|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
16-478 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 808.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 16 STVLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIHPGY 95
Cdd:COG4770 3 KKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 96 GFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSAG 175
Cdd:COG4770 83 GFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 176 GGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEEA 255
Cdd:COG4770 163 GGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 256 PSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDpsSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGRP 335
Cdd:COG4770 243 PSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADG--NFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 336 LPVAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQAL 415
Cdd:COG4770 321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896156295 416 ERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDRVAEGFATSETPDDVYLAAAM 478
Cdd:COG4770 401 ARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEELALAAAM 463
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
15-458 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 641.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 15 LSTVLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIHPG 94
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 95 YGFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGlSRPGLSD-EDLIEAAPSIGFPVLIKPS 173
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPG-SDGPVDDeEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 174 AGGGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIE 253
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 254 EAPSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDpsSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASG 333
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNG--EFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 334 RPLPVAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQ 413
Cdd:PRK08591 319 EPLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 896156295 414 ALERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDR 458
Cdd:PRK08591 399 AIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEK 443
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
15-458 |
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: 528.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 15 LSTVLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIHPG 94
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 95 YGFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSA 174
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 175 GGGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEE 254
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 255 APSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKdpSSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGR 334
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKN--GEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 335 PLPVAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQA 414
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 896156295 415 LERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDR 458
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-337 |
8.14e-88 |
|
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: 273.80 E-value: 8.14e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 128 DKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENAADLPAALATARREAAGAFGD 207
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 208 DSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEEAPSPLLDEETRSAIGEAACDAARSVGYVGAGTV 287
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 896156295 288 EFIVpakDPSS--FFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGRPLP 337
Cdd:pfam02786 161 EFAL---DPFSgeYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
351-457 |
2.53e-47 |
|
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: 162.20 E-value: 2.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 351 EARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQALERLDRALGDTVVAGV 430
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*..
gi 896156295 431 GVNIDFCRYLLNVPEVRAGDLDTGLLD 457
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
625-690 |
2.08e-22 |
|
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: 90.94 E-value: 2.08e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896156295 625 VIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEV-SFTVAPGDQVAGDQQLAVI 690
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVkEILVKEGDQVEAGQLLVVI 67
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
618-690 |
1.32e-18 |
|
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: 90.91 E-value: 1.32e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896156295 618 ADAGGSGVIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQVAGDQQLAVI 690
Cdd:COG1038 1071 ADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKeVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
610-690 |
8.98e-17 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 84.80 E-value: 8.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 610 EVVTTGAE-ADAGGSGVIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQVAGDQQL 687
Cdd:PRK12999 1062 KSTVAAREkADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKrVLVKAGDQVEAGDLL 1141
|
...
gi 896156295 688 AVI 690
Cdd:PRK12999 1142 VEL 1144
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
554-690 |
9.67e-17 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 84.12 E-value: 9.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 554 PRNYKVSVfrDGEHLRIVRDGVAQHflvetidnagSANHEEYVVAGAHGTWVLPRTEVVTTGAEADAGGSGVIQAPMPGA 633
Cdd:PRK09282 465 PTEFKVEV--DGEKYEVKIEGVKAE----------GKRPFYLRVDGMPEEVVVEPLKEIVVGGRPRASAPGAVTSPMPGT 532
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 896156295 634 IIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQVAGDQQLAVI 690
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKeILVKEGDRVNPGDVLMEI 590
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
553-690 |
6.74e-14 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 69.15 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 553 EPRNYKVSVFRDGEHLRIVRDGVAQHFLVETIDNAGSANHEEyvvagahgtwvlprtevVTTGAEADAGGSGVIQAPMPG 632
Cdd:COG0511 7 ESGLTELEVEEGEYKVRIKRGGAAAAAPVAAPAAAAPAAAAP-----------------AAAAAAAAASGGGAVKSPMVG 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156295 633 AIIALA-------VEEGARVEAGEALLVMEAMKMEHTLTAEIAGEV-SFTVAPGDQVAGDQQLAVI 690
Cdd:COG0511 70 TFYRAPspgakpfVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVvEILVENGQPVEYGQPLFVI 135
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
617-690 |
2.55e-10 |
|
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: 64.08 E-value: 2.55e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896156295 617 EADAGGSGVIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEV-SFTVAPGDQVAGDQQLAVI 690
Cdd:TIGR01235 1068 KADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIkEVLVKAGEQIDAKDLLLVL 1142
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
625-690 |
1.81e-09 |
|
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: 54.53 E-value: 1.81e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896156295 625 VIQAPMPG-----AIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVSFTVAP-GDQVAGDQQLAVI 690
Cdd:pfam00364 2 EIKSPMIGesvreGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
16-478 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 808.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 16 STVLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIHPGY 95
Cdd:COG4770 3 KKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 96 GFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSAG 175
Cdd:COG4770 83 GFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 176 GGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEEA 255
Cdd:COG4770 163 GGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 256 PSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDpsSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGRP 335
Cdd:COG4770 243 PSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADG--NFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 336 LPVAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQAL 415
Cdd:COG4770 321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896156295 416 ERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDRVAEGFATSETPDDVYLAAAM 478
Cdd:COG4770 401 ARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEELALAAAM 463
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
15-458 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 641.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 15 LSTVLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIHPG 94
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 95 YGFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGlSRPGLSD-EDLIEAAPSIGFPVLIKPS 173
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPG-SDGPVDDeEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 174 AGGGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIE 253
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 254 EAPSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDpsSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASG 333
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNG--EFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 334 RPLPVAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQ 413
Cdd:PRK08591 319 EPLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 896156295 414 ALERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDR 458
Cdd:PRK08591 399 AIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEK 443
