|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-314 |
1.56e-142 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 415.24 E-value: 1.56e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVPSETeydeyklpahFEwTSGISVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:PRK12564 47 SYAGQIVTFTYPLIGNYGVNRED----------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 81 RALTKKIRENGSILGRIVQNLPSPHSDYKFL----DPNTRNLVAECSVKTTITYNQQGS---PRICAVDCGLKLNQIRCF 153
Cdd:PRK12564 116 RALTRKLREKGAMKGVIATEDFDAEELLEKArafpGLLGLDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILREL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 154 LARGARVDLVPWNH------NLNPeefDGLFISNGPGDPVVCVDTVKQIKKvLIESEKPVFGICLGHQLLSTAIGCTTYK 227
Cdd:PRK12564 196 AERGCRVTVVPATTtaeeilALNP---DGVFLSNGPGDPAALDYAIEMIRE-LLEKKIPIFGICLGHQLLALALGAKTYK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 228 MKYGNRGHNLPCIHHSTGRCFMTSQNHGFAVDADTLPPDWEPLFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPQDLEL 307
Cdd:PRK12564 272 MKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAY 351
|
....*..
gi 817639577 308 LFDVFLE 314
Cdd:PRK12564 352 LFDEFVE 358
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-318 |
6.39e-139 |
|
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: 406.24 E-value: 6.39e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVPSEteydeyklpaHFEwTSGISVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:TIGR01368 43 SYKGQIVVFTYPLIGNYGVNDE----------DAE-SKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 81 RALTKKIRENGSILGRIVQNLPSPHSDYKFL----DPNTRNLVAECSVKTTITYNQQGSP--RICAVDCGLKLNQIRCFL 154
Cdd:TIGR01368 112 RALVKKIREKGTMKGVISTEDSNDEELVEKArvspDITGINLVAEVSTKEPYTWGQRGGKgkRVVVIDFGVKRNILRRLV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 155 ARGARVDLVPWNH------NLNPeefDGLFISNGPGDPVVCVDTVKQIKKVLieSEKPVFGICLGHQLLSTAIGCTTYKM 228
Cdd:TIGR01368 192 KRGCEVTVVPYDTdaeeikKYNP---DGIFLSNGPGDPAAVEPAIETIRKLL--EKIPIFGICLGHQLLALAFGAKTYKM 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 229 KYGNRGHNLPCIHHSTGRCFMTSQNHGFAVDADTLPP-DWEPLFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPQDLEL 307
Cdd:TIGR01368 267 KFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEY 346
|
330
....*....|.
gi 817639577 308 LFDVFLETVKE 318
Cdd:TIGR01368 347 LFDEFIDLMKK 357
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-317 |
1.07e-138 |
|
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: 405.56 E-value: 1.07e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVPSEteydeyklpaHFEwTSGISVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:COG0505 47 SYAGQIVTFTYPHIGNYGVNDE----------DFE-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 81 RALTKKIRENGSILGRIVQNLPSPHSDYK----FLDPNTRNLVAECSVKTTITYNQQG--SPRICAVDCGLKLNQIRCFL 154
Cdd:COG0505 116 RALTRHLREKGAMKGVISTGDLDIEELLEkaraAPGMEGLDLVKEVSTKEPYEWTEAPgaGFHVVALDFGVKRNILRELA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 155 ARGARVDLVPWN------HNLNPeefDGLFISNGPGDPVVCVDTVKQIKKvLIESEKPVFGICLGHQLLSTAIGCTTYKM 228
Cdd:COG0505 196 ERGCRVTVVPATtsaeeiLALNP---DGVFLSNGPGDPAALDYAIETIRE-LLGKGIPIFGICLGHQLLALALGAKTYKL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 229 KYGNRGHNLPCIHHSTGRCFMTSQNHGFAVDADTLPP-DWEPLFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPQDLEL 307
Cdd:COG0505 272 KFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAY 351
|
330
....*....|
gi 817639577 308 LFDVFLETVK 317
Cdd:COG0505 352 LFDRFIELME 361
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
347-549 |
2.99e-106 |
|
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: 341.98 E-value: 2.99e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 347 TKPRKVLILGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLTRDYVEQVIKAERPN 426
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 427 GVLLTFGGQTALNCGVELDRAGIFEKYNVKILGTPIKSIIETEDRKIFAERVAEIGEKVAPSEAVYSIQEALDAADRLGY 506
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 817639577 507 PVMARAAFSLGGLGSGFANNKEELISLAQQALPHS--NQLIIDKS 549
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKS 208
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
138-313 |
7.25e-104 |
|
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: 309.81 E-value: 7.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 138 ICAVDCGLKLNQIRCFLARGARVDLVPWNH------NLNPeefDGLFISNGPGDPVVCVDTVKQIKKvLIESEKPVFGIC 211
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTdaeeilKLDP---DGIFLSNGPGDPALLDEAIKTVRK-LLGKKIPIFGIC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 212 LGHQLLSTAIGCTTYKMKYGNRGHNLPCIHHSTGRCFMTSQNHGFAVDADTLPPDWEPLFTNANDNTNEGIIHKSKPYFS 291
Cdd:cd01744 77 LGHQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFS 156
|
170 180
....*....|....*....|..
gi 817639577 292 VQFHPEHTAGPQDLELLFDVFL 313
Cdd:cd01744 157 VQFHPEASPGPHDTEYLFDEFL 178
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
350-549 |
1.65e-94 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 310.88 E-value: 1.65e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 350 RKVLILGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLTRDYVEQVIKAERPNGVL 429
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 430 LTFGGQTALNCGVELDRAGIFEKYNVKILGTPIKSIIETEDRKIFAERVAEIGEKVAPSEAVYSIQEALDAADRLGYPVM 509
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 817639577 510 ARAAFSLGGLGSGFANNKEELISLAQQALPHS--NQLIIDKS 549
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEES 209
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
355-549 |
1.04e-87 |
|
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: 280.61 E-value: 1.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 355 LGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLTRDYVEQVIKAERPNGVLLTFGG 434
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 435 QTALNCGVELDRAGIFEkyNVKILGTPIKSIIETEDRKIFAERVAEIGEKVAPSEAVYSIQEALDAADRLGYPVMARAAF 514
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 817639577 515 SLGGLGSGFANNKEELISLAQQALPHS--NQLIIDKS 549
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDES 195
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
141-314 |
3.99e-61 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 199.77 E-value: 3.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 141 VDCGL--KLNQIRCFLARGARVDLVPWNHNLN---PEEFDGLFISNGPGDPVVCVDTVKQIKKvLIESEKPVFGICLGHQ 215
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTPAEeilEENPDGIILSGGPGSPGAAGGAIEAIRE-ARELKIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 216 LLSTAIGCTTYKMK-YGNRGHNLPCIHHS------TGRCFMTSQNHGFAVDADTLPPDWEPLFTNANDNTNEGIIHKSKP 288
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDDGcglfygLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*.
