|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
129-675 |
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: 865.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 129 PKPIEVSKVLILGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQTNEvgtKQADSVYFLPITPDFVTEVI 208
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDP---EMADKVYIEPLTPEAVEKII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 209 KAERPDGILLSMGGQTALNCGVELFKRGTLKEYGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVEDAVKA 288
Cdd:TIGR01369 78 EKERPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 289 AEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEAATVAFSLT--NQILVEQSLIGWKEVEYEVVRDAADNCVTVCNMENMD 366
Cdd:TIGR01369 158 AKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 367 PMGIHTGDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHPSSLEYCIIEVNARLSRSSALASKATGYPL 446
Cdd:TIGR01369 238 PMGVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 447 AFIAAKLALGISLPDIKNMVSGKTTACFEPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTFEESFQKALR 526
Cdd:TIGR01369 318 AKVAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 527 MCHPSIDGFmsELPMKKPWqDDFNYQKELSVPSSTRTYAVAKALQSGVSVDDIYQLTAIDKWFLYRMQGIVQVENMLKKH 606
Cdd:TIGR01369 398 SLEIGATGF--DLPDREVE-PDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEV 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 607 TRANISEDLLIKAKQDGFSDRQIGKLMQSSEAD-RNLRLKKNIKPWVKQIDTLAAEYPAITNYLYCTYNG 675
Cdd:TIGR01369 475 KLTDLDPELLRRAKKLGFSDAQIARLIGVTEAEvRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEG 544
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
129-674 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 825.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 129 PKPIEVSKVLILGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQTNevgTKQADSVYFLPITPDFVTEVI 208
Cdd:PRK05294 2 PKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTD---PEMADATYIEPITPEFVEKII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 209 KAERPDGILLSMGGQTALNCGVELFKRGTLKEYGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVEDAVKA 288
Cdd:PRK05294 79 EKERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 289 AEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEAATVAFSL--TNQILVEQSLIGWKEVEYEVVRDAADNCVTVCNMENMD 366
Cdd:PRK05294 159 AEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENID 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 367 PMGIHTGDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGII-GECNIQYALHPSSLEYCIIEVNARLSRSSALASKATGYP 445
Cdd:PRK05294 239 PMGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 446 LAFIAAKLALGISLPDIKNMVSGKTTACFEPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTFEESFQKAL 525
Cdd:PRK05294 319 IAKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 526 RMCHPSIDGFmsELPMKKPWQDDfNYQKELSVPSSTRTYAVAKALQSGVSVDDIYQLTAIDKWFLYRMQGIVQVENMLKK 605
Cdd:PRK05294 399 RSLEIGVTGL--DEDLFEEESLE-ELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKE 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 606 HtRANISEDLLIKAKQDGFSDRQIGKLMQSSEAD-RNLRLKKNIKPWVKQIDTLAAEYPAITNYLYCTYN 674
Cdd:PRK05294 476 N-GLPLDAELLREAKRLGFSDARIAKLLGVTEDEvRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYE 544
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
140-673 |
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: 619.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 140 LGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQT-NEVgtkqADSVYFLPITPDFVTEVIKAERPDGILL 218
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTdYDT----ADRLYFEPLTVEDVLDIIEKEKPDGVIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 219 SMGGQTALNCGVELFKRGTLKeyGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVEDAVKAAEKIGYPVMI 298
Cdd:COG0458 77 QFGGQTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 299 RSAYALGGLGSGLCVNKEKLVEAATVAF--SLTNQILVEQSLIGWKEVEYEVVRDAADNCVTVCNMENMDPMGIHTGDSI 376
Cdd:COG0458 155 RPSYVLGGRGMGIVYNEEELEEYLERALkvSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 377 VVAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHpsSLEYCIIEVNARLSRSSALASKATGYPLAFIAAKLALG 456
Cdd:COG0458 235 CVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 457 ISLPDIKNmvsgktTACFEPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIDG-- 534
Cdd:COG0458 313 YTLDELGN------DTGFEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtv 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 535 FMSELpmkkpwQDDFNYQKELSVPSSTRTYAVAKALQSGVSVDDIYQLTAIDKWFLYRMQGIVQVENMLKKHTRANIsed 614
Cdd:COG0458 387 LLSLV------ADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVIN--- 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 615 LLIKAKQDGFSDRQIGKLMQSSEAD-RNLRLKKNIKPWVKQIDTLAAEYPAITNYLYCTY 673
Cdd:COG0458 458 TLLGAKSLGDSDGIIRRALAAKVPYvTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTY 517
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
258-460 |
6.46e-103 |
|
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: 312.32 E-value: 6.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 258 DRQLFSDKLLEINENIAPSIA--VESVEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEAATVAFSLT------ 329
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 330 NQILVEQSLIGWKEVEYEVVRDAADNCVTVCNMENMDPMgiHTGDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGIIGEC 409
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 300720954 410 NIQYALHPSSLEYCIIEVNARLSRSSALASKATGYPLAFIAAKLALGISLP 460
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
1-107 |
3.77e-68 |
|
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: 220.45 E-value: 3.77e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLNMMSGQAFITAQNHGYGIDTSSLPLGWKPLFVNVNDGTNEGIMHET 80
Cdd:cd01744 72 IFGICLGHQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKD 151
|
90 100
....*....|....*....|....*..
