|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
352-976 |
0e+00 |
|
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: 1089.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 352 ERPKKVLILGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYFLPITPEYVEQVIKAERPT 431
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 432 GVLLTFGGQTALNCGVELQKSRIFEKYNVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPSAAVTSVEEALVAAIQIGY 511
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 512 PVMARSAFSLGGLGSGFANNEEELRALAHQALSHS--DQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHT 589
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 590 GESIVVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALNPNSEEFYIIEVNARLSRSSALASKATGYPLAYVAAK 669
Cdd:TIGR01369 244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 670 LALGIPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRSFEEAFQKALRMVDENV 749
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 750 NGFDPNIKQVNENE-----LREPTDKRMFVLAAALKQEYSVEKLYELTKIDIWFLEKFKNIIDYYKTLETLDNKPVTFDI 824
Cdd:TIGR01369 404 TGFDLPDREVEPDEdlwraLKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 825 LKKAKKIGFSDKQIAVAIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYLYLTYNGSTHDIQFP-GEHIMVLGSG 903
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTdKKKVLVLGSG 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158451323 904 VYRIGSSVEFDWCAVGCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIERPDGVILS 976
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
355-975 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 981.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 355 KKVLILGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYFLPITPEYVEQVIKAERPTGVL 434
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 435 LTFGGQTALNCGVELQKSRIFEKYNVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPSAAVTSVEEALVAAIQIGYPVM 514
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 515 ARSAFSLGGLGSGFANNEEELRALAHQALSHS--DQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGES 592
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 593 IVVAPSQTLSNRDYYMLRNTAIKVIRHFGII-GECNIQYALNPNSEEFYIIEVNARLSRSSALASKATGYPLAYVAAKLA 671
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 672 LGIPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRSFEEAFQKALRMVDENVNG 751
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 752 FDP-NIKQVNENELRE----PTDKRMFVLAAALKQEYSVEKLYELTKIDIWFLEKFKNIIDYYKTLETLDNkPVTFDILK 826
Cdd:PRK05294 408 LDEdLFEEESLEELREelkePTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGL-PLDAELLR 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 827 KAKKIGFSDKQIAVAIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYLYLTYNGSTHDIQFPGEHIMVLGSGVYR 906
Cdd:PRK05294 487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158451323 907 IGSSVEFDWCAVGCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIERPDGVIL 975
Cdd:PRK05294 567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIV 635
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
360-902 |
0e+00 |
|
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: 635.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 360 LGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYFLPITPEYVEQVIKAERPTGVLLTFGG 439
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 440 QTALNCGVELQKSRIFEkyNVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPSAAVTSVEEALVAAIQIGYPVMARSAF 519
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 520 SLGGLGSGFANNEEELRALAHQALSHSD--QLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGESIVVAP 597
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPdhPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 598 SQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALnpNSEEFYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 677
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAV--DDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 678 IIKNSvTGvttacFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRSFEEAFQKALRMVDENVNG--FDPN 755
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 756 IKQVNENELRE--PTDKRMFVLAAALKQEYSVEKLYELTKIDIWFLEKFKNIIdyyKTLETLDNKPVTFDILKKAKKIGF 833
Cdd:COG0458 391 VADDDKEEALLlaRRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPII---VDEIELEEIILVINTLLGAKSLGD 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158451323 834 SDKQIAVAIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYLYLTYNGSTHDIQFPGEHIMVLGS 902
Cdd:COG0458 468 SDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-323 |
2.88e-141 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 426.03 E-value: 2.88e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDdrdenglprwFESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:PRK12564 38 GYQEILTDPSYAGQIVTFTYPLIGNYGVNRED----------FESDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 81 PGLCDIDTRALTYRLRE-GVTLGRIVQGVPPFGPLP----ALTDPNSRNLVAEVSTKGSKIF---NPNGNLTILAVDCGL 152
Cdd:PRK12564 108 PGISGIDTRALTRKLREkGAMKGVIATEDFDAEELLekarAFPGLLGLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 153 KYNQIRCLIKRNAKVILVPWDH------KMDPsqyDGLFISNGPGDPVMCKKVVDNLRAVIENKnniKPIFGICLGHQLL 226
Cdd:PRK12564 188 KRNILRELAERGCRVTVVPATTtaeeilALNP---DGVFLSNGPGDPAALDYAIEMIRELLEKK---IPIFGICLGHQLL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 227 STAAGCNTYKTTYGNRGHNLPCTHNGTGRCFMTSQNHGFAVDANSLPDEWKILFTNENDKTNEGIIHKTDPYFSVQFHPE 306
Cdd:PRK12564 262 ALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPE 341
|
330
....*....|....*..
gi 158451323 307 HTAGPTDLECLFDIFID 323
Cdd:PRK12564 342 ASPGPHDSAYLFDEFVE 358
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-326 |
2.82e-138 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 418.18 E-value: 2.82e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDdrdenglprwFESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:TIGR01368 34 GYQEILTDPSYKGQIVVFTYPLIGNYGVNDED----------AESKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 81 PGLCDIDTRALTYRLRE-GVTLGRIVQGVPPFGPL----PALTDPNSRNLVAEVSTKGSKIFNP--NGNLTILAVDCGLK 153
Cdd:TIGR01368 104 PGIYGVDTRALVKKIREkGTMKGVISTEDSNDEELvekaRVSPDITGINLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 154 YNQIRCLIKRNAKVILVPWDH------KMDPsqyDGLFISNGPGDPVMCKKVVDNLRAVIENKnnikPIFGICLGHQLLS 227
Cdd:TIGR01368 184 RNILRRLVKRGCEVTVVPYDTdaeeikKYNP---DGIFLSNGPGDPAAVEPAIETIRKLLEKI----PIFGICLGHQLLA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 228 TAAGCNTYKTTYGNRGHNLPCTHNGTGRCFMTSQNHGFAVDANSLP-DEWKILFTNENDKTNEGIIHKTDPYFSVQFHPE 306
Cdd:TIGR01368 257 LAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPaGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPE 336
|
330 340
....*....|....*....|
gi 158451323 307 HTAGPTDLECLFDIFIDVVK 326
Cdd:TIGR01368 337 ASPGPHDTEYLFDEFIDLMK 356
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-326 |
2.51e-135 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 410.57 E-value: 2.51e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDdrdenglprwFESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:COG0505 38 GYQEILTDPSYAGQIVTFTYPHIGNYGVNDED----------FESDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 81 PGLCDIDTRALTYRLRE-GVTLGRIVQGVPPFGPLPAL----TDPNSRNLVAEVSTKGSKIFNPNGN--LTILAVDCGLK 153
Cdd:COG0505 108 PGISGIDTRALTRHLREkGAMKGVISTGDLDIEELLEKaraaPGMEGLDLVKEVSTKEPYEWTEAPGagFHVVALDFGVK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 154 YNQIRCLIKRNAKVILVPWD------HKMDPsqyDGLFISNGPGDPVMCKKVVDNLRAVIENKnniKPIFGICLGHQLLS 227
Cdd:COG0505 188 RNILRELAERGCRVTVVPATtsaeeiLALNP---DGVFLSNGPGDPAALDYAIETIRELLGKG---IPIFGICLGHQLLA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 228 TAAGCNTYKTTYGNRGHNLPCTHNGTGRCFMTSQNHGFAVDANSLPD-EWKILFTNENDKTNEGIIHKTDPYFSVQFHPE 306
Cdd:COG0505 262 LALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPE 341
|
330 340
....*....|....*....|
gi 158451323 307 HTAGPTDLECLFDIFIDVVK 326
Cdd:COG0505 342 ASPGPHDSAYLFDRFIELME 361
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
475-677 |
2.50e-101 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 315.40 E-value: 2.50e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 475 DRKIFAEKINAIGEKVAPSAA--VTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANNEEELRALAHQALSHS------ 546
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 547 DQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLgiHTGESIVVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGEC 626
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 158451323 627 NIQYALNPNSEEFYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 677
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
145-322 |
1.25e-94 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 296.72 E-value: 1.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 145 ILAVDCGLKYNQIRCLIKRNAKVILVPWDHKMDPS---QYDGLFISNGPGDPVMCKKVVDNLRAVIENKnniKPIFGICL 221
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlklDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK---IPIFGICL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 222 GHQLLSTAAGCNTYKTTYGNRGHNLPCTHNGTGRCFMTSQNHGFAVDANSLPDEWKILFTNENDKTNEGIIHKTDPYFSV 301
Cdd:cd01744 78 GHQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSV 157
|
170 180
....*....|....*....|.
gi 158451323 302 QFHPEHTAGPTDLECLFDIFI 322
Cdd:cd01744 158 QFHPEASPGPHDTEYLFDEFL 178
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
146-324 |
2.39e-61 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 206.70 E-value: 2.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 146 LAVDCGL--KYNQIRCLIKRNAKVILVPWDH---KMDPSQYDGLFISNGPGDPVMCKKVVDNLRAVIENKnniKPIFGIC 220
Cdd:pfam00117 1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREARELK---IPILGIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 221 LGHQLLSTAAGCNTYK-TTYGNRGHNLPCTHN------GTGRCFMTSQNHGFAVDANSLPDEWKILFTNENDKTNEGIIH 293
Cdd:pfam00117 78 LGHQLLALAFGGKVVKaKKFGHHGKNSPVGDDgcglfyGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRH 157
|
170 180 190
....*....|....*....|....*....|.
