|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
18-483 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 794.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 18 PIQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPLAAESYLNMDKIINSALRSGAQAIHP 97
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 98 GYGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAV 177
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 178 YGGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKIIE 257
Cdd:COG4770 161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 258 EAPAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGEK 337
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 338 LPLKQSEIPLNGHAFECRVYAEDTRKGaFMPTAGRLNYVDFP--EDARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAVA 415
Cdd:COG4770 321 LPFTQEDIKLRGHAIECRINAEDPARG-FLPSPGTITRLRPPggPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259707361 416 AAKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPDHQKELFAESETPaeiyvESAVAHA 483
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE-----ELALAAA 462
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
19-457 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 610.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 19 IQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPLAAESYLNMDKIINSALRSGAQAIHPG 98
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 99 YGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAVY 178
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 179 GGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKIIEE 258
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 259 APAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGEKL 338
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 339 PLKQSEIPLNGHAFECRVYAEDTRKGaFMPTAGRLNYVDFPED--ARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAVAA 416
Cdd:PRK08591 322 SIKQEDIVFRGHAIECRINAEDPAKN-FMPSPGKITRYHPPGGpgVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 259707361 417 AKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFI 457
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
19-466 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 608.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 19 IQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPLAAESYLNMDKIINSALRSGAQAIHPG 98
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 99 YGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAVY 178
Cdd:PRK06111 82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 179 GGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKIIEE 258
Cdd:PRK06111 162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 259 APAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGEKL 338
Cdd:PRK06111 242 APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 339 PLKQSEIPLNGHAFECRVYAEDTRkgAFMPTAGRLNYVDFP--EDARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAVAA 416
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDPK--TFFPSPGKITDLTLPggEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 259707361 417 AKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPDHQKELFA 466
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQLVKKST 449
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
16-465 |
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: 581.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 16 IRPIQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGP---PLAAesYLNMDKIINSALRSGA 92
Cdd:COG1038 1 MKKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEgkgPVDA--YLDIEEIIRVAKEKGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 93 QAIHPGYGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPV 172
Cdd:COG1038 79 DAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 173 MLKAVYGGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRH 252
Cdd:COG1038 159 MLKAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 253 QKIIEEAPAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRV 332
Cdd:COG1038 239 QKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 333 AQGEKL-------PlKQSEIPLNGHAFECRVYAEDTRKGaFMPTAGRLnyvdfpeDA---------RIDTGVV-SGDEVS 395
Cdd:COG1038 319 AEGYSLddpeigiP-SQEDIRLNGYAIQCRITTEDPANN-FMPDTGRI-------TAyrsaggfgiRLDGGNAyTGAVIT 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 396 IHYDPMIAKVVVWGQDRAVAAAKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPDHqKELF 465
Cdd:COG1038 390 PYYDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDET-PELF 458
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
16-466 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 578.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 16 IRPIQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPLA-AESYLNMDKIINSALRSGAQA 94
Cdd:PRK12999 2 MKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHpVRAYLDIDEIIRVAKQAGVDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 95 IHPGYGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVML 174
Cdd:PRK12999 82 IHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 175 KAVYGGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQK 254
Cdd:PRK12999 162 KASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 255 IIEEAPAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQ 334
Cdd:PRK12999 242 VVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 335 GEKL------PLKQSEIPLNGHAFECRVYAEDTRKGaFMPTAGRLN-Y-------VdfpedaRIDTGVV-SGDEVSIHYD 399
Cdd:PRK12999 322 GATLhdleigIPSQEDIRLRGYAIQCRITTEDPANN-FMPDTGRITaYrspggfgV------RLDGGNAfAGAEITPYYD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259707361 400 PMIAKVVVWGQDRAVAAAKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPDHqKELFA 466
Cdd:PRK12999 395 SLLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDET-PELFD 460
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
21-462 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 559.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 21 RVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPLAAESYLNMDKIINSALRSGAQAIHPGYG 100
Cdd:PRK08654 4 KILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 101 FLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAVYGG 180
Cdd:PRK08654 84 FLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 181 GGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKIIEEAP 260
Cdd:PRK08654 164 GGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 261 APNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDpRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGEKLPL 340
