NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|145332705|ref|NP_001078218|]
View 

carbamoyl phosphate synthetase A [Arabidopsis thaliana]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02771 super family cl31930
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
1-344 0e+00

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


The actual alignment was detected with superfamily member PLN02771:

Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 688.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705   1 MAMATRTLGFVLPTSLSSQPSFDRRGGgFRVSVIRCSTSPLTFPTSGVVEKPWTSYNARLVLEDGSIWPAKSFGAPGTRI 80
Cdd:PLN02771   1 EAMATRPLGFVLPTSLSSQPSFDRRGG-VRVSVIRCSSSPLTSDGAGVVERPWKTSDARLVLEDGSVWKAKSFGARGTQV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  81 AELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDE------------------------------------- 123
Cdd:PLN02771  80 GEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEesrqcflaglvirslsistsnwrctktlgdylaerni 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 124 -----------------------------------LLQMSRSWDIVGIDLISDVSCKSPYEWVDKTNAEWDFNTNSRDGK 168
Cdd:PLN02771 160 mgiydvdtraitrrlredgsligvlstedsktdeeLLKMSRSWDIVGIDLISGVSCKSPYEWVDKTNPEWDFNTNSRDGE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 169 SYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMG 248
Cdd:PLN02771 240 SYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 249 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQ 328
Cdd:PLN02771 320 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQ 399
                        410
                 ....*....|....*.
gi 145332705 329 YHPEASPGPHDSDNAF 344
Cdd:PLN02771 400 YHPEASPGPHDSDNAF 415
 
Name Accession Description Interval E-value
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
1-344 0e+00

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 688.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705   1 MAMATRTLGFVLPTSLSSQPSFDRRGGgFRVSVIRCSTSPLTFPTSGVVEKPWTSYNARLVLEDGSIWPAKSFGAPGTRI 80
Cdd:PLN02771   1 EAMATRPLGFVLPTSLSSQPSFDRRGG-VRVSVIRCSSSPLTSDGAGVVERPWKTSDARLVLEDGSVWKAKSFGARGTQV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  81 AELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDE------------------------------------- 123
Cdd:PLN02771  80 GEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEesrqcflaglvirslsistsnwrctktlgdylaerni 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 124 -----------------------------------LLQMSRSWDIVGIDLISDVSCKSPYEWVDKTNAEWDFNTNSRDGK 168
Cdd:PLN02771 160 mgiydvdtraitrrlredgsligvlstedsktdeeLLKMSRSWDIVGIDLISGVSCKSPYEWVDKTNPEWDFNTNSRDGE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 169 SYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMG 248
Cdd:PLN02771 240 SYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 249 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQ 328
Cdd:PLN02771 320 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQ 399
                        410
                 ....*....|....*.
gi 145332705 329 YHPEASPGPHDSDNAF 344
Cdd:PLN02771 400 YHPEASPGPHDSDNAF 415
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
54-352 2.47e-177

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: 496.08  E-value: 2.47e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  54 TSYNARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDD----------- 122
Cdd:COG0505    1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDfesdrpwvagl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 123 ------------------------------------------------------------ELLQMSRSW-DIVGIDLISD 141
Cdd:COG0505   81 vvrelsrrpsnwrseesldeylkehgipgisgidtraltrhlrekgamkgvistgdldieELLEKARAApGMEGLDLVKE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 142 VSCKSPYEWvdktnaewdfntNSRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPG 221
Cdd:COG0505  161 VSTKEPYEW------------TEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 222 DPSAVPYAVETVKELLGK-VPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPG 300
Cdd:COG0505  229 DPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPA 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 145332705 301 -GVEVTHVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMK 352
Cdd:COG0505  309 tDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
58-353 1.25e-168