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
16-458 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 602.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 16 STVLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIHPGY 95
Cdd:PRK06111 3 QKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 96 GFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSAG 175
Cdd:PRK06111 83 GLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 176 GGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEEA 255
Cdd:PRK06111 163 GGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 256 PSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVpaKDPSSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGRP 335
Cdd:PRK06111 243 PSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLV--DEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 336 LPVAQEDVTLTGHSIEARVYAEDPAAgFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQAL 415
Cdd:PRK06111 321 LSFTQDDIKRSGHAIEVRIYAEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 896156295 416 ERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDR 458
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
18-457 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 595.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 18 VLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIHPGYGF 97
Cdd:PRK08654 5 ILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 98 LSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSAGGG 177
Cdd:PRK08654 85 LAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 178 GKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEEAPS 257
Cdd:PRK08654 165 GIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 258 PLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVpakDPSSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGRPLP 337
Cdd:PRK08654 245 PIMTPELRERMGEAAVKAAKAINYENAGTVEFLY---SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 338 VAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQALER 417
Cdd:PRK08654 322 FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIAR 401
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 896156295 418 LDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLD 457
Cdd:PRK08654 402 MRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIE 441
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
18-470 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 572.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 18 VLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIG--PSPAReSYLVIDKIIDAARRCDADGIHPGY 95
Cdd:PRK12999 8 VLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGegKHPVR-AYLDIDEIIRVAKQAGVDAIHPGY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 96 GFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSAG 175
Cdd:PRK12999 87 GFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKASAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 176 GGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEEA 255
Cdd:PRK12999 167 GGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 256 PSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKdpSSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGRP 335
Cdd:PRK12999 247 PAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDAD--GNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGAT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 336 L------PVAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIV-DGSEVSSLYDPMLMKIISHG 408
Cdd:PRK12999 325 LhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAfAGAEITPYYDSLLVKLTAWG 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896156295 409 ENREQALERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDrvaegfatsETPD 470
Cdd:PRK12999 405 RTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFID---------ETPE 457
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
18-470 |
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: 565.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 18 VLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHvRM-ADMAIHIGP--SPAReSYLVIDKIIDAARRCDADGIHPG 94
Cdd:COG1038 7 VLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLH-RFkADEAYLIGEgkGPVD-AYLDIEEIIRVAKEKGVDAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 95 YGFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSA 174
Cdd:COG1038 85 YGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 175 GGGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEE 254
Cdd:COG1038 165 GGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 255 APSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDpsSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGR 334
Cdd:COG1038 245 APAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDG--NFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 335 PL-------PvAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVD-GSEVSSLYDPMLMKIIS 406
Cdd:COG1038 323 SLddpeigiP-SQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYtGAVITPYYDSLLVKVTA 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896156295 407 HGENREQALERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDrvaegfatsETPD 470
Cdd:COG1038 402 WGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFID---------ETPE 456
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
15-458 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 556.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 15 LSTVLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIHPG 94
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 95 YGFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSA 174
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 175 GGGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEE 254
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 255 APSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPaKDpSSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGR 334
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KD-GNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 335 PLPVAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQA 414
Cdd:PRK05586 320 KLSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 896156295 415 LERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDR 458
Cdd:PRK05586 400 IQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
15-458 |
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: 528.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 15 LSTVLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIHPG 94
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 95 YGFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSA 174
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 175 GGGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEE 254
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 255 APSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKdpSSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGR 334
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKN--GEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 335 PLPVAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQA 414
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 896156295 415 LERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDR 458
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
13-457 |
1.74e-171 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 498.90 E-value: 1.74e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 13 GSLSTVLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIH 92
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 93 PGYGFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGlSRPGLSD-EDLIEAAPSIGFPVLIK 171
Cdd:PRK12833 83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPG-SDGVVASlDAALEVAARIGYPLMIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 172 PSAGGGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHgNVIHLGERECSLQRRHQKV 251
Cdd:PRK12833 162 AAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 252 IEEAPSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDpSSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIA 331
Cdd:PRK12833 241 LEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDAR-GEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 332 SGRPLPVAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENR 411
Cdd:PRK12833 320 DGEPLRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 896156295 412 EQALERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLD 457
Cdd:PRK12833 400 AAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
18-477 |
6.20e-171 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 497.70 E-value: 6.20e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 18 VLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPArESYLVIDKIIDAARRCDADGIHPGYGF 97
Cdd:PRK07178 5 ILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPL-AGYLNPRRLVNLAVETGCDALHPGYGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 98 LSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGlSRPGLSD-EDLIEAAPSIGFPVLIKPSAGG 176
Cdd:PRK07178 84 LSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPG-SEGNLADlDEALAEAERIGYPVMLKATSGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 177 GGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEEAP 256
Cdd:PRK07178 163 GGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 257 SPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDpsSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGRPL 336
Cdd:PRK07178 243 SPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADG--EVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 337 PVAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQALE 416
Cdd:PRK07178 321 SYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALD 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896156295 417 RLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDRVAE--GFATSETPDDVYLAAA 477
