|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
5-445 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 677.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 5 LIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANALDSYLNIDRIISAAQITGANAIHPGYGFL 84
Cdd:COG4770 6 LIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGYGFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 85 SESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGGG 164
Cdd:COG4770 86 SENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASAGGGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 165 KGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPCA 244
Cdd:COG4770 166 KGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 245 ALTEERRQQICNDAVKVARAANYRSAGTIEFLV-TDNAHYFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPFSQ 323
Cdd:COG4770 246 ALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPFTQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 324 SDIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLKA 403
Cdd:COG4770 326 EDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRR 405
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 616690887 404 TLDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLEKH 445
Cdd:COG4770 406 ALAEFVIEGVKTNIPFLRALLAHPDFRAG---DVDTGFIERE 444
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
5-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 649.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 5 LIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANALDSYLNIDRIISAAQITGANAIHPGYGFL 84
Cdd:PRK08591 6 LIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPGYGFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 85 SESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGGG 164
Cdd:PRK08591 86 SENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATAGGGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 165 KGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPCA 244
Cdd:PRK08591 166 RGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 245 ALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDNAH-YFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPFSQ 323
Cdd:PRK08591 246 AITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEfYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSIKQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 324 SDIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLKA 403
Cdd:PRK08591 326 EDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIARMKR 405
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 616690887 404 TLDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLEKH 445
Cdd:PRK08591 406 ALSEFVIDGIKTTIPLHLRLLNDPNFQAG---DYNIHYLEKK 444
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
5-444 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 559.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 5 LIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANALDSYLNIDRIISAAQITGANAIHPGYGFL 84
Cdd:PRK05586 6 LIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPGFGFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 85 SESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGGG 164
Cdd:PRK05586 86 SENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASAGGGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 165 KGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPCA 244
Cdd:PRK05586 166 RGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 245 ALTEERRQQICNDAVKVARAANYRSAGTIEFLV-TDNAHYFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPFSQ 323
Cdd:PRK05586 246 VMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 324 SDIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLKA 403
Cdd:PRK05586 326 EDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKR 405
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 616690887 404 TLDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLEK 444
Cdd:PRK05586 406 ALGEFIIEGVNTNIDFQFIILEDEEFIKG---TYDTSFIEK 443
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
5-445 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 552.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 5 LIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANA-LDSYLNIDRIISAAQITGANAIHPGYGF 83
Cdd:PRK12999 9 LVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHpVRAYLDIDEIIRVAKQAGVDAIHPGYGF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 84 LSESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGG 163
Cdd:PRK12999 89 LSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKASAGGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 164 GKGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPC 243
Cdd:PRK12999 169 GRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 244 AALTEERRQQICNDAVKVARAANYRSAGTIEFLVT-DNAHYFIEMNARIQVEHTVTEMRAERDLVAAQ--------LYLL 314
Cdd:PRK12999 249 PGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDaDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQiliaegatLHDL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 315 EHNHLpfSQSDIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDS-LLYHGYQVSPYYDSLVAKVIVKSHD 393
Cdd:PRK12999 329 EIGIP--SQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVKLTAWGRT 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 616690887 394 RASAIDKLKATLDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLEKH 445
Cdd:PRK12999 407 FEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAG---DYTTSFIDET 455
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
5-445 |
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: 550.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 5 LIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEAN-ALDSYLNIDRIISAAQITGANAIHPGYGF 83
Cdd:COG1038 8 LVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKgPVDAYLDIEEIIRVAKEKGVDAIHPGYGF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 84 LSESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGG 163
Cdd:COG1038 88 LSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAAAGGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 164 GKGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPC 243