gi 158451323 294 KTDPYFSVQFHPEHTAGPTDLECLFDIFIDV 324
Cdd:pfam00117 158 KKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
761-883 |
5.10e-55 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 186.50 E-value: 5.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 761 ENELREPTDKRMFVLAAALKQEYSVEKLYELTKIDIWFLEKFKNIIDYYKTLETLDNKPVTFDILKKAKKIGFSDKQIAV 840
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 158451323 841 AIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYLYLTY 883
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-104 |
1.47e-48 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses 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 synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 168.32 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDdrdenglprwFESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:smart01097 36 GYQEILTDPSYAGQIVVFTYPLIGNYGVNDED----------FESDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGI 105
|
90 100
....*....|....*....|....*
gi 158451323 81 PGLCDIDTRALTYRLRE-GVTLGRI 104
Cdd:smart01097 106 PGISGIDTRALTRKLREkGAMKGVI 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
352-976 |
0e+00 |
|
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: 1089.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 352 ERPKKVLILGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYFLPITPEYVEQVIKAERPT 431
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 432 GVLLTFGGQTALNCGVELQKSRIFEKYNVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPSAAVTSVEEALVAAIQIGY 511
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 512 PVMARSAFSLGGLGSGFANNEEELRALAHQALSHS--DQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHT 589
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 590 GESIVVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALNPNSEEFYIIEVNARLSRSSALASKATGYPLAYVAAK 669
Cdd:TIGR01369 244 GDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 670 LALGIPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRSFEEAFQKALRMVDENV 749
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 750 NGFDPNIKQVNENE-----LREPTDKRMFVLAAALKQEYSVEKLYELTKIDIWFLEKFKNIIDYYKTLETLDNKPVTFDI 824
Cdd:TIGR01369 404 TGFDLPDREVEPDEdlwraLKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 825 LKKAKKIGFSDKQIAVAIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYLYLTYNGSTHDIQFP-GEHIMVLGSG 903
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTdKKKVLVLGSG 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158451323 904 VYRIGSSVEFDWCAVGCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIERPDGVILS 976
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
355-975 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 981.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 355 KKVLILGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYFLPITPEYVEQVIKAERPTGVL 434
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 435 LTFGGQTALNCGVELQKSRIFEKYNVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPSAAVTSVEEALVAAIQIGYPVM 514
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 515 ARSAFSLGGLGSGFANNEEELRALAHQALSHS--DQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGES 592
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 593 IVVAPSQTLSNRDYYMLRNTAIKVIRHFGII-GECNIQYALNPNSEEFYIIEVNARLSRSSALASKATGYPLAYVAAKLA 671
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 672 LGIPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRSFEEAFQKALRMVDENVNG 751
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 752 FDP-NIKQVNENELRE----PTDKRMFVLAAALKQEYSVEKLYELTKIDIWFLEKFKNIIDYYKTLETLDNkPVTFDILK 826
Cdd:PRK05294 408 LDEdLFEEESLEELREelkePTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGL-PLDAELLR 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 827 KAKKIGFSDKQIAVAIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYLYLTYNGSTHDIQFPGEHIMVLGSGVYR 906
Cdd:PRK05294 487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158451323 907 IGSSVEFDWCAVGCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIERPDGVIL 975
Cdd:PRK05294 567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIV 635
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
355-975 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 769.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 355 KKVLILGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYFLPITPEYVEQVIKAERPTGVL 434
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 435 LTFGGQTALNCGVELQKSRIFEKYNVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPSAAVTSVEEALVAAIQIGYPVM 514
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 515 ARSAFSLGGLGSGFANNEEELRALAHQAL--SHSDQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGES 592
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLqaSPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 593 IVVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALNPNSEEFYIIEVNARLSRSSALASKATGYPLAYVAAKLAL 672
Cdd:PRK12815 248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 673 GIPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRSFEEAFQKALRMVDENVNGF 752
Cdd:PRK12815 328 GYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 753 D--PNIKQVNENELRE----PTDKRMFVLAAALKQEYSVEKLYELTKIDIWFLEKFKNIIDYYKTL--ETLDnkpVTFDI 824
Cdd:PRK12815 408 SlpIELSGKSDEELLQdlrhPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLaeDGLD---LSADL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 825 LKKAKKIGFSDKQIAVAIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYLYLTYNGSThDIQFPGEH--IMVLGS 902
Cdd:PRK12815 485 LRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGES-EAEPSSEKkkVLILGS 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158451323 903 GVYRIGSSVEFDWCAVGCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIERPDGVIL 975
Cdd:PRK12815 564 GPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIV 636
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
336-975 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 644.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 336 IDEIITKKFEFIPTIHERP--KKVLILGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYF 413
Cdd:PLN02735 3 LADTVTRAWSAATKAGKRTdlKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 414 LPITPEYVEQVIKAERPTGVLLTFGGQTALNCGVELQKSRIFEKYNVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPS 493
Cdd:PLN02735 83 APMTPELVEQVIAKERPDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 494 AAVTSVEEALVAAIQIG-YPVMARSAFSLGGLGSGFANNEEELRALAHQAL--SHSDQLIIDKSLKGWKEVEYEVVRDAY 570
Cdd:PLN02735 163 GIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLaaSITSQVLVEKSLLGWKEYELEVMRDLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 571 DNCITVCNMENVDPLGIHTGESIVVAPSQTLSNRDYYMLRNTAIKVIRHFGIigEC---NIQYALNPNSEEFYIIEVNAR 647
Cdd:PLN02735 243 DNVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 648 LSRSSALASKATGYPLAYVAAKLALGIPLPIIKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEV 727
Cdd:PLN02735 321 VSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 728 MSIGRSFEEAFQKALRMVD--------ENVNGFDPNIKQVNENeLREPTDKRMFVLAAALKQEYSVEKLYELTKIDIWFL 799
Cdd:PLN02735 401 MALGRTFQESFQKALRSLEtgfsgwgcAKVKELDWDWEQLKYK-LRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 800 EKFKNIIDYYKTLETLDNKPVTFDILKKAKKIGFSDKQIAVAIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYL 879
Cdd:PLN02735 480 TQLKELVDVEQFLKSRSLSELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYM 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 880 YLTYNGSTHDIQFPGEHIMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFE 959
Cdd:PLN02735 560 YSSYDGECESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVE 639
|
650
....*....|....*.
gi 158451323 960 VVMDIYNIERPDGVIL 975
Cdd:PLN02735 640 DVLNVIDLERPDGIIV 655
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
360-902 |
0e+00 |
|
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: 635.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 360 LGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYFLPITPEYVEQVIKAERPTGVLLTFGG 439
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 440 QTALNCGVELQKSRIFEkyNVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPSAAVTSVEEALVAAIQIGYPVMARSAF 519
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 520 SLGGLGSGFANNEEELRALAHQALSHSD--QLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGESIVVAP 597
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPdhPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 598 SQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALnpNSEEFYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 677
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAV--DDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 678 IIKNSvTGvttacFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRSFEEAFQKALRMVDENVNG--FDPN 755
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 756 IKQVNENELRE--PTDKRMFVLAAALKQEYSVEKLYELTKIDIWFLEKFKNIIdyyKTLETLDNKPVTFDILKKAKKIGF 833
Cdd:COG0458 391 VADDDKEEALLlaRRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPII---VDEIELEEIILVINTLLGAKSLGD 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158451323 834 SDKQIAVAIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYLYLTYNGSTHDIQFPGEHIMVLGS 902
Cdd:COG0458 468 SDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-323 |
2.88e-141 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 426.03 E-value: 2.88e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDdrdenglprwFESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:PRK12564 38 GYQEILTDPSYAGQIVTFTYPLIGNYGVNRED----------FESDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 81 PGLCDIDTRALTYRLRE-GVTLGRIVQGVPPFGPLP----ALTDPNSRNLVAEVSTKGSKIF---NPNGNLTILAVDCGL 152
Cdd:PRK12564 108 PGISGIDTRALTRKLREkGAMKGVIATEDFDAEELLekarAFPGLLGLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 153 KYNQIRCLIKRNAKVILVPWDH------KMDPsqyDGLFISNGPGDPVMCKKVVDNLRAVIENKnniKPIFGICLGHQLL 226
Cdd:PRK12564 188 KRNILRELAERGCRVTVVPATTtaeeilALNP---DGVFLSNGPGDPAALDYAIEMIRELLEKK---IPIFGICLGHQLL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 227 STAAGCNTYKTTYGNRGHNLPCTHNGTGRCFMTSQNHGFAVDANSLPDEWKILFTNENDKTNEGIIHKTDPYFSVQFHPE 306
Cdd:PRK12564 262 ALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPE 341
|
330
....*....|....*..