Cdd:PRK07178 401 RGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPEltNYSIKRKPEELAAAIA 463
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
15-458 |
2.18e-162 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 474.62 E-value: 2.18e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 15 LSTVLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIHPG 94
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 95 YGFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGlSRPGLSD-EDLIEAAPSIGFPVLIKPS 173
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPG-SDGALKSyEEAKKIAKEIGYPVILKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 174 AGGGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIE 253
Cdd:PRK08462 163 AGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 254 EAPSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDpsSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASG 333
Cdd:PRK08462 243 ESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNL--DFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 334 RPLPvAQEDVTLTGHSIEARVYAEDPAAgFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQ 413
Cdd:PRK08462 321 EELP-SQESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 896156295 414 ALERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDR 458
Cdd:PRK08462 399 AIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
18-458 |
1.01e-149 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 443.49 E-value: 1.01e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 18 VLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPAReSYLVIDKIIDAARRCDADGIHPGYGF 97
Cdd:PRK08463 5 ILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIK-GYLDVKRIVEIAKACGADAIHPGYGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 98 LSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSRpgLSD---EDLIEAAPSIGFPVLIKPSA 174
Cdd:PRK08463 84 LSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEK--LNSesmEEIKIFARKIGYPVILKASG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 175 GGGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEE 254
Cdd:PRK08463 162 GGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 255 APSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVpaKDPSSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGR 334
Cdd:PRK08463 242 APCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLL--DDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 335 PLPVAQEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQA 414
Cdd:PRK08463 320 ILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 896156295 415 LERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDR 458
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIET 443
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
18-463 |
8.31e-149 |
|
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: 461.99 E-value: 8.31e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 18 VLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPAR---ESYLVIDKIIDAARRCDADGIHPG 94
Cdd:TIGR01235 2 ILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLgpiEAYLSIDEIIRVAKLNGVDAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 95 YGFLSENADFATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSA 174
Cdd:TIGR01235 82 YGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKASW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 175 GGGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEE 254
Cdd:TIGR01235 162 GGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 255 APSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKdpSSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGR 334
Cdd:TIGR01235 242 APAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDND--GKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 335 PLPVA------QEDVTLTGHSIEARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSG-IVDGSEVSSLYDPMLMKIISH 407
Cdd:TIGR01235 320 SLPTPqlgvpnQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGnSYAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 896156295 408 GENREQALERLDRALGDTVVAGVGVNIDFCRYLLNVPEVRAGDLDTGLLDRVAEGF 463
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELF 455
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-337 |
8.14e-88 |
|
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: 273.80 E-value: 8.14e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 128 DKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENAADLPAALATARREAAGAFGD 207
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 208 DSLFIEHFVDTPRHIEVQILADKHGNVIHLGERECSLQRRHQKVIEEAPSPLLDEETRSAIGEAACDAARSVGYVGAGTV 287
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 896156295 288 EFIVpakDPSS--FFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGRPLP 337
Cdd:pfam02786 161 EFAL---DPFSgeYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
76-340 |
2.89e-58 |
|
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: 197.79 E-value: 2.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 76 IDKIIDAA----RRCDADGIhpgygfLSENAD----FATACEEAGIEfiGPPASAINTMGDKISARAAVEARDVPTVPgl 147
Cdd:COG0439 2 IDAIIAAAaelaRETGIDAV------LSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPG-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 148 SRPGLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENAADLPAALATARREAAGAFGDDSLFIEHFVDTpRHIEVQIL 227
Cdd:COG0439 72 FALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 228 ADkHGNVIHlgereCSLQRRHQK---VIE---EAPSPlLDEETRSAIGEAACDAARSVGYV-GAGTVEFIVPAKDpsSFF 300
Cdd:COG0439 151 VR-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDG--EPY 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 896156295 301 FMEMNTRLQVEH--PVTEQVTGLDLVALQVDIASGRPLPVAQ 340
Cdd:COG0439 222 LIEINARLGGEHipPLTELATGVDLVREQIRLALGEPRILDP 263
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
18-122 |
4.37e-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: 191.55 E-value: 4.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 18 VLVANRGEIACRIIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPARESYLVIDKIIDAARRCDADGIHPGYGF 97
Cdd:pfam00289 4 VLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPGYGF 83
|
90 100
....*....|....*....|....*
gi 896156295 98 LSENADFATACEEAGIEFIGPPASA 122
Cdd:pfam00289 84 LSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
351-457 |
2.53e-47 |
|
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: 162.20 E-value: 2.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 351 EARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQALERLDRALGDTVVAGV 430
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*..
gi 896156295 431 GVNIDFCRYLLNVPEVRAGDLDTGLLD 457
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
351-458 |
4.84e-46 |
|
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: 158.81 E-value: 4.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 351 EARVYAEDPAAGFLPTGGTVTRVVEPSGAGIRVDSGIVDGSEVSSLYDPMLMKIISHGENREQALERLDRALGDTVVAGV 430
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*...
gi 896156295 431 GVNIDFCRYLLNVPEVRAGDLDTGLLDR 458
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
625-690 |
2.08e-22 |
|
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: 90.94 E-value: 2.08e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896156295 625 VIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEV-SFTVAPGDQVAGDQQLAVI 690
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVkEILVKEGDQVEAGQLLVVI 67
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
96-306 |
1.13e-19 |
|
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: 90.17 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 96 GFLSENADFATACEEAGIEFIGPP--ASAInTMgDKISARAAVEARDVPTVPG--LSRPGLSDEDLIEAApsIGFPVLIK 171
Cdd:COG1181 63 GRGGEDGTIQGLLELLGIPYTGSGvlASAL-AM-DKALTKRVLAAAGLPTPPYvvLRRGELADLEAIEEE--LGLPLFVK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 172 PSAGGGGKGMHRVENAADLPAALATARREaagafgDDSLFIEHFVDtPRHIEVQILADKHGNVIHLGERE-----CSLQR 246
Cdd:COG1181 139 PAREGSSVGVSKVKNAEELAAALEEAFKY------DDKVLVEEFID-GREVTVGVLGNGGPRALPPIEIVpengfYDYEA 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896156295 247 RHQ--KVIEEAPSPlLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDpsSFFFMEMNT 306
Cdd:COG1181 212 KYTdgGTEYICPAR-LPEELEERIQELALKAFRALGCRGYARVDFRLDEDG--EPYLLEVNT 270
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
618-690 |
1.32e-18 |
|
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: 90.91 E-value: 1.32e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896156295 618 ADAGGSGVIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQVAGDQQLAVI 690
Cdd:COG1038 1071 ADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKeVLVKEGDQVEAGDLLIEL 1144
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
30-341 |
2.61e-17 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 84.21 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 30 IIRTLRDNGIRSVAVYSDADADAPHVRMADmAIHIGPSPARESYLVIDKIIDAARRCDADGIHPGY----GFLSENADFA 105
Cdd:COG3919 20 VARSLGEAGVRVIVVDRDPLGPAARSRYVD-EVVVVPDPGDDPEAFVDALLELAERHGPDVLIPTGdeyvELLSRHRDEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 106 taceEAGIEFIGPPASAINTMGDKISARAAVEARDVPtVPGLSRPGlSDEDLIEAAPSIGFPVLIKPSAG--------GG 177
Cdd:COG3919 99 ----EEHYRLPYPDADLLDRLLDKERFYELAEELGVP-VPKTVVLD-SADDLDALAEDLGFPVVVKPADSvgydelsfPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 178 GKGMHRVENAADLPAALATARREaagafgDDSLFIEHFVDTPRHIE--VQILADKHGNVIHLgereCSLQRRHQKVIEEA 255
Cdd:COG3919 173 KKKVFYVDDREELLALLRRIAAA------GYELIVQEYIPGDDGEMrgLTAYVDRDGEVVAT----FTGRKLRHYPPAGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 256 PSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDpSSFFFMEMNTRLQVEHPVTeQVTGLDLVALQVDIASGRP 335
Cdd:COG3919 243 NSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRD-GEYKLIEINPRFWRSLYLA-TAAGVNFPYLLYDDAVGRP 320
|
....*.