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: 474.04  E-value: 1.25e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705   58 ARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDD--------------- 122
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDaeskgihvsglvvre 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  123 ---------------------------------------------------------ELLQMSRSWDIVGIDLISDVSCK 145
Cdd:TIGR01368  81 lsdrysnwratesldqflkrhgipgiygvdtralvkkirekgtmkgvistedsndeeLVEKARVSPDITGINLVAEVSTK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  146 SPYEWVDktnaewdfntnsRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSA 225
Cdd:TIGR01368 161 EPYTWGQ------------RGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  226 VPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGG-VEV 304
Cdd:TIGR01368 229 VEPAIETIRKLLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGdLEV 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 145332705  305 THVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMKR 353
Cdd:TIGR01368 309 THVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
172-348 7.26e-114

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: 328.30  E-value: 7.26e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 172 VIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGK-VPVYGICMGHQ 250
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 251 LLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQYH 330
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160
                        170
                 ....*....|....*...
gi 145332705 331 PEASPGPHDSDNAFREFI 348
Cdd:cd01744  161 PEASPGPHDTEYLFDEFL 178
GATase pfam00117
Glutamine amidotransferase class-I;
176-350 1.02e-67

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 211.33  E-value: 1.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  176 DFG--IKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLG-KVPVYGICMGHQLL 252
Cdd:pfam00117   4 DNGdsFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLGHQLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  253 GQALGGKTFKMK-FGHHGGNHPVRNNR------TGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVM 325
Cdd:pfam00117  84 ALAFGGKVVKAKkFGHHGKNSPVGDDGcglfygLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLPIF 163
                         170       180
                  ....*....|....*....|....*
gi 145332705  326 SLQYHPEASPGPHDSDNAFREFIEL 350
Cdd:pfam00117 164 GVQFHPESILTPHGPEILFNFFIKA 188
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
57-122 2.42e-39

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: 135.96  E-value: 2.42e-39
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145332705    57 NARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDD 122
Cdd:smart01097   2 KAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDED 67
 
Name Accession Description Interval E-value
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
1-344 0e+00

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 688.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705   1 MAMATRTLGFVLPTSLSSQPSFDRRGGgFRVSVIRCSTSPLTFPTSGVVEKPWTSYNARLVLEDGSIWPAKSFGAPGTRI 80
Cdd:PLN02771   1 EAMATRPLGFVLPTSLSSQPSFDRRGG-VRVSVIRCSSSPLTSDGAGVVERPWKTSDARLVLEDGSVWKAKSFGARGTQV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  81 AELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDE------------------------------------- 123
Cdd:PLN02771  80 GEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEesrqcflaglvirslsistsnwrctktlgdylaerni 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 124 -----------------------------------LLQMSRSWDIVGIDLISDVSCKSPYEWVDKTNAEWDFNTNSRDGK 168
Cdd:PLN02771 160 mgiydvdtraitrrlredgsligvlstedsktdeeLLKMSRSWDIVGIDLISGVSCKSPYEWVDKTNPEWDFNTNSRDGE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 169 SYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMG 248
Cdd:PLN02771 240 SYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 249 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQ 328
Cdd:PLN02771 320 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQ 399
                        410
                 ....*....|....*.
gi 145332705 329 YHPEASPGPHDSDNAF 344
Cdd:PLN02771 400 YHPEASPGPHDSDNAF 415
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
54-352 2.47e-177

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: 496.08  E-value: 2.47e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  54 TSYNARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDD----------- 122
Cdd:COG0505    1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDfesdrpwvagl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 123 ------------------------------------------------------------ELLQMSRSW-DIVGIDLISD 141
Cdd:COG0505   81 vvrelsrrpsnwrseesldeylkehgipgisgidtraltrhlrekgamkgvistgdldieELLEKARAApGMEGLDLVKE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 142 VSCKSPYEWvdktnaewdfntNSRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPG 221
Cdd:COG0505  161 VSTKEPYEW------------TEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 222 DPSAVPYAVETVKELLGK-VPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPG 300
Cdd:COG0505  229 DPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPA 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 145332705 301 -GVEVTHVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMK 352
Cdd:COG0505  309 tDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
57-351 6.36e-173