Cdd:COG1038 168 GRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 244 AALTEERRQQICNDAVKVARAANYRSAGTIEFLVT-DNAHYFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHL--- 319
Cdd:COG1038 248 PNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDdDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLddp 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 320 ----PfSQSDIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDS-LLYHGYQVSPYYDSLVAKVIVKSHDR 394
Cdd:COG1038 328 eigiP-SQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGgNAYTGAVITPYYDSLLVKVTAWGRTF 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 616690887 395 ASAIDKLKATLDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLEKH 445
Cdd:COG1038 407 EEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAG---ECTTSFIDET 454
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
5-445 |
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: 542.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 5 LIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANALDSYLNIDRIISAAQITGANAIHPGYGFL 84
Cdd:TIGR00514 6 LIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPGYGFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 85 SESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGGG 164
Cdd:TIGR00514 86 SENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATAGGGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 165 KGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPCA 244
Cdd:TIGR00514 166 RGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 245 ALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDNAH-YFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPFSQ 323
Cdd:TIGR00514 246 ALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEfYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPLSLKQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 324 SDIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLKA 403
Cdd:TIGR00514 326 EDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIARMKR 405
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 616690887 404 TLDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLEKH 445
Cdd:TIGR00514 406 ALSEFIIDGIKTTIPFHQRILEDENFQHG---GTNIHYLEKK 444
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
5-450 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 536.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 5 LIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANALDSYLNIDRIISAAQITGANAIHPGYGFL 84
Cdd:PRK06111 6 LIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPGYGLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 85 SESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGGG 164
Cdd:PRK06111 86 SENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASAGGGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 165 KGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPCA 244
Cdd:PRK06111 166 IGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 245 ALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDNAH-YFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPFSQ 323
Cdd:PRK06111 246 FLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNfYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 324 SDIQFNGHVIEARINAENPeKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLKA 403
Cdd:PRK06111 326 DDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHD 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 616690887 404 TLDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLEKHQIVKG 450
Cdd:PRK06111 405 ALEELKVEGIKTNIPLLLQVLEDPVFKAG---GYTTGFLTKQLVKKS 448
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
5-446 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 533.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 5 LIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANALDSYLNIDRIISAAQITGANAIHPGYGFL 84
Cdd:PRK08654 6 LIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYGFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 85 SESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGGG 164
Cdd:PRK08654 86 AENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 165 KGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPCA 244
Cdd:PRK08654 166 IGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 245 ALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDNAHYFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPFSQS 324
Cdd:PRK08654 246 IMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSFKQE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 325 DIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLKAT 404
Cdd:PRK08654 326 DITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIARMRRA 405
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 616690887 405 LDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLEKHQ 446
Cdd:PRK08654 406 LYEYVIVGVKTNIPFHKAVMENENFVRG---NLHTHFIEEET 444
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
5-443 |
1.26e-176 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 502.75 E-value: 1.26e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 5 LIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANALDSYLNIDRIISAAQITGANAIHPGYGFL 84
Cdd:PRK12833 9 LVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGYGFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 85 SESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGGG 164
Cdd:PRK12833 89 SENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAGGGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 165 KGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQdNYVHLGERDCSVQRKNQKLIEESPCA 244
Cdd:PRK12833 169 RGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 245 ALTEERRQQICNDAVKVARAANYRSAGTIEFLVTD--NAHYFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPFS 322
Cdd:PRK12833 248 SLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRFA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 323 QSDIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLK 402
Cdd:PRK12833 328 QGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALARAA 407
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 616690887 403 ATLDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLE 443
Cdd:PRK12833 408 RALRELRIDGMKTTAPLHRALLADADVRAG---RFHTNFLE 445