gi 817639577 289 YFSVQFHPEHTAGPQDLELLFDVFLE 314
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-97 |
4.23e-41 |
|
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: 144.44 E-value: 4.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVPSETeydeyklpahFEwTSGISVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:smart01097 45 SYAGQIVVFTYPLIGNYGVNDED----------FE-SDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDT 113
|
90
....*....|....*..
gi 817639577 81 RALTKKIRENGSILGRI 97
Cdd:smart01097 114 RALTRKLREKGAMKGVI 130
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
470-549 |
3.34e-23 |
|
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: 97.76 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 470 DRKIFAERVAEIGEKVAPSEAVY--SIQEALDAADRLGYPVMARAAFSLGGLGSGFANNKEELISLAQQALPHS------ 541
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
....*...
gi 817639577 542 NQLIIDKS 549
Cdd:pfam02786 81 PQVLVEKS 88
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-314 |
1.56e-142 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 415.24 E-value: 1.56e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVPSETeydeyklpahFEwTSGISVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:PRK12564 47 SYAGQIVTFTYPLIGNYGVNRED----------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 81 RALTKKIRENGSILGRIVQNLPSPHSDYKFL----DPNTRNLVAECSVKTTITYNQQGS---PRICAVDCGLKLNQIRCF 153
Cdd:PRK12564 116 RALTRKLREKGAMKGVIATEDFDAEELLEKArafpGLLGLDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILREL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 154 LARGARVDLVPWNH------NLNPeefDGLFISNGPGDPVVCVDTVKQIKKvLIESEKPVFGICLGHQLLSTAIGCTTYK 227
Cdd:PRK12564 196 AERGCRVTVVPATTtaeeilALNP---DGVFLSNGPGDPAALDYAIEMIRE-LLEKKIPIFGICLGHQLLALALGAKTYK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 228 MKYGNRGHNLPCIHHSTGRCFMTSQNHGFAVDADTLPPDWEPLFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPQDLEL 307
Cdd:PRK12564 272 MKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAY 351
|
....*..
gi 817639577 308 LFDVFLE 314
Cdd:PRK12564 352 LFDEFVE 358
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-318 |
6.39e-139 |
|
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: 406.24 E-value: 6.39e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVPSEteydeyklpaHFEwTSGISVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:TIGR01368 43 SYKGQIVVFTYPLIGNYGVNDE----------DAE-SKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 81 RALTKKIRENGSILGRIVQNLPSPHSDYKFL----DPNTRNLVAECSVKTTITYNQQGSP--RICAVDCGLKLNQIRCFL 154
Cdd:TIGR01368 112 RALVKKIREKGTMKGVISTEDSNDEELVEKArvspDITGINLVAEVSTKEPYTWGQRGGKgkRVVVIDFGVKRNILRRLV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 155 ARGARVDLVPWNH------NLNPeefDGLFISNGPGDPVVCVDTVKQIKKVLieSEKPVFGICLGHQLLSTAIGCTTYKM 228
Cdd:TIGR01368 192 KRGCEVTVVPYDTdaeeikKYNP---DGIFLSNGPGDPAAVEPAIETIRKLL--EKIPIFGICLGHQLLALAFGAKTYKM 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 229 KYGNRGHNLPCIHHSTGRCFMTSQNHGFAVDADTLPP-DWEPLFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPQDLEL 307
Cdd:TIGR01368 267 KFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEY 346
|
330
....*....|.
gi 817639577 308 LFDVFLETVKE 318
Cdd:TIGR01368 347 LFDEFIDLMKK 357
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-317 |
1.07e-138 |
|
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: 405.56 E-value: 1.07e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVPSEteydeyklpaHFEwTSGISVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:COG0505 47 SYAGQIVTFTYPHIGNYGVNDE----------DFE-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 81 RALTKKIRENGSILGRIVQNLPSPHSDYK----FLDPNTRNLVAECSVKTTITYNQQG--SPRICAVDCGLKLNQIRCFL 154
Cdd:COG0505 116 RALTRHLREKGAMKGVISTGDLDIEELLEkaraAPGMEGLDLVKEVSTKEPYEWTEAPgaGFHVVALDFGVKRNILRELA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 155 ARGARVDLVPWN------HNLNPeefDGLFISNGPGDPVVCVDTVKQIKKvLIESEKPVFGICLGHQLLSTAIGCTTYKM 228
Cdd:COG0505 196 ERGCRVTVVPATtsaeeiLALNP---DGVFLSNGPGDPAALDYAIETIRE-LLGKGIPIFGICLGHQLLALALGAKTYKL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 229 KYGNRGHNLPCIHHSTGRCFMTSQNHGFAVDADTLPP-DWEPLFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPQDLEL 307
Cdd:COG0505 272 KFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAY 351
|
330
....*....|
gi 817639577 308 LFDVFLETVK 317
Cdd:COG0505 352 LFDRFIELME 361
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
1-320 |
1.93e-113 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 340.72 E-value: 1.93e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVPSEteYDEYKLPahfewtsgiSVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:PRK12838 45 SYKGQIVVFTYPLIGNYGINAD--DYESKQP---------QVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 81 RALTKKIRENGSILGRIVQNLPSPHSDYKFLDPNTRNLVAECSVKTTITYNQQGsPRICAVDCGLKLNQIRCFLARGARV 160
Cdd:PRK12838 114 RALVKHIREKGTMKASITTTDDAHAFDQIKALVLPKNVVAQVSTKEPYTYGNGG-KHVALIDFGYKKSILRSLSKRGCKV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 161 DLVPWN------HNLNPeefDGLFISNGPGDPVVCVDTVKQIKKvLIESeKPVFGICLGHQLLSTAIGCTTYKMKYGNRG 234
Cdd:PRK12838 193 TVLPYDtsleeiKNLNP---DGIVLSNGPGDPKELQPYLPEIKK-LISS-YPILGICLGHQLIALALGADTEKLPFGHRG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 235 HNLPCIHHSTGRCFMTSQNHGFAVDADTLPPD-WEPLFTNANDNTNEGIIHKSKPYFSVQFHPEHTAGPQDLELLFDVFL 313
Cdd:PRK12838 268 ANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGTpLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFL 347
|
....*..