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 484.96  E-value: 6.36e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  57 NARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDD-------------- 122
Cdd:PRK12564   4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDfesdrphakglivr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 123 ---------------------------------------------------------ELLQMSRSW-DIVGIDLISDVSC 144
Cdd:PRK12564  84 elsdipsnwrsemsldeylkengipgisgidtraltrklrekgamkgviatedfdaeELLEKARAFpGLLGLDLVKEVST 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 145 KSPYEWvdktnaewdfnTNSRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPS 224
Cdd:PRK12564 164 KEPYPW-----------PGPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPA 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 225 AVPYAVETVKELLG-KVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVE 303
Cdd:PRK12564 233 ALDYAIEMIRELLEkKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLE 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 145332705 304 VTHVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELM 351
Cdd:PRK12564 313 VTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
58-353 1.25e-168

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: 474.04  E-value: 1.25e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705   58 ARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDD--------------- 122
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDaeskgihvsglvvre 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  123 ---------------------------------------------------------ELLQMSRSWDIVGIDLISDVSCK 145
Cdd:TIGR01368  81 lsdrysnwratesldqflkrhgipgiygvdtralvkkirekgtmkgvistedsndeeLVEKARVSPDITGINLVAEVSTK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  146 SPYEWVDktnaewdfntnsRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSA 225
Cdd:TIGR01368 161 EPYTWGQ------------RGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  226 VPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGG-VEV 304
Cdd:TIGR01368 229 VEPAIETIRKLLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGdLEV 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 145332705  305 THVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMKR 353
Cdd:TIGR01368 309 THVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
57-352 3.19e-118

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 346.11  E-value: 3.19e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  57 NARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDD-------------- 122
Cdd:PRK12838   2 KAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDyeskqpqvkgvivy 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 123 ----------------ELLQMsrsWDIVGI-----------------------------------------DLISDVSCK 145
Cdd:PRK12838  82 elsregshyrakqsldDFLKE---WNIPGIsgvdtralvkhirekgtmkasitttddahafdqikalvlpkNVVAQVSTK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 146 SPYewvdktnaewdfntnSRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSA 225
Cdd:PRK12838 159 EPY---------------TYGNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKE 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 226 VPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPG-GVEV 304
Cdd:PRK12838 224 LQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGtPLSV 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 145332705 305 THVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMK 352
Cdd:PRK12838 304 RFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMME 351
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
172-348 7.26e-114

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: 328.30  E-value: 7.26e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 172 VIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGK-VPVYGICMGHQ 250
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 251 LLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQYH 330
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160
                        170
                 ....*....|....*...
gi 145332705 331 PEASPGPHDSDNAFREFI 348
Cdd:cd01744  161 PEASPGPHDTEYLFDEFL 178
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
58-358 5.78e-113

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 333.69  E-value: 5.78e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  58 ARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDD--------------E 123
Cdd:CHL00197   7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDiesvkiqvkgiiakN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 124 LLQMSRSW----------------DIVGID------------------------------------------LISDVSCK 145
Cdd:CHL00197  87 ICKSSSNWrqqeslvsylqrhkipFIFGIDtraltqhlrrfgtmngcisnqnlnlsylrakikesphmpssdLIPRVTTS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 146 SPYEWVDKTNAEWDFNTNSRDGKSY--KVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDP 223
Cdd:CHL00197 167 SYYEWDEKSHPSFYLADNKRPHSSYqlKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGDP 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 224 SAVPYAVETVKELLG-KVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRtgQVEISAQNHNYAVDPASL-PGG 301
Cdd:CHL00197 247 SAIHYGIKTVKKLLKyNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSGLNQ--QVEITSQNHGFAVNLESLaKNK 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145332705 302 VEVTHVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMKRSKQSS 358
Cdd:CHL00197 325 FYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSSK 381
GATase pfam00117
Glutamine amidotransferase class-I;
176-350 1.02e-67