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-445 |
1.22e-168 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 481.55 E-value: 1.22e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 3 RCLIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANALDSYLNIDRIISAAQITGANAIHPGYG 82
Cdd:PRK08462 6 RILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGYG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 83 FLSESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGG 162
Cdd:PRK08462 86 FLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 163 GGKGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESP 242
Cdd:PRK08462 166 GGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 243 CAALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDNAH-YFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPf 321
Cdd:PRK08462 246 AVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDfYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELP- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 322 SQSDIQFNGHVIEARINAENPeKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKL 401
Cdd:PRK08462 325 SQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAKM 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 616690887 402 KATLDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLEKH 445
Cdd:PRK08462 404 KRALKEFKVEGIKTTIPFHLEMMENADFINN---KYDTKYLEEH 444
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
5-445 |
4.47e-161 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 463.42 E-value: 4.47e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 5 LIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGeANALDSYLNIDRIISAAQITGANAIHPGYGFL 84
Cdd:PRK07178 6 LIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIG-ADPLAGYLNPRRLVNLAVETGCDALHPGYGFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 85 SESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGGG 164
Cdd:PRK07178 85 SENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATSGGGG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 165 KGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPCA 244
Cdd:PRK07178 165 RGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 245 ALTEERRQQICNDAVKVARAANYRSAGTIEFLV-TDNAHYFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPFSQ 323
Cdd:PRK07178 245 QLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSYKQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 324 SDIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLKA 403
Cdd:PRK07178 325 EDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALDRGRR 404
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 616690887 404 TLDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLEKH 445
Cdd:PRK07178 405 ALDDMRVQGVKTTIPYYQEILRNPEFRSG---QFNTSFVESH 443
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
5-445 |
1.37e-148 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 431.54 E-value: 1.37e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 5 LIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEaNALDSYLNIDRIISAAQITGANAIHPGYGFL 84
Cdd:PRK08463 6 LIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGT-DPIKGYLDVKRIVEIAKACGADAIHPGYGFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 85 SESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNH-VSEIEKLAKDIGYPVVIKAASGGG 163
Cdd:PRK08463 85 SENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSEsMEEIKIFARKIGYPVILKASGGGG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 164 GKGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPC 243
Cdd:PRK08463 165 GRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 244 AALTEERRQQICNDAVKVARAANYRSAGTIEFLVTD-NAHYFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPFS 322
Cdd:PRK08463 245 PSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDyNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 323 QSDIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLK 402
Cdd:PRK08463 325 QSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLAVNKLE 404
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 616690887 403 ATLDEMVIDGFSTTADFLYAVLNYPLYRDGdakDVDIKFLEKH 445
Cdd:PRK08463 405 RALKEFVIDGIRTTIPFLIAITKTREFRRG---YFDTSYIETH 444
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
114-311 |
1.05e-64 |
|
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: 207.16 E-value: 1.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 114 DKITARQTVHHAGVPVIPGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGGGKGIRIVKKAEDLEKAFKEAKSEGKKYFDD 193
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 194 DRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPCAALTEERRQQICNDAVKVARAANYRSAGTI 273
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616690887 274 EFLV--TDNAHYFIEMNARIQVEHTVTEMRAERDLVAAQL 311
Cdd:pfam02786 161 EFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAA 200
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
3-108 |
3.15e-58 |
|
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: 186.92 E-value: 3.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 3 RCLIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANALDSYLNIDRIISAAQITGANAIHPGYG 82
Cdd:pfam00289 3 KVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPGYG 82
|
90 100
....*....|....*....|....*.
gi 616690887 83 FLSESTKFAQTVEEQGIAFIGPTKKT 108
Cdd:pfam00289 83 FLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
61-311 |
9.43e-52 |
|
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: 175.45 E-value: 9.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 61 NIDRIISAAQitganAIHPGYGF---LSES----TKFAQTVEEQGIAfiGPTKKTMEMMGDKITARQTVHHAGVPViPGS 133
Cdd:COG0439 1 DIDAIIAAAA-----ELARETGIdavLSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 134 nGAVNHVSEIEKLAKDIGYPVVIKAASGGGGKGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPvAKHVEVQVM 213
Cdd:COG0439 73 -ALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLE-GREYSVEGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 214 GDgQDNYVHlgerdCSVQRKNQK------LIEESPcAALTEERRQQICNDAVKVARAANY-RSAGTIEFLVT-DNAHYFI 285
Cdd:COG0439 151 VR-DGEVVV-----CSITRKHQKppyfveLGHEAP-SPLPEELRAEIGELVARALRALGYrRGAFHTEFLLTpDGEPYLI 223
|
250 260
....*....|....*....|....*...