gi 817639577 314 ETVKENK 320
Cdd:PRK12838 348 EMMEKAR 354
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
347-549 |
2.99e-106 |
|
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: 341.98 E-value: 2.99e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 347 TKPRKVLILGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLTRDYVEQVIKAERPN 426
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 427 GVLLTFGGQTALNCGVELDRAGIFEKYNVKILGTPIKSIIETEDRKIFAERVAEIGEKVAPSEAVYSIQEALDAADRLGY 506
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 817639577 507 PVMARAAFSLGGLGSGFANNKEELISLAQQALPHS--NQLIIDKS 549
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKS 208
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
138-313 |
7.25e-104 |
|
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: 309.81 E-value: 7.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 138 ICAVDCGLKLNQIRCFLARGARVDLVPWNH------NLNPeefDGLFISNGPGDPVVCVDTVKQIKKvLIESEKPVFGIC 211
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTdaeeilKLDP---DGIFLSNGPGDPALLDEAIKTVRK-LLGKKIPIFGIC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 212 LGHQLLSTAIGCTTYKMKYGNRGHNLPCIHHSTGRCFMTSQNHGFAVDADTLPPDWEPLFTNANDNTNEGIIHKSKPYFS 291
Cdd:cd01744 77 LGHQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFS 156
|
170 180
....*....|....*....|..
gi 817639577 292 VQFHPEHTAGPQDLELLFDVFL 313
Cdd:cd01744 157 VQFHPEASPGPHDTEYLFDEFL 178
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
350-549 |
1.65e-94 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 310.88 E-value: 1.65e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 350 RKVLILGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLTRDYVEQVIKAERPNGVL 429
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 430 LTFGGQTALNCGVELDRAGIFEKYNVKILGTPIKSIIETEDRKIFAERVAEIGEKVAPSEAVYSIQEALDAADRLGYPVM 509
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 817639577 510 ARAAFSLGGLGSGFANNKEELISLAQQALPHS--NQLIIDKS 549
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEES 209
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
355-549 |
1.04e-87 |
|
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: 280.61 E-value: 1.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 355 LGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLTRDYVEQVIKAERPNGVLLTFGG 434
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 435 QTALNCGVELDRAGIFEkyNVKILGTPIKSIIETEDRKIFAERVAEIGEKVAPSEAVYSIQEALDAADRLGYPVMARAAF 514
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 817639577 515 SLGGLGSGFANNKEELISLAQQALPHS--NQLIIDKS 549
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDES 195
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-320 |
1.95e-68 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 225.45 E-value: 1.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVPSEtEYDEYKlpahfewtsgISVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:CHL00197 49 SYFEQIVTFTYPEIGNTGINLE-DIESVK----------IQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 81 RALTKKIRENGSILGRIV-QNL---------------PSP--------HSDYKFLDPNTRNLVAECSVKTTITYNQqgsp 136
Cdd:CHL00197 118 RALTQHLRRFGTMNGCISnQNLnlsylrakikesphmPSSdliprvttSSYYEWDEKSHPSFYLADNKRPHSSYQL---- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 137 RICAVDCGLKLNQIRCFLARGARVDLVP-------WNhNLNPeefDGLFISNGPGDPVVCVDTVKQIKKvLIESEKPVFG 209
Cdd:CHL00197 194 KIIVIDFGVKYNILRRLKSFGCSITVVPatspyqdIL-SYQP---DGILLSNGPGDPSAIHYGIKTVKK-LLKYNIPIFG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 210 ICLGHQLLSTAIGCTTYKMKYGNRGhnlpcIHHSTG---RCFMTSQNHGFAVDADTLPPDwePLFT---NANDNTNEGII 283
Cdd:CHL00197 269 ICMGHQILSLALEAKTFKLKFGHRG-----LNHPSGlnqQVEITSQNHGFAVNLESLAKN--KFYIthfNLNDGTVAGIS 341
|
330 340 350
....*....|....*....|....*....|....*..
gi 817639577 284 HKSKPYFSVQFHPEHTAGPQDLELLFDVFLETVKENK 320
Cdd:CHL00197 342 HSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSK 378
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
350-549 |
1.48e-66 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 233.32 E-value: 1.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 350 RKVLILGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLTRDYVEQVIKAERPNGVL 429
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 430 LTFGGQTALNCGVELDRAGIFEKYNVKILGTPIKSIIETEDRKIFAERVAEIGEKVAPSEAVYSIQEALDAADRLGYPVM 509
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 817639577 510 ARAAFSLGGLGSGFANNKEELISLAQQALPHS--NQLIIDKS 549
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQASpiHQCLLEES 209
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
141-314 |
3.99e-61 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 199.77 E-value: 3.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 141 VDCGL--KLNQIRCFLARGARVDLVPWNHNLN---PEEFDGLFISNGPGDPVVCVDTVKQIKKvLIESEKPVFGICLGHQ 215
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTPAEeilEENPDGIILSGGPGSPGAAGGAIEAIRE-ARELKIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 216 LLSTAIGCTTYKMK-YGNRGHNLPCIHHS------TGRCFMTSQNHGFAVDADTLPPDWEPLFTNANDNTNEGIIHKSKP 288
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDDGcglfygLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*.