Cdd:PRK08654 244 SPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 341 KQSEIPLNGHAFECRVYAEDTRKGaFMPTAGRLNYVDFP--EDARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAVAAAK 418
Cdd:PRK08654 323 KQEDITIRGHAIECRINAEDPLND-FAPSPGKIKRYRSPggPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIAR 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 259707361 419 LESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPDHQK 462
Cdd:PRK08654 402 MRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETT 445
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
20-457 |
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: 558.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 20 QRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPLAAESYLNMDKIINSALRSGAQAIHPGY 99
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 100 GFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGfHGEDQSDANLKKKSAEIGYPVMLKAVYG 179
Cdd:TIGR02712 82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPG-TGLLSSLDEALEAAKEIGYPVMLKSTAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 180 GGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKIIEEA 259
Cdd:TIGR02712 161 GGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 260 PAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDP-RGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGEKL 338
Cdd:TIGR02712 241 PAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEaRDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 339 PLKQS--EIPLNGHAFECRVYAEDTRKGaFMPTAGRLNYVDFPEDARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAVAA 416
Cdd:TIGR02712 321 DFASLniSLTPRGAAIEARVYAENPAKN-FQPSPGLLTDVQFPDDVRVDTWVETGTEVSPEYDPMLAKIIVHGSDREDAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 259707361 417 AKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFI 457
Cdd:TIGR02712 400 LKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTL 440
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
19-464 |
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: 529.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 19 IQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPLAAESYLNMDKIINSALRSGAQAIHPG 98
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 99 YGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAVY 178
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 179 GGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKIIEE 258
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 259 APAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGEKL 338
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 339 PLKQSEIPLNGHAFECRVYAEDTRKGaFMPTAGRLNYVDFPED--ARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAVAA 416
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKT-FLPSPGRITRYLPPGGpgVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 259707361 417 AKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPDHQKEL 464
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGMG 448
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
19-459 |
1.67e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 520.04 E-value: 1.67e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 19 IQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPLAAESYLNMDKIINSALRSGAQAIHPG 98
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 99 YGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAVY 178
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 179 GGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKIIEE 258
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 259 APAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGEKL 338
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 339 PLKQSEIPLNGHAFECRVYAEDTRKGaFMPTAGRLNYVDFPE--DARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAVAA 416
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNG-FMPCPGKIEELYIPGglGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 259707361 417 AKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPD 459
Cdd:PRK05586 401 QKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
18-476 |
7.17e-171 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 496.20 E-value: 7.17e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 18 PIQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPLAAESYLNMDKIINSALRSGAQAIHP 97
Cdd:PRK12833 4 RIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 98 GYGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAV 177
Cdd:PRK12833 84 GYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 178 YGGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHgNYVHLWERDCSVQRRHQKIIE 257
Cdd:PRK12833 164 AGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 258 EAPAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMD-PRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGE 336
Cdd:PRK12833 243 EAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 337 KLPLKQSEIPLNGHAFECRVYAEDTRKGaFMPTAGRLNYVDFP--EDARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAV 414
Cdd:PRK12833 323 PLRFAQGDIALRGAALECRINAEDPLRD-FFPNPGRIDALVWPqgPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAA 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259707361 415 AAAKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPDHQKELFAESETPAEIYV 476
Cdd:PRK12833 402 ALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAALDAAASAAV 463
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
19-486 |
2.53e-169 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 492.70 E-value: 2.53e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 19 IQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGP-PLAAesYLNMDKIINSALRSGAQAIHP 97
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAdPLAG--YLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 98 GYGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAV 177
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 178 YGGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKIIE 257
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 258 EAPAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGEK 337
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 338 LPLKQSEIPLNGHAFECRVYAEDTRKGaFMPTAGRLN--YVDFPEDARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAVA 415
Cdd:PRK07178 320 LSYKQEDIQHRGFALQFRINAEDPKND-FLPSFGKITryYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259707361 416 AAKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPDHQKELFAESETPAEiYVESAVAHALAA 486