gi 158451323 307 HTAGPTDLECLFDIFID 323
Cdd:PRK12564 342 ASPGPHDSAYLFDEFVE 358
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-326 |
2.82e-138 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 418.18 E-value: 2.82e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDdrdenglprwFESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:TIGR01368 34 GYQEILTDPSYKGQIVVFTYPLIGNYGVNDED----------AESKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 81 PGLCDIDTRALTYRLRE-GVTLGRIVQGVPPFGPL----PALTDPNSRNLVAEVSTKGSKIFNP--NGNLTILAVDCGLK 153
Cdd:TIGR01368 104 PGIYGVDTRALVKKIREkGTMKGVISTEDSNDEELvekaRVSPDITGINLVAEVSTKEPYTWGQrgGKGKRVVVIDFGVK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 154 YNQIRCLIKRNAKVILVPWDH------KMDPsqyDGLFISNGPGDPVMCKKVVDNLRAVIENKnnikPIFGICLGHQLLS 227
Cdd:TIGR01368 184 RNILRRLVKRGCEVTVVPYDTdaeeikKYNP---DGIFLSNGPGDPAAVEPAIETIRKLLEKI----PIFGICLGHQLLA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 228 TAAGCNTYKTTYGNRGHNLPCTHNGTGRCFMTSQNHGFAVDANSLP-DEWKILFTNENDKTNEGIIHKTDPYFSVQFHPE 306
Cdd:TIGR01368 257 LAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPaGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPE 336
|
330 340
....*....|....*....|
gi 158451323 307 HTAGPTDLECLFDIFIDVVK 326
Cdd:TIGR01368 337 ASPGPHDTEYLFDEFIDLMK 356
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-326 |
2.51e-135 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 410.57 E-value: 2.51e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDdrdenglprwFESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:COG0505 38 GYQEILTDPSYAGQIVTFTYPHIGNYGVNDED----------FESDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 81 PGLCDIDTRALTYRLRE-GVTLGRIVQGVPPFGPLPAL----TDPNSRNLVAEVSTKGSKIFNPNGN--LTILAVDCGLK 153
Cdd:COG0505 108 PGISGIDTRALTRHLREkGAMKGVISTGDLDIEELLEKaraaPGMEGLDLVKEVSTKEPYEWTEAPGagFHVVALDFGVK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 154 YNQIRCLIKRNAKVILVPWD------HKMDPsqyDGLFISNGPGDPVMCKKVVDNLRAVIENKnniKPIFGICLGHQLLS 227
Cdd:COG0505 188 RNILRELAERGCRVTVVPATtsaeeiLALNP---DGVFLSNGPGDPAALDYAIETIRELLGKG---IPIFGICLGHQLLA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 228 TAAGCNTYKTTYGNRGHNLPCTHNGTGRCFMTSQNHGFAVDANSLPD-EWKILFTNENDKTNEGIIHKTDPYFSVQFHPE 306
Cdd:COG0505 262 LALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPE 341
|
330 340
....*....|....*....|
gi 158451323 307 HTAGPTDLECLFDIFIDVVK 326
Cdd:COG0505 342 ASPGPHDSAYLFDRFIELME 361
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
1-327 |
6.27e-107 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 336.09 E-value: 6.27e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDdrdenglprwFESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:PRK12838 36 GYQEVLTDPSYKGQIVVFTYPLIGNYGINADD----------YESKQPQVKGVIVYELSREGSHYRAKQSLDDFLKEWNI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 81 PGLCDIDTRALTYRLRE-GVTLGRIVQG--VPPFGPLPALTDPnsRNLVAEVSTKGSKIFnPNGNLTILAVDCGLKYNQI 157
Cdd:PRK12838 106 PGISGVDTRALVKHIREkGTMKASITTTddAHAFDQIKALVLP--KNVVAQVSTKEPYTY-GNGGKHVALIDFGYKKSIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 158 RCLIKRNAKVILVPWD------HKMDPsqyDGLFISNGPGDPVMCKKVVDNLRAVIENKnnikPIFGICLGHQLLSTAAG 231
Cdd:PRK12838 183 RSLSKRGCKVTVLPYDtsleeiKNLNP---DGIVLSNGPGDPKELQPYLPEIKKLISSY----PILGICLGHQLIALALG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 232 CNTYKTTYGNRGHNLPCTHNGTGRCFMTSQNHGFAVDANSL-PDEWKILFTNENDKTNEGIIHKTDPYFSVQFHPEHTAG 310
Cdd:PRK12838 256 ADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPG 335
|
330
....*....|....*..
gi 158451323 311 PTDLECLFDIFIDVVKS 327
Cdd:PRK12838 336 PHDAEYIFDEFLEMMEK 352
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
475-677 |
2.50e-101 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 315.40 E-value: 2.50e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 475 DRKIFAEKINAIGEKVAPSAA--VTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANNEEELRALAHQALSHS------ 546
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 547 DQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLgiHTGESIVVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGEC 626
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 158451323 627 NIQYALNPNSEEFYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 677
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
145-322 |
1.25e-94 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 296.72 E-value: 1.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 145 ILAVDCGLKYNQIRCLIKRNAKVILVPWDHKMDPS---QYDGLFISNGPGDPVMCKKVVDNLRAVIENKnniKPIFGICL 221
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlklDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK---IPIFGICL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 222 GHQLLSTAAGCNTYKTTYGNRGHNLPCTHNGTGRCFMTSQNHGFAVDANSLPDEWKILFTNENDKTNEGIIHKTDPYFSV 301
Cdd:cd01744 78 GHQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSV 157
|
170 180
....*....|....*....|.
gi 158451323 302 QFHPEHTAGPTDLECLFDIFI 322
Cdd:cd01744 158 QFHPEASPGPHDTEYLFDEFL 178
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
355-741 |
8.27e-85 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 295.73 E-value: 8.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 355 KKVLILGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYFLPITPEYVEQVIKAERPTGVL 434
Cdd:PRK12815 556 KKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVI 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 435 LTFGGQTALNCGVELqksrifEKYNVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPSAAVTSVEEALVAAIQIGYPVM 514
Cdd:PRK12815 636 VQFGGQTAINLAKGL------EEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVL 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 515 ARSAFSLGGLGSGFANNEEELRALAHQALSHSDQLIIDKSLKGwKEVEYEVVRDAYDncITVCN-MENVDPLGIHTGESI 593
Cdd:PRK12815 710 IRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPILIDQFIDG-KEYEVDAISDGED--VTIPGiIEHIEQAGVHSGDSI 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 594 VVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALnpNSEEFYIIEVNARLSRSSALASKATGYPLAYVAAKLALG 673
Cdd:PRK12815 787 AVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL--ANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLG 864
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158451323 674 iplpiiKNSVTGVTTACFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRSFEEAFQKA 741
Cdd:PRK12815 865 ------KSLAELGYPNGLWPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKG 926
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
353-743 |
2.78e-84 |
|
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: 293.83 E-value: 2.78e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 353 RPKKVLILGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYFLPITPEYVEQVIKAERPTG 432
Cdd:TIGR01369 553 DKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEG 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 433 VLLTFGGQTALNCGVELqksrifEKYNVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPSAAVTSVEEALVAAIQIGYP 512
Cdd:TIGR01369 633 VIVQFGGQTPLNLAKAL------EEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYP 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 513 VMARSAFSLGGLGSGFANNEEELRALAHQALSHSDQ--LIIDKSLKGWKEVEYEVVrdAYDNCITVCN-MENVDPLGIHT 589
Cdd:TIGR01369 707 VLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAV--SDGEEVLIPGiMEHIEEAGVHS 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 590 GESIVVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALNPNseEFYIIEVNARLSRSSALASKATGYPLAYVAAK 669
Cdd:TIGR01369 785 GDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDG--EVYVIEVNPRASRTVPFVSKATGVPLAKLAVR 862
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158451323 670 LALGIPLpiiKNSVTGvttacFEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRSFEEAFQKALR 743
Cdd:TIGR01369 863 VMLGKKL---EELGVG-----KEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQL 928
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
355-741 |
1.01e-80 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 283.91 E-value: 1.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 355 KKVLILGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYFLPITPEYVEQVIKAERPTGVL 434
Cdd:PRK05294 555 KKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVI 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 435 LTFGGQTALNCGVELqksrifEKYNVSVLGTPIKSIvDT-EDRKIFAEKINAIGEKVAPSAAVTSVEEALVAAIQIGYPV 513
Cdd:PRK05294 635 VQFGGQTPLKLAKAL------EAAGVPILGTSPDAI-DLaEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPV 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 514 MARSAFSLGGLGSGFANNEEELRALAHQALSHSDQ--LIIDKSLKGWKEVeyEVvrDAydncitVCN---------MENV 582
Cdd:PRK05294 708 LVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDhpVLIDKFLEGAIEV--DV--DA------ICDgedvliggiMEHI 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 583 DPLGIHTGESIVVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALnpNSEEFYIIEVNARLSRSSALASKATGYP 662
Cdd:PRK05294 778 EEAGVHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAV--KDDEVYVIEVNPRASRTVPFVSKATGVP 855
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158451323 663 LAYVAAKLALGIPLPIIknsvtGVTTacfEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRSFEEAFQKA 741
Cdd:PRK05294 856 LAKIAARVMLGKKLAEL-----GYTK---GLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKA 926
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-332 |
2.78e-67 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 230.45 E-value: 2.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDdrdenglprwFESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:CHL00197 40 GYQEIITDPSYFEQIVTFTYPEIGNTGINLED----------IESVKIQVKGIIAKNICKSSSNWRQQESLVSYLQRHKI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 81 PGLCDIDTRALTYRLRE-GVTLGRIVQGVPPFGPLPAL----TDPNSRNLVAEVST--------KGSKIFNPNGN----- 142
Cdd:CHL00197 110 PFIFGIDTRALTQHLRRfGTMNGCISNQNLNLSYLRAKikesPHMPSSDLIPRVTTssyyewdeKSHPSFYLADNkrphs 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 143 ---LTILAVDCGLKYNQIRCLIKRNAKVILVPWD---HKMDPSQYDGLFISNGPGDPVMCKKVVDNLRAVIenKNNIkPI 216
Cdd:CHL00197 190 syqLKIIVIDFGVKYNILRRLKSFGCSITVVPATspyQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLL--KYNI-PI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 217 FGICLGHQLLSTAAGCNTYKTTYGNRGHNLPCTHNGtgRCFMTSQNHGFAVDANSL-PDEWKILFTNENDKTNEGIIHKT 295
Cdd:CHL00197 267 FGICMGHQILSLALEAKTFKLKFGHRGLNHPSGLNQ--QVEITSQNHGFAVNLESLaKNKFYITHFNLNDGTVAGISHSP 344
|
330 340 350
....*....|....*....|....*....|....*..