gi 817639577 289 YFSVQFHPEHTAGPQDLELLFDVFLE 314
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
350-549 |
2.13e-55 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 201.55 E-value: 2.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 350 RKVLILGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLTRDYVEQVIKAERPNGVL 429
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 430 LTFGGQTALNCGVELDRAGIFEKYNVKILGTPIKSIIETEDRKIFAERVAEIGEKVAPSEAVYSIQEALDAADRLG-YPV 508
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 817639577 509 MARAAFSLGGLGSGFANNKEELISLAQQAL--PHSNQLIIDKS 549
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLaaSITSQVLVEKS 226
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
1-309 |
2.81e-52 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 183.64 E-value: 2.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVpsetEYDEyklpahfEWTSGISVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:PLN02771 99 SYAGQFVLMTNPHIGNTGV----NFDD-------EESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 81 RALTKKIRENGSILGriVQNLPSPHSDYKFL------DPNTRNLVAECSVKTTITYNQQGSP--------------RICA 140
Cdd:PLN02771 168 RAITRRLREDGSLIG--VLSTEDSKTDEELLkmsrswDIVGIDLISGVSCKSPYEWVDKTNPewdfntnsrdgesyHVIA 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 141 VDCGLKLNQIRCFLARGARVDLVPWNH------NLNPeefDGLFISNGPGDPVVCVDTVKQIKKVLieSEKPVFGICLGH 214
Cdd:PLN02771 246 YDFGIKHNILRRLASYGCKITVVPSTWpasealKMKP---DGVLFSNGPGDPSAVPYAVETVKELL--GKVPVFGICMGH 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 215 QLLSTAIGCTTYKMKYGNRGHNLPCIHHSTGRCFMTSQNHGFAVDADTLPPDWEPLFTNANDNTNEGIIHKSKPYFSVQF 294
Cdd:PLN02771 321 QLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQY 400
|
330
....*....|....*
gi 817639577 295 HPEHTAGPQDLELLF 309
Cdd:PLN02771 401 HPEASPGPHDSDNAF 415
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
330-548 |
5.07e-49 |
|
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: 182.51 E-value: 5.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 330 KINEMFS-YTVKPDSVPATKPRKVLILGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYF 408
Cdd:TIGR01369 534 QTPYLYStYEGERDDVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYF 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 409 LPLTRDYVEQVIKAERPNGVLLTFGGQTALNCGVELDRAGifekynVKILGTPIKSIIETEDRKIFAERVAEIGEKVAPS 488
Cdd:TIGR01369 614 EPLTFEDVMNIIELEKPEGVIVQFGGQTPLNLAKALEEAG------VPILGTSPESIDRAEDREKFSELLDELGIPQPKW 687
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 817639577 489 EAVYSIQEALDAADRLGYPVMARAAFSLGGLGSGFANNKEELISLAQQALPHSNQ--LIIDK 548
Cdd:TIGR01369 688 KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDK 749
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
334-548 |
7.69e-48 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 179.14 E-value: 7.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 334 MFS-YTVKPDSVPATKPrKVLILGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLT 412
Cdd:PRK05294 539 YYStYEEECESNPSDRK-KVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLT 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 413 RDYVEQVIKAERPNGVLLTFGGQTALNCGVELdragifEKYNVKILGTPIKSIIETEDRKIFAERVAEIGEKVAPSEAVY 492
Cdd:PRK05294 618 LEDVLEIIEKEKPKGVIVQFGGQTPLKLAKAL------EAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTAT 691
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 817639577 493 SIQEALDAADRLGYPVMARAAFSLGGLGSGFANNKEELISLAQQALPHSNQ--LIIDK 548
Cdd:PRK05294 692 SVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDhpVLIDK 749
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
336-548 |
7.21e-45 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 170.15 E-value: 7.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 336 SYTVKPDSVPATKPRKVLILGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLTRDY 415
Cdd:PRK12815 542 TYFGESEAEPSSEKKKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLED 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 416 VEQVIKAERPNGVLLTFGGQTALNCGVELdragifEKYNVKILGTPIKSIIETEDRKIFAERVAEIGEKVAPSEAVYSIQ 495
Cdd:PRK12815 622 VLNVAEAENIKGVIVQFGGQTAINLAKGL------EEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEE 695
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 817639577 496 EALDAADRLGYPVMARAAFSLGGLGSGFANNKEELISLAQQALPHSNQLIIDK 548
Cdd:PRK12815 696 EAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPILIDQ 748
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-97 |
1.30e-44 |
|
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: 153.64 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVPSEtEYDEyklpahfewtSGISVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:pfam00988 41 SYAGQIVVFTYPLIGNYGVNPE-DFES----------DKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDT 109
|
90
....*....|....*..
gi 817639577 81 RALTKKIRENGSILGRI 97
Cdd:pfam00988 110 RALTRKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-97 |
4.23e-41 |
|
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: 144.44 E-value: 4.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 1 SYRAQILVLTYPIIGNYGVPSETeydeyklpahFEwTSGISVSGLVVGEICETPSHWRQDKTLSDWMREQGVPGISGIDT 80
Cdd:smart01097 45 SYAGQIVVFTYPLIGNYGVNDED----------FE-SDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDT 113
|
90
....*....|....*..
gi 817639577 81 RALTKKIRENGSILGRI 97
Cdd:smart01097 114 RALTRKLREKGAMKGVI 130
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
336-538 |
2.58e-36 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 144.54 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 336 SYTVKPDSVPATKpRKVLILGSGGLSIGQAGEFDYSGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLTRDY 415
Cdd:PLN02735 562 SYDGECESAPTNK-KKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVED 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 416 VEQVIKAERPNGVLLTFGGQTALNCGVELDRAgiFEKY---------NVKILGTPIKSIIETEDRKIFAERVAEIGEKVA 486
Cdd:PLN02735 641 VLNVIDLERPDGIIVQFGGQTPLKLALPIQKY--LDKNpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQP 718
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 817639577 487 PSEAVYSIQEALDAADRLGYPVMARAAFSLGGLGSGFANNKEELISLAQQAL 538
Cdd:PLN02735 719 KGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAV 770
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
470-549 |
3.34e-23 |
|
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: 97.76 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 470 DRKIFAERVAEIGEKVAPSEAVY--SIQEALDAADRLGYPVMARAAFSLGGLGSGFANNKEELISLAQQALPHS------ 541
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
....*...
gi 817639577 542 NQLIIDKS 549
Cdd:pfam02786 81 PQVLVEKS 88
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
157-297 |
1.14e-20 |
|
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: 89.52 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 157 GARVDLVPwNHNLNPEE-----FDGLFISNGPGDPV---VCVDTVKQIKKvliesEKPVFGICLGHQLLSTAIGCTTYKM 228
Cdd:cd01743 22 GAEVVVVR-NDEITLEElellnPDAIVISPGPGHPEdagISLEIIRALAG-----KVPILGVCLGHQAIAEAFGGKVVRA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 229 KYGNRGHNLPcIHHSTGRCFMTSQN-------HGFAVDADTLPPDWEplFTNANDntnEGII----HKSKPYFSVQFHPE 297
Cdd:cd01743 96 PEPMHGKTSE-IHHDGSGLFKGLPQpftvgryHSLVVDPDPLPDLLE--VTASTE---DGVImalrHRDLPIYGVQFHPE 169
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
137-300 |
3.76e-19 |
|
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: 86.54 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 137 RICAVDC----GLKLNQIRCFLA-RGARVDLV------PWNHNLNPEEFDGLFISNGPG---DPVVCVDTVKQIKKVLIE 202
Cdd:COG0518 1 KILILDHdpfgGQYPGLIARRLReAGIELDVLrvyageILPYDPDLEDPDGLILSGGPMsvyDEDPWLEDEPALIREAFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 203 SEKPVFGICLGHQLLSTAIGCTTYKMKYGNRG-------------HNLPcihhSTGRCFMTsqnHGFAVdaDTLPPDWEP 269
Cdd:COG0518 81 LGKPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelteadplfAGLP----DEFTVWMS---HGDTV--TELPEGAEV 151
|
170 180 190
....*....|....*....|....*....|.