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIKRKPE-ELAAAIAAAIAA 468
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
17-460 |
3.28e-160 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 468.46 E-value: 3.28e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 17 RPIQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPLAAESYLNMDKIINSALRSGAQAIH 96
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 97 PGYGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKA 176
Cdd:PRK08462 82 PGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 177 VYGGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKII 256
Cdd:PRK08462 162 AAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 257 EEAPAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGE 336
Cdd:PRK08462 242 EESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 337 KLPlKQSEIPLNGHAFECRVYAEDTRKgaFMPTAGRLNYVDFP--EDARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAV 414
Cdd:PRK08462 322 ELP-SQESIKLKGHAIECRITAEDPKK--FYPSPGKITKWIAPggRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 259707361 415 AAAKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPDH 460
Cdd:PRK08462 399 AIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
21-465 |
1.85e-150 |
|
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: 465.46 E-value: 1.85e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 21 RVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIG--PPLA-AESYLNMDKIINSALRSGAQAIHP 97
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGegPDLGpIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 98 GYGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAV 177
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 178 YGGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKIIE 257
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 258 EAPAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGEK 337
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 338 LPLKQSEIP------LNGHAFECRVYAEDTRKGaFMPTAGRLNYVDFPE--DARIDTG-VVSGDEVSIHYDPMIAKVVVW 408
Cdd:TIGR01235 321 LPTPQLGVPnqedirTNGYAIQCRVTTEDPANN-FQPDTGRIEAYRSAGgfGIRLDGGnSYAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 259707361 409 GQDRAVAAAKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPDHqKELF 465
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTT-PELF 455
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
19-489 |
4.75e-147 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 435.78 E-value: 4.75e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 19 IQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPlAAESYLNMDKIINSALRSGAQAIHPG 98
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTD-PIKGYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 99 YGFLSENAGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHG-EDQSDANLKKKSAEIGYPVMLKAV 177
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 178 YGGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKIIE 257
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 258 EAPAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGEK 337
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 338 LPLKQSEIPLNGHAFECRVYAEDTRKGaFMPTAGRLN--YVDFPEDARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAVA 415
Cdd:PRK08463 321 LDLEQSDIKPRGFAIEARITAENVWKN-FIPSPGKITeyYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259707361 416 AAKLESALARTRISGLPTNIDFVRRVLAHPEFAAGNVYTDFIPDHQKELFAESETPAEIYVESAVAHALAALQK 489
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKTEDRHQENKEEVIAAIAAALKK 473
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
133-339 |
1.07e-79 |
|
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: 251.84 E-value: 1.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 133 KNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAVYGGGGKGMRIAWNEAEFEEKLASARNEAKKSFGND 212
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 213 EMLVEKFVEKPRHVEVQVFGDHHGNYVHLWERDCSVQRRHQKIIEEAPAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVE 292
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 259707361 293 FIMDPR-GEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQGEKLP 339
Cdd:pfam02786 162 FALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
19-126 |
1.52e-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: 203.10 E-value: 1.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 19 IQRVLVANRGEIAIRVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIGPPLAAESYLNMDKIINSALRSGAQAIHPG 98
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 259707361 99 YGFLSENAGFAEKCAQAGLVFIGPPAQA 126
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
87-337 |
4.72e-54 |
|
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: 185.85 E-value: 4.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 87 ALRSGAQAIHPGYGF---LSENAG----FAEKCAQAGLvfIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDA 159
Cdd:COG0439 4 AIIAAAAELARETGIdavLSESEFavetAAELAEELGL--PGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 160 nlKKKSAEIGYPVMLKAVYGGGGKGMRIAWNEAEFEEKLASARNEAKKSFGNDEMLVEKFVEKpRHVEVQVFGdHHGNYV 239
Cdd:COG0439 82 --LAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV-RDGEVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 240 HlwerdCSVQRRHQK---IIE---EAPAPnMEHDTRVKLGESAVRAAAAVGYVG-AGTVEFIMDPRGEFYFMEMNTRLQV 312
Cdd:COG0439 158 V-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYLIEINARLGG 231
|
250 260
....*....|....*....|....*..
gi 259707361 313 EH--PVSEAITGTDLVEWQLRVAQGEK 337
Cdd:COG0439 232 EHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
353-457 |
3.72e-48 |
|
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: 164.51 E-value: 3.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 353 ECRVYAEDTRKGaFMPTAGRLNYVDFPE--DARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAVAAAKLESALARTRISG 430
Cdd:smart00878 1 ECRINAEDPANG-FLPSPGRITRYRFPGgpGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*..
gi 259707361 431 LPTNIDFVRRVLAHPEFAAGNVYTDFI 457
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFL 106
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
353-457 |
7.33e-48 |
|
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: 163.43 E-value: 7.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 353 ECRVYAEDTRKGaFMPTAGRLNYVDFPE--DARIDTGVVSGDEVSIHYDPMIAKVVVWGQDRAVAAAKLESALARTRISG 430
Cdd:pfam02785 1 EARIYAEDPDNN-FLPSPGKVTRYRFPGgpGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*..