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 211.33  E-value: 1.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  176 DFG--IKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLG-KVPVYGICMGHQLL 252
Cdd:pfam00117   4 DNGdsFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLGHQLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  253 GQALGGKTFKMK-FGHHGGNHPVRNNR------TGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVM 325
Cdd:pfam00117  84 ALAFGGKVVKAKkFGHHGKNSPVGDDGcglfygLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLPIF 163
                         170       180
                  ....*....|....*....|....*
gi 145332705  326 SLQYHPEASPGPHDSDNAFREFIEL 350
Cdd:pfam00117 164 GVQFHPESILTPHGPEILFNFFIKA 188
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
57-122 2.42e-39

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: 135.96  E-value: 2.42e-39
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145332705    57 NARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDD 122
Cdd:smart01097   2 KAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDED 67
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
60-122 1.06e-38

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: 133.99  E-value: 1.06e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145332705   60 LVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDD 122
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPED 63
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
182-332 5.05e-30

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: 113.40  E-value: 5.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 182 NILRRLSSYGCQITVVPSTFPAAEALK-MNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKT 260
Cdd:cd01743   13 NLVQYLRELGAEVVVVRNDEITLEELElLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGHQAIAEAFGGKV 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332705 261 FKMKFGHHGGNHPVRNNRTG------QVEISAQNHNYAVDPASLPGGVEVTHVNlNDGSCAGLSFPEMNVMSLQYHPE 332
Cdd:cd01743   93 VRAPEPMHGKTSEIHHDGSGlfkglpQPFTVGRYHSLVVDPDPLPDLLEVTAST-EDGVIMALRHRDLPIYGVQFHPE 169
PRK05670 PRK05670
anthranilate synthase component II; Provisional
182-332 7.85e-25

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 99.43  E-value: 7.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 182 NILRRLSSYGCQITVVPSTFPA-AEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKT 260
Cdd:PRK05670  14 NLVQYLGELGAEVVVYRNDEITlEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCLGHQAIGEAFGGKV 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145332705 261 FKMKFGHHGGNHPVRNNRTG-------QVEIsAQNHNYAVDPASLPGGVEVTHVnLNDGSCAGLSFPEMNVMSLQYHPE 332
Cdd:PRK05670  94 VRAKEIMHGKTSPIEHDGSGifaglpnPFTV-TRYHSLVVDRESLPDCLEVTAW-TDDGEIMGVRHKELPIYGVQFHPE 170
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
182-332 4.59e-23

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: 94.72  E-value: 4.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 182 NILRRLSSYGCQITVVPST-FPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKT 260
Cdd:COG0512   13 NLVQYLGELGAEVVVVRNDeITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGHQAIGEAFGGKV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 261 FKMKFGHHGGNHPVRNNRTG---------QVeisAQNHNYAVDPASLPGGVEVTHVNlNDGSCAGLSFPEMNVMSLQYHP 331
Cdd:COG0512   93 VRAPEPMHGKTSPITHDGSGlfaglpnpfTA---TRYHSLVVDRETLPDELEVTAWT-EDGEIMGIRHRELPIEGVQFHP 168

                 .
gi 145332705 332 E 332
Cdd:COG0512  169 E 169
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
196-348 1.96e-22

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 98.25  E-value: 1.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 196 VVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVR 275
Cdd:PRK14607  30 VRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPID 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145332705 276 NNRTG------QVEISAQNHNYAVDPASLPGGVEVThVNLNDGSCAGLSFPEMNVMSLQYHPEaSPGPHDSDNAFREFI 348
Cdd:PRK14607 110 HNGKGlfrgipNPTVATRYHSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPE-SILTEEGKRILKNFL 186
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
182-333 1.16e-16