gi 616690887 286 EMNARIQVEH--TVTEMRAERDLVAAQL 311
Cdd:COG0439 224 EINARLGGEHipPLTELATGVDLVREQI 251
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
334-444 |
3.69e-50 |
|
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: 165.74 E-value: 3.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 334 EARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLKATLDEMVIDGF 413
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100 110
....*....|....*....|....*....|.
gi 616690887 414 STTADFLYAVLNYPLYRDGdakDVDIKFLEK 444
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAG---EVDTGFLEE 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
334-443 |
2.28e-46 |
|
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: 155.65 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 334 EARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLKATLDEMVIDGF 413
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100 110
....*....|....*....|....*....|
gi 616690887 414 STTADFLYAVLNYPLYRDGdakDVDIKFLE 443
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAG---DVDTGFLE 107
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
89-297 |
1.80e-13 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 72.69 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 89 KFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGsnGAVNHVSEIEKLAKDIGYPVVIKAASGGGGKGIR 168
Cdd:PRK12815 645 NLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMA 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 169 IVKKAEDLEKAFKEAKSEgkkyfdDDRVYVEAFIPvAKHVEVQVMGDGQDNY------------VHLGERDCSVQRKNqk 236
Cdd:PRK12815 723 VVYDEPALEAYLAENASQ------LYPILIDQFID-GKEYEVDAISDGEDVTipgiiehieqagVHSGDSIAVLPPQS-- 793
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690887 237 lieespcaaLTEERRQQICNDAVKVARAANYRSAGTIEFLVTDNAHYFIEMNARiqVEHTV 297
Cdd:PRK12815 794 ---------LSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPR--ASRTV 843
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
97-290 |
7.91e-13 |
|
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: 70.29 E-value: 7.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 97 QGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPgsNGAVNHVSEIEKLAKDIGYPVVIK-------AASggggkgiRI 169
Cdd:COG0458 97 EGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPK--SGTATSVEEALAIAEEIGYPVIVRpsyvlggRGM-------GI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 170 VKKAEDLEKAFKEAksegKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNY-------------VHLGERDCSvqrknqk 236
Cdd:COG0458 168 VYNEEELEEYLERA----LKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNViivgimehiepagVHSGDSICV------- 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 616690887 237 lieeSPCAALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDNAHYFIEMNAR 290
Cdd:COG0458 237 ----APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPR 286
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
89-290 |
3.95e-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: 68.49 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 89 KFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGsnGAVNHVSEIEKLAKDIGYPVVIKAASGGGGKGIR 168
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAME 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 169 IVKKAEDLEKAFKEAKSEGKKYfdddRVYVEAFIPVAKHVEVQVMGDGQDNY------------VHLGERDCSVqrknqk 236
Cdd:TIGR01369 722 IVYNEEELRRYLEEAVAVSPEH----PVLIDKYLEDAVEVDVDAVSDGEEVLipgimehieeagVHSGDSTCVL------ 791
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 616690887 237 lieesPCAALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDNAHYFIEMNAR 290
Cdd:TIGR01369 792 -----PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPR 840
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
114-288 |
1.35e-11 |
|
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: 65.13 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 114 DKITARQTVHHAGVPVIPGSngAVNH--VSEIEKLAKDIGYPVVIKAASGGGGKGIRIVKKAEDLEKAFKEAKSEgkkyf 191
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYV--VLRRgeLADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY----- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 192 dDDRVYVEAFIPvAKHVEVQVMGDGQDNYVHLGERDcsVQRK----NQKLIEES-----PcAALTEERRQQICNDAVKVA 262
Cdd:COG1181 168 -DDKVLVEEFID-GREVTVGVLGNGGPRALPPIEIV--PENGfydyEAKYTDGGteyicP-ARLPEELEERIQELALKAF 242
|
170 180
....*....|....*....|....*..