gi 300720954 81 KPIFTAQFHPEANGGPTDTEFLFDAFI 107
Cdd:cd01744 152 LPVFSVQFHPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
553-673 |
4.18e-54 |
|
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: 181.11 E-value: 4.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 553 KELSVPSSTRTYAVAKALQSGVSVDDIYQLTAIDKWFLYRMQGIVQVENMLKKHTRANISEDLLIKAKQDGFSDRQIGKL 632
Cdd:smart01096 3 EELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAKL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 300720954 633 MQSSEAD-RNLRLKKNIKPWVKQIDTLAAEYPAITNYLYCTY 673
Cdd:smart01096 83 LGVTEAEvRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-112 |
8.49e-54 |
|
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: 188.60 E-value: 8.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLNMMSGQAFITAQNHGYGIDTSSLPLG-WKPLFVNVNDGTNEGIMHE 79
Cdd:TIGR01368 245 IFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGdLEVTHVNLNDGTVEGIRHK 324
|
90 100 110
....*....|....*....|....*....|...
gi 300720954 80 TKPIFTAQFHPEANGGPTDTEFLFDAFIDLIKK 112
Cdd:TIGR01368 325 DLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-110 |
2.89e-52 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 184.51 E-value: 2.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLNMMSGQAFITAQNHGYGIDTSSLPLGWKPLFVNVNDGTNEGIMHET 80
Cdd:PRK12564 251 IFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKD 330
|
90 100 110
....*....|....*....|....*....|
gi 300720954 81 KPIFTAQFHPEANGGPTDTEFLFDAFIDLI 110
Cdd:PRK12564 331 LPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-111 |
6.94e-50 |
|
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: 177.91 E-value: 6.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLNMMSGQAFITAQNHGYGIDTSSLP-LGWKPLFVNVNDGTNEGIMHE 79
Cdd:COG0505 250 IFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPaTDLEVTHVNLNDGTVEGLRHK 329
|
90 100 110
....*....|....*....|....*....|..
gi 300720954 80 TKPIFTAQFHPEANGGPTDTEFLFDAFIDLIK 111
Cdd:COG0505 330 DLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
1-109 |
6.87e-34 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 127.74 E-value: 6.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPM-ANRGQNQPVLNMMS------GQAFITAQNHGYGIDTSSLPLGWKPLFVNVNDGTN 73
Cdd:pfam00117 73 ILGICLGHQLLALAFGGKVVKAKKfGHHGKNSPVGDDGCglfyglPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTI 152
|
90 100 110
....*....|....*....|....*....|....*.
gi 300720954 74 EGIMHETKPIFTAQFHPEANGGPTDTEFLFDAFIDL 109
Cdd:pfam00117 153 MGIRHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
129-675 |
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: 865.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 129 PKPIEVSKVLILGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQTNEvgtKQADSVYFLPITPDFVTEVI 208
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDP---EMADKVYIEPLTPEAVEKII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 209 KAERPDGILLSMGGQTALNCGVELFKRGTLKEYGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVEDAVKA 288
Cdd:TIGR01369 78 EKERPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 289 AEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEAATVAFSLT--NQILVEQSLIGWKEVEYEVVRDAADNCVTVCNMENMD 366
Cdd:TIGR01369 158 AKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 367 PMGIHTGDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHPSSLEYCIIEVNARLSRSSALASKATGYPL 446
Cdd:TIGR01369 238 PMGVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 447 AFIAAKLALGISLPDIKNMVSGKTTACFEPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTFEESFQKALR 526
Cdd:TIGR01369 318 AKVAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 527 MCHPSIDGFmsELPMKKPWqDDFNYQKELSVPSSTRTYAVAKALQSGVSVDDIYQLTAIDKWFLYRMQGIVQVENMLKKH 606
Cdd:TIGR01369 398 SLEIGATGF--DLPDREVE-PDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEV 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 607 TRANISEDLLIKAKQDGFSDRQIGKLMQSSEAD-RNLRLKKNIKPWVKQIDTLAAEYPAITNYLYCTYNG 675
Cdd:TIGR01369 475 KLTDLDPELLRRAKKLGFSDAQIARLIGVTEAEvRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEG 544
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
129-674 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 825.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 129 PKPIEVSKVLILGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQTNevgTKQADSVYFLPITPDFVTEVI 208
Cdd:PRK05294 2 PKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTD---PEMADATYIEPITPEFVEKII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 209 KAERPDGILLSMGGQTALNCGVELFKRGTLKEYGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVEDAVKA 288
Cdd:PRK05294 79 EKERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 289 AEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEAATVAFSL--TNQILVEQSLIGWKEVEYEVVRDAADNCVTVCNMENMD 366
Cdd:PRK05294 159 AEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENID 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 367 PMGIHTGDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGII-GECNIQYALHPSSLEYCIIEVNARLSRSSALASKATGYP 445
Cdd:PRK05294 239 PMGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 446 LAFIAAKLALGISLPDIKNMVSGKTTACFEPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTFEESFQKAL 525
Cdd:PRK05294 319 IAKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 526 RMCHPSIDGFmsELPMKKPWQDDfNYQKELSVPSSTRTYAVAKALQSGVSVDDIYQLTAIDKWFLYRMQGIVQVENMLKK 605
Cdd:PRK05294 399 RSLEIGVTGL--DEDLFEEESLE-ELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKE 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 606 HtRANISEDLLIKAKQDGFSDRQIGKLMQSSEAD-RNLRLKKNIKPWVKQIDTLAAEYPAITNYLYCTYN 674
Cdd:PRK05294 476 N-GLPLDAELLREAKRLGFSDARIAKLLGVTEDEvRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYE 544
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
129-675 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 651.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 129 PKPIEVSKVLILGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQTNEvgtKQADSVYFLPITPDFVTEVI 208
Cdd:PRK12815 2 PKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDP---APADTVYFEPLTVEFVKRII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 209 KAERPDGILLSMGGQTALNCGVELFKRGTLKEYGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVEDAVKA 288