gi 259707361 431 LPTNIDFVRRVLAHPEFAAGNVYTDFI 457
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFL 106
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
606-670 |
3.14e-21 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 87.47 E-value: 3.14e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259707361 606 VAPMPGIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNVPKNAVLVQF 670
Cdd:cd06850 3 TAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
527-669 |
1.20e-15 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 74.51 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 527 RLTVSYDGNSYETllnDIESTTDGSFKFTLEanGRRWSTVVKNLGNSLmvnGVGQNEYETPQIHETFDSLSG-------- 598
Cdd:PRK05641 3 KVKVIVDGVEYEV---EVEELGPGKFRVSFE--GKTYEVEAKGLGIDL---SAVQEQVPTPAPAPAPAVPSAptpvapaa 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259707361 599 -----GAASHSAV-APMPGIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNVPKNAVLVQ 669
Cdd:PRK05641 75 papapASAGENVVtAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIE 151
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
607-661 |
1.45e-13 |
|
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: 74.35 E-value: 1.45e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 259707361 607 APMPGIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNV 661
Cdd:COG1038 1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQV 1135
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
607-661 |
7.36e-13 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 72.09 E-value: 7.36e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 259707361 607 APMPGIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNV 661
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQV 1135
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
600-661 |
3.23e-12 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 64.06 E-value: 3.23e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259707361 600 AASHSAVAPMPGIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNV 661
Cdd:PRK06549 59 AGADAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVV 120
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
606-668 |
5.34e-12 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 68.72 E-value: 5.34e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259707361 606 VAPMPGIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNVPKNAVLV 668
Cdd:PRK09282 526 TSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLM 588
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
599-671 |
7.17e-12 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 68.42 E-value: 7.17e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259707361 599 GAASHSAVAPMPGIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNVPKNAVLVQFA 671
Cdd:PRK14040 521 AAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
133-308 |
2.21e-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: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 133 KNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAVYGGGGKGMRIAWNEAEFEEKLASARNEakksfgND 212
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 213 EMLVEKFVEkPRHVEVQVFGD-------------HHG--NYVHLWERDcsvqrrhqKIIEEAPAPnMEHDTRVKLGESAV 277
Cdd:COG1181 170 KVLVEEFID-GREVTVGVLGNggpralppieivpENGfyDYEAKYTDG--------GTEYICPAR-LPEELEERIQELAL 239
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 259707361 278 ------------RaaaavgyvgagtVEFIMDPRGEFYFMEMNT 308
Cdd:COG1181 240 kafralgcrgyaR------------VDFRLDEDGEPYLLEVNT 270
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
599-668 |
8.59e-11 |
|
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: 65.62 E-value: 8.59e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 599 GAASHSAvAPMPGIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNVPKNAVLV 668
Cdd:TIGR01235 1072 GNPAHVG-APMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLL 1140
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
109-338 |
9.94e-11 |
|
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: 65.02 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 109 AEKCAQAGLVFIGPPAQAIrDMgAKNVSK--QIMEDAKVPVVKGfhGEDQSDANLKKKSAEIGYPVMLKAVYGGGGKGMR 186
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESI-DR-AEDREKfsELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAME 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 187 IAWNEAEFEEKLasarNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDH-----HGNYVHlwerdcsvqrrhqkiIEEA-- 259
Cdd:TIGR01369 722 IVYNEEELRRYL----EEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGeevliPGIMEH---------------IEEAgv 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 260 ---------PAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDpRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQL 330
Cdd:TIGR01369 783 hsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAV 861
|
....*...