gi 896156295 336 LPVAQE 341
Cdd:COG3919 321 LEPVPA 326
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
610-690 |
8.98e-17 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 84.80 E-value: 8.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 610 EVVTTGAE-ADAGGSGVIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQVAGDQQL 687
Cdd:PRK12999 1062 KSTVAAREkADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKrVLVKAGDQVEAGDLL 1141
|
...
gi 896156295 688 AVI 690
Cdd:PRK12999 1142 VEL 1144
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
554-690 |
9.67e-17 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 84.12 E-value: 9.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 554 PRNYKVSVfrDGEHLRIVRDGVAQHflvetidnagSANHEEYVVAGAHGTWVLPRTEVVTTGAEADAGGSGVIQAPMPGA 633
Cdd:PRK09282 465 PTEFKVEV--DGEKYEVKIEGVKAE----------GKRPFYLRVDGMPEEVVVEPLKEIVVGGRPRASAPGAVTSPMPGT 532
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 896156295 634 IIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQVAGDQQLAVI 690
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKeILVKEGDRVNPGDVLMEI 590
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
105-336 |
1.31e-14 |
|
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: 77.73 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 105 ATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSrpGLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRV 184
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKT--ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 185 ENAADLPAALatarREAAGAFGDDSLFIEHFVDTPRHIEVQILADkHGNVIHLGEREcslqrrHqkvIEEA--------- 255
Cdd:TIGR01369 724 YNEEELRRYL----EEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVLIPGIME------H---IEEAgvhsgdstc 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 256 --PSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDPssfFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASG 333
Cdd:TIGR01369 790 vlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEV---YVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLG 866
|
...
gi 896156295 334 RPL 336
Cdd:TIGR01369 867 KKL 869
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
553-690 |
6.74e-14 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 69.15 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 553 EPRNYKVSVFRDGEHLRIVRDGVAQHFLVETIDNAGSANHEEyvvagahgtwvlprtevVTTGAEADAGGSGVIQAPMPG 632
Cdd:COG0511 7 ESGLTELEVEEGEYKVRIKRGGAAAAAPVAAPAAAAPAAAAP-----------------AAAAAAAAASGGGAVKSPMVG 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156295 633 AIIALA-------VEEGARVEAGEALLVMEAMKMEHTLTAEIAGEV-SFTVAPGDQVAGDQQLAVI 690
Cdd:COG0511 70 TFYRAPspgakpfVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVvEILVENGQPVEYGQPLFVI 135
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
47-307 |
1.61e-13 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 72.22 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 47 DADADAPHVRMADMAIhIGPSPARESYlvIDKIIDAARRCDADGIHPGY----GFLSENADfatACEEAGIEFIGPPASA 122
Cdd:PRK12767 32 DISELAPALYFADKFY-VVPKVTDPNY--IDRLLDICKKEKIDLLIPLIdpelPLLAQNRD---RFEEIGVKVLVSSKEV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 123 INTMGDKISARAAVEARDVPTVPGLSRPGLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENAADLPAALATArreaa 202
Cdd:PRK12767 106 IEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYV----- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 203 gafgdDSLFIEHFVDTPRhIEVQILADKHGNVIHlgerecSLQRRHQKVIeeapspllDEETRSAI-------GEAACDA 275
Cdd:PRK12767 181 -----PNLIIQEFIEGQE-YTVDVLCDLNGEVIS------IVPRKRIEVR--------AGETSKGVtvkdpelFKLAERL 240
|
250 260 270
....*....|....*....|....*....|..
gi 896156295 276 ARSVGYVGAGTVEFIVpakDPSSFFFMEMNTR 307
Cdd:PRK12767 241 AEALGARGPLNIQCFV---TDGEPYLFEINPR 269
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
109-336 |
2.81e-13 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 73.46 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 109 EEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSrpGLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENAA 188
Cdd:PRK12815 651 EEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLT--ATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEP 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 189 DLPAALATArreaagAFGDDSLFIEHFVDTpRHIEVQILADkhGNVIHLG---ErecslqrrHqkvIEEA---------- 255
Cdd:PRK12815 729 ALEAYLAEN------ASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiE--------H---IEQAgvhsgdsiav 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 256 -PSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKDpssFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGR 334
Cdd:PRK12815 789 lPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDE---IYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGK 865
|
..