Cdd:PRK12815 79 AREKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 289 AEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEAAT--VAFSLTNQILVEQSLIGWKEVEYEVVRDAADNCVTVCNMENMD 366
Cdd:PRK12815 159 AEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKqgLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENID 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 367 PMGIHTGDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHPSSLEYCIIEVNARLSRSSALASKATGYPL 446
Cdd:PRK12815 239 PVGIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 447 AFIAAKLALGISLPDIKNMVSGKTTACFEPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTFEESFQKALR 526
Cdd:PRK12815 319 AKIAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 527 mchpSIDGF---------MSELPMKKPWQDdfnyqkeLSVPSSTRTYAVAKALQSGVSVDDIYQLTAIDKWFLYRMQGIV 597
Cdd:PRK12815 399 ----SLEIKrnglslpieLSGKSDEELLQD-------LRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIV 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300720954 598 QVENMLKKHTRaNISEDLLIKAKQDGFSDRQIGKLMQSSEAD-RNLRLKKNIKPWVKQIDTLAAEYPAITNYLYCTYNG 675
Cdd:PRK12815 468 ALEKKLAEDGL-DLSADLLRKVKEKGFSDALLAELTGVTEEEvRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFG 545
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
140-673 |
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: 619.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 140 LGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQT-NEVgtkqADSVYFLPITPDFVTEVIKAERPDGILL 218
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTdYDT----ADRLYFEPLTVEDVLDIIEKEKPDGVIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 219 SMGGQTALNCGVELFKRGTLKeyGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVEDAVKAAEKIGYPVMI 298
Cdd:COG0458 77 QFGGQTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 299 RSAYALGGLGSGLCVNKEKLVEAATVAF--SLTNQILVEQSLIGWKEVEYEVVRDAADNCVTVCNMENMDPMGIHTGDSI 376
Cdd:COG0458 155 RPSYVLGGRGMGIVYNEEELEEYLERALkvSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 377 VVAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHpsSLEYCIIEVNARLSRSSALASKATGYPLAFIAAKLALG 456
Cdd:COG0458 235 CVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 457 ISLPDIKNmvsgktTACFEPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIDG-- 534
Cdd:COG0458 313 YTLDELGN------DTGFEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtv 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 535 FMSELpmkkpwQDDFNYQKELSVPSSTRTYAVAKALQSGVSVDDIYQLTAIDKWFLYRMQGIVQVENMLKKHTRANIsed 614
Cdd:COG0458 387 LLSLV------ADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVIN--- 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 615 LLIKAKQDGFSDRQIGKLMQSSEAD-RNLRLKKNIKPWVKQIDTLAAEYPAITNYLYCTY 673
Cdd:COG0458 458 TLLGAKSLGDSDGIIRRALAAKVPYvTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTY 517
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
130-675 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 561.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 130 KPIEVSKVLILGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQTNevgTKQADSVYFLPITPDFVTEVIK 209
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTD---PETADRTYIAPMTPELVEQVIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 210 AERPDGILLSMGGQTALNCGVELFKRGTLKEYGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVEDAVKAA 289
Cdd:PLN02735 96 KERPDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 290 EKIG-YPVMIRSAYALGGLGSGLCVNKEKLVEAAT--VAFSLTNQILVEQSLIGWKEVEYEVVRDAADNCVTVCNMENMD 366
Cdd:PLN02735 176 EDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKagLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENID 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 367 PMGIHTGDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGIigEC---NIQYALHPSSLEYCIIEVNARLSRSSALASKATG 443
Cdd:PLN02735 256 PMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 444 YPLAFIAAKLALGISLPDIKNMVSGKTTACFEPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTFEESFQK 523
Cdd:PLN02735 334 FPIAKMAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 524 ALRMCHPSIDGFMSELPMKKPWqDDFNYQKELSVPSSTRTYAVAKALQSGVSVDDIYQLTAIDKWFLYRMQGIVQVENML 603
Cdd:PLN02735 414 ALRSLETGFSGWGCAKVKELDW-DWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFL 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300720954 604 KKHTRANISEDLLIKAKQDGFSDRQIGKLMQSSEAD-RNLRLKKNIKPWVKQIDTLAAEYPAITNYLYCTYNG 675
Cdd:PLN02735 493 KSRSLSELSKDDFYEVKRRGFSDKQIAFATKSTEKEvRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDG 565
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
258-460 |
6.46e-103 |
|
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: 312.32 E-value: 6.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 258 DRQLFSDKLLEINENIAPSIA--VESVEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEAATVAFSLT------ 329
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 330 NQILVEQSLIGWKEVEYEVVRDAADNCVTVCNMENMDPMgiHTGDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGIIGEC 409
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 300720954 410 NIQYALHPSSLEYCIIEVNARLSRSSALASKATGYPLAFIAAKLALGISLP 460
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
136-528 |
2.27e-86 |
|
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: 292.29 E-value: 2.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 136 KVLILGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQTNevgTKQADSVYFLPITPDFVTEVIKAERPDG 215
Cdd:TIGR01369 556 KVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTD---YDTSDRLYFEPLTFEDVMNIIELEKPEG 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 216 ILLSMGGQTALNCGVELFKRGtlkeygVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVEDAVKAAEKIGYP 295
Cdd:TIGR01369 633 VIVQFGGQTPLNLAKALEEAG------VPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYP 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 296 VMIRSAYALGGLGSGLCVNKEKLVEAATVAFSLTNQ--ILVEQSLIGWKEVEYEVVRDaaDNCVTVCN-MENMDPMGIHT 372
Cdd:TIGR01369 707 VLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAVSD--GEEVLIPGiMEHIEEAGVHS 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 373 GDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHPSSLEycIIEVNARLSRSSALASKATGYPLAFIAAK 452