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: 77.14  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  182 NILRRLSSYGCQITVV---PSTFPAAEALKmnPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGG 258
Cdd:TIGR00566  14 NLVQYFCELGAEVVVKrndSLTLQEIEALL--PLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQAFGG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  259 KTFKMKFGHHGGNHPVRNNRTGQVE------ISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQYHPE 332
Cdd:TIGR00566  92 DVVRANTVMHGKTSEIEHNGAGIFRglfnplTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPE 171

                  .
gi 145332705  333 A 333
Cdd:TIGR00566 172 S 172
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
204-333 2.10e-16

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 76.49  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 204 AEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVE 283
Cdd:PRK08007  37 ADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFR 116
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145332705 284 ------ISAQNHNYAVDPASLPGGVEVTHVNlNDGSCAGLSFPEMNVMSLQYHPEA 333
Cdd:PRK08007 117 glanplTVTRYHSLVVEPDSLPACFEVTAWS-ETREIMGIRHRQWDLEGVQFHPES 171
PLN02335 PLN02335
anthranilate synthase
182-333 2.80e-16

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 76.76  E-value: 2.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 182 NILRRLSSYGCQITVVPSTFPAAEALK-MNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKT 260
Cdd:PLN02335  33 NLCQYMGELGCHFEVYRNDELTVEELKrKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 261 FKMKFG-HHGGNHPVRNNRTGQVEI---------SAQNHNYAVDPASLPG-GVEVTHVNlNDGSCAGLSFPEM-NVMSLQ 328
Cdd:PLN02335 113 VRSPFGvMHGKSSPVHYDEKGEEGLfsglpnpftAGRYHSLVIEKDTFPSdELEVTAWT-EDGLIMAARHRKYkHIQGVQ 191

                 ....*
gi 145332705 329 YHPEA 333
Cdd:PLN02335 192 FHPES 196
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
208-333 2.16e-15

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 73.74  E-value: 2.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 208 KMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTG------Q 281
Cdd:PRK06774  41 QLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGvfrglnQ 120
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145332705 282 VEISAQNHNYAVDPASLPGGVEVTHVNLNDGS---CAGLSFPEMNVMSLQYHPEA 333
Cdd:PRK06774 121 PLTVTRYHSLVIAADSLPGCFELTAWSERGGEmdeIMGIRHRTLPLEGVQFHPES 175
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
204-358 7.65e-15

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 72.14  E-value: 7.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 204 AEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVE 283
Cdd:PRK07649  37 SDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFS 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 284 ------ISAQNHNYAVDPASLPGGVEVThVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDnAFREFIELMKRSKQS 357
Cdd:PRK07649 117 dipnpfTATRYHSLIVKKETLPDCLEVT-SWTEEGEIMAIRHKTLPIEGVQFHPESIMTSHGKE-LLQNFIRKYSPSVTS 194

                 .
gi 145332705 358 S 358
Cdd:PRK07649 195 C 195
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
182-333 6.77e-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: 69.20  E-value: 6.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 182 NILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYA-VETVKELL-----GKVPVYGICMGHQLLGQA 255
Cdd:cd01741   18 DLLREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEDDYPwLKKLKELIrqalaAGKPVLGICLGHQLLARA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 256 LGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQN----------HNYAVDpaSLPGGVEVthvnL--NDGS-CAGLSFPEm 322
Cdd:cd01741   98 LGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGlpdefpvfhwHGDTVV--ELPPGAVL----LasSEACpNQAFRYGD- 170
                        170
                 ....*....|.
gi 145332705 323 NVMSLQYHPEA 333
Cdd:cd01741  171 RALGLQFHPEE 181
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
172-332 1.06e-13