gi 896156295 335 PL 336
Cdd:PRK12815 866 SL 867
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
31-344 |
2.65e-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: 70.41 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 31 IRTLRDNGIRSVAVYSDADADAPHVRMADmAIHIGP-SPAresylVIDKIIDAARrcdADGIHPGYG-----FLSENADF 104
Cdd:TIGR01369 33 CKALKEEGYRVILVNSNPATIMTDPEMAD-KVYIEPlTPE-----AVEKIIEKER---PDAILPTFGgqtalNLAVELEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 105 ATACEEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPglSRPGLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRV 184
Cdd:TIGR01369 104 SGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPE--SEIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 185 ENAADLpaalataRREAAGAFGD---DSLFIEHFVDTPRHIEVQILADKHGNVI-------------HLGERecslqrrh 248
Cdd:TIGR01369 182 YNREEL-------KEIAERALSAspiNQVLVEKSLAGWKEIEYEVMRDSNDNCItvcnmenfdpmgvHTGDS-------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 249 qkvIEEAPSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFivpAKDPSS--FFFMEMNTRLQVEHPVTEQVTGLDLVAL 326
Cdd:TIGR01369 247 ---IVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQF---ALNPDSgrYYVIEVNPRVSRSSALASKATGYPIAKV 320
|
330
....*....|....*...
gi 896156295 327 QVDIASGRPLPVAQEDVT 344
Cdd:TIGR01369 321 AAKLAVGYTLDELKNPVT 338
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
91-227 |
5.51e-12 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 67.45 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 91 IHPGYGflsENADFATACEEAGIEFIGPP--ASAInTMgDKISARAAVEARDVPTVPG--LSRPGLSDEDLIEAAPSIGF 166
Cdd:PRK01966 89 LHGPPG---EDGTIQGLLELLGIPYVGCGvlASAL-SM-DKILTKRLLAAAGIPVAPYvvLTRGDWEEASLAEIEAKLGL 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896156295 167 PVLIKPSAGGGGKGMHRVENAADLPAALATARREaagafgDDSLFIEHFVDtPRHIEVQIL 227
Cdd:PRK01966 164 PVFVKPANLGSSVGISKVKNEEELAAALDLAFEY------DRKVLVEQGIK-GREIECAVL 217
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
38-289 |
4.80e-11 |
|
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: 64.71 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 38 GIRsVAVYsDADADAPHVRMADMAIHigpsparESYLVIDKIIDAARRCDAdgIhpgyGFLSENADFATACEEAGIEFIG 117
Cdd:COG0026 14 GYR-VHVL-DPDPDSPAAQVADEHIV-------ADYDDEEALREFAERCDV--V----TFEFENVPAEALEALEAEVPVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 118 PPASAINTMGDKISARAAVEARDVPTVPglSRPGLSDEDLIEAAPSIGFPVLIKPSAGG-GGKGMHRVENAADLPAALAt 196
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAP--FAAVDSLEDLEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADLEAAWA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 197 arreaagAFGDDSLFIEHFVDTPRhiEVQILA--DKHGNVIH--LGErecSLQRRHQ--KVIeeAPSPlLDEETRSAIGE 270
Cdd:COG0026 156 -------ALGGGPCILEEFVPFER--ELSVIVarSPDGEVATypVVE---NVHRNGIldESI--APAR-ISEALAAEAEE 220
|
250
....*....|....*....
gi 896156295 271 AACDAARSVGYVGAGTVEF 289
Cdd:COG0026 221 IAKRIAEALDYVGVLAVEF 239
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
607-687 |
7.68e-11 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 61.03 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 607 PRTEVVTTGAEADAGgSGVIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQVAGDQ 685
Cdd:PRK05641 69 PVAPAAPAPAPASAG-ENVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKkILVKEGDTVDTGQ 147
|
..
gi 896156295 686 QL 687
Cdd:PRK05641 148 PL 149
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
136-306 |
1.51e-10 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 61.18 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 136 VEARDVPTVP--GLSRPG---LSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENAADLPAALATARREaagafgDDSL 210
Cdd:pfam07478 2 LKAAGLPVVPfvTFTRADwklNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------DEKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 211 FIEHFVDTpRHIEVQILADKHGNVIHLGER--ECSLQRRHQKVIEEA-----PSPlLDEETRSAIGEAACDAARSVGYVG 283
Cdd:pfam07478 76 LVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPAD-LEEEQEEQIQELALKAYKALGCRG 153
|
170 180
....*....|....*....|...
gi 896156295 284 AGTVEFIVPAKDpsSFFFMEMNT 306
Cdd:pfam07478 154 LARVDFFLTEDG--EIVLNEVNT 174
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
616-687 |
1.96e-10 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 63.80 E-value: 1.96e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896156295 616 AEADAGGSGVIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQVAGDQQL 687
Cdd:PRK14040 517 AAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRgIAVKEGDAVAVGDTL 589
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
25-306 |
2.15e-10 |
|
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273498 [Multi-domain] Cd Length: 315 Bit Score: 62.69 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 25 EIACR----IIRTLRDNGIRSVAVYSDADADAPHVRMADMAIHIGPSPAResylvIDKIIDAarrcdadgIHPGYGflsE 100
Cdd:TIGR01205 14 EISLVsaaaVLKALRDLGYDVYPVDIDKMGSWTYKDLPQLILELGALLEG-----IDVVFPV--------LHGRYG---E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 101 NADFATACEEAGIEFIGPP--ASAInTMgDKISARAAVEARDVPTVP--GLSRPGLSDEDLI--EAAPSIGFPVLIKPSA 174