Cdd:TIGR01369 785 GDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVY--VIEVNPRASRTVPFVSKATGVPLAKLAVR 862
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300720954 453 LALGislPDIKNMVSGKttacfEPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTFEESFQKALRMC 528
Cdd:TIGR01369 863 VMLG---KKLEELGVGK-----EKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSS 930
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
136-524 |
3.20e-84 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 286.87 E-value: 3.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 136 KVLILGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQTNevgTKQADSVYFLPITPDFVTEVIKAERPDG 215
Cdd:PRK12815 557 KVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTD---YDTADRLYFEPLTLEDVLNVAEAENIKG 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 216 ILLSMGGQTALNCgvelfkRGTLKEYGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVEDAVKAAEKIGYP 295
Cdd:PRK12815 634 VIVQFGGQTAINL------AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYP 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 296 VMIRSAYALGGLGSGLCVNKEKLVEAATVAFSLTNQILVEQSLIGwKEVEYEVVRDAADncVTVCN-MENMDPMGIHTGD 374
Cdd:PRK12815 708 VLIRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPILIDQFIDG-KEYEVDAISDGED--VTIPGiIEHIEQAGVHSGD 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 375 SIVVAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALhpSSLEYCIIEVNARLSRSSALASKATGYPLAFIAAKLA 454
Cdd:PRK12815 785 SIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL--ANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVL 862
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 455 LGISLPDIknmvsGKTTACfEPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTFEESFQKA 524
Cdd:PRK12815 863 LGKSLAEL-----GYPNGL-WPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKG 926
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
136-524 |
1.80e-82 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 281.60 E-value: 1.80e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 136 KVLILGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQTnEVGTkqADSVYFLPITPDFVTEVIKAERPDG 215
Cdd:PRK05294 556 KVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVST-DYDT--SDRLYFEPLTLEDVLEIIEKEKPKG 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 216 ILLSMGGQTALNcgveLFKRgtLKEYGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVEDAVKAAEKIGYP 295
Cdd:PRK05294 633 VIVQFGGQTPLK----LAKA--LEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYP 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 296 VMIRSAYALGGLGSGLCVNKEKLVEAATVAFSLTNQ--ILVEQSLIGWKEVEYEVVRDAADncVTVCN-MENMDPMGIHT 372
Cdd:PRK05294 707 VLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDhpVLIDKFLEGAIEVDVDAICDGED--VLIGGiMEHIEEAGVHS 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 373 GDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHPSSLeYcIIEVNARLSRSSALASKATGYPLAFIAAK 452
Cdd:PRK05294 785 GDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEV-Y-VIEVNPRASRTVPFVSKATGVPLAKIAAR 862
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300720954 453 LALGISLPDIknmvsGKTTacfEPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTFEESFQKA 524
Cdd:PRK05294 863 VMLGKKLAEL-----GYTK---GLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKA 926
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
131-524 |
3.94e-70 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 247.38 E-value: 3.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 131 PIEVSKVLILGSGGLSIGQAGEFDYSGSQAIKALKEESKKTILMNPNIASVQTNevgTKQADSVYFLPITPDFVTEVIKA 210
Cdd:PLN02735 571 PTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTD---YDTSDRLYFEPLTVEDVLNVIDL 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 211 ERPDGILLSMGGQTALNCGVELFKrgTLKEY---------GVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVES 281
Cdd:PLN02735 648 ERPDGIIVQFGGQTPLKLALPIQK--YLDKNpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARS 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 282 VEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEAATVAFSLTNQ--ILVEQSLIGWKEVEYEVVRDAADNCVTV 359
Cdd:PLN02735 726 EADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPErpVLVDKYLSDATEIDVDALADSEGNVVIG 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 360 CNMENMDPMGIHTGDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHPSSLEYcIIEVNARLSRSSALAS 439
Cdd:PLN02735 806 GIMEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVY-IIEANPRASRTVPFVS 884
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 440 KATGYPLAFIAAKLALGISLPDIknmvsgkttaCF--EPSLDYIVTKIPRWDLDRFQGTTGQIGSSMKSVGEVMAIGRTF 517
Cdd:PLN02735 885 KAIGHPLAKYASLVMSGKSLKDL----------GFteEVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEF 954
|
....*..
gi 300720954 518 EESFQKA 524
Cdd:PLN02735 955 SKAFAKA 961
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
1-107 |
3.77e-68 |
|
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: 220.45 E-value: 3.77e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLNMMSGQAFITAQNHGYGIDTSSLPLGWKPLFVNVNDGTNEGIMHET 80
Cdd:cd01744 72 IFGICLGHQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKD 151
|
90 100
....*....|....*....|....*..
gi 300720954 81 KPIFTAQFHPEANGGPTDTEFLFDAFI 107
Cdd:cd01744 152 LPVFSVQFHPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
553-673 |
4.18e-54 |
|
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: 181.11 E-value: 4.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 553 KELSVPSSTRTYAVAKALQSGVSVDDIYQLTAIDKWFLYRMQGIVQVENMLKKHTRANISEDLLIKAKQDGFSDRQIGKL 632
Cdd:smart01096 3 EELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAKL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 300720954 633 MQSSEAD-RNLRLKKNIKPWVKQIDTLAAEYPAITNYLYCTY 673
Cdd:smart01096 83 LGVTEAEvRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-112 |
8.49e-54 |
|
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: 188.60 E-value: 8.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLNMMSGQAFITAQNHGYGIDTSSLPLG-WKPLFVNVNDGTNEGIMHE 79
Cdd:TIGR01368 245 IFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGdLEVTHVNLNDGTVEGIRHK 324
|
90 100 110
....*....|....*....|....*....|...