gi 616690887 263 RAANYRSAGTIEFLVT-DNAHYFIEMN 288
Cdd:COG1181 243 RALGCRGYARVDFRLDeDGEPYLLEVN 269
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
95-291 |
6.56e-09 |
|
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: 58.47 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 95 EEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGsnGAVNHVSEIEKLAKDIGYPVVIKAASGGGGKGIRIVKKAE 174
Cdd:TIGR01369 108 EKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNRE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 175 DL----EKAFKEAksegkkyfDDDRVYVEAFIPVAKHVEVQVMGDGQDNY-------------VHLGERdcsvqrknqkl 237
Cdd:TIGR01369 186 ELkeiaERALSAS--------PINQVLVEKSLAGWKEIEYEVMRDSNDNCitvcnmenfdpmgVHTGDS----------- 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616690887 238 IEESPCAALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDNAH--YFIEMNARI 291
Cdd:TIGR01369 247 IVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGryYVIEVNPRV 302
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
125-288 |
1.91e-08 |
|
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: 54.24 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 125 AGVPVIP----GSNGAVNHVSEI-EKLAKDIGYPVVIKAASGGGGKGIRIVKKAEDLEKAFKEAksegKKYfdDDRVYVE 199
Cdd:pfam07478 5 AGLPVVPfvtfTRADWKLNPKEWcAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEA----FQY--DEKVLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 200 AFIPvAKHVEVQVMGDGqDNYVH-LGER--DCSVQRKNQKLIEES-----PcAALTEERRQQICNDAVKVARAANYRSAG 271
Cdd:pfam07478 79 EGIE-GREIECAVLGNE-DPEVSpVGEIvpSGGFYDYEAKYIDDSaqivvP-ADLEEEQEEQIQELALKAYKALGCRGLA 155
|
170
....*....|....*...
gi 616690887 272 TIEFLVT-DNAHYFIEMN 288
Cdd:pfam07478 156 RVDFFLTeDGEIVLNEVN 173
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
114-286 |
6.31e-08 |
|
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: 54.31 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 114 DKITARQTVHHAGVPVIPGSngAVNHVSEIEKLAKDIGYPVVIKAAsggggkgiR---------IVKKAEDLEKAFKEak 184
Cdd:COG0026 89 DRLLEKAFLAELGIPVAPFA--AVDSLEDLEAAIAELGLPAVLKTR--------RggydgkgqvVIKSAADLEAAWAA-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 185 segkkyFDDDRVYVEAFIPVAKhvEVQVMG----DGQDNYVHLGErdcSVQRKNQkLIE-ESPcAALTEERRQQICNDAV 259
Cdd:COG0026 157 ------LGGGPCILEEFVPFER--ELSVIVarspDGEVATYPVVE---NVHRNGI-LDEsIAP-ARISEALAAEAEEIAK 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 616690887 260 KVARAANYRsaGT--IEFLVTDNA---------------HYFIE 286
Cdd:COG0026 224 RIAEALDYV--GVlaVEFFVTKDGellvneiaprphnsgHWTIE 265
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
96-291 |
1.24e-07 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 53.39 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 96 EQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPViPGSNgAVNHVSEIEKLAKDIGYPVVIKAASGGGGKG--------I 167
Cdd:COG3919 99 EEHYRLPYPDADLLDRLLDKERFYELAEELGVPV-PKTV-VLDSADDLDALAEDLGFPVVVKPADSVGYDElsfpgkkkV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 168 RIVKKAEDLEKAFKEAKSEGkkyfddDRVYVEAFIPVAKHVEVQVMG----DGQDNYVHLGerdcsvqrknQKLIEESPC 243
Cdd:COG3919 177 FYVDDREELLALLRRIAAAG------YELIVQEYIPGDDGEMRGLTAyvdrDGEVVATFTG----------RKLRHYPPA 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 616690887 244 ----AALTEERRQQICNDAVKVARAANYRSAGTIEFLV--TDNAHYFIEMNARI 291
Cdd:COG3919 241 ggnsAARESVDDPELEEAARRLLEALGYHGFANVEFKRdpRDGEYKLIEINPRF 294
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
114-219 |
