------------IHLGERDCSIqrrhqklleeaPSPFLTP 250
Cdd:PLN02735 769 AVEVDPERP-----VLVDKYLSDATEIDVDALADSEGNVviggimehieqagVHSGDSACSL-----------PTQTIPS 832
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488822547 251 HLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNTRIQVEHPVTEMITGIDLIREQILVAQGEKLQ 323
Cdd:PLN02735 833 SCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSLK 905
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
91-291 |
4.02e-12 |
|
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: 66.50 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 91 RFAEICADHQLTFIgPSPSAILAMGDKSTAKKTMQKAGVPTIPGsgGLITSEAEAKRIADDIGYPVLIKATAGGGGRGMR 170
Cdd:COG0189 72 ALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPT--LVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 171 LVKSADELGNMLKAAQGEaeaafGNSGVYLEKFIECPRHIEFQILAdSHGNVIHlgerdcSIQR-------RHQKLLEEA 243
Cdd:COG0189 149 LVEDEDALESILEALTEL-----GSEPVLVQEFIPEEDGRDIRVLV-VGGEPVA------AIRRipaegefRTNLARGGR 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488822547 244 PSPF-LTPHLRskmgNAAVKAAKSINYvGVGTVEFLVDKHGnFYFMEMN 291
Cdd:COG0189 217 AEPVeLTDEER----ELALRAAPALGL-DFAGVDLIEDDDG-PLVLEVN 259
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
104-294 |
4.73e-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: 68.10 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 104 IGPSPSAILAMGDKSTAKKTMQKAGVPTIPGsgGLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGNMlk 183
Cdd:TIGR01369 115 LGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEI-- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 184 aaqgeAEAAFGNSG---VYLEKFIECPRHIEFQILADSHGNVI-------------HLGErdcSIQrrhqklleEAPSPF 247
Cdd:TIGR01369 191 -----AERALSASPinqVLVEKSLAGWKEIEYEVMRDSNDNCItvcnmenfdpmgvHTGD---SIV--------VAPSQT 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488822547 248 LTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVD-KHGNFYFMEMNTRI 294
Cdd:TIGR01369 255 LTDKEYQMLRDASIKIIRELGIEGGCNVQFALNpDSGRYYVIEVNPRV 302
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
107-312 |
3.26e-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: 63.52 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 107 SPSAILAMGDKSTAKKTMQKAGVPTiPGSGgLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGNMLKAAQ 186
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPL-PRTG-LAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 187 GEAEAAfgnSGVYLEKFIECPRHIEFQILADShGNVIHLGERDCSIQRRHQKLLEEAPSPF-LTPHLRskmgNAAVKAAK 265
Cdd:TIGR00768 157 QLNGPQ---NLFLVQEYIKKPGGRDIRVFVVG-DEVVAAIYRITSGHWRSNLARGGKAEPCsLTEEIE----ELAIKAAK 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488822547 266 SINyVGVGTVEFLVDKHGnFYFMEMNTRIQVEHpvTEMITGIDLIRE 312
Cdd:TIGR00768 229 ALG-LDVAGVDLLESEDG-LLVNEVNANPEFKN--SVKTTGVNIAGK 271
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
124-292 |
4.25e-10 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 59.25 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 124 MQKAGVPTIP------GSGGLITSEAEAKrIADDIGYPVLIKATAGGGGRGMRLVKSADELgnmlKAAqgeAEAAFGNSG 197
Cdd:pfam07478 2 LKAAGLPVVPfvtftrADWKLNPKEWCAQ-VEEALGYPVFVKPARLGSSVGVSKVESREEL----QAA---IEEAFQYDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 198 -VYLEKFIECpRHIEFQILADSHGNVIHLGER--DCSIQRRHQKLLEEA-----PSPfLTPHLRSKMGNAAVKAAKSINY 269
Cdd:pfam07478 74 kVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPAD-LEEEQEEQIQELALKAYKALGC 151
|
170 180
....*....|....*....|...