gi 300720954 80 TKPIFTAQFHPEANGGPTDTEFLFDAFIDLIKK 112
Cdd:TIGR01368 325 DLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-110 |
2.89e-52 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 184.51 E-value: 2.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLNMMSGQAFITAQNHGYGIDTSSLPLGWKPLFVNVNDGTNEGIMHET 80
Cdd:PRK12564 251 IFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKD 330
|
90 100 110
....*....|....*....|....*....|
gi 300720954 81 KPIFTAQFHPEANGGPTDTEFLFDAFIDLI 110
Cdd:PRK12564 331 LPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-111 |
6.94e-50 |
|
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: 177.91 E-value: 6.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLNMMSGQAFITAQNHGYGIDTSSLP-LGWKPLFVNVNDGTNEGIMHE 79
Cdd:COG0505 250 IFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPaTDLEVTHVNLNDGTVEGLRHK 329
|
90 100 110
....*....|....*....|....*....|..
gi 300720954 80 TKPIFTAQFHPEANGGPTDTEFLFDAFIDLIK 111
Cdd:COG0505 330 DLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
1-114 |
5.33e-43 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 158.52 E-value: 5.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLNMMSGQAFITAQNHGYGIDTSSLPL-GWKPLFVNVNDGTNEGIMHE 79
Cdd:PRK12838 240 ILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGtPLSVRFFNVNDGSIEGLRHK 319
|
90 100 110
....*....|....*....|....*....|....*
gi 300720954 80 TKPIFTAQFHPEANGGPTDTEFLFDAFIDLIKKGK 114
Cdd:PRK12838 320 KKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKAR 354
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
1-109 |
6.87e-34 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 127.74 E-value: 6.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPM-ANRGQNQPVLNMMS------GQAFITAQNHGYGIDTSSLPLGWKPLFVNVNDGTN 73
Cdd:pfam00117 73 ILGICLGHQLLALAFGGKVVKAKKfGHHGKNSPVGDDGCglfyglPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTI 152
|
90 100 110
....*....|....*....|....*....|....*.
gi 300720954 74 EGIMHETKPIFTAQFHPEANGGPTDTEFLFDAFIDL 109
Cdd:pfam00117 153 MGIRHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
553-632 |
5.49e-31 |
|
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: 115.55 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 553 KELSVPSSTRTYAVAKALQSGVSVDDIYQLTAIDKWFLYRMQGIVQVENMLKKHTrANISEDLLIKAKQDGFSDRQIGKL 632
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAG-LDLDAELLREAKRLGFSDRQIAKL 79
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-114 |
1.46e-27 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 115.28 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVlnMMSGQAFITAQNHGYGIDTSSL-PLGWKPLFVNVNDGTNEGIMHE 79
Cdd:CHL00197 266 IFGICMGHQILSLALEAKTFKLKFGHRGLNHPS--GLNQQVEITSQNHGFAVNLESLaKNKFYITHFNLNDGTVAGISHS 343
|
90 100 110
....*....|....*....|....*....|....*
gi 300720954 80 TKPIFTAQFHPEANGGPTDTEFLFDAFIDLIKKGK 114
Cdd:CHL00197 344 PKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSK 378
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
1-103 |
3.74e-24 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 105.45 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLNMMSGQAFITAQNHGYGIDTSSLPLGWKPLFVNVNDGTNEGIMHET 80
Cdd:PLN02771 313 VFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPA 392
|
90 100
....*....|....*....|...
gi 300720954 81 KPIFTAQFHPEANGGPTDTEFLF 103
Cdd:PLN02771 393 LNVMSLQYHPEASPGPHDSDNAF 415
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
202-456 |
2.88e-19 |
|
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: 88.01 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 202 DFVTEVIKAERPDGILlsmggqtALNC-GVELFKRgTLKEYGVKvlGTSVESIMATEDRQLFSDKLLEINENIAPSIAVE 280
Cdd:COG0439 7 AAAAELARETGIDAVL-------SESEfAVETAAE-LAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 281 SVEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEAA------TVAFSLTNQILVEQSLIGwKEVEYEVVrdAAD 354
Cdd:COG0439 77 SPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALaearaeAKAGSPNGEVLVEEFLEG-REYSVEGL--VRD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 355 NCVTVCNM---ENMDPMGIHTGDsivVAPSQtLSNEEFHKLRETAIKVVRHLGII-GECNIQYALHPSSlEYCIIEVNAR 430
Cdd:COG0439 154 GEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEFLLTPDG-EPYLIEINAR 228
|
250 260
....*....|....*....|....*...