gi 158451323 296 DPYFSVQFHPEHTAGPTDLECLFDIFIDVVKSYKNNK 332
Cdd:CHL00197 345 KPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSSK 381
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
355-741 |
1.37e-63 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 234.29 E-value: 1.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 355 KKVLILGSGGLCIGQAGEFDYSGSQGVKAMQEEKIQTVLINPNIATVQTSKGLADKVYFLPITPEYVEQVIKAERPTGVL 434
Cdd:PLN02735 575 KKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGII 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 435 LTFGGQTALNCGVELQKSriFEKY---------NVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPSAAVTSVEEALVA 505
Cdd:PLN02735 655 VQFGGQTPLKLALPIQKY--LDKNpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAI 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 506 AIQIGYPVMARSAFSLGGLGSGFANNEEELRALAHQALSHSDQ--LIIDKSLKGWKEVEYEVVRDAYDNCITVCNMENVD 583
Cdd:PLN02735 733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPErpVLVDKYLSDATEIDVDALADSEGNVVIGGIMEHIE 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 584 PLGIHTGESIVVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALNPnSEEFYIIEVNARLSRSSALASKATGYPL 663
Cdd:PLN02735 813 QAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITP-SGEVYIIEANPRASRTVPFVSKAIGHPL 891
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158451323 664 AYVAAKLALGIPLPIIknsvtGVTTacfEPSLDYCVVKIPRWDLAKFNRVSTKIGSSMKSVGEVMSIGRSFEEAFQKA 741
Cdd:PLN02735 892 AKYASLVMSGKSLKDL-----GFTE---EVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKA 961
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
146-324 |
2.39e-61 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 206.70 E-value: 2.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 146 LAVDCGL--KYNQIRCLIKRNAKVILVPWDH---KMDPSQYDGLFISNGPGDPVMCKKVVDNLRAVIENKnniKPIFGIC 220
Cdd:pfam00117 1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREARELK---IPILGIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 221 LGHQLLSTAAGCNTYK-TTYGNRGHNLPCTHN------GTGRCFMTSQNHGFAVDANSLPDEWKILFTNENDKTNEGIIH 293
Cdd:pfam00117 78 LGHQLLALAFGGKVVKaKKFGHHGKNSPVGDDgcglfyGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRH 157
|
170 180 190
....*....|....*....|....*....|.
gi 158451323 294 KTDPYFSVQFHPEHTAGPTDLECLFDIFIDV 324
Cdd:pfam00117 158 KKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
761-883 |
5.10e-55 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 186.50 E-value: 5.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 761 ENELREPTDKRMFVLAAALKQEYSVEKLYELTKIDIWFLEKFKNIIDYYKTLETLDNKPVTFDILKKAKKIGFSDKQIAV 840
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 158451323 841 AIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYLYLTY 883
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
1-318 |
9.06e-54 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 193.27 E-value: 9.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDDrdenglprwfESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:PLN02771 90 GYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDE----------ESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 81 PGLCDIDTRALTYRLREGVTLGRIV--QGVPPFGPLPALT---DPNSRNLVAEVS----------TKGSKIFNPNGN--- 142
Cdd:PLN02771 160 MGIYDVDTRAITRRLREDGSLIGVLstEDSKTDEELLKMSrswDIVGIDLISGVSckspyewvdkTNPEWDFNTNSRdge 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 143 -LTILAVDCGLKYNQIRCLIKRNAKVILVP--WDH----KMDPsqyDGLFISNGPGDPVMCKKVVDNLRAVIENKnnikP 215
Cdd:PLN02771 240 sYHVIAYDFGIKHNILRRLASYGCKITVVPstWPAsealKMKP---DGVLFSNGPGDPSAVPYAVETVKELLGKV----P 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 216 IFGICLGHQLLSTAAGCNTYKTTYGNRGHNLPCTHNGTGRCFMTSQNHGFAVDANSLPDEWKILFTNENDKTNEGIIHKT 295
Cdd:PLN02771 313 VFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPA 392
|
330 340
....*....|....*....|...
gi 158451323 296 DPYFSVQFHPEHTAGPTDLECLF 318
Cdd:PLN02771 393 LNVMSLQYHPEASPGPHDSDNAF 415
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-104 |
2.65e-50 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. 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 pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 173.28 E-value: 2.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDdrdenglprwFESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:pfam00988 32 GYQEILTDPSYAGQIVVFTYPLIGNYGVNPED----------FESDKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGI 101
|
90 100
....*....|....*....|....*
gi 158451323 81 PGLCDIDTRALTYRLRE-GVTLGRI 104
Cdd:pfam00988 102 PGISGVDTRALTRKIREkGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-104 |
1.47e-48 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses 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 synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 168.32 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 1 GYPESLTDPSYHAQLLVLTYPLIGNYGVPDEDdrdenglprwFESERIWAAGLIVGEVSTRACHWRAKQSLGSWLAEHGI 80
Cdd:smart01097 36 GYQEILTDPSYAGQIVVFTYPLIGNYGVNDED----------FESDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGI 105
|
90 100
....*....|....*....|....*
gi 158451323 81 PGLCDIDTRALTYRLRE-GVTLGRI 104
Cdd:smart01097 106 PGISGIDTRALTRKLREkGAMKGVI 130
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
900-976 |
1.51e-34 |
|
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: 139.63 E-value: 1.51e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158451323 900 LGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMINYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIERPDGVILS 976
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQ 77
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
763-839 |
1.66e-32 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 120.56 E-value: 1.66e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158451323 763 ELREPTDKRMFVLAAALKQEYSVEKLYELTKIDIWFLEKFKNIIDYYKTLETlDNKPVTFDILKKAKKIGFSDKQIA 839
Cdd:pfam02787 2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKE-AGLDLDAELLREAKRLGFSDRQIA 77
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
154-306 |
4.23e-21 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 91.83 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 154 YNQIRCLIKRNAKVILVPWDH----KMDPSQYDGLFISNGPGDPvmckKVVDNLRAVIENKNNIKPIFGICLGHQLLSTA 229
Cdd:cd01743 12 YNLVQYLRELGAEVVVVRNDEitleELELLNPDAIVISPGPGHP----EDAGISLEIIRALAGKVPILGVCLGHQAIAEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 230 AGCNTYKTTYGNRGHNLPCTHNGTGRCFMTSQN------HGFAVDANSLPDEWKILftnenDKTNEGII----HKTDPYF 299
Cdd:cd01743 88 FGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLEVT-----ASTEDGVImalrHRDLPIY 162
|
....*..