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: 68.72  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 172 VIAYDFGIK--QNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGP------GDPSAVPYAVETvkellgKVPVY 243
Cdd:cd01742    1 ILILDFGSQytHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPssvyeeDAPRVDPEIFEL------GVPVL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 244 GICMGHQLLGQALGGK---TFKMKFGHHGGNHPVRNNRTGQVEISAQ---NHNYAVDpaSLPGGVEVTHVNLNDGsCAGL 317
Cdd:cd01742   75 GICYGMQLIAKALGGKverGDKREYGKAEIEIDDSSPLFEGLPDEQTvwmSHGDEVV--KLPEGFKVIASSDNCP-VAAI 151
                        170
                 ....*....|....*
gi 145332705 318 SFPEMNVMSLQYHPE 332
Cdd:cd01742  152 ANEEKKIYGVQFHPE 166
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
176-260 1.63e-13

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: 68.11  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  176 DFGIK--QNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSA--VPYAVETVKELlgKVPVYGICMGHQL 251
Cdd:TIGR00888   5 DFGSQytQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAenAPRADEKIFEL--GVPVLGICYGMQL 82

                  ....*....
gi 145332705  252 LGQALGGKT 260
Cdd:TIGR00888  83 MAKQLGGEV 91
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
182-333 5.29e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 66.82  E-value: 5.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 182 NILRRLSSYGCQITVVPST---FPAAEALkmNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGG 258
Cdd:PRK08857  14 NLYQYFCELGAQVKVVRNDeidIDGIEAL--NPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 259 KTFKMKFGHHGGNHPVRNNrtGQVEISAQN--------HNYAVDPASLPGGVEVTH-VNLNDGS---CAGLSFPEMNVMS 326
Cdd:PRK08857  92 QVVRARQVMHGKTSPIRHT--GRSVFKGLNnpltvtryHSLVVKNDTLPECFELTAwTELEDGSmdeIMGFQHKTLPIEA 169

                 ....*..
gi 145332705 327 LQYHPEA 333
Cdd:PRK08857 170 VQFHPES 176
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
203-332 1.53e-12

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 65.84  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 203 AAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLG-KVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQ 281
Cdd:PRK07765  39 DEAAVAAQFDGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGV 118
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145332705 282 VE------ISAQNHNYAVDPASLPGGVEVThVNLNDGSCAGLSFPEMNVMSLQYHPE 332
Cdd:PRK07765 119 LAglpdpfTATRYHSLTILPETLPAELEVT-ARTDSGVIMAVRHRELPIHGVQFHPE 174
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
181-335 2.41e-12

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: 65.74  E-value: 2.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 181 QNILRRLSSYGCQITVV--------PSTFPAAealkmNPDGILFSNGPGDPSAVPYAVETVKELL-----GKVPVYGICM 247
Cdd:COG0518   16 GLIARRLREAGIELDVLrvyageilPYDPDLE-----DPDGLILSGGPMSVYDEDPWLEDEPALIreafeLGKPVLGICY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 248 GHQLLGQALGGKTFKMKfGHHGGNHPVRnnRTGQVEISA---------QNHNYAVDpaSLPGGVEVTHVNlNDGSCAGLS 318
Cdd:COG0518   91 GAQLLAHALGGKVEPGP-GREIGWAPVE--LTEADPLFAglpdeftvwMSHGDTVT--ELPEGAEVLASS-DNCPNQAFR 164
                        170
                 ....*....|....*..
gi 145332705 319 FPEmNVMSLQYHPEASP 335
Cdd:COG0518  165 YGR-RVYGVQFHPEVTH 180
trpG CHL00101
anthranilate synthase component 2
208-333 2.56e-12

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 64.75  E-value: 2.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 208 KMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVE---- 283
Cdd:CHL00101  41 NLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQglpn 120
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145332705 284 --ISAQNHNYAVDPASLPGGVEVTHVNlNDG---SCAGLSFPEMNvmSLQYHPEA 333
Cdd:CHL00101 121 pfTATRYHSLIIDPLNLPSPLEITAWT-EDGlimACRHKKYKMLR--GIQFHPES 172
PRK13566 PRK13566
anthranilate synthase component I;
187-332 4.31e-12