Cdd:TIGR01205 78 DGTIQGLLELMGIPYTGSGvlASAL-SM-DKLLTKLLWKALGLPTPDyiVLTQNRASADELEceQVAEPLGFPVIVKPAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 175 GGGGKGMHRVENAADLPAALATARREaagafgDDSLFIEHFVDtPRHIEVQIL-ADKHGNVIHLGERECS--------LQ 245
Cdd:TIGR01205 156 EGSSVGVSKVKSEEELQAALDEAFEY------DEEVLVEQFIK-GRELEVSILgNEEALPIIEIVPEIEGfydyeakyLD 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896156295 246 RRHQKVIeeaPSPlLDEETRSAIGEAACDAARSVGYVGAGTVEFIVPAKdpSSFFFMEMNT 306
Cdd:TIGR01205 229 GSTEYVI---PAP-LDEELEEKIKELALKAYKALGCRGLARVDFFLDEE--GEIYLNEINT 283
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
617-690 |
2.55e-10 |
|
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: 64.08 E-value: 2.55e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896156295 617 EADAGGSGVIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEV-SFTVAPGDQVAGDQQLAVI 690
Cdd:TIGR01235 1068 KADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIkEVLVKAGEQIDAKDLLLVL 1142
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
117-306 |
4.26e-10 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 61.28 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 117 GPPASAInTMgDKISARAAVEARDVPTVPG--LSRpglsDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENAADLPAAL 194
Cdd:PRK01372 89 GVLASAL-AM-DKLRTKLVWQAAGLPTPPWivLTR----EEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAAL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 195 ATARREaagafgDDSLFIEHFVDTpRHIEVQILADKHGNVIHLgereCSLQR---RHQKVIEEA-----PSPlLDEETRS 266
Cdd:PRK01372 163 ELAFKY------DDEVLVEKYIKG-RELTVAVLGGKALPVIEI----VPAGEfydYEAKYLAGGtqyicPAG-LPAEIEA 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 896156295 267 AIGEAACDAARSVGYVGAGTVEFIVpaKDPSSFFFMEMNT 306
Cdd:PRK01372 231 ELQELALKAYRALGCRGWGRVDFML--DEDGKPYLLEVNT 268
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
38-289 |
5.54e-10 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 61.71 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 38 GIRsVAVYsDADADAPHVRMADMAIhigpspaRESYLVIDKIIDAARRCDAdgIhpGYGFlsENADFATACEEAGIEFIG 117
Cdd:PRK06019 25 GYK-VIVL-DPDPDSPAAQVADEVI-------VADYDDVAALRELAEQCDV--I--TYEF--ENVPAEALDALAARVPVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 118 PPASAINTMGDKISARAAVEARDVPTVPglSRPGLSDEDLIEAAPSIGFPVLIKPSAGG-GGKGMHRVENAADLPAALAt 196
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAP--FAVVDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAWA- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 197 arreaagAFGDDSLFIEHFVDTPRhiEVQILA--DKHGNVIH--LGErecSLQRRHQKVIEEAPSPLLDEetrsaIGEAA 272
Cdd:PRK06019 167 -------LLGSVPCILEEFVPFER--EVSVIVarGRDGEVVFypLVE---NVHRNGILRTSIAPARISAE-----LQAQA 229
|
250 260
....*....|....*....|.
gi 896156295 273 CDAARSV----GYVGAGTVEF 289
Cdd:PRK06019 230 EEIASRIaeelDYVGVLAVEF 250
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
625-690 |
1.81e-09 |
|
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: 54.53 E-value: 1.81e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896156295 625 VIQAPMPG-----AIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVSFTVAP-GDQVAGDQQLAVI 690
Cdd:pfam00364 2 EIKSPMIGesvreGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
117-335 |
3.73e-09 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 60.25 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 117 GPPASAINTMGDKisARAAVEARD----VPTVPGLSrpglSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENAADLPA 192
Cdd:PRK02186 96 AANTEAIRTCRDK--KRLARTLRDhgidVPRTHALA----LRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 193 ALATARREAAGAFgddslFIEHFVDTPRHiEVQILADKHGNVI------HLGERECSLQRRHqkvieEAPSPlLDEETRS 266
Cdd:PRK02186 170 HCAALRRAGTRAA-----LVQAYVEGDEY-SVETLTVARGHQVlgitrkHLGPPPHFVEIGH-----DFPAP-LSAPQRE 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896156295 267 AIGEAACDAARSVGY-VGAGTVEFIVPAKDPSsffFMEMNTRLQVEH-PVT-EQVTGLDLVALQVDIASGRP 335
Cdd:PRK02186 238 RIVRTVLRALDAVGYaFGPAHTELRVRGDTVV---IIEINPRLAGGMiPVLlEEAFGVDLLDHVIDLHLGVA 306
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
105-291 |
1.27e-08 |
|
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: 57.97 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 105 ATACEEA----GIEFIGPPASAINTMGDKISARAAVEARDVPTVPglSRPGLSDEDLIEAAPSIGFPVLIKPSAGGGGKG 180
Cdd:COG0458 87 AVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPK--SGTATSVEEALAIAEEIGYPVIVRPSYVLGGRG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 181 MHRVENAADLPAALatarREAAGAFGDDSLFIEHFVDTPRHIEVQILADKHGNV-------------IHLGERECSlqrr 247
Cdd:COG0458 165 MGIVYNEEELEEYL----ERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNViivgimehiepagVHSGDSICV---- 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 896156295 248 hqkvieeAPSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFIV 291
Cdd:COG0458 237 -------APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAV 273
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
614-693 |
2.33e-08 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 52.89 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 614 TGAEADAGGSGVIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQV-AGDqqlAVIT 691
Cdd:PRK06549 52 APQPAAAAGADAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTaIHVTPGQVVnPGD---GLIT 128
|
..