1.42e-07 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 54.01 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 114 DKITARQTVHHAGVPVIPGsnGAVNHVSEIEKLAKDIGYPVVIKAASGGGGKGIRI-VKKAEDLEKAFKEAKSEGKKyfd 192
Cdd:PRK14016 214 DKELTKRLLAAAGVPVPEG--RVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESSD--- 288
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 616690887 193 ddrVYVEAFIP---------------VAKHVEVQVMGDGQDN 219
Cdd:PRK14016 289 ---VIVERYIPgkdhrllvvggklvaAARREPPHVIGDGKHT 327
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
114-203 |
3.10e-07 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 52.04 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 114 DKITARQTVHHAGVPVIPGSngAVNHVSEIEKLAKDIGYPVVIKAASGGGGKGIRIVKKAEDLEKAFKEAksegKKYfdD 193
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWI--VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELA----FKY--D 169
|
90
....*....|
gi 616690887 194 DRVYVEAFIP 203
Cdd:PRK01372 170 DEVLVEKYIK 179
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
114-288 |
5.36e-07 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 51.27 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 114 DKITARQTVHHAGVPVIPG-----SNGAVNHVSEIEKlakDIGYPVVIKAASGGGGKGIRIVKKAEDLEKAFKEAKSEgk 188
Cdd:PRK01966 123 DKILTKRLLAAAGIPVAPYvvltrGDWEEASLAEIEA---KLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEY-- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 189 kyfdDDRVYVEAFIpVAKHVEVQVMGDGQDNYVhLGErdcsVQRKN------QKLIEES-----PcAALTEERRQQICND 257
Cdd:PRK01966 198 ----DRKVLVEQGI-KGREIECAVLGNDPKASV-PGE----IVKPDdfydyeAKYLDGSaeliiP-ADLSEELTEKIREL 266
|
170 180 190
....*....|....*....|....*....|..
gi 616690887 258 AVKVARAANYRSAGTIEFLVTDNAH-YFIEMN 288
Cdd:PRK01966 267 AIKAFKALGCSGLARVDFFLTEDGEiYLNEIN 298
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
91-280 |
2.91e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 49.00 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 91 AQTVEEQGIAFIGPtkKTMEMMGDKITARQTVHHAGVPVIPGSngAVNHVSEIEKLAKDIGYPVVIKAAsggggkgiR-- 168
Cdd:PRK06019 79 LDALAARVPVPPGP--DALAIAQDRLTEKQFLDKLGIPVAPFA--VVDSAEDLEAALADLGLPAVLKTR--------Rgg 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 169 -------IVKKAEDLEKAFKEaksegkkyFDDDRVYVEAFIPVAKhvEVQVMG--DGQDNYVH--LGErdcSVQRKNQKL 237
Cdd:PRK06019 147 ydgkgqwVIRSAEDLEAAWAL--------LGSVPCILEEFVPFER--EVSVIVarGRDGEVVFypLVE---NVHRNGILR 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 616690887 238 IEESPcAALTEERRQQICNDAVKVARAANYRsaGT--IEFLVTDN 280
Cdd:PRK06019 214 TSIAP-ARISAELQAQAEEIASRIAEELDYV--GVlaVEFFVTGD 255
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
15-289 |
7.91e-06 |
|
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: 47.24 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 15 RIIRACREYGIETVavyakgdeqslHVHLADQAICIGEANALDSYLNIDriisaaqitGANAIHPGYGFLSESTKFAQTV 94
Cdd:COG0189 18 ALIEAAQRRGHEVE-----------VIDPDDLTLDLGRAPELYRGEDLS---------EFDAVLPRIDPPFYGLALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 95 EEQGIAFIGPTKkTMEMMGDKITARQTVHHAGVPVIPgsNGAVNHVSEIEKLAKDIGYPVVIKAASGGGGKGIRIVKKAE 174
Cdd:COG0189 78 EAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPP--TLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 175 DLEKAFKEAKSEGKKYFdddrvYVEAFIPVAKHVEVQVM----------------GDGQDNyVHLGERDCSVQrknqkli 238
Cdd:COG0189 155 ALESILEALTELGSEPV-----LVQEFIPEEDGRDIRVLvvggepvaairripaeGEFRTN-LARGGRAEPVE------- 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 616690887 239 eespcaaLTEErrqqICNDAVKVARAANYRSAGtIEFLVTDNAHYFIEMNA 289