gi 488822547 270 VGVGTVEFLVDKHGNFYFMEMNT 292
Cdd:pfam07478 152 RGLARVDFFLTEDGEIVLNEVNT 174
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
104-293 |
7.51e-10 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 61.27 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 104 IGPSPSAILAMGDKSTAKKTMQKAGVPTIPGsgGLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGNMLK 183
Cdd:PRK05294 657 LGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMR 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 184 aaqgEAEAAFGNSGVYLEKFIECPRHIEFQILADsHGNV-------------IHLGERDCSIqrrhqklleeaPSPFLTP 250
Cdd:PRK05294 735 ----EAVKVSPDHPVLIDKFLEGAIEVDVDAICD-GEDVliggimehieeagVHSGDSACSL-----------PPQTLSE 798
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488822547 251 HLRSKMGNAAVKAAKSINYVGVGTVEFLVdKHGNFYFMEMNTR 293
Cdd:PRK05294 799 EIIEEIREYTKKLALELNVVGLMNVQFAV-KDDEVYVIEVNPR 840
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
108-294 |
1.45e-09 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 60.37 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 108 PSAILAMG-DKSTAKKTMQKAGVPTipGSGGLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGNMLKaaQ 186
Cdd:PRK12815 119 NIEAIQKGeDRERFRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFK--Q 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 187 GEAEAAFGNsgVYLEKFIECPRHIEFQILADSHGNV-------------IHLGErdcSIQrrhqklleEAPSPFLT---- 249
Cdd:PRK12815 195 GLQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCitvcnmenidpvgIHTGD---SIV--------VAPSQTLTddey 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488822547 250 PHLRSkmgnAAVKAAKSINYVGVGTVEFLVDKHG-NFYFMEMNTRI 294
Cdd:PRK12815 262 QMLRS----ASLKIISALGVVGGCNIQFALDPKSkQYYLIEVNPRV 303
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
103-293 |
3.56e-09 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 58.96 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 103 FIGPSPSAILAMGDKSTAKKTMQKAGVPTIPGsgGLITSEAEAKRIADDIGYPVLIKA--TAGGGGRGMrlVKSADELGN 180
Cdd:PRK05294 115 LIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVIIRPsfTLGGTGGGI--AYNEEELEE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 181 MLKAAQgeaeAAFGNSGVYLEKFIECPRHIEFQILADSHGNVI-------------HLGErdcSIQrrhqklleEAPSPF 247
Cdd:PRK05294 191 IVERGL----DLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIivcsienidpmgvHTGD---SIT--------VAPAQT 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488822547 248 LTPHLRSKMGNAAVKAAKSInyvGVGT----VEFLVD-KHGNFYFMEMNTR 293
Cdd:PRK05294 256 LTDKEYQMLRDASIAIIREI---GVETggcnVQFALNpKDGRYIVIEMNPR 303
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
115-293 |
2.03e-08 |
|
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: 54.21 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 115 GDKSTAKKTMQKAGVPTipGSGGLITSEAEAKRIADDIGYPVL-IKATAGGGGRGMRLVKSADElgnMLKAAQGEAEA-A 192
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPT--AEYETFTDPEEAKSYIQEAGFPAIvVKADGLAAGKGVIVASSNEE---AIKAVDEILEQkK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 193 FGNSG--VYLEKFIECPrhiEFQILADSHG-NVIHLGerdcsIQRRHQKLLEE------------APSPFLTPHLRSKMG 257
Cdd:pfam01071 76 FGEAGetVVIEEFLEGE---EVSVLAFVDGkTVKPLP-----PAQDHKRAGEGdtgpntggmgaySPAPVITPELLERIK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488822547 258 NAAVK------AAKSINYVGVGTVEFLVDKHGNfYFMEMNTR 293
Cdd:pfam01071 148 ETIVEptvdglRKEGIPFKGVLYAGLMLTKDGP-KVLEFNCR 188
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
125-293 |
3.46e-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: 53.03 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 125 QKAGVPTIPGSggLITSEAEAKRIADDIGYPVLIKATAGG-GGRGMRLVKSADELgnmlkaaqGEAEAAFGNSGVYLEKF 203
Cdd:pfam02222 1 QKLGLPTPRFM--AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADL--------PQAWEELGDGPVIVEEF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 204 IECPRHIEFQILADSHGN-----VIHlgerdcSIQRRHQKLLEEAPSPFlTPHLRSKMGNAAVKAAKSINYVGVGTVEFL 278
Cdd:pfam02222 71 VPFDRELSVLVVRSVDGEtafypVVE------TIQEDGICRLSVAPARV-PQAIQAEAQDIAKRLVDELGGVGVFGVELF 143
|
170
....*....|....*
gi 488822547 279 VDKHGNFYFMEMNTR 293
Cdd:pfam02222 144 VTEDGDLLINELAPR 158
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
116-205 |
5.47e-08 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 55.16 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 116 DKSTAKKTMQKAGVPtIPgSGGLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLvksadELGNmlkaaQGEAEAAFGN 195
Cdd:PRK14016 214 DKELTKRLLAAAGVP-VP-EGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTV-----NITT-----REEIEAAYAV 281
|
90
....*....|....*
gi 488822547 196 -----SGVYLEKFIE 205
Cdd:PRK14016 282 askesSDVIVERYIP 296
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
105-294 |
1.27e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 54.08 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 105 GPSPSAILAMGDKSTAKKTMQKAGVPtIPGSGgLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGnmlka 184
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGID-VPRTH-ALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAA----- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 185 AQGEAEAAFGNSGVYLEKFIECPrhiEF--QILADSHGNVI------HLGERDCSIQRRHqklleEAPSPFLTPHlRSKM 256
Cdd:PRK02186 169 AHCAALRRAGTRAALVQAYVEGD---EYsvETLTVARGHQVlgitrkHLGPPPHFVEIGH-----DFPAPLSAPQ-RERI 239
|
170 180 190
....*....|....*....|....*....|....*....