gi 817639577 270 LFTNANDnTNEGIIHkSKPYFSVQFHPEHTA 300
Cdd:COG0518 152 LASSDNC-PNQAFRY-GRRVYGVQFHPEVTH 180
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
159-297 |
9.12e-17 |
|
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: 78.54 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 159 RVDLVPWNHnLNPEEFDGLFISNGPGDPV---VCVDTVKQIKKvliesEKPVFGICLGHQllstAIGCTtykmkYGNRGH 235
Cdd:COG0512 29 RNDEITLEE-IEALAPDGIVLSPGPGTPEeagISLEVIRAFAG-----KIPILGVCLGHQ----AIGEA-----FGGKVV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 236 NLPCIHHstGRCFMTSQN-----------------HGFAVDADTLPPDWEPlftNANDNTNE--GIIHKSKPYFSVQFHP 296
Cdd:COG0512 94 RAPEPMH--GKTSPITHDgsglfaglpnpftatryHSLVVDRETLPDELEV---TAWTEDGEimGIRHRELPIEGVQFHP 168
|
.
gi 817639577 297 E 297
Cdd:COG0512 169 E 169
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
171-298 |
1.15e-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: 72.28 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 171 PEEFDGLFISNGPGDPVVC-----VDTVKQIKKVlIESEKPVFGICLGHQLLSTAIGCTTYKMKYG-----------NRG 234
Cdd:cd01741 44 LDDYDGLVILGGPMSVDEDdypwlKKLKELIRQA-LAAGKPVLGICLGHQLLARALGGKVGRNPKGweigwfpvtltEAG 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817639577 235 HNLPcIHHSTGRCFMTSQNHGFAVDAdtLPPDWEPLFTNAnDNTNEGIIhKSKPYFSVQFHPEH 298
Cdd:cd01741 123 KADP-LFAGLPDEFPVFHWHGDTVVE--LPPGAVLLASSE-ACPNQAFR-YGDRALGLQFHPEE 181
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
169-334 |
1.42e-14 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 76.29 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 169 LNPEEfdgLFISNGPGDPV---VCVDTVKQIKKVLiesekPVFGICLGHQLLSTAIGCTTYKMKYGNRGHNLPCIHHSTG 245
Cdd:PRK14607 43 LNPSH---IVISPGPGRPEeagISVEVIRHFSGKV-----PILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 246 rCFMTSQN-------HGFAVDADTLPPDWEPLfTNANDNTNEGIIHKSKPYFSVQFHPEhTAGPQDLELLFDVFLetvke 318
Cdd:PRK14607 115 -LFRGIPNptvatryHSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPE-SILTEEGKRILKNFL----- 186
|
170
....*....|....*.
gi 817639577 319 NKTNTSISLKDKINEM 334
Cdd:PRK14607 187 NYQREEIDIKSYLKKL 202
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
172-297 |
5.33e-13 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 68.15 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 172 EEFDGLFISNGPGDPV---VCVDTVKqikkVLIESEKPVFGICLGHQLLSTAIGCTTYKMKYGNRGHNLPCIHHSTG--- 245
Cdd:PRK07765 45 AQFDGVLLSPGPGTPEragASIDMVR----ACAAAGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGvla 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 817639577 246 ---RCFMTSQNHGFAVDADTLPPDWEplftnANDNTNEGII----HKSKPYFSVQFHPE 297
Cdd:PRK07765 121 glpDPFTATRYHSLTILPETLPAELE-----VTARTDSGVImavrHRELPIHGVQFHPE 174
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
169-308 |
5.35e-13 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 67.46 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 169 LNPeefDGLFISNGPGDPV---VCVDTVKQIKKvliesEKPVFGICLGHQLLSTAIGCT-----------TYKMKYGNRG 234
Cdd:PRK05670 42 LNP---DAIVLSPGPGTPAeagISLELIREFAG-----KVPILGVCLGHQAIGEAFGGKvvrakeimhgkTSPIEHDGSG 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817639577 235 --HNLPcihhstgRCFMTSQNHGFAVDADTLPPDWEPLFTnANDNTNEGIIHKSKPYFSVQFHPEHTAGPQDLELL 308
Cdd:PRK05670 114 ifAGLP-------NPFTVTRYHSLVVDRESLPDCLEVTAW-TDDGEIMGVRHKELPIYGVQFHPESILTEHGHKLL 181
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
153-314 |
1.03e-11 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 64.11 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 153 FLARGARVdLVPWNHNLNPEEFDGL-----FISNGPGDPVVCVDTVKQIKKvlIESEKPVFGICLGHQLLSTAIGCTTYK 227
Cdd:PRK06774 19 FCELGTEV-MVKRNDELQLTDIEQLapshlVISPGPCTPNEAGISLAVIRH--FADKLPILGVCLGHQALGQAFGARVVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 228 MKYGNRGHNlPCIHHSTGRCF-------MTSQNHGFAVDADTLPPDWE-PLFTNANDNTNE--GIIHKSKPYFSVQFHPE 297
Cdd:PRK06774 96 ARQVMHGKT-SAICHSGQGVFrglnqplTVTRYHSLVIAADSLPGCFElTAWSERGGEMDEimGIRHRTLPLEGVQFHPE 174
|
170
....*....|....*..