gi 259707361 331 RVAQGEKL 338
Cdd:TIGR01369 862 RVMLGKKL 869
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
109-237 |
1.00e-10 |
|
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: 64.51 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 109 AEKCAQAGLV----FIGPPAQAIRDmgAKNVS--KQIMEDAKVPVVKGFHGEDQSDAnlKKKSAEIGYPVMLKAVYGGGG 182
Cdd:COG0458 87 AVELEEAGILegvkILGTSPDAIDL--AEDRElfKELLDKLGIPQPKSGTATSVEEA--LAIAEEIGYPVIVRPSYVLGG 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 259707361 183 KGMRIAWNEAEFEEKLasarNEAKKSFGNDEMLVEKFVEKPRHVEVQVFGDHHGN 237
Cdd:COG0458 163 RGMGIVYNEEELEEYL----ERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDN 213
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
607-668 |
1.26e-10 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 59.52 E-value: 1.26e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259707361 607 APMPGII-------EKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNVPKNAVLV 668
Cdd:COG0511 65 SPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLF 133
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
607-668 |
3.25e-10 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 56.45 E-value: 3.25e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259707361 607 APMPG-----IIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNVPKNAVLV 668
Cdd:pfam00364 5 SPMIGesvreGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
606-669 |
1.45e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 54.79 E-value: 1.45e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259707361 606 VAPMPGIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNVPKNAVLVQ 669
Cdd:PRK08225 5 YASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLE 68
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
14-237 |
1.69e-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: 61.17 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 14 PLIRPIQRVLVANRGEIAI-----------RVQNTARKMGIETVAVFSDADRNSLFVKKADKAYHIgpPLAAESylnMDK 82
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIgqaaefdysgsQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIE--PLTPEA---VEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 83 IINsalRSGAQAIHPGYGFLS--------ENAGFAEKCaqaGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGE 154
Cdd:TIGR01369 76 IIE---KERPDAILPTFGGQTalnlavelEESGVLEKY---GVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 155 DQSDAnlKKKSAEIGYPVMLKAVYGGGGKGMRIAWNEAEFEEKlasARNEAKKSFGNdEMLVEKFVEKPRHVEVQVFGDH 234
Cdd:TIGR01369 150 SVEEA--LAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEI---AERALSASPIN-QVLVEKSLAGWKEIEYEVMRDS 223
|
...
gi 259707361 235 HGN 237
Cdd:TIGR01369 224 NDN 226
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
114-339 |
3.15e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 59.17 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 114 QAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDanLKKKSAEIGYPVMLKAVYG--------GGGKGM 185
Cdd:COG3919 99 EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADD--LDALAEDLGFPVVVKPADSvgydelsfPGKKKV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 186 RIAWNEAEFEEKLASARNEAkksfgnDEMLVEKFVEKPRHVEVQVFG--DHHGNYVHLwerdCSVQRRHQK--------I 255
Cdd:COG3919 177 FYVDDREELLALLRRIAAAG------YELIVQEYIPGDDGEMRGLTAyvDRDGEVVAT----FTGRKLRHYppaggnsaA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 256 IEEAPAPNMEHDTRvKLGES------AvraaaavgyvgagTVEFIMDPR-GEFYFMEMNTRLQVEHPVSEAiTGTDLVEW 328
Cdd:COG3919 247 RESVDDPELEEAAR-RLLEAlgyhgfA-------------NVEFKRDPRdGEYKLIEINPRFWRSLYLATA-AGVNFPYL 311
|
250
....*....|.
gi 259707361 329 QLRVAQGEKLP 339
Cdd:COG3919 312 LYDDAVGRPLE 322
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
37-338 |
7.61e-09 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 59.21 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 37 TARKMGIETVAVFSDADRNSLFVKKADKAYHigPPLAAESYL------NMDKIINSAlrSGAQAIhpgygflsenaGFAE 110
Cdd:PRK12815 584 ALKKEGYETIMINNNPETVSTDYDTADRLYF--EPLTLEDVLnvaeaeNIKGVIVQF--GGQTAI-----------NLAK 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 111 KCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDAnlKKKSAEIGYPVMLKAVYGGGGKGMRIAWN 190
Cdd:PRK12815 649 GLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEA--FAFAKRIGYPVLIRPSYVIGGQGMAVVYD 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 191 EAEFEEKLASArneakkSFGNDEMLVEKFVEKpRHVEVQVFGDHHGNYV-----HlwerdcsvqrrhqkiIEEA------ 259
Cdd:PRK12815 727 EPALEAYLAEN------ASQLYPILIDQFIDG-KEYEVDAISDGEDVTIpgiieH---------------IEQAgvhsgd 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 260 -----PAPNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDpRGEFYFMEMNTRLQVEHPVSEAITGTDLVEWQLRVAQ 334
Cdd:PRK12815 785 siavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLA-NDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLL 863
|
....