gi 896156295 692 VA 693
Cdd:PRK06549 129 IG 130
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
31-308 |
3.66e-08 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 56.90 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 31 IRTLRDNGIRSVAVYSDadadaPHVRMADmaihigPSPARESYL------VIDKIIdaaRRCDADGIHPGYGflSENA-D 103
Cdd:PRK12815 34 CLALKEEGYQVVLVNPN-----PATIMTD------PAPADTVYFepltveFVKRII---AREKPDALLATLG--GQTAlN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 104 FATACEEAGI------EFIGPPASAINTMGDKISARAAVEARDVPTvpGLSRPGLSDEDLIEAAPSIGFPVLIKPSAGGG 177
Cdd:PRK12815 98 LAVKLHEDGIleqygvELLGTNIEAIQKGEDRERFRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 178 GKGMHRVENAADLpaaLATARREAAGAFGDDSLfIEHFVDTPRHIEVQILADKHGNV-------------IHLGERecsl 244
Cdd:PRK12815 176 GTGGGIAENLEEL---EQLFKQGLQASPIHQCL-LEESIAGWKEIEYEVMRDRNGNCitvcnmenidpvgIHTGDS---- 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156295 245 qrrhqkvIEEAPSPLLDEETRSAIGEAACDAARSVGYVGAGTVEFivpAKDPSS--FFFMEMNTRL 308
Cdd:PRK12815 248 -------IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQF---ALDPKSkqYYLIEVNPRV 303
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
153-337 |
1.32e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 55.17 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 153 SDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENAADLPAALATARREAAgafgDDSLFIEHFVDTPRHIEVQILADKHG 232
Cdd:PLN02735 725 SEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDP----ERPVLVDKYLSDATEIDVDALADSEG 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 233 NV-------------IHLGERECSLqrrhqkvieeaPSPLLDEETRSAIGEAACDAARSVGYVGAGTVEF-IVPAKDPss 298
Cdd:PLN02735 801 NVviggimehieqagVHSGDSACSL-----------PTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEV-- 867
|
170 180 190
....*....|....*....|....*....|....*....
gi 896156295 299 fFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGRPLP 337
Cdd:PLN02735 868 -YIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSLK 905
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
109-331 |
4.78e-07 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 51.96 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 109 EEAGIEFIGPPaSAINTMGDKISARAAVEARDVPT-VPGLSrpgLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENA 187
Cdd:TIGR00768 70 ESLGVPVINSS-DAILNAGDKFLSHQLLAKAGIPLpRTGLA---GSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 188 ADLpAALATARREAAGAFGddSLFIEHFVDTP--RHIEVQILADKHGNVIHLGERE-----CSLQRRhqkvieEAPSPLL 260
Cdd:TIGR00768 146 QAA-ESLLEHFEQLNGPQN--LFLVQEYIKKPggRDIRVFVVGDEVVAAIYRITSGhwrsnLARGGK------AEPCSLT 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896156295 261 DEETRSAIGeaacdAARSVGyVGAGTVEFIvpaKDPSSFFFMEMNTRLQVEHpvTEQVTGLDLVALQVDIA 331
Cdd:TIGR00768 217 EEIEELAIK-----AAKALG-LDVAGVDLL---ESEDGLLVNEVNANPEFKN--SVKTTGVNIAGKLLDYI 276
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
38-359 |
9.13e-07 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 51.46 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 38 GIRSVAV--YSDAD--ADAPHVRMADmaihiGPSPARESYLVIDKIIDAARRCDADGIHPGYGFLSENADFATAceEAGI 113
Cdd:COG2232 25 GYRVYAVdlFADLDtrALAERWVRLD-----AESCGFDLEDLPAALLELAAADDPDGLVYGSGFENFPELLERL--ARRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 114 EFIGPPASAINTMGDKISARAAVEARDVPtVPglsrpglsdeDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENaadlpaa 193
Cdd:COG2232 98 PLLGNPPEVVRRVKDPLRFFALLDELGIP-HP----------ETRFEPPPDPGPWLVKPIGGAGGWHIRPADS------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 194 latarreaaGAFGDDSLFIEHFVDTpRHIEVQILADKHGNVIhLGereCSLQrrhqkVIEEAP----------SPL-LDE 262
Cdd:COG2232 160 ---------EAPPAPGRYFQRYVEG-TPASVLFLADGSDARV-LG---FNRQ-----LIGPAGerpfryggniGPLaLPP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 263 ETRSAIGEAACDAARSVGYVGAGTVEFIVpakDPSSFFFMEMNTRLQVEHPVTEQVTGLDLVALQVDIASGR-PLPVAQE 341
Cdd:COG2232 221 ALAEEMRAIAEALVAALGLVGLNGVDFIL---DGDGPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRGElPEVPRPK 297
|
330
....*....|....*...
gi 896156295 342 DVTLTGHSIearVYAEDP 359
Cdd:COG2232 298 PRRVAAKAI---LYAPRD 312
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
103-218 |
1.80e-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: 50.32 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 103 DFATACEEAGIEFIGPPAsAINTMGDKISARAAVEARDVPTVP-GLSRpglSDEDLIEAAPSIGFPVLIKPSAGGGGKGM 181
Cdd:COG0189 72 ALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPPtLVTR---DPDDLRAFLEELGGPVVLKPLDGSGGRGV 147
|
90 100 110
....*....|....*....|....*....|....*..
gi 896156295 182 HRVENAADLPAALATARREaagafGDDSLFIEHFVDT 218
Cdd:COG0189 148 FLVEDEDALESILEALTEL-----GSEPVLVQEFIPE 179
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
622-693 |
2.00e-06 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 50.88 E-value: 2.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896156295 622 GSGVIQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQVAGDQQLAVITVA 693
Cdd:PRK14042 524 GPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAeILCQKGDKVTPGQVLIRVEVS 596
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
153-291 |
6.11e-06 |
|
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: 46.86 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 153 SDEDLIEAAPSIGFPVLIKPSAGG-GGKGMHRVENAADLPaalatarrEAAGAFGDDSLFIEHFVDTPRHIEVQILADKH 231
Cdd:pfam02222 15 SLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP--------QAWEELGDGPVIVEEFVPFDRELSVLVVRSVD 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896156295 232 GN-----VIHlgerecSLQRRHQKVIEEAPSPLLDEETRSAiGEAACDAARSVGYVGAGTVEFIV 291
Cdd:pfam02222 87 GEtafypVVE------TIQEDGICRLSVAPARVPQAIQAEA-QDIAKRLVDELGGVGVFGVELFV 144
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
626-681 |
7.05e-06 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 44.39 E-value: 7.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 896156295 626 IQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEV-SFTVAPGDQV 681
Cdd:PRK08225 4 VYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVkKINVQEGDFV 60
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
109-217 |
2.75e-05 |
|
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439798 [Multi-domain] Cd Length: 393 Bit Score: 47.04 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 109 EEAGIEFIgPPASAINTMGDKISAR--AAVEARdVPTVPglSRPGLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVEN 186
Cdd:COG0027 95 EAEGFRVV-PTARAVRLTMNREGIRrlAAEELG-LPTSP--YRFADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRS 170
|
90 100 110
....*....|....*....|....*....|.