gi 817639577 298 HTAGPQDLELLfDVFLE 314
Cdd:PRK06774 175 SILSEQGHQLL-DNFLK 190
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
172-314 |
2.55e-11 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 62.56 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 172 EEFDGLFISNGPGdpvvcVDTVKQIKKVLIESEKPVFGICLGHQLLSTAIGCTTYKMKYGNRGH-NLPCIHHST-----G 245
Cdd:PRK00758 40 AFEDGLILSGGPD-----IERAGNCPEYLKELDVPILGICLGHQLIAKAFGGEVGRGEYGEYALvEVEILDEDDilkglP 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817639577 246 RCFMTSQNHgfavdAD---TLPPDWEPLftnANDNT--NEGIIHKSKPYFSVQFHPE--HTagpQDLELLFDVFLE 314
Cdd:PRK00758 115 PEIRVWASH-----ADevkELPDGFEIL---ARSDIceVEAMKHKEKPIYGVQFHPEvaHT---EYGEEIFKNFLE 179
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
201-297 |
3.54e-11 |
|
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: 63.04 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 201 IESEKPVFGICLGHQLLSTAIGCTTY---KMKYGNRGHNLPC------IHHS----TGRCF--MTSQN-------HGFAV 258
Cdd:pfam07722 102 LARGKPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyaPSHAvnvePGSLLasLLGSEefrvnslHHQAI 181
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 817639577 259 daDTLPPDWEPLFTnANDNTNEGIIHKSKPYF--SVQFHPE 297
Cdd:pfam07722 182 --DRLAPGLRVEAV-APDGTIEAIESPNAKGFalGVQWHPE 219
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
148-315 |
1.21e-10 |
|
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: 60.96 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 148 NQIRCFLARGARVdLVPWNHNLNPEEFDGLF-----ISNGPGDPVVCVDTVKQIKKvlIESEKPVFGICLGHQLLSTAIG 222
Cdd:TIGR00566 14 NLVQYFCELGAEV-VVKRNDSLTLQEIEALLpllivISPGPCTPNEAGISLEAIRH--FAGKLPILGVCLGHQAMGQAFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 223 CTTYKMKYGNRGHNLPCIHHSTGRC------FMTSQNHGFAVDADTLPPDWEPLFTNANDNTNEGIIHKSKPYFSVQFHP 296
Cdd:TIGR00566 91 GDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHP 170
|
170
....*....|....*....
gi 817639577 297 EHTAGPQDLELLfDVFLET 315
Cdd:TIGR00566 171 ESILSEQGHQLL-ANFLHR 188
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
150-217 |
1.58e-10 |
|
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: 58.38 E-value: 1.58e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817639577 150 IRCFLARGARVDLVPWNH-----NLNPEEFDGLFISNGPGDP---VVCVDTVKQIKKVlIESEKPVFGICLGHQLL 217
Cdd:cd01653 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPddlARDEALLALLREA-AAAGKPILGICLGAQLL 92
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
162-308 |
1.66e-10 |
|
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: 60.41 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 162 LVPWNHNL------NPEefdGLFISNGPgDPVVCVDTVKQIKKVLiESEKPVFGICLGHQLLSTAIG---CTTYKMKYGN 232
Cdd:TIGR00888 27 LVPNTTPLeeirekNPK---GIILSGGP-SSVYAENAPRADEKIF-ELGVPVLGICYGMQLMAKQLGgevGRAEKREYGK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817639577 233 ---RGHNLPCIHHSTGRCFMTSQNHGFAVDAdtLPPDWEPLFTNANdNTNEGIIHKSKPYFSVQFHPEHTAGPQDLELL 308
Cdd:TIGR00888 102 aelEILDEDDLFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDN-CPVAAMAHEEKPIYGVQFHPEVTHTEYGNELL 177
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
157-299 |
1.98e-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: 59.86 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 157 GARVDLVPWNHNLNPEE---FDGLFISNGPgdPVVCVDTVKQIKKVLIESEKPVFGICLGHQLLSTAIGCTTYKMKYGNR 233
Cdd:cd01742 22 GVYSEILPNTTPLEEIKlknPKGIILSGGP--SSVYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALGGKVERGDKREY 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 817639577 234 GHNLPCIHHSTG---------RCFMtsqNHGFAVDAdtLPPDWEPLFTNANdNTNEGIIHKSKPYFSVQFHPE--HT 299
Cdd:cd01742 100 GKAEIEIDDSSPlfeglpdeqTVWM---SHGDEVVK--LPEGFKVIASSDN-CPVAAIANEEKKIYGVQFHPEvtHT 170
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
150-217 |
5.34e-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: 56.44 E-value: 5.34e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 817639577 150 IRCFLARGARVDLVPWNH-----NLNPEEFDGLFISNGPGDPVVCVDTVKQIKKV--LIESEKPVFGICLGHQLL 217
Cdd:cd03128 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPDDLAWDEALLALLreAAAAGKPVLGICLGAQLL 92
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
157-300 |
5.77e-10 |
|
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: 60.41 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 157 GARVdlVPWNHNLNPEEFDGLFIS-NG---PGDPVV-----CVDTVKQIKKVLIESEK-----PVFGICLGHQLLS---- 218
Cdd:cd01747 33 GARV--VPIWINESEEYYDKLFKSiNGilfPGGAVDidtsgYARTAKIIYNLALERNDagdyfPVWGTCLGFELLTylts 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 219 ------TAIGCTTYKMKYGNRGHNLPC----------IHHSTGRCFmTSQNHGFAV-----DADTLPPDWEP-LFTNAND 276
Cdd:cd01747 111 getlllEATEATNSALPLNFTEDALQSrlfkrfppdlLKSLATEPL-TMNNHRYGIspenfTENGLLSDFFNvLTTNDDW 189
|
170 180
....*....|....*....|....*..
gi 817639577 277 NTNEGII---HKSKPYFSVQFHPEHTA 300
Cdd:cd01747 190 NGVEFIStveAYKYPIYGVQWHPEKNA 216
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
169-308 |
1.46e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 57.58 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 169 LNPEEfdgLFISNGPGDPVVCVDTVKQIKKvlIESEKPVFGICLGHQLLSTAIGCTTYKMKYGNRGHNLPCIHhsTGRCF 248
Cdd:PRK08857 42 LNPTH---LVISPGPCTPNEAGISLQAIEH--FAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSV 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 817639577 249 MTSQN--------HGFAVDADTLPPDWE-PLFTNANDNTNE---GIIHKSKPYFSVQFHPEHTAGPQDLELL 308
Cdd:PRK08857 115 FKGLNnpltvtryHSLVVKNDTLPECFElTAWTELEDGSMDeimGFQHKTLPIEAVQFHPESIKTEQGHQLL 186
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
148-308 |
1.47e-09 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 57.62 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 148 NQIRCFLARGARVdLVPWNHNLNPEEFDGL-----FISNGPGDPV---VCVDTVKQIKKVLiesekPVFGICLGHQLLST 219
Cdd:PRK08007 14 NLYQYFCELGADV-LVKRNDALTLADIDALkpqkiVISPGPCTPDeagISLDVIRHYAGRL-----PILGVCLGHQAMAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 220 AIGCTTYKMKYGNRGHNLPCIHHSTG------RCFMTSQNHGFAVDADTLPPDWEplfTNANDNTNE--GIIHKSKPYFS 291
Cdd:PRK08007 88 AFGGKVVRAAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEG 164
|
170
....*....|....*..