gi 259707361 335 GEKL 338
Cdd:PRK12815 864 GKSL 867
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
107-231 |
1.50e-08 |
|
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: 56.49 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 107 GFAEKCAQAGLVFIGPPaQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDanLKKKSAEIGYPVMLKAVYGGGGKGMR 186
Cdd:COG0189 72 ALLRQLEAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDD--LRAFLEELGGPVVLKPLDGSGGRGVF 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 259707361 187 IAWNEAEFEEKLasarnEAKKSFGNDEMLVEKFVEKPRHVEVQVF 231
Cdd:COG0189 149 LVEDEDALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVL 188
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
611-670 |
1.63e-07 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 48.98 E-value: 1.63e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 611 GIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNVPKNAVLVQF 670
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
100-490 |
3.37e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 53.70 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 100 GFLSENAGFAEKCAQAG--LVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFhgEDQSDANLKKKSAEIGYPVMLKAV 177
Cdd:PRK02186 73 GIMSSSEYFIEVASEVArrLGLPAANTEAIRTCRDKKRLARTLRDHGIDVPRTH--ALALRAVALDALDGLTYPVVVKPR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 178 YGGGGKGMRIAWNEAEFEEKLASARNEAKKSFgndemLVEKFVEKPRHvEVQVFGDHHGNYV------HLWERDCSVQRR 251
Cdd:PRK02186 151 MGSGSVGVRLCASVAEAAAHCAALRRAGTRAA-----LVQAYVEGDEY-SVETLTVARGHQVlgitrkHLGPPPHFVEIG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 252 HqkiieEAPAPnMEHDTRVKLGESAVRAAAAVGYVGAGT-VEFIMdpRGE-FYFMEMNTRLQ---VEHPVSEAiTGTDLV 326
Cdd:PRK02186 225 H-----DFPAP-LSAPQRERIVRTVLRALDAVGYAFGPAhTELRV--RGDtVVIIEINPRLAggmIPVLLEEA-FGVDLL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 327 EWQLRVAQGEKLplkqseiplnghafecrvYAEDTRKG------AFMPTAGRLNYVDFPED---ARIDTGVVS----GDE 393
Cdd:PRK02186 296 DHVIDLHLGVAA------------------FADPTAKRygairfVLPARSGVLRGLLFLPDdiaARPELRFHPlkqpGDA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 394 VSIHYD--PMIAKVVVWGQDRAVAAAKLESALARTRIsglptNIDFVRRVLAHPEFAAGNVYTDFIPDHQKELFAesetP 471
Cdd:PRK02186 358 LRLEGDfrDRIAAVVCAGDHRDSVAAAAERAVAGLSI-----DIGDAARAAALNDAGAGAARPGLPPEAQAIVYG----P 428
|
410
....*....|....*....
gi 259707361 472 AEIYVESAVAHALAALQKS 490
Cdd:PRK02186 429 GASEAPLAELDHLAAIDEA 447
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
609-669 |
3.69e-07 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 53.19 E-value: 3.69e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259707361 609 MPGIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNVPKNAVLVQ 669
Cdd:PRK14042 532 IPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIR 592
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
611-671 |
3.00e-06 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 45.44 E-value: 3.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259707361 611 GIIEKILVKPGEQVTTGQALV-VMTAmK--MEyiIRAPEDSTVEHIKCQAGKNVPKNAVLVQFA 671
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAeVETD-KatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
109-228 |
6.64e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 49.71 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 109 AEKCAQAGLVFIGPPAQAIrDMgAKNVSK--QIMEDAKVPVVKGFHGEDQSDAnlKKKSAEIGYPVMLKAVYGGGGKGMR 186
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAI-DL-AEDRERfsKLLEKLGIPQPPNGTATSVEEA--LEVAEEIGYPVLVRPSYVLGGRAME 721
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 259707361 187 IAWNEAEFEEKLasarNEAKKSFGNDEMLVEKFVEKPRHVEV 228