gi 300720954 431 LS--RSSALASKATGYPLAFIAAKLALG 456
Cdd:COG0439 229 LGgeHIPPLTELATGVDLVREQIRLALG 256
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
136-470 |
4.35e-13 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 70.68 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 136 KVLILGSGGlsigqagefdysGSQAIKALKEEskktiLMNPNIASVQTNEV--GTKQADSVYFLP-ITP----DFVTEVI 208
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKS-----LLKGRVIGADISELapALYFADKFYVVPkVTDpnyiDRLLDIC 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 209 KAERPDGIL-LSmggqtalncGVELFK----RGTLKEYGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAVESVE 283
Cdd:PRK12767 66 KKEKIDLLIpLI---------DPELPLlaqnRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 284 DAVKA--AEKIGYPVMIRSAYALGGLGSGLCVNKEKLveaaTVAFSLTNQILVEQSLIGwKEVEYEVVRDAADNCVTVCN 361
Cdd:PRK12767 137 DFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEEL----EFLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 362 MENMDPMGIHTGDSIVVapsqtlsneEFHKLRETAIKVVRHLGIIGECNIQYALHPSslEYCIIEVNARLSrssalaska 441
Cdd:PRK12767 212 RKRIEVRAGETSKGVTV---------KDPELFKLAERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFG--------- 271
|
330 340 350
....*....|....*....|....*....|
gi 300720954 442 TGYPLAFIAaklalGISLPD-IKNMVSGKT 470
Cdd:PRK12767 272 GGYPLSYMA-----GANEPDwIIRNLLGGE 296
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
240-463 |
3.65e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 65.89 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 240 EYGVKVLGTSVESImatedRQLfSDKLLEINENIAPSIAV--------ESVEDAVKAAEKIGYPVMIRSAYALGGLGSGL 311
Cdd:PRK07178 96 ERGIKFIGPSAEVI-----RRM-GDKTEARRAMIKAGVPVtpgsegnlADLDEALAEAERIGYPVMLKATSGGGGRGIRR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 312 C-------VNKEKLVEAATVAFSLTnQILVEQSLIGWKEVEYEVVRDAADNCVTV----CNMENMDPMGIHtgdsivVAP 380
Cdd:PRK07178 170 CnsreeleQNFPRVISEATKAFGSA-EVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQRRNQKLIE------IAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 381 SQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALhPSSLEYCIIEVNARLSRSSALASKATGYPLA----FIAAKLALG 456
Cdd:PRK07178 243 SPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL-DADGEVYFMEMNTRVQVEHTITEEITGIDIVreqiRIASGLPLS 321
|
....*..
gi 300720954 457 ISLPDIK 463
Cdd:PRK07178 322 YKQEDIQ 328
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
275-541 |
3.35e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 62.74 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 275 PSIAVESVEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEA-------ATVAFSlTNQILVEQSLIGWKEVEYE 347
Cdd:PRK06111 134 ITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAfesnkkrAANFFG-NGEMYIEKYIEDPRHIEIQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 348 VVRDAADNCVTV----CNMENMDPMGIHTgdsivvAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYaLHPSSLEYC 423
Cdd:PRK06111 213 LLADTHGNTVYLwereCSVQRRHQKVIEE------APSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFY 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 424 IIEVNARLSRSSALASKATGYPLA----FIAAKLALGISLPDIKnmVSGKTTAC---------FEPSldyiVTKIPRWDL 490
Cdd:PRK06111 286 FLEMNTRLQVEHPVTEEITGIDLVeqqlRIAAGEKLSFTQDDIK--RSGHAIEVriyaedpktFFPS----PGKITDLTL 359
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300720954 491 DRFQG----TTGQIGS-------SMksVGEVMAIGRTFEESFQK---ALRMCHpsIDGFMSELPM 541
Cdd:PRK06111 360 PGGEGvrhdHAVENGVtvtpfydPM--IAKLIAHGETREEAISRlhdALEELK--VEGIKTNIPL 420
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
239-461 |
9.11e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 61.30 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 239 KEYGVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSI--AVESVEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKE 316
Cdd:PRK08462 98 SHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDES 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 317 KLVEA-------ATVAFSlTNQILVEQSLIGWKEVEYEVVRDAADNCVTV----CNMENmdpmgiHTGDSIVVAPSQTLS 385
Cdd:PRK08462 178 DLENLylaaeseALSAFG-DGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVLD 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300720954 386 NEEFHKLRETAIKVVRHLGIIGECNIQYaLHPSSLEYCIIEVNARLSRSSALASKATGYPLAFIAAKLALGISLPD 461
Cdd:PRK08462 251 EKTRERLHETAIKAAKAIGYEGAGTFEF-LLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
278-431 |
6.05e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 58.84 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 278 AVESVEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEA-------ATVAFSLTNqILVEQSLIGWKEVEYEVVR 350
Cdd:PRK08654 137 GIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAiestqsiAQSAFGDST-VFIEKYLEKPRHIEIQILA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 351 DAADNCvtvcnmenmdpmgIHTGDS-----------IVVAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYaLHpSS 419
Cdd:PRK08654 216 DKHGNV-------------IHLGDRecsiqrrhqklIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEF-LY-SN 280
|
170
....*....|..
gi 300720954 420 LEYCIIEVNARL 431
Cdd:PRK08654 281 GNFYFLEMNTRL 292
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
278-473 |
3.90e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 56.26 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 278 AVESVEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEA-------ATVAFSlTNQILVEQSLIGWKEVEYEVVR 350
Cdd:PRK05586 137 EIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAfntakseAKAAFG-DDSMYIEKFIENPKHIEFQILG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 351 DAADNCVTV----CNMENMDPMGIHTgdsivvAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHPSSlEYCIIE 426
Cdd:PRK05586 216 DNYGNVVHLgerdCSLQRRNQKVLEE------APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDG-NFYFME 288
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 300720954 427 VNARLSRSSALASKATGYPLA----FIAAKLALGISLPDIKnmVSGKTTAC 473
Cdd:PRK05586 289 MNTRIQVEHPITEMITGVDLVkeqiKIAYGEKLSIKQEDIK--INGHSIEC 337
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
202-460 |
4.74e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 55.70 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 202 DFVTEVIKAERPDgILLSMGgqtalNCGVELF--KRGTLKEYgVKVLGTSVESIMATEDRQLFSDKLLEINENIAPSIAV 279
Cdd:COG3919 66 DALLELAERHGPD-VLIPTG-----DEYVELLsrHRDELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 280 ESVEDAVKAAEKIGYPVMIRSAYAlGGLGSGLCVNKEKLVEAATVA--------FSLTNQILVEQSLI-GWKEVEY--EV 348
Cdd:COG3919 139 DSADDLDALAEDLGFPVVVKPADS-VGYDELSFPGKKKVFYVDDREellallrrIAAAGYELIVQEYIpGDDGEMRglTA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 349 VRDAADNCVTVCNMEN--MDPMGIhtGDSIVVapsQTLSNEEfhkLRETAIKVVRHLGIIGECNIQYALHPSSLEYCIIE 426
Cdd:COG3919 218 YVDRDGEVVATFTGRKlrHYPPAG--GNSAAR---ESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIE 289
|
250 260 270
....*....|....*....|....*....|....