gi 488822547 257 GNAAVKAAKSINY-VGVGTVEFLVdKHGNFYFMEMNTRI 294
Cdd:PRK02186 240 VRTVLRALDAVGYaFGPAHTELRV-RGDTVVIIEINPRL 277
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
86-294 |
2.23e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 53.24 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 86 LAENArfaeICADHQLTFIGPSPSAILAMGDKSTAKKTMQKAGVPTIPgsGGLITSEAEAKRIADDIG-YPVLIKATAGG 164
Cdd:PLN02735 118 LAESG----ILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP--SGIATTLDECFEIAEDIGeFPLIIRPAFTL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 165 GGRGMRLVKSADELGNMLKAAQgeaeAAFGNSGVYLEKFIECPRHIEFQILADSHGNVIHLgerdCSIQR------RHQK 238
Cdd:PLN02735 192 GGTGGGIAYNKEEFETICKAGL----AASITSQVLVEKSLLGWKEYELEVMRDLADNVVII----CSIENidpmgvHTGD 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488822547 239 LLEEAPSPFLTPHLRSKMGNAAVKAAKSINY-VGVGTVEFLVD-KHGNFYFMEMNTRI 294
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGVeCGGSNVQFAVNpVDGEVMIIEMNPRV 321
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
106-279 |
5.51e-07 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 51.98 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 106 PSPSAILAMGDKSTAKKTMQKAGVPTIPGSGglITSEAEAKRIADDIGYPVLIKATAGG-GGRGMRLVKSADELGNMLKA 184
Cdd:PLN02948 111 PKSSTIRIIQDKYAQKVHFSKHGIPLPEFME--IDDLESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTEEDLSSAVAA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 185 AQGEAEaafgnsGVYLEKFIecPRHIEfqiLAdshgnVIHLGERDCS---------IQRRHQKLLEEAPSPfLTPHLRSK 255
Cdd:PLN02948 189 LGGFER------GLYAEKWA--PFVKE---LA-----VMVARSRDGStrcypvvetIHKDNICHVVEAPAN-VPWKVAKL 251
|
170 180
....*....|....*....|....*
gi 488822547 256 MGNAAVKAAKSINYVGVGTVE-FLV 279
Cdd:PLN02948 252 ATDVAEKAVGSLEGAGVFGVElFLL 276
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
90-272 |
9.92e-05 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 44.62 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 90 ARFAEicaDHQ--LTFIGPS--------------------PSAILAM--GDKSTAKKTMQKAGVPTipGSGGLITSEAEA 145
Cdd:COG0151 55 VAFAK---EENidLVVVGPEaplvagivdafraagipvfgPSKAAAQleGSKAFAKEFMARYGIPT--AAYRVFTDLEEA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 146 KRIADDIGYPVLIKA---TAGGGgrgmrlVKSADELgnmlkaaqGEAEAA---------FGNSG--VYLEKFIECPrhiE 211
Cdd:COG0151 130 LAYLEEQGAPIVVKAdglAAGKG------VVVAETL--------EEALAAvddmladgkFGDAGarVVIEEFLEGE---E 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 212 FQILADSHG-NVIHLGE-RDcsiqrrHQKLLEE------------APSPFLTPHLRSKMGNAAVK------AAKSINYVG 271
Cdd:COG0151 193 ASLFALTDGkTVLPLPTaQD------HKRAGDGdtgpntggmgaySPAPVVTEELLEKIMEEIIEptvagmAAEGIPYRG 266
|
.