gi 896156295 187 AADLPAALATARreAAGAFGDDSLFIEHFVD 217
Cdd:COG0027 171 PADIEAAWEYAQ--EGGRGGAGRVIVEGFVD 199
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
626-690 |
5.26e-05 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 41.92 E-value: 5.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896156295 626 IQAPMPGAIIALA-------VEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQVAGDQQLAVI 690
Cdd:PRK07051 6 IVSPLPGTFYRRPspdappyVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVeFLVEDGEPVEAGQVLARI 78
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
639-690 |
7.31e-05 |
|
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: 41.27 E-value: 7.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 896156295 639 VEEGARVEAGEALLVMEAMKMEHTLTAEIAGEV-SFTVAPGDQVAGDQQLAVI 690
Cdd:cd06663 21 KKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVkKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
626-691 |
9.13e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 40.95 E-value: 9.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896156295 626 IQAPMPGAIIALAVEEGARVEAGEALLVMEAMKMEHTLTAEIAGEVS-FTVAPGDQVAGDQQLAVIT 691
Cdd:PRK05889 5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSkVSVSVGDVIQAGDLIAVIS 71
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
164-217 |
1.15e-04 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 43.04 E-value: 1.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896156295 164 IGFPVLIKPSAGGGGKGMHRVENAADLPAALATARRE--------AAGAFGDDSLFIEHFVD 217
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEieqwkemyPEAVVDGGSFLVEEYIE 62
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
65-306 |
1.47e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 44.28 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 65 GPSPARESYL-----VIDKIIDA---ARRCDADG---------IHPGYGFLS------ENADFATACEEAGIEFIGPP-A 120
Cdd:PRK14569 12 GDSPEREVSLksgkaVLDSLISQgydAVGVDASGkelvaklleLKPDKCFVAlhgedgENGRVSALLEMLEIKHTSSSmK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 121 SAINTMGDKISARAAVEARdvptVPGLSRPGLSDEdlIEAAPSIGFPVLIKPSAGGGGKGMHRVENAADLPAALatarrE 200
Cdd:PRK14569 92 SSVITMDKMISKEILMHHR----MPTPMAKFLTDK--LVAEDEISFPVAVKPSSGGSSIATFKVKSIQELKHAY-----E 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 201 AAGAFGDdsLFIEHFVdTPRHIEVQILADKHGNVI---HLGERECSLQRRHQKVIEEAPSPLLdEETRSAIGEAACDAAR 277
Cdd:PRK14569 161 EASKYGE--VMIEQWV-TGKEITVAIVNDEVYSSVwiePQNEFYDYESKYSGKSIYHSPSGLC-EQKELEVRQLAKKAYD 236
|
250 260
....*....|....*....|....*....
gi 896156295 278 SVGYVGAGTVEFIVpaKDPSSFFFMEMNT 306
Cdd:PRK14569 237 LLGCSGHARVDFIY--DDRGNFYIMEINS 263
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
109-229 |
1.52e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 45.09 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 109 EEAGIEFIGPPASAINTMGDKISARAAVEARDVPTVPGLSrpGLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENAA 188
Cdd:PRK05294 650 EAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGT--ATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEE 727
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 896156295 189 DLPAALatarREAAGAFGDDSLFIEHFVDTPRHIEVQILAD 229
Cdd:PRK05294 728 ELERYM----REAVKVSPDHPVLIDKFLEGAIEVDVDAICD 764
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
27-181 |
3.06e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 44.32 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 27 ACRiirTLRDNGIRSVAVYS-------DADadaphvrMADmAIHIGPsparesyL---VIDKIIDAARrcdADGIHPGYG 96
Cdd:PRK05294 33 ACK---ALREEGYRVVLVNSnpatimtDPE-------MAD-ATYIEP-------ItpeFVEKIIEKER---PDAILPTMG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 97 ---FLseNAdfATACEEAGI------EFIGPPASAINTMGDKISARAAVEARDVPTVPglSRPGLSDEDLIEAAPSIGFP 167
Cdd:PRK05294 92 gqtAL--NL--AVELAESGVlekygvELIGAKLEAIDKAEDRELFKEAMKKIGLPVPR--SGIAHSMEEALEVAEEIGYP 165
|
170
....*....|....*.
gi 896156295 168 VLIKPS--AGGGGKGM 181
Cdd:PRK05294 166 VIIRPSftLGGTGGGI 181
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
109-217 |
3.84e-04 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 43.20 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 109 EEAGIEFIgPPASAIN-TMGDKISARAAVEARDVPTVPglSRPGLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMHRVENA 187
Cdd:PRK09288 95 EKEGFNVV-PTARATRlTMNREGIRRLAAEELGLPTSP--YRFADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP 171
|
90 100 110
....*....|....*....|....*....|.
gi 896156295 188 ADLPAALATArreAAGAFGDDSLFI-EHFVD 217
Cdd:PRK09288 172 EDIEKAWEYA---QEGGRGGAGRVIvEEFID 199
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
125-200 |
4.29e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 43.61 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156295 125 TMGDKISARAAVEARD------------VPtVPgLSRPGLSDEDLIEAAPSIGFPVLIKPSAGGGGKGMH-RVENAADLP 191
Cdd:PRK14016 199 AETDQTSAIAVDIACDkeltkrllaaagVP-VP-EGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTvNITTREEIE 276
|
....*....
gi 896156295 192 AALATARRE 200
Cdd:PRK14016 277 AAYAVASKE 285
|
|
| |