gi 158451323 300 SVQFHPE 306
Cdd:cd01743 163 GVQFHPE 169
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
476-675 |
3.83e-20 |
|
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: 91.09 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 476 RKIFAEKinaiGEKVAPSAAVTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANNEEELRALAHQALSH------SDQL 549
Cdd:COG0439 59 REALAAA----GVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEakagspNGEV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 550 IIDKSLKGwKEVEYEVVrdAYDNCITVCNM---ENVDPLGIHTGEsivVAPSQtLSNRDYYMLRNTAIKVIRHFGII-GE 625
Cdd:COG0439 135 LVEEFLEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 158451323 626 CNIQYALNPNsEEFYIIEVNARLS--RSSALASKATGYPLAYVAAKLALGIP 675
Cdd:COG0439 208 FHTEFLLTPD-GEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
158-306 |
3.34e-15 |
|
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 74.69 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 158 RCLIKRNAKVilvPWDHkMDPSQYDGLFISNGPGDPvmckKVVDNLRAVIENKNNIKPIFGICLGHQLLSTAAGCntyKT 237
Cdd:COG0512 24 EVVVVRNDEI---TLEE-IEALAPDGIVLSPGPGTP----EEAGISLEVIRAFAGKIPILGVCLGHQAIGEAFGG---KV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 238 TYGNR---GHNLPCTHNGTGrCFmtsQN----------HGFAVDANSLPDEWKILFTNEnDKTNEGIIHKTDPYFSVQFH 304
Cdd:COG0512 93 VRAPEpmhGKTSPITHDGSG-LF---AGlpnpftatryHSLVVDRETLPDELEVTAWTE-DGEIMGIRHRELPIEGVQFH 167
|
..
gi 158451323 305 PE 306
Cdd:COG0512 168 PE 169
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
145-323 |
3.82e-15 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 75.75 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 145 ILAVDCGL---KYNQI--RCLIKRNAKVILV------PWDHKMDPSQYDGLFISNGPG----DPVMCKKVVDNLRAVIEN 209
Cdd:COG0518 2 ILILDHDPfggQYPGLiaRRLREAGIELDVLrvyageILPYDPDLEDPDGLILSGGPMsvydEDPWLEDEPALIREAFEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 210 KnniKPIFGICLGHQLLSTAAGCNTYKTTYGNRG-------------HNLPcthnGTGRCFMTsqnHGFAVDAnsLPDEW 276
Cdd:COG0518 82 G---KPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelteadplfAGLP----DEFTVWMS---HGDTVTE--LPEGA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 158451323 277 KILFTNENDKtNEGIIHKtDPYFSVQFHPEHTagPTDLECLFDIFID 323
Cdd:COG0518 150 EVLASSDNCP-NQAFRYG-RRVYGVQFHPEVT--HTMMEAWLEERAD 192
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
145-308 |
5.50e-14 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 71.19 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 145 ILAVDCGLKYNQircLIKRNAKVI-----LVPWD------HKMDPSqydGLFISNGP-----GDPVMCKKVVDNLRavie 208
Cdd:TIGR00888 1 ILVLDFGSQYTQ---LIARRLRELgvyseLVPNTtpleeiREKNPK---GIILSGGPssvyaENAPRADEKIFELG---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 209 nknniKPIFGICLGHQLLSTAAGCNTYKTTYGNRGH------NLPCTHNGTGRCFMTSQNHGFAVDAnsLPDEWKILFTN 282
Cdd:TIGR00888 71 -----VPVLGICYGMQLMAKQLGGEVGRAEKREYGKaeleilDEDDLFRGLPDESTVWMSHGDKVKE--LPEGFKVLATS 143
|
170 180
....*....|....*....|....*...
gi 158451323 283 ENDKtNEGIIHKTDPYFSVQFHPE--HT 308
Cdd:TIGR00888 144 DNCP-VAAMAHEEKPIYGVQFHPEvtHT 170
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
154-306 |
9.07e-14 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 70.54 E-value: 9.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 154 YN---QIRCL-----IKRNAKVILVPWDhKMDPsqyDGLFISNGPGDPvmckKVVDNLRAVIENKNNIKPIFGICLGHQL 225
Cdd:PRK05670 13 YNlvqYLGELgaevvVYRNDEITLEEIE-ALNP---DAIVLSPGPGTP----AEAGISLELIREFAGKVPILGVCLGHQA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 226 LSTAagcntykttYG---NRGHNL------PCTHNGTG------RCFMTSQNHGFAVDANSLPDEWKILFTNEnDKTNEG 290
Cdd:PRK05670 85 IGEA---------FGgkvVRAKEImhgktsPIEHDGSGifaglpNPFTVTRYHSLVVDRESLPDCLEVTAWTD-DGEIMG 154
|
170
....*....|....*.
gi 158451323 291 IIHKTDPYFSVQFHPE 306
Cdd:PRK05670 155 VRHKELPIYGVQFHPE 170
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
177-307 |
9.96e-14 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 70.74 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 177 DPSQYDGLFISNGP------GDPVMcKKVVDNLRAVIENKnniKPIFGICLGHQLLSTAAGCNTYKTTYG---------- 240
Cdd:cd01741 43 DLDDYDGLVILGGPmsvdedDYPWL-KKLKELIRQALAAG---KPVLGICLGHQLLARALGGKVGRNPKGweigwfpvtl 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158451323 241 -NRGHNLPCTHNGtGRCFMTSQNHGFAVDAnsLPDEWKILFTNENDKtNEGIIhKTDPYFSVQFHPEH 307
Cdd:cd01741 119 tEAGKADPLFAGL-PDEFPVFHWHGDTVVE--LPPGAVLLASSEACP-NQAFR-YGDRALGLQFHPEE 181
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
480-756 |
4.14e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 72.75 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 480 AEKINAIGEKVA---------------PSAAVTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANNEEELRAL------ 538
Cdd:PRK06111 107 ADIIAKMGSKIEarramqaagvpvvpgITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAfesnkk 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 539 -AHQALSHSdQLIIDKSLKGWKEVEYEVVRDAYDNCitvcnmenvdplgIHTGE---SI------VV--APSQTLSNRDY 606
Cdd:PRK06111 187 rAANFFGNG-EMYIEKYIEDPRHIEIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPFLDEETR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 607 YMLRNTAIKVIRHFGIIGECNIQYaLNPNSEEFYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPIIKNSVTGV 686
Cdd:PRK06111 253 KAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQDDIKRS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 687 TTA-----------CFEPSLDycvvKIPRWDLAK--FNRVSTKIGSSMK-------SVGEVMSIGRSFEEAFQKALRMVD 746
Cdd:PRK06111 332 GHAievriyaedpkTFFPSPG----KITDLTLPGgeGVRHDHAVENGVTvtpfydpMIAKLIAHGETREEAISRLHDALE 407
|
330
....*....|.
gi 158451323 747 E-NVNGFDPNI 756
Cdd:PRK06111 408 ElKVEGIKTNI 418
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
160-306 |
5.10e-13 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 68.66 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 160 LIKRNAKVilvpWDHKMDPSQYDGLFISNGPGDPVMCKKVVDnlraVIENKNNIKPIFGICLGHQLLSTAAGCNTYKTTY 239
Cdd:TIGR00566 27 VVKRNDSL----TLQEIEALLPLLIVISPGPCTPNEAGISLE----AIRHFAGKLPILGVCLGHQAMGQAFGGDVVRANT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158451323 240 GNRGHNLPCTHNGTGRC------FMTSQNHGFAVDANSLPDEWKILFTNENDKTNEGIIHKTDPYFSVQFHPE 306
Cdd:TIGR00566 99 VMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPE 171
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
356-679 |
1.20e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 70.30 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 356 KVLILGSGGlcigqagefdysGSQGVKAMQEE----KIQTVLINPNIATVQtskgLADKVYFLP-IT-PEYVEQVI---K 426
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSllkgRVIGADISELAPALY----FADKFYVVPkVTdPNYIDRLLdicK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 427 AERPTGVLLTFGgqtalncgVEL-----QKSRiFEKYNVSVLGTPiKSIVDT-EDRKIFAEKINAIGEKVAPSAAVTSVE 500
Cdd:PRK12767 67 KEKIDLLIPLID--------PELpllaqNRDR-FEEIGVKVLVSS-KEVIEIcNDKWLTYEFLKENGIPTPKSYLPESLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 501 EAL--VAAIQIGYPVMARSAFSLGGLGSGFANNEEELRalahQALSHSDQLIIDKSLKGwKEVEYEVVRDAYDNCITVCN 578
Cdd:PRK12767 137 DFKaaLAKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 579 MENVDPLGihtGESivvapSQTLSnRDYYMLRNTAIKVIRHFGIIGECNIQYALNPNseEFYIIEVNARLSrssalaska 658
Cdd:PRK12767 212 RKRIEVRA---GET-----SKGVT-VKDPELFKLAERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFG--------- 271
|
330 340 350
....*....|....*....|....*....|
gi 158451323 659 TGYPLAYVA---------AKLALGIPLPII 679
Cdd:PRK12767 272 GGYPLSYMAganepdwiiRNLLGGENEPII 301
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
160-306 |
6.57e-12 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 65.27 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 160 LIKRNAKVILVPWDhKMDPSQydgLFISNGPGDPvmcKKVVDNLRAVIENKNNIkPIFGICLGHQLLSTAAGCNTYKTTY 239
Cdd:PRK06774 27 MVKRNDELQLTDIE-QLAPSH---LVISPGPCTP---NEAGISLAVIRHFADKL-PILGVCLGHQALGQAFGARVVRARQ 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158451323 240 GNRGHNLPCTHNGTG------RCFMTSQNHGFAVDANSLPDEWKILFTNEND-KTNE--GIIHKTDPYFSVQFHPE 306
Cdd:PRK06774 99 VMHGKTSAICHSGQGvfrglnQPLTVTRYHSLVIAADSLPGCFELTAWSERGgEMDEimGIRHRTLPLEGVQFHPE 174
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
157-306 |
2.63e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 64.30 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 157 IRCLIKRNAKVILVpwDHKMDPSQYDGLFISNGPGDPVMCKKVVDNLRAVIENKnniKPIFGICLGHQLLSTAAGCNTYK 236
Cdd:PRK07765 25 VEAEVWRNDDPRLA--DEAAVAAQFDGVLLSPGPGTPERAGASIDMVRACAAAG---TPLLGVCLGHQAIGVAFGATVDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 237 TTYGNRGHNLPCTHNGTG------RCFMTSQNHGFAVDANSLPDEWKILftnenDKTNEGII----HKTDPYFSVQFHPE 306
Cdd:PRK07765 100 APELLHGKTSSVHHTGVGvlaglpDPFTATRYHSLTILPETLPAELEVT-----ARTDSGVImavrHRELPIHGVQFHPE 174