gi 488822547 272 V 272
Cdd:COG0151 267 V 267
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
120-205 |
1.12e-04 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 44.36 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 120 AKKTM----------QKAGVPTIPGsgGLITSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELGNMLKAAQGEA 189
Cdd:PRK09288 108 TRLTMnregirrlaaEELGLPTSPY--RFADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPEDIEKAWEYAQEGG 185
|
90
....*....|....*.
gi 488822547 190 EAafGNSGVYLEKFIE 205
Cdd:PRK09288 186 RG--GAGRVIVEEFID 199
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
103-292 |
1.16e-04 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 43.96 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 103 FIGPSP--SAiLAMgDKSTAKKTMQKAGVPTIPGSggLITSEAEAKRIADDI----GYPVLIKATAGGGGRGMRLVKSAD 176
Cdd:PRK01966 110 YVGCGVlaSA-LSM-DKILTKRLLAAAGIPVAPYV--VLTRGDWEEASLAEIeaklGLPVFVKPANLGSSVGISKVKNEE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 177 ELGNMLKAAQGEAEAafgnsgVYLEKFIEcPRHIEFQILadshGN-----VIhlGErdcsIQRRHQ-------------K 238
Cdd:PRK01966 186 ELAAALDLAFEYDRK------VLVEQGIK-GREIECAVL----GNdpkasVP--GE----IVKPDDfydyeakyldgsaE 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488822547 239 LLEEAPspfLTPHLRSKMGNAAVKAAKSINYVGVGTVEFLVDKHGNFYFMEMNT 292
Cdd:PRK01966 249 LIIPAD---LSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINT 299
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
44-293 |
1.56e-04 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 43.72 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 44 QLADESVcIGPPPSSKSYlnIPNIISAALTRNATAIHPGY----GFLAENA-RFAEicadHQLTFIGPSPSAILAMGDKS 118
Cdd:PRK12767 41 YFADKFY-VVPKVTDPNY--IDRLLDICKKEKIDLLIPLIdpelPLLAQNRdRFEE----IGVKVLVSSKEVIEICNDKW 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 119 TAKKTMQKAGVPT----IPGSggliTSEAEAKRIADDIGYPVLIKATAGGGGRGMRLVKSADELgnmlkaaqgEAEAAFg 194
Cdd:PRK12767 114 LTYEFLKENGIPTpksyLPES----LEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEEL---------EFLLEY- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 195 NSGVYLEKFIECPrhiEFQI--LADSHGNVIHL----------GERDCSIQRRHQKLLEeapspfltphlrskmgnAAVK 262
Cdd:PRK12767 180 VPNLIIQEFIEGQ---EYTVdvLCDLNGEVISIvprkrievraGETSKGVTVKDPELFK-----------------LAER 239
|
250 260 270
....*....|....*....|....*....|.
gi 488822547 263 AAKSINYVGVGTVEFLVDKhGNFYFMEMNTR 293
Cdd:PRK12767 240 LAEALGARGPLNIQCFVTD-GEPYLFEINPR 269
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
102-293 |
3.87e-04 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 42.80 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 102 TFiGPSPSAILAMGDKSTAKKTMQKAGVPTipGSGGLITSEAEAKRIADDIGYPVLIKATAGGGGRG----MRLVKSADE 177
Cdd:PLN02257 89 TF-GPSAEAAALEGSKNFMKDLCDKYKIPT--AKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGvvvaMTLEEAYEA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488822547 178 LGNMLkaaqgeAEAAFGNSG--VYLEKFIEcPRHIEFQILADSHGNVIHLGERDcsiqrrHQKLLE------------EA 243
Cdd:PLN02257 166 VDSML------VKGAFGSAGseVVVEEFLD-GEEASFFALVDGENAIPLESAQD------HKRVGDgdtgpntggmgaYS 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488822547 244 PSPFLTPHLRSKMGNAAVK------AAKSINYVGVGTVEFLVD-KHGNFYFMEMNTR 293
Cdd:PLN02257 233 PAPVLTPELESKVMETIIYptvkgmAAEGCKFVGVLYAGLMIEkKSGLPKLLEYNVR 289
|
|
| |