Cdd:PRK05294 722 IVYDEEELERYM----REAVKVSPDHPVLIDKFLEGAIEVDV 759
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
133-308 |
6.99e-06 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 48.57 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 133 KNVSKQIMEDAKVPVVKGfhGEDQSDANLKKKSAEIGYPVMLKAVYGGGGKGMRIAWNEAEfeekLASARNEAKKsFGnD 212
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPW--IVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDE----LQAALELAFK-YD-D 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 213 EMLVEKFVeKPRHVEVQVFGD----------HHGNY-----------VHLwerdC------SVQRRHQKIIEEApapnme 265
Cdd:PRK01372 171 EVLVEKYI-KGRELTVAVLGGkalpvieivpAGEFYdyeakylaggtQYI----CpaglpaEIEAELQELALKA------ 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 259707361 266 HDTrvkLG-ESAVRaaaavgyvgagtVEFIMDPRGEFYFMEMNT 308
Cdd:PRK01372 240 YRA---LGcRGWGR------------VDFMLDEDGKPYLLEVNT 268
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
40-337 |
5.86e-05 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 45.65 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 40 KMGIETVAVFSdADRNSLF--VKKADKAYhIGPPLAAESYLnmDKIINSALRSGAQAIHPGY----GFLSENAgfaEKCA 113
Cdd:PRK12767 20 KKSLLKGRVIG-ADISELApaLYFADKFY-VVPKVTDPNYI--DRLLDICKKEKIDLLIPLIdpelPLLAQNR---DRFE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 114 QAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANLKKKSAEIGYPVMLKAVYGGGGKGMRIAWNEAE 193
Cdd:PRK12767 93 EIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 194 FEEKLASarneakksfgNDEMLVEKFVEkprHVE--VQVFGDHHGNYVHlwerdcSVQRRH---------QKIIEEAPap 262
Cdd:PRK12767 173 LEFLLEY----------VPNLIIQEFIE---GQEytVDVLCDLNGEVIS------IVPRKRievragetsKGVTVKDP-- 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259707361 263 nmehdtrvKLGESAVRAAAAVGYVGAGTVEFIMDPrGEFYFMEMNTRLQVEHPVSeAITGTDLVEWQLRVAQGEK 337
Cdd:PRK12767 232 --------ELFKLAERLAEALGARGPLNIQCFVTD-GEPYLFEINPRFGGGYPLS-YMAGANEPDWIIRNLLGGE 296
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
139-308 |
7.19e-05 |
|
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: 44.23 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 139 IMEDAKVPVV-------KGFHGEDqsDANLKKKSAEIGYPVMLKAVYGGGGKGMRIAWNEAEfeekLASARNEAkksFGN 211
Cdd:pfam07478 1 LLKAAGLPVVpfvtftrADWKLNP--KEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREE----LQAAIEEA---FQY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 212 DE-MLVEKFVEKpRHVEVQVFGDHHGNYVHLWER--DCSVQRRHQKIIEEA-----PAPnMEHDTRVKLGESAVRAAAAV 283
Cdd:pfam07478 72 DEkVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPAD-LEEEQEEQIQELALKAYKAL 149
|
170 180
....*....|....*....|....*
gi 259707361 284 GYVGAGTVEFIMDPRGEFYFMEMNT 308
Cdd:pfam07478 150 GCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
133-221 |
8.22e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.92 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 133 KNVSKQIMEDAKVPVVKGfhGEDQSDANLKKKSAEIGYPVMLKAVYGGGGKGMRIawnEAEFEEKLASARNEAKKSFgnD 212
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEG--RVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTV---NITTREEIEAAYAVASKES--S 287
|
....*....
gi 259707361 213 EMLVEKFVE 221
Cdd:PRK14016 288 DVIVERYIP 296
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
106-221 |
9.31e-05 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 45.50 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 106 AGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDAnlKKKSAEIGYPVMLKAVYGGGGKGM 185
Cdd:PLN02257 76 AGLADDLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAA--KKYIKEQGAPIVVKADGLAAGKGV 153
|
90 100 110
....*....|....*....|....*....|....*....