gi 817639577 292 VQFHPEHTAGPQDLELL 308
Cdd:PRK08007 165 VQFHPESILSEQGHQLL 181
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
168-317 |
1.56e-08 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 54.81 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 168 NLNPeefDGLFISNGPGDPVVCVDTVKQIKKvlIESEKPVFGICLGHQLLSTAIGCTTYKM------KYGNRGHNLPCIH 241
Cdd:PRK07649 41 NMKP---DFLMISPGPCSPNEAGISMEVIRY--FAGKIPIFGVCLGHQSIAQVFGGEVVRAerlmhgKTSLMHHDGKTIF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 242 HSTGRCFMTSQNHGFAVDADTLPPDWEplftnANDNTNEG----IIHKSKPYFSVQFHPEHTAGPQDLELLFDvFLETVK 317
Cdd:PRK07649 116 SDIPNPFTATRYHSLIVKKETLPDCLE-----VTSWTEEGeimaIRHKTLPIEGVQFHPESIMTSHGKELLQN-FIRKYS 189
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
201-312 |
2.29e-08 |
|
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: 54.12 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 201 IESEKPVFGICLGHQLLSTAIGCTTYkmkygnrghnlpcihhstgRCFMTSQNHGFAVDAdtLPPDWEPLFTnANDNTNE 280
Cdd:cd01745 97 LERGKPILGICRGMQLLNVALGGTLY-------------------QDIRVNSLHHQAIKR--LADGLRVEAR-APDGVIE 154
|
90 100 110
....*....|....*....|....*....|....
gi 817639577 281 GIIHKSKPY-FSVQFHPEHTAGPQDLEL-LFDVF 312
Cdd:cd01745 155 AIESPDRPFvLGVQWHPEWLADTDPDSLkLFEAF 188
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
172-297 |
2.55e-08 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 53.97 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 172 EEFDGLFISNGPGDPVVCVDTVKQIKKVLieSEKPVFGICLGHQLLSTAIGCTTYkmkygnrghNLPCIHHSTGRCFMTS 251
Cdd:PRK06895 42 ENFSHILISPGPDVPRAYPQLFAMLERYH--QHKSILGVCLGHQTLCEFFGGELY---------NLNNVRHGQQRPLKVR 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817639577 252 QN----------------HGFAVDADTLPpdwEPLFTNA--NDNTNEGIIHKSKPYFSVQFHPE 297
Cdd:PRK06895 111 SNsplfdglpeefniglyHSWAVSEENFP---TPLEITAvcDENVVMAMQHKTLPIYGVQFHPE 171
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
176-297 |
1.13e-07 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 52.88 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 176 GLFISNGPGDPV---VCVDTVKQIKKVLiesekPVFGICLGHQLLSTAIGCTTYKMKYG-NRGHNLPCIHHSTG------ 245
Cdd:PLN02335 65 GVLISPGPGTPQdsgISLQTVLELGPLV-----PLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYDEKGeeglfs 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 817639577 246 ---RCFMTSQNHGFAVDADTLPPDWEPLFTNANDNTNEGIIHKSKPYFS-VQFHPE 297
Cdd:PLN02335 140 glpNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPE 195
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
168-297 |
2.42e-07 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 51.27 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 168 NLNPEefdGLFISNGPGDPV---VCVDTVKQIKkvlieSEKPVFGICLGHQLLSTAIGCTTYKMKYGNRGhNLPCIHHST 244
Cdd:CHL00101 41 NLNIR---HIIISPGPGHPRdsgISLDVISSYA-----PYIPILGVCLGHQSIGYLFGGKIIKAPKPMHG-KTSKIYHNH 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 817639577 245 GRCFMTSQN-------HGFAVDADTLPpdwEPLFTNAndNTNEGII----HKSKPY-FSVQFHPE 297
Cdd:CHL00101 112 DDLFQGLPNpftatryHSLIIDPLNLP---SPLEITA--WTEDGLImacrHKKYKMlRGIQFHPE 171
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
174-359 |
2.70e-06 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 50.23 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 174 FDGLFISNGPGDPVvCVDTVKQIKKVLIESEK-PVFGICLGHQLLSTAIGCTTYKMKYGNRGHnLPCIHHSTGRCFM--- 249
Cdd:PLN02889 132 FDNIVISPGPGSPT-CPADIGICLRLLLECRDiPILGVCLGHQALGYVHGARIVHAPEPVHGR-LSEIEHNGCRLFDdip 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 250 TSQNHGFAV--------DADTLPPDWEPLFTNANDNTNE----------------------------------------- 280
Cdd:PLN02889 210 SGRNSGFKVvryhslviDAESLPKELVPIAWTSSSDTLSflesqksglvpdayesqigqsgssdpfssklkngtswpssh 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 281 -----------GIIHKSKPYFSVQFHPEHTA---GPQdlelLFDVFLE-TVKENKTNTSISLKDKINEMFSYTVKPDsvp 345
Cdd:PLN02889 290 sermqngkilmGIMHSTRPHYGLQFHPESIAtcyGRQ----IFKNFREiTQDYWLRLRSTSLRRRNSNLTANMQVPD--- 362
|
250
....*....|....
gi 817639577 346 ATKPRKVLILGSGG 359
Cdd:PLN02889 363 ASQLFKVPRRGQLG 376
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
451-537 |
2.96e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 49.98 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 451 EKYNVKILGtPIKSIIETEDRKIFAERV-AEIGEKVAP--SEAVYSIQEALDAADRLGYPVMARAAFSLGGLGSGFANNK 527
Cdd:PRK08654 96 EKAGIVFIG-PSSDVIEAMGSKINAKKLmKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSE 174
|
90
....*....|....*..