gi 300720954 427 VNARLSRSSALASKAtGYPLAFIAAKLALGISLP 460
Cdd:COG3919 290 INPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLE 322
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
278-431 |
2.01e-07 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 53.87 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 278 AVESVEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEA-------ATVAFSltN-QILVEQSLIGWKEVEYEVV 349
Cdd:COG4770 137 PVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAfesarreAKAAFG--DdRVYLEKYIERPRHIEVQVL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 350 RDAADNCVtvcnmenmdpmgiHTGD---SI------VV--APSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHPs 418
Cdd:COG4770 215 ADKHGNVV-------------HLGErdcSIqrrhqkVIeeAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDA- 280
|
170
....*....|...
gi 300720954 419 SLEYCIIEVNARL 431
Cdd:COG4770 281 DGNFYFLEMNTRL 293
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
278-431 |
3.25e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 53.27 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 278 AVESVEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEA-------ATVAFSlTNQILVEQSLIGWKEVEYEVVR 350
Cdd:PRK08591 137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAfsmaraeAKAAFG-NPGVYMEKYLENPRHIEIQVLA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 351 DAADNcvtvcnmenmdpmGIHTGD---SI------VV--APSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYaLHPSS 419
Cdd:PRK08591 216 DGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKN 281
|
170
....*....|..
gi 300720954 420 LEYCIIEVNARL 431
Cdd:PRK08591 282 GEFYFIEMNTRI 293
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
278-431 |
3.73e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 53.60 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 278 AVESVEDAVKAAEKIGYPVMIRSayALGGLGSGLCV--NKEKLVEAATVAFSLTNQ------ILVEQSLIGWKEVEYEVV 349
Cdd:PRK12999 141 PIDDIEEALEFAEEIGYPIMLKA--SAGGGGRGMRIvrSEEELEEAFERAKREAKAafgndeVYLEKYVENPRHIEVQIL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 350 RDAADNCVTV----CnmenmdpmgihtgdSI------VV--APSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHP 417
Cdd:PRK12999 219 GDKHGNVVHLyerdC--------------SVqrrhqkVVeiAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDA 284
|
170
....*....|....
gi 300720954 418 SSlEYCIIEVNARL 431
Cdd:PRK12999 285 DG-NFYFIEVNPRI 297
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
290-462 |
6.30e-06 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 47.70 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 290 EKIGYPVMIRSAYALGGLGSGLCVNKEKLVEAATVAFSLTNQILVEQSLIGwKEVEyevvrdaadncVTVCNMENMDPMG 369
Cdd:pfam07478 33 EALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGIEG-REIE-----------CAVLGNEDPEVSP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 370 IH----------------TGDSIVVAPSQtLSNEEFHKLRETAIKVVRHLGIIGECNIQYALhPSSLEYCIIEVN----- 428
Cdd:pfam07478 101 VGeivpsggfydyeakyiDDSAQIVVPAD-LEEEQEEQIQELALKAYKALGCRGLARVDFFL-TEDGEIVLNEVNtipgf 178
|
170 180 190
....*....|....*....|....*....|....
gi 300720954 429 ARLSRssalaskatgYPLAFIAAklalGISLPDI 462
Cdd:pfam07478 179 TSISM----------FPKLAAAA----GVSFPDL 198
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
1-93 |
7.63e-06 |
|
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: 47.63 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRG-------QNQPVLNMMSGQaFITAQNHGYGIDTssLPLGWKPLFVNVNDgTN 73
Cdd:COG0518 85 VLGICYGAQLLAHALGGKVEPGPGREIGwapveltEADPLFAGLPDE-FTVWMSHGDTVTE--LPEGAEVLASSDNC-PN 160
|
90 100
....*....|....*....|
gi 300720954 74 EGIMHEtKPIFTAQFHPEAN 93
Cdd:COG0518 161 QAFRYG-RRVYGVQFHPEVT 179
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
278-462 |
2.02e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 47.44 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 278 AVESVEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEA-------ATVAFSlTNQILVEQSLIGWKEVEYEVVR 350
Cdd:PRK12833 140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAElplaqreAQAAFG-DGGVYLERFIARARHIEVQILG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 351 DaADNCVTV----CNMENMDPMGIHTgdsivvAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHPSSLEYCIIE 426
Cdd:PRK12833 219 D-GERVVHLfereCSLQRRRQKILEE------APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIE 291
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 300720954 427 VNARLSRSSALASKATGYPLA----FIAAKLALGISLPDI 462
Cdd:PRK12833 292 MNTRIQVEHPVTEAITGIDLVqemlRIADGEPLRFAQGDI 331
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
1-107 |
3.20e-05 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 47.02 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLNMMSG------QAFITAQNHGYGIDTSSLPLGWKPLfVNVNDGTNE 74
Cdd:PRK14607 76 ILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGlfrgipNPTVATRYHSLVVEEASLPECLEVT-AKSDDGEIM 154
|
90 100 110
....*....|....*....|....*....|...