Cdd:COG0189 222 -------LTDE----ERELALRAAPALGLDFAG-VDLIEDDDGPLVLEVNV 260
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
125-214 |
1.75e-05 |
|
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: 44.94 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 125 AGVPVIPGSngAVNHVSEIEKLAKDIGYPVVIKAASGGGG-KGIRIVKKAEDLEKAFKEAKSEgkkyfdddRVYVEAFIP 203
Cdd:pfam02222 3 LGLPTPRFM--AAESLEELIEAGQELGYPCVVKARRGGYDgKGQYVVRSEADLPQAWEELGDG--------PVIVEEFVP 72
|
90
....*....|.
gi 616690887 204 VAKhvEVQVMG 214
Cdd:pfam02222 73 FDR--ELSVLV 81
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
95-291 |
2.96e-05 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 46.50 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 95 EEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVipGSNGAVNHVSEIEKLAKDIGYPVVIKAASGGGGKGIRIVKKAE 174
Cdd:PRK12815 109 EQYGVELLGTNIEAIQKGEDRERFRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 175 DLEKAFKEAKSEgkkyfDDDRVY-VEAFIPVAKHVEVQVMGDGQDNY-------------VHLGERdcsvqrknqklIEE 240
Cdd:PRK12815 187 ELEQLFKQGLQA-----SPIHQClLEESIAGWKEIEYEVMRDRNGNCitvcnmenidpvgIHTGDS-----------IVV 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616690887 241 SPCAALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDNA--HYFIEMNARI 291
Cdd:PRK12815 251 APSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSkqYYLIEVNPRV 303
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
142-204 |
5.42e-05 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 45.13 E-value: 5.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690887 142 EIEKLAKDIGYPVVIKAA--------SggggkgirIVKKAEDLEKAFKEAKSEGKKyfDDDRVYVEAFIPV 204
Cdd:PRK09288 140 ELRAAVEEIGYPCVVKPVmsssgkgqS--------VVRSPEDIEKAWEYAQEGGRG--GAGRVIVEEFIDF 200
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
67-291 |
2.61e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 43.68 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 67 SAAQITGANAIHPGY-GFLSESTKFAQTVEEQGIAFIGPTKKT--MEMMGDKITARQTVHHAGVPViPGSNgAVNHVSEI 143
Cdd:PRK02186 57 DPDRIHRFVSSLDGVaGIMSSSEYFIEVASEVARRLGLPAANTeaIRTCRDKKRLARTLRDHGIDV-PRTH-ALALRAVA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 144 EKLAKDIGYPVVIKAASGGGGKGIRIVKKAEDLEKAFKEAKSEGKKYFdddrvYVEAFIPvAKHVEVQVMGDGQDNYV-- 221
Cdd:PRK02186 135 LDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTRAA-----LVQAYVE-GDEYSVETLTVARGHQVlg 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690887 222 ----HLGERDCSVQrknqkLIEESPcAALTEERRQQICNDAVKVARAANYR-SAGTIEFLVTDNAHYFIEMNARI 291
Cdd:PRK02186 209 itrkHLGPPPHFVE-----IGHDFP-APLSAPQRERIVRTVLRALDAVGYAfGPAHTELRVRGDTVVIIEINPRL 277
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
50-290 |
6.09e-04 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 41.79 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 50 IGEANALDSYLNIdriISAAQItgaNAIHPGY----GFLSESTKfaqTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHA 125
Cdd:PRK12767 52 VTDPNYIDRLLDI---CKKEKI---DLLIPLIdpelPLLAQNRD---RFEEIGVKVLVSSKEVIEICNDKWLTYEFLKEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 126 GVPViPGS--NGAVNHVSEIEKLAKdIGYPVVIKAASGGGGKGIRIVKKAEDLEKAFKEAKSegkkyfdddrVYVEAFIp 203
Cdd:PRK12767 123 GIPT-PKSylPESLEDFKAALAKGE-LQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPN----------LIIQEFI- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 204 vakhvevqvmgDGQ----DNYVHL-GERDCSVQRKNQKLIEESPCAALTEErRQQICNDAVKVARAANYRSAGTIEFLVT 278
Cdd:PRK12767 190 -----------EGQeytvDVLCDLnGEVISIVPRKRIEVRAGETSKGVTVK-DPELFKLAERLAEALGARGPLNIQCFVT 257
|
250
....*....|..