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
175-306 |
3.42e-11 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 67.05 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 175 KMDPSQydgLFISNGPGDPV---MCKKVVDNLRAVIenknnikPIFGICLGHQLLSTAAGCNTYKTTYGNRGHNLPCTHN 251
Cdd:PRK14607 42 ALNPSH---IVISPGPGRPEeagISVEVIRHFSGKV-------PILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHN 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158451323 252 GTGrCFMTSQN-------HGFAVDANSLPDEWKILFTNEnDKTNEGIIHKTDPYFSVQFHPE 306
Cdd:PRK14607 112 GKG-LFRGIPNptvatryHSLVVEEASLPECLEVTAKSD-DGEIMGIRHKEHPIFGVQFHPE 171
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
157-226 |
3.55e-11 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 61.08 E-value: 3.55e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158451323 157 IRCLIKRNAKVILVPWDHKM-----DPSQYDGLFISNGPGDPVMCKKVVDNLRAVIENKNNIKPIFGICLGHQLL 226
Cdd:cd01653 18 LDALREAGAEVDVVSPDGGPvesdvDLDDYDGLILPGGPGTPDDLARDEALLALLREAAAAGKPILGICLGAQLL 92
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
160-306 |
1.41e-10 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 61.47 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 160 LIKRNAKVILVPWDhKMDPSQydgLFISNGPGDPVMCKKVVDnlraVIENKNNIKPIFGICLGHQLLSTAAGCNTYKTTY 239
Cdd:PRK08007 27 LVKRNDALTLADID-ALKPQK---IVISPGPCTPDEAGISLD----VIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAK 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158451323 240 GNRGHNLPCTHNGTG------RCFMTSQNHGFAVDANSLPDEWKILFTNENDKTnEGIIHKTDPYFSVQFHPE 306
Cdd:PRK08007 99 VMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFEVTAWSETREI-MGIRHRQWDLEGVQFHPE 170
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
157-226 |
1.57e-10 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 58.75 E-value: 1.57e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158451323 157 IRCLIKRNAKVILVPWDHKM-----DPSQYDGLFISNGPGDPVMCKKVVDNLRAVIENKNNIKPIFGICLGHQLL 226
Cdd:cd03128 18 LDALREAGAEVDVVSPDGGPvesdvDLDDYDGLILPGGPGTPDDLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
145-308 |
2.54e-10 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 60.63 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 145 ILAVDCGLKYNQircLIKRNAKVI-----LVPWDHKMDP---SQYDGLFISNGP------GDPVMCKKVVDNlravienk 210
Cdd:cd01742 1 ILILDFGSQYTH---LIARRVRELgvyseILPNTTPLEEiklKNPKGIILSGGPssvyeeDAPRVDPEIFEL-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 211 nnIKPIFGICLGHQLLSTAAGCNTYKTTYGNRGH-NLPCTHN--------GTGRCFMtsqNHGFAVDAnsLPDEWKILFT 281
Cdd:cd01742 70 --GVPVLGICYGMQLIAKALGGKVERGDKREYGKaEIEIDDSsplfeglpDEQTVWM---SHGDEVVK--LPEGFKVIAS 142
|
170 180
....*....|....*....|....*....
gi 158451323 282 NENDKtNEGIIHKTDPYFSVQFHPE--HT 308
Cdd:cd01742 143 SDNCP-VAAIANEEKKIYGVQFHPEvtHT 170
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
454-677 |
4.82e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 62.84 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 454 IFEKYNVSVLGTPIKSIVDTEDRKIFAEKINAIGEKVAPSA--AVTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANN 531
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 532 EEELR----ALAHQALSH--SDQLIIDKSLKGWKEVEYEVVRDAYDNCITV----CNMENvdplgiHTGESIVVAPSQTL 601
Cdd:PRK08462 176 ESDLEnlylAAESEALSAfgDGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158451323 602 SNRDYYMLRNTAIKVIRHFGIIGECNIQYALNPNsEEFYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 677
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSN-LDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELP 324
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
165-306 |
7.92e-10 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 63.01 E-value: 7.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 165 AKVILVPWDH---KMDPSQYDGLFISNGPGDPV--MCKKVVDNLRAvienkNNIkPIFGICLGHQLLSTAAGcntyktty 239
Cdd:PRK13566 551 AEVTTVRYGFaeeMLDRVNPDLVVLSPGPGRPSdfDCKATIDAALA-----RNL-PIFGVCLGLQAIVEAFG-------- 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 240 GNRGH-NLPCtH---------------NGTGRCFMTSQNHGFAVDANSLPDEWKILFTNEnDKTNEGIIHKTDPYFSVQF 303
Cdd:PRK13566 617 GELGQlAYPM-HgkpsrirvrgpgrlfSGLPEEFTVGRYHSLFADPETLPDELLVTAETE-DGVIMAIEHKTLPVAAVQF 694
|
...
gi 158451323 304 HPE 306
Cdd:PRK13566 695 HPE 697
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
179-328 |
1.46e-09 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 58.32 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 179 SQYDGLFISNGP-----GDpvmCKKVVDNLravienknNIkPIFGICLGHQLLSTAAGCNTYKTTYGNRG--------HN 245
Cdd:PRK00758 40 AFEDGLILSGGPdieraGN---CPEYLKEL--------DV-PILGICLGHQLIAKAFGGEVGRGEYGEYAlveveildED 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 246 LPCthNGTGRCFMTSQNHGFAVdaNSLPDEWKILFTNENDKTnEGIIHKTDPYFSVQFHPE--HTAGPTDlecLFDIFID 323
Cdd:PRK00758 108 DIL--KGLPPEIRVWASHADEV--KELPDGFEILARSDICEV-EAMKHKEKPIYGVQFHPEvaHTEYGEE---IFKNFLE 179
|
....*
gi 158451323 324 VVKSY 328
Cdd:PRK00758 180 ICGKY 184
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
480-678 |
3.08e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 60.50 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 480 AEKINAIGEKVAPSAA---------------VTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANNEEELRALAHQALS 544
Cdd:PRK07178 106 AEVIRRMGDKTEARRAmikagvpvtpgsegnLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVIS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 545 H------SDQLIIDKSLKGWKEVEYEVVRDAYDNCITV----CNMENvdplgiHTGESIVVAPSQTLSNRDYYMLRNTAI 614
Cdd:PRK07178 186 EatkafgSAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAV 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158451323 615 KVIRHFGIIGECNIQYALNPNSeEFYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPI 678
Cdd:PRK07178 260 RAAKAVGYENAGTVEFLLDADG-EVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSY 322
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
495-686 |
4.28e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 59.56 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 495 AVTSVEEALVAAIQIGYPVM--------ARSAFSLGGLGSGFANNEEELRALAHQALSHSDQLIIDkslkgwkevEYEVV 566
Cdd:COG3919 137 VLDSADDLDALAEDLGFPVVvkpadsvgYDELSFPGKKKVFYVDDREELLALLRRIAAAGYELIVQ---------EYIPG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 567 RDAYDNCITVCNMENVDPLGIHTGESIVVAPSQ--------TLSNRDyymLRNTAIKVIRHFGIIGECNIQYALNPNSEE 638
Cdd:COG3919 208 DDGEMRGLTAYVDRDGEVVATFTGRKLRHYPPAggnsaareSVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGE 284
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 158451323 639 FYIIEVNARLSRSSALASKAtGYPLAYVAAKLALGIPLPIIKNSVTGV 686
Cdd:COG3919 285 YKLIEINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREGV 331
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
176-306 |
7.78e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 56.42 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 176 MDPSQydgLFISNGPGDPvmcKKVVDNLRAvIENKNNIKPIFGICLGHQLLSTAAGCNTYKTTYGNRGHNLPCTHNGTGr 255
Cdd:PRK08857 42 LNPTH---LVISPGPCTP---NEAGISLQA-IEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRS- 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158451323 256 CFMTSQN-------HGFAVDANSLPDEWKILFTNENDKTN----EGIIHKTDPYFSVQFHPE 306
Cdd:PRK08857 114 VFKGLNNpltvtryHSLVVKNDTLPECFELTAWTELEDGSmdeiMGFQHKTLPIEAVQFHPE 175
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
160-306 |
1.10e-08 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 55.97 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 160 LIKRNAKVILVPWDhKMDPsqyDGLFISNGPGDPvmcKKVVDNLRAVIENKNNIkPIFGICLGHQLLSTAAGCNTYKTTY 239
Cdd:PRK07649 27 VVKRNDEVTISDIE-NMKP---DFLMISPGPCSP---NEAGISMEVIRYFAGKI-PIFGVCLGHQSIAQVFGGEVVRAER 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158451323 240 GNRGHNLPCTHNGTG------RCFMTSQNHGFAVDANSLPDEWKIlftneNDKTNEG----IIHKTDPYFSVQFHPE 306
Cdd:PRK07649 99 LMHGKTSLMHHDGKTifsdipNPFTATRYHSLIVKKETLPDCLEV-----TSWTEEGeimaIRHKTLPIEGVQFHPE 170
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
495-677 |
1.67e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 58.23 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 495 AVTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANNEEELRA---LAH---QALSHSDQLIIDKSLKGWKEVEYEVVRD 568
Cdd:PRK12833 140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpLAQreaQAAFGDGGVYLERFIARARHIEVQILGD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 569 AYDnciTVCNMENVDPLGIHTGESIVVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALNPNSEEFYIIEVNARL 648
Cdd:PRK12833 220 GER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRI 296
|
170 180
....*....|....*....|....*....