gi 300720954 75 GIMHETKPIFTAQFHPEANgGPTDTEFLFDAFI 107
Cdd:PRK14607 155 GIRHKEHPIFGVQFHPESI-LTEEGKRILKNFL 186
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
278-404 |
3.22e-05 |
|
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: 47.38 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 278 AVESVEDAVKAAEKIGYPVMIRSayALGGLGSGLCV--NKEKLVEA-------ATVAFSlTNQILVEQSLIGWKEVEYEV 348
Cdd:COG1038 140 PVDDLEEALAFAEEIGYPVMLKA--AAGGGGRGMRVvrSEEELEEAfesarreAKAAFG-DDEVFLEKYIERPKHIEVQI 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300720954 349 VRDAADNCVTV----CnmenmdpmgihtgdSI------VV--APSQTLSNEEFHKLRETAIKVVRHLG 404
Cdd:COG1038 217 LGDKHGNIVHLferdC--------------SVqrrhqkVVeiAPAPNLDEELREAICEAAVKLAKAVG 270
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
1-91 |
1.78e-04 |
|
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: 42.91 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQ------NQPVLNMMSGQAFITAQNHGYGIDTSSLPLGWKplfvnVNDGTNE 74
Cdd:cd01743 74 ILGVCLGHQAIAEAFGGKVVRAPEPMHGKtseihhDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLE-----VTASTED 148
|
90 100
....*....|....*....|.
gi 300720954 75 G-IM---HETKPIFTAQFHPE 91
Cdd:cd01743 149 GvIMalrHRDLPIYGVQFHPE 169
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
280-463 |
2.15e-04 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 44.42 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 280 ESVEDAVKAAEKIGYPVMIRSAYalGGLGSGL-CVNKEKLVEAA-------TVAFSLTNQILVEQSLIGWKEVEYEVVRD 351
Cdd:PRK08463 139 ESMEEIKIFARKIGYPVILKASG--GGGGRGIrVVHKEEDLENAfesckreALAYFNNDEVFMEKYVVNPRHIEFQILGD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 352 AADNCVTVCnmENMDPMGIHTGDSIVVAPSQTLSNEEFHKLRETAIKVVRHLGIIGECNIQYALHPSSLEYcIIEVNARL 431
Cdd:PRK08463 217 NYGNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFY-FMEMNTRI 293
|
170 180 190
....*....|....*....|....*....|....*.
gi 300720954 432 SRSSALASKATGYPLAF----IAAKLALGISLPDIK 463
Cdd:PRK08463 294 QVEHGVTEEITGIDLIVrqirIAAGEILDLEQSDIK 329
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
279-340 |
3.40e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 43.99 E-value: 3.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300720954 279 VESVEDAVKAAEKIGYPVMIRSAYALGGLGSGLCVNKEKLVEAA-TVAFSLTNQILVEQSLIG 340
Cdd:PRK14016 235 VTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVNITTREEIEAAyAVASKESSDVIVERYIPG 297
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
1-92 |
4.03e-04 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 42.03 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVLN-----MMSG--QAFITAQNHGYGIDTSSLPlgwKPLFVNV--NDG 71
Cdd:PRK06895 75 ILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVrsnspLFDGlpEEFNIGLYHSWAVSEENFP---TPLEITAvcDEN 151
|
90 100
....*....|....*....|.
gi 300720954 72 TNEGIMHETKPIFTAQFHPEA 92
Cdd:PRK06895 152 VVMAMQHKTLPIYGVQFHPES 172
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
1-91 |
4.40e-04 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 43.37 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKL--PM---ANRGQNQPVLNMMSG--QAFITAQNHGYGIDTSSLPlgwKPLFVNV--NDG 71
Cdd:PRK13566 601 IFGVCLGLQAIVEAFGGELGQLayPMhgkPSRIRVRGPGRLFSGlpEEFTVGRYHSLFADPETLP---DELLVTAetEDG 677
|
90 100
....*....|....*....|
gi 300720954 72 TNEGIMHETKPIFTAQFHPE 91
Cdd:PRK13566 678 VIMAIEHKTLPVAAVQFHPE 697
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
283-429 |
2.78e-03 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 39.41 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 283 EDAVKAAEKIG--YPVMIRSAYALGGLGSGLCVNKEKLVEaatVAFSLTNQILVEQSLigwKEVEYEVVRDAADNCVTVC 360
Cdd:pfam08443 28 EDAEQFIEQIKrqFPVIVKSIYGSQGIGVFLAEDEQKLRQ---TLSATNEQILVQEFI---AEANNEDIRCLVVGDQVVG 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300720954 361 NMENMDPMG-----IHTGDsivVAPSQTLSNEEfhklRETAIKVVRHLGIIgECNIQyaLHPSSLEYCIIEVNA 429
Cdd:pfam08443 102 ALHRQSNEGdfrsnLHRGG---VGEKYQLSQEE----TELAIKAAQAMQLD-VAGVD--LLRQKRGLLVCEVNS 165
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
1-92 |
7.83e-03 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 38.32 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300720954 1 VFGICMGNQMAALAAGAKSYKLPMANRGQNQPVlnMMSGQAFITAQN--------HGYGIDTSSLP-----LGWKPLfvn 67
Cdd:PRK08857 75 ILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPI--RHTGRSVFKGLNnpltvtryHSLVVKNDTLPecfelTAWTEL--- 149
|
90 100
....*....|....*....|....*...
gi 300720954 68 vNDGTNEGIM---HETKPIFTAQFHPEA 92
Cdd:PRK08857 150 -EDGSMDEIMgfqHKTLPIEAVQFHPES 176
|
|
| |