gi 259707361 186 RIAwneAEFEEKLASARNE-AKKSFGN--DEMLVEKFVE 221
Cdd:PLN02257 154 VVA---MTLEEAYEAVDSMlVKGAFGSagSEVVVEEFLD 189
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
106-221 |
1.02e-04 |
|
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: 45.39 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 106 AGFAEKCAQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKG--FHGEDQSDANLKKKsaeiGYPVMLKAVYGGGGK 183
Cdd:COG0151 76 AGIVDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYrvFTDLEEALAYLEEQ----GAPIVVKADGLAAGK 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 259707361 184 GMRIAWNEAEfeeklasARNEAK-----KSFGN--DEMLVEKFVE 221
Cdd:COG0151 152 GVVVAETLEE-------ALAAVDdmladGKFGDagARVVIEEFLE 189
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
105-220 |
3.35e-04 |
|
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: 43.52 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 105 NAGFAEKCAQAGLVFigPPAQAIR---DmgaKNVSKQIMEDAKVPVVKGFHGEDQSDanLKKKSAEIGYPVMLKAVYGG- 180
Cdd:COG0026 64 PAEALEALEAEVPVR--PGPEALEiaqD---RLLEKAFLAELGIPVAPFAAVDSLED--LEAAIAELGLPAVLKTRRGGy 136
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 259707361 181 GGKGMRIAWNEAEFEeklasarnEAKKSFGNDEMLVEKFV 220
Cdd:COG0026 137 DGKGQVVIKSAADLE--------AAWAALGGGPCILEEFV 168
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
156-220 |
3.59e-04 |
|
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: 41.86 E-value: 3.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259707361 156 QSDANLKKKSAEIGYPVMLKAVYGG-GGKGMRIAWNEAEFEeklasarnEAKKSFGNDEMLVEKFV 220
Cdd:pfam02222 14 ESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP--------QAWEELGDGPVIVEEFV 71
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
102-196 |
3.66e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 43.93 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 102 LSENaGFAEKCaqaGLVFIGPPAQAI-----RDMgaknvSKQIMEDAKVPVVKGF--HGEDQSdanlKKKSAEIGYPVML 174
Cdd:PRK05294 102 LAES-GVLEKY---GVELIGAKLEAIdkaedREL-----FKEAMKKIGLPVPRSGiaHSMEEA----LEVAEEIGYPVII 168
|
90 100
....*....|....*....|....
gi 259707361 175 KAVY--GGGGKGmrIAWNEAEFEE 196
Cdd:PRK05294 169 RPSFtlGGTGGG--IAYNEEELEE 190
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
137-220 |
4.86e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 42.83 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 137 KQIMEDAKVPVVKgFHgEDQSDANLKKKSAEIGYPVMLKAVYGG-GGKGMRIAWNEAEFEeklasarnEAKKSFGNDEML 215
Cdd:PRK06019 105 KQFLDKLGIPVAP-FA-VVDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLE--------AAWALLGSVPCI 174
|
....*
gi 259707361 216 VEKFV 220
Cdd:PRK06019 175 LEEFV 179
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
139-239 |
1.10e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.46 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 139 IMEDAKVPVVKGfhGEDQSDANLKKKSAEIGYPVMLKAVYGGGGKGMRIAWNeaefEEKLASARNEAKKSFGNDEMLVEK 218
Cdd:PLN02735 709 ILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYS----DDKLKTYLETAVEVDPERPVLVDK 782
|
90 100
....*....|....*....|.
gi 259707361 219 FVEKPRHVEVQVFGDHHGNYV 239
Cdd:PLN02735 783 YLSDATEIDVDALADSEGNVV 803
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
113-310 |
5.79e-03 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 39.95 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 113 AQAGLVFIGPPAQAIRDMGAKNVSKQIMEDAKVPVVKGFHGEDQSDANlkKKSAEIGYPVMLKAVYGGGGKGMRIAWNEA 192
Cdd:PRK12815 109 EQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEAL--AFAEKIGFPIIVRPAYTLGGTGGGIAENLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 193 EFEEKLASARNEakkSFGNDeMLVEKFVEKPRHVEVQVFGDHHGNYVHLwerdCSVQRrhqkiIEE-----------APA 261
Cdd:PRK12815 187 ELEQLFKQGLQA---SPIHQ-CLLEESIAGWKEIEYEVMRDRNGNCITV----CNMEN-----IDPvgihtgdsivvAPS 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 259707361 262 PNMEHDTRVKLGESAVRAAAAVGYVGAGTVEFIMDPRG-EFYFMEMNTRL 310
Cdd:PRK12815 254 QTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSkQYYLIEVNPRV 303
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
607-632 |
6.48e-03 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 37.57 E-value: 6.48e-03
10 20
....*....|....*....|....*.
gi 259707361 607 APMPGIIEKILVKPGEQVTTGQALVV 632
Cdd:COG0511 109 APVSGTVVEILVENGQPVEYGQPLFV 134
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
611-670 |
8.13e-03 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 39.47 E-value: 8.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 259707361 611 GIIEKILVKPGEQVTTGQALVVMTAMKMEYIIRAPEDSTVEHIKCQAGKNVPKNAVLVQF 670
Cdd:TIGR01348 14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATL 73
|
|
| |