gi 158451323 649 SRSSALASKATGYPLAYVAAKLALGIPLP 677
Cdd:PRK12833 297 QVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
480-648 |
3.20e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 57.12 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 480 AEKINAIGEKVAPSAA---------------VTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANNEEELRALAHQALS 544
Cdd:PRK08591 107 AETIRLMGDKVTAKATmkkagvpvvpgsdgpVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 545 HS------DQLIIDKSLKGWKEVEYEVVRDAYDNcitvcnmenvdplGIHTGE---SI------VV--APSQTLSNRDYY 607
Cdd:PRK08591 187 EAkaafgnPGVYMEKYLENPRHIEIQVLADGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRR 253
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 158451323 608 MLRNTAIKVIRHFGIIGECNIQYALNPNSeEFYIIEVNARL 648
Cdd:PRK08591 254 KIGEAAVKAAKAIGYRGAGTIEFLYEKNG-EFYFIEMNTRI 293
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
154-306 |
3.31e-08 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 54.74 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 154 YNQIRCLIKRNAKVILVPWDhKMDPSQYD-----GLFISNGPGDPV---MCKKVVDNLRAVIenknnikPIFGICLGHQL 225
Cdd:CHL00101 13 YNLVQSLGELNSDVLVCRND-EIDLSKIKnlnirHIIISPGPGHPRdsgISLDVISSYAPYI-------PILGVCLGHQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 226 LSTAAGCNTYKTTYGNRGHNLPCTHNGTG------RCFMTSQNHGFAVDANSLPDEWKILftnenDKTNEGII----HKT 295
Cdd:CHL00101 85 IGYLFGGKIIKAPKPMHGKTSKIYHNHDDlfqglpNPFTATRYHSLIIDPLNLPSPLEIT-----AWTEDGLImacrHKK 159
|
170
....*....|..
gi 158451323 296 DPY-FSVQFHPE 306
Cdd:CHL00101 160 YKMlRGIQFHPE 171
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
180-306 |
4.46e-08 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 54.36 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 180 QYDGLFISNGPGDPvmckKVVDNLRAVIENKNNIKPIFGICLGHQLLstaagCNTYkttyGNRGHNLPCTHNGTGRCFMT 259
Cdd:PRK06895 43 NFSHILISPGPDVP----RAYPQLFAMLERYHQHKSILGVCLGHQTL-----CEFF----GGELYNLNNVRHGQQRPLKV 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158451323 260 SQN----------------HGFAVDANSLPDEWKIlfTNENDktnEGII----HKTDPYFSVQFHPE 306
Cdd:PRK06895 110 RSNsplfdglpeefniglyHSWAVSEENFPTPLEI--TAVCD---ENVVmamqHKTLPIYGVQFHPE 171
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
203-306 |
1.91e-07 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 53.03 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 203 LRAVIENKnniKPIFGICLGHQLLSTAAGCNTY---KTTYGNRGHNLPC-------THN---GTGRCF--MTSQN----- 262
Cdd:pfam07722 98 IRAALARG---KPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapSHAvnvEPGSLLasLLGSEefrvn 174
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 158451323 263 --HGFAVDAnsLPDEWKILFTNEnDKTNEGIIHKTDPYF--SVQFHPE 306
Cdd:pfam07722 175 slHHQAIDR--LAPGLRVEAVAP-DGTIEAIESPNAKGFalGVQWHPE 219
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
203-322 |
2.75e-07 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 51.81 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 203 LRAVIENKnniKPIFGICLGHQLLSTAAGcntykttygnrghnlpcthnGT-GRCFMTSQNHGFAVDAnsLPDEWKILFT 281
Cdd:cd01745 93 LRAALERG---KPILGICRGMQLLNVALG--------------------GTlYQDIRVNSLHHQAIKR--LADGLRVEAR 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 158451323 282 nENDKTNEGIIHKTDPY-FSVQFHPEHTAgPTDLEC--LFDIFI 322
Cdd:cd01745 148 -APDGVIEAIESPDRPFvLGVQWHPEWLA-DTDPDSlkLFEAFV 189
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
495-756 |
3.64e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 53.95 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 495 AVTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANNEEELRALAHQALSHS------DQLIIDKSLKGWKEVEYEVVRD 568
Cdd:PRK05586 137 EIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAkaafgdDSMYIEKFIENPKHIEFQILGD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 569 AYDNCITV----CNMENvdplgiHTGESIVVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALNPNsEEFYIIEV 644
Cdd:PRK05586 217 NYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKD-GNFYFMEM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 645 NARLSRSSALASKATGYPLAYVAAKLALGIPLPIIKN--SVTGVTTAC----------FEPS----------------LD 696
Cdd:PRK05586 290 NTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQEdiKINGHSIECrinaedpkngFMPCpgkieelyipgglgvrVD 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158451323 697 ---YCVVKIPR-WDlakfnrvstkigsSMksVGEVMSIGRSFEEAFQKALRMVDE-NVNGFDPNI 756
Cdd:PRK05586 370 savYSGYTIPPyYD-------------SM--IGKLIVYGKDREEAIQKMKRALGEfIIEGVNTNI 419
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
456-580 |
5.17e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 53.45 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 456 EKYNVSVLGTPIKSIvdtedrKIFAEKINA------IGEKVAP--SAAVTSVEEALVAAIQIGYPVMARSAFSLGGLGSG 527
Cdd:PRK08654 96 EKAGIVFIGPSSDVI------EAMGSKINAkklmkkAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMR 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 528 FANNEEEL-------RALAHQALSHSdQLIIDKSLKGWKEVEYEVVRDAYDNCITVCNME 580
Cdd:PRK08654 170 VVYSEEELedaiestQSIAQSAFGDS-TVFIEKYLEKPRHIEIQILADKHGNVIHLGDRE 228
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
495-648 |
5.35e-07 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 53.10 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 495 AVTSVEEALVAAIQIGYPVMARSAFslGGLGSGF--ANNEEELRALAHQALS------HSDQLIIDKSLKGWKEVEYEVV 566
Cdd:COG4770 137 PVQDAEEALAIAEEIGYPVLIKASA--GGGGKGMrvVRSEEELEEAFESARReakaafGDDRVYLEKYIERPRHIEVQVL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 567 RDAYDNCitvcnmenvdplgIHTGE---SI------VV--APSQTLSNRdyymLR----NTAIKVIRHFGIIGECNIQYA 631
Cdd:COG4770 215 ADKHGNV-------------VHLGErdcSIqrrhqkVIeeAPSPALTEE----LRermgEAAVRAAKAVGYVGAGTVEFL 277
|
170
....*....|....*..