gi 616690887 279 DNAHYFIEMNAR 290
Cdd:PRK12767 258 DGEPYLFEINPR 269
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
134-290 |
3.14e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 40.08 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 134 NGAVNHVSEIEKLAKDIGYPVVI--------KAasggggkgIRIVKKAEDLEKAFKEAksegKKYFDDDRVYVEAFIPVA 205
Cdd:PRK05294 687 NGTATSVEEALEVAEEIGYPVLVrpsyvlggRA--------MEIVYDEEELERYMREA----VKVSPDHPVLIDKFLEGA 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 206 KHVEVQVMGDGQDNYV-----HlgerdcsvqrknqklIEE-------SPCA----ALTEERRQQICNDAVKVARAANYRS 269
Cdd:PRK05294 755 IEVDVDAICDGEDVLIggimeH---------------IEEagvhsgdSACSlppqTLSEEIIEEIREYTKKLALELNVVG 819
|
170 180
....*....|....*....|.
gi 616690887 270 AGTIEFLVTDNAHYFIEMNAR 290
Cdd:PRK05294 820 LMNVQFAVKDDEVYVIEVNPR 840
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
86-289 |
3.70e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 39.27 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 86 ESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPViPGSNGAVNHVSEieklAKDIGYPVVIKAASGGGGK 165
Cdd:PRK14569 70 ENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPT-PMAKFLTDKLVA----EDEISFPVAVKPSSGGSSI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 166 GIRIVKKAEDLEKAFKEAKSEGKkyfdddrVYVEAFIpVAKHVEVQVMGDGQDNYV---HLGERDCSVQRKNQKLIEESP 242
Cdd:PRK14569 145 ATFKVKSIQELKHAYEEASKYGE-------VMIEQWV-TGKEITVAIVNDEVYSSVwiePQNEFYDYESKYSGKSIYHSP 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 616690887 243 cAALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDNAHYFI-EMNA 289
Cdd:PRK14569 217 -SGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYImEINS 263
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
111-235 |
5.45e-03 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 39.14 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690887 111 MMGDKITARQTVHHAGVPViPGS------NGAVNHVSEIEklakdiGYPVVIKAASGGGGKGIRIVKKA---EDLEKAFK 181
Cdd:PRK02471 485 IMENKVVTKKILAEAGFPV-PAGdeftslEEALADYSLFA------DKAIVVKPKSTNFGLGISIFKEPaslEDYEKALE 557
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690887 182 EAKSEgkkyfdDDRVYVEAFIP---------------VAKHVEVQVMGDGQDNYVHLgerdcsVQRKNQ 235
Cdd:PRK02471 558 IAFRE------DSSVLVEEFIVgteyrffvldgkveaVLLRVPANVVGDGIHTVREL------VAQKNQ 614
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
95-159 |
9.68e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 38.54 E-value: 9.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690887 95 EEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGsnGAVNHVSEIEKLAKDIGYPVVIKAA 159
Cdd:PRK05294 109 EKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVIIRPS 171
|
|
| |