gi 817639577 528 EELI-------SLAQQA 537
Cdd:PRK08654 175 EELEdaiestqSIAQSA 191
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
461-530 |
2.74e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 46.56 E-value: 2.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817639577 461 PIKSIIETEDRKIFAER-VAEIGEKVAP--SEAVYSIQEALDAADRLGYPVMARAAFSLGGLGSGFANNKEEL 530
Cdd:PRK06111 105 PSADIIAKMGSKIEARRaMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEL 177
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
476-538 |
4.86e-05 |
|
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: 45.25 E-value: 4.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817639577 476 ERVAEIGEKVAPSEAVYSIQEALDAADRLGYPVMARAAFSLGGLGSGFANNKEELISLAQQAL 538
Cdd:COG0439 60 EALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
447-537 |
7.61e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 45.48 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 447 AGIFEKYNVKILGtPIKSIIETEDRKIFAERVA-EIGEKVAP-SEA-VYSIQEALDAADRLGYPVMARAAFSLGGLGSGF 523
Cdd:PRK07178 91 AEICAERGIKFIG-PSAEVIRRMGDKTEARRAMiKAGVPVTPgSEGnLADLDEALAEAERIGYPVMLKATSGGGGRGIRR 169
|
90 100
....*....|....*....|.
gi 817639577 524 ANNKEEL-------ISLAQQA 537
Cdd:PRK07178 170 CNSREELeqnfprvISEATKA 190
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
447-532 |
9.77e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 45.09 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 447 AGIFEKYNVKILGtPIKSIIETEDRKIFAERV-AEIGEKVAP-SE-AVYSIQEALDAADRLGYPVMARAAFSLGGLGSGF 523
Cdd:PRK05586 92 AKMCKECNIVFIG-PDSETIELMGNKSNAREImIKAGVPVVPgSEgEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRI 170
|
....*....
gi 817639577 524 ANNKEELIS 532
Cdd:PRK05586 171 VRSEEELIK 179
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
461-530 |
1.07e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 44.75 E-value: 1.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817639577 461 PIKSIIETEDRKIFAERVA-EIGEKVAPSE--AVYSIQEALDAADRLGYPVMARAAFSLGGLGSGFANNKEEL 530
Cdd:PRK12833 108 PDAQTIRTMGDKARARRTArRAGVPTVPGSdgVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQL 180
|
|
| PRK08250 |
PRK08250 |
glutamine amidotransferase; Provisional |
170-222 |
1.27e-04 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181323 [Multi-domain] Cd Length: 235 Bit Score: 43.80 E-value: 1.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 817639577 170 NPEEFDGLFISNGPGDPVVCVDT---------VKQIKKVlIESEKPVFGICLGHQLLSTAIG 222
Cdd:PRK08250 42 NADGFDLLIVMGGPQSPRTTREEcpyfdskaeQRLINQA-IKAGKAVIGVCLGAQLIGEALG 102
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
472-537 |
1.51e-04 |
|
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: 44.69 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817639577 472 KIFAERVA-EIGEKVAPS--EAVYSIQEALDAADRLGYPVMARAAFSLGGLGSGFANNKEELISLAQQA 537
Cdd:COG1038 119 KVAARAAAiEAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESA 187
|
|
| PfpI |
TIGR01382 |
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ... |
169-220 |
2.13e-04 |
|
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273591 [Multi-domain] Cd Length: 166 Bit Score: 42.02 E-value: 2.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 817639577 169 LNPEEFDGLFISNGPGDPVVCVDT-VKQIKKVLIESEKPVFGICLGHQLLSTA 220
Cdd:TIGR01382 56 VNPEEYDALVIPGGRAPEYLRLNNkAVRLVREFVEKGKPVAAICHGPQLLISA 108
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
490-537 |
2.48e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 43.64 E-value: 2.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 817639577 490 AVYSIQEALDAADRLGYPVMARAAFSLGGLGSGFANNKEELISLAQQA 537
Cdd:PRK08591 137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMA 184
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
449-533 |
3.00e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 43.58 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 449 IFEKYNVKILGTPIKSIIETEDRKIFAERVAEIGEKVAP-SE-AVYSIQEALDAADRLGYPVMARAAFSLGGLGSGFANN 526
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
....*..
gi 817639577 527 KEELISL 533
Cdd:PRK08462 176 ESDLENL 182
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
472-537 |
3.40e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 43.59 E-value: 3.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817639577 472 KIFAERVA-EIGEKVAPS--EAVYSIQEALDAADRLGYPVMARAAFSLGGLGSGFANNKEELISLAQQA 537
Cdd:PRK12999 120 KVAARNAAiKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERA 188
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
459-544 |
3.83e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 40.22 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 459 GTPIKSIIETEDRKIFAERVAEIGEKVAPSEAVYSIQEALDAADRLGYPVMARAAFSLGGLGSgfannkeELISLAQQAL 538
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGV-------RLCASVAEAA 168
|
....*.
gi 817639577 539 PHSNQL 544
Cdd:PRK02186 169 AHCAAL 174
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
193-217 |
5.72e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 38.19 E-value: 5.72e-03
10 20
....*....|....*....|....*
gi 817639577 193 VKQIKKVlIESEKPVFGICLGHQLL 217
Cdd:PRK13141 62 DEVIKEA-VASGKPLLGICLGMQLL 85
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
351-535 |
6.03e-03 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 39.10 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 351 KVLILGSGGlsigqagefdysGSQAIKAMREEKIQTILINPNIATVQTSKGLADKVYFLPLTRD--YVEQVI---KAERP 425
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPKVTDpnYIDRLLdicKKEKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817639577 426 NGVLLTFGGQTALNCGvELDRagiFEKYNVKILGTPiKSIIET-EDRKIFAERVAEIGEKVAPSEAVYSIQEAL--DAAD 502
Cdd:PRK12767 71 DLLIPLIDPELPLLAQ-NRDR---FEEIGVKVLVSS-KEVIEIcNDKWLTYEFLKENGIPTPKSYLPESLEDFKaaLAKG 145
|
170 180 190
....*....|....*....|....*....|...
gi 817639577 503 RLGYPVMARAAFSLGGLGSGFANNKEELISLAQ 535
Cdd:PRK12767 146 ELQFPLFVKPRDGSASIGVFKVNDKEELEFLLE 178
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
198-217 |
6.59e-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: 38.25 E-value: 6.59e-03
|
| |