gi 158451323 632 LNPNsEEFYIIEVNARL 648
Cdd:COG4770 278 VDAD-GNFYFLEMNTRL 293
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
480-648 |
9.92e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 52.83 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 480 AEKINAIGEKVA-------------PS--AAVTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANNEEELRALAHQALS 544
Cdd:PRK12999 111 AEVLRLLGDKVAarnaaikagvpviPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 545 H------SDQLIIDKSLKGWKEVEYEVVRDAYDNCitvcnmenvdplgIHTGE---SI------VV--APSQTLSN--RD 605
Cdd:PRK12999 191 EakaafgNDEVYLEKYVENPRHIEVQILGDKHGNV-------------VHLYErdcSVqrrhqkVVeiAPAPGLSEelRE 257
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 158451323 606 yyMLRNTAIKVIRHFGIIGECNIQYALNPNSeEFYIIEVNARL 648
Cdd:PRK12999 258 --RICEAAVKLARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
181-328 |
1.99e-06 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 51.77 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 181 YDGLFISNGPGDPVMCKKVVDNLRAVIENKNniKPIFGICLGHQLLSTAAGCNTYKTTYGNRGHNLPCTHNG-------- 252
Cdd:PLN02889 132 FDNIVISPGPGSPTCPADIGICLRLLLECRD--IPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGcrlfddip 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 253 TGR--CFMTSQNHGFAVDANSLPDE--------------------------------------------------WKILF 280
Cdd:PLN02889 210 SGRnsGFKVVRYHSLVIDAESLPKElvpiawtsssdtlsflesqksglvpdayesqigqsgssdpfssklkngtsWPSSH 289
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 158451323 281 TN--ENDKTNEGIIHKTDPYFSVQFHPEhTAGPTDLECLFDIFIDVVKSY 328
Cdd:PLN02889 290 SErmQNGKILMGIMHSTRPHYGLQFHPE-SIATCYGRQIFKNFREITQDY 338
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
175-306 |
4.28e-06 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 49.03 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 175 KMDPSqydGLFISNGPGDPVmckkvvDN---LRAVIENKNNIkPIFGICLGHQLLSTAAGCNTYKTTYG-NRGHNLPCTH 250
Cdd:PLN02335 60 RKNPR---GVLISPGPGTPQ------DSgisLQTVLELGPLV-PLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHY 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158451323 251 ---------NGTGRCFMTSQNHGFAVDANSLP-DEWKILFTNEnDKTNEGIIHKTDPYFS-VQFHPE 306
Cdd:PLN02335 130 dekgeeglfSGLPNPFTAGRYHSLVIEKDTFPsDELEVTAWTE-DGLIMAARHRKYKHIQgVQFHPE 195
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
495-647 |
5.13e-06 |
|
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: 50.46 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 495 AVTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANNEEELRALAHQALSH------SDQLIIDKSLKGWKEVEYEVVRD 568
Cdd:COG1038 140 PVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREakaafgDDEVFLEKYIERPKHIEVQILGD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 569 AYDNCitvcnmenvdplgIHTGE---SI------VV--APSQTLSNRdyymLR----NTAIKVIRHFGIIGECNIQYALN 633
Cdd:COG1038 220 KHGNI-------------VHLFErdcSVqrrhqkVVeiAPAPNLDEE----LReaicEAAVKLAKAVGYVNAGTVEFLVD 282
|
170
....*....|....
gi 158451323 634 PNsEEFYIIEVNAR 647
Cdd:COG1038 283 DD-GNFYFIEVNPR 295
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
498-683 |
6.76e-06 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 49.81 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 498 SVEEALVAAIQIGYPVMARSAFSLGGLGSGFANNEEEL----RALAHQALSH--SDQLIIDKSLKGWKEVEYEVVRDAYD 571
Cdd:PRK08463 140 SMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLenafESCKREALAYfnNDEVFMEKYVVNPRHIEFQILGDNYG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 572 NCITVCnmENVDPLGIHTGESIVVAPSQTLSNRDYYMLRNTAIKVIRHFGIIGECNIQYALNPNSeEFYIIEVNARLSRS 651
Cdd:PRK08463 220 NIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYN-RFYFMEMNTRIQVE 296
|
170 180 190
....*....|....*....|....*....|..
gi 158451323 652 SALASKATGYPLAYVAAKLALGIPLPIIKNSV 683
Cdd:PRK08463 297 HGVTEEITGIDLIVRQIRIAAGEILDLEQSDI 328
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
165-309 |
1.14e-04 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153218 [Multi-domain] Cd Length: 273 Bit Score: 45.00 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 165 AKVILVPWDHkmDPSQYDGLFIS-NG---PG-----DPVMCKKVVDNL--RAVIENKNNIK-PIFGICLGHQLLST-AAG 231
Cdd:cd01747 34 ARVVPIWINE--SEEYYDKLFKSiNGilfPGgavdiDTSGYARTAKIIynLALERNDAGDYfPVWGTCLGFELLTYlTSG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 232 CNTYKTTYGNRGHNLPC---THNGTGRCF---------------MTSQNHGFAVDANS------LPDEWKILFTNENDKT 287
Cdd:cd01747 112 ETLLLEATEATNSALPLnftEDALQSRLFkrfppdllkslatepLTMNNHRYGISPENftenglLSDFFNVLTTNDDWNG 191
|
170 180
....*....|....*....|....*
gi 158451323 288 NEGII---HKTDPYFSVQFHPEHTA 309
Cdd:cd01747 192 VEFIStveAYKYPIYGVQWHPEKNA 216
|
|
| GATase1_PfpI_1 |
cd03169 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
170-231 |
2.45e-04 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.
Pssm-ID: 153243 [Multi-domain] Cd Length: 180 Bit Score: 43.02 E-value: 2.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158451323 170 VPWDhKMDPSQYDGLFISNG--PGDPVMCKKVVDNLRAVIENKnniKPIFGICLGHQLLsTAAG 231
Cdd:cd03169 67 ADFD-EVDPDDYDALVIPGGraPEYLRLDEKVLAIVRHFAEAN---KPVAAICHGPQIL-AAAG 125
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
613-687 |
5.75e-04 |
|
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.
Pssm-ID: 434824 [Multi-domain] Cd Length: 131 Bit Score: 41.06 E-value: 5.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158451323 613 AIKVIRHFGIIGECNIQYALnpNSEEFYIIEVNARLsrSSALA-SKATGYPLAYVAAKLALGIPLPIIKNSVTGVT 687
Cdd:pfam15632 53 ARRLAEAFGLDGLFNVQFRY--DGDGPKLLEINPRM--SGGIGySCLAGVNLPYLALKLLLGLETPDPVEPRLGLR 124
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
452-646 |
9.33e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 42.35 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 452 SRIFEKYNVSVLGTPIKSIVDTEDRKIFAEkinAIGEKVAPSAAVTSVEEALVAAIQIGYPVMARSAFSLGGLGSGFANN 531
Cdd:PRK14569 75 SALLEMLEIKHTSSSMKSSVITMDKMISKE---ILMHHRMPTPMAKFLTDKLVAEDEISFPVAVKPSSGGSSIATFKVKS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 532 EEELRAlAHQALSHSDQLIIDKSLKGwKEVEYEVVR-DAYDNCITVCNMENVDPLGIHTGESIVVAPSqTLSNRDYYMLR 610
Cdd:PRK14569 152 IQELKH-AYEEASKYGEVMIEQWVTG-KEITVAIVNdEVYSSVWIEPQNEFYDYESKYSGKSIYHSPS-GLCEQKELEVR 228
|
170 180 190
....*....|....*....|....*....|....*.
gi 158451323 611 NTAIKVIRHFGIIGECNIQYALNpNSEEFYIIEVNA 646
Cdd:PRK14569 229 QLAKKAYDLLGCSGHARVDFIYD-DRGNFYIMEINS 263
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
141-226 |
5.23e-03 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 39.40 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 141 GNLTilAVDCGLKYNQIRCLIKRNAKVILvpwdhkmdpsQYDGLFIsngPG----DPVMckkvvDNLR------AVIENK 210
Cdd:cd01748 9 GNLR--SVANALERLGAEVIITSDPEEIL----------SADKLIL---PGvgafGDAM-----ANLRerglieALKEAI 68
|
90
....*....|....*.
gi 158451323 211 NNIKPIFGICLGHQLL 226
Cdd:cd01748 69 ASGKPFLGICLGMQLL 84
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
177-309 |
6.15e-03 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 39.56 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 177 DPSQYDGLFISngpGDPVMckkVVDN----------LRAVIENKnniKPIFGICLGHQLLSTAAGcntykttyGNRGHN- 245
Cdd:PRK09065 51 APDDFAGVIIT---GSWAM---VTDRldwsertadwLRQAAAAG---MPLLGICYGHQLLAHALG--------GEVGYNp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 246 ------------LPCTHN-----GTGRCFMTSQNHGFAVDAnsLPDEWKILFTNENDKTNegIIHKTDPYFSVQFHPEHT 308
Cdd:PRK09065 114 agresgtvtvelHPAAADdplfaGLPAQFPAHLTHLQSVLR--LPPGAVVLARSAQDPHQ--AFRYGPHAWGVQFHPEFT 189
|
.
gi 158451323 309 A 309
Cdd:PRK09065 190 A 190
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
141-226 |
6.60e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 38.96 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158451323 141 GNLTilAVDCGLKYNQIRCLIKRNAKVILvpwdhkmdpsQYDGLFIsngPG----DPVMCK----KVVDNLRAVIENKnn 212
Cdd:PRK13141 10 GNLR--SVEKALERLGAEAVITSDPEEIL----------AADGVIL---PGvgafPDAMANlrerGLDEVIKEAVASG-- 72
|
90
....*....|....
gi 158451323 213 iKPIFGICLGHQLL 226
Cdd:PRK13141 73 -KPLLGICLGMQLL 85
|
|
| |