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 67.25  E-value: 4.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 187 LSSY----GCQITVVPSTFPAAEALKMNPDGILFSNGPGDPS--AVPyavETVKELLGK-VPVYGICMGHQLLGQALGGK 259
Cdd:PRK13566 542 LANYfrqtGAEVTTVRYGFAEEMLDRVNPDLVVLSPGPGRPSdfDCK---ATIDAALARnLPIFGVCLGLQAIVEAFGGE 618
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 260 TFKMKFGHHGGNHPVRNNRTGQV------EISA-QNHNYAVDPASLPGGVEVTHVNlNDGSCAGLSFPEMNVMSLQYHPE 332
Cdd:PRK13566 619 LGQLAYPMHGKPSRIRVRGPGRLfsglpeEFTVgRYHSLFADPETLPDELLVTAET-EDGVIMAIEHKTLPVAAVQFHPE 697
guaA PRK00074
GMP synthase; Reviewed
171-259 6.30e-12

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 66.61  E-value: 6.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 171 KVIAYDFG--IKQNILRRLSSYG--CQItvVPSTFPAAEALKMNPDGILFSNGPG---DPSAvPYAVETVKELlgKVPVY 243
Cdd:PRK00074   5 KILILDFGsqYTQLIARRVRELGvySEI--VPYDISAEEIRAFNPKGIILSGGPAsvyEEGA-PRADPEIFEL--GVPVL 79
                         90
                 ....*....|....*.
gi 145332705 244 GICMGHQLLGQALGGK 259
Cdd:PRK00074  80 GICYGMQLMAHQLGGK 95
PRK00758 PRK00758
GMP synthase subunit A; Validated
183-353 1.19e-11

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 62.95  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 183 ILRRLSSYGCQITVVPSTFPAAEaLKMNPDGILFSNGPgDPSAVPYAVETVKELlgKVPVYGICMGHQLLGQALGGKTFK 262
Cdd:PRK00758  15 IHRTLRYLGVDAKIIPNTTPVEE-IKAFEDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICLGHQLIAKAFGGEVGR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 263 mkfGHHGGnhpvrnnrTGQVEISAQNHNyavDP-----------AS-------LPGGVEVThvnLNDGSCA--GLSFPEM 322
Cdd:PRK00758  91 ---GEYGE--------YALVEVEILDED---DIlkglppeirvwAShadevkeLPDGFEIL---ARSDICEveAMKHKEK 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 145332705 323 NVMSLQYHPEASPGPHDSDnAFREFIELMKR 353
Cdd:PRK00758 154 PIYGVQFHPEVAHTEYGEE-IFKNFLEICGK 183
PLN02347 PLN02347
GMP synthetase
172-338 2.58e-11

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 64.71  E-value: 2.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 172 VIAYDFGIK--QNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGP------GDPSAVPYAVETVKEllGKVPVY 243
Cdd:PLN02347  13 VLILDYGSQytHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYCRE--RGVPVL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 244 GICMGHQLLGQALGGktfKMKFGHHG--GNHPVR---------NNRTGQVEISAQNHNYAVdpASLPGGVEVTHVNLNdG 312
Cdd:PLN02347  91 GICYGMQLIVQKLGG---EVKPGEKQeyGRMEIRvvcgsqlfgDLPSGETQTVWMSHGDEA--VKLPEGFEVVAKSVQ-G 164
                        170       180
                 ....*....|....*....|....*.
gi 145332705 313 SCAGLSFPEMNVMSLQYHPEASPGPH 338
Cdd:PLN02347 165 AVVAIENRERRIYGLQYHPEVTHSPK 190
PRK05637 PRK05637
anthranilate synthase component II; Provisional
187-337 3.10e-10

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 59.09  E-value: 3.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 187 LSSYGCqiTVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGK------- 259
Cdd:PRK05637  23 VAGYKC--TVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLGFQALLEHHGGKvepcgpv 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 260 ---TFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPA----SLpGGVEVTHVNLNDGSCAGLSFP--------EMNV 324
Cdd:PRK05637 101 hgtTDNMILTDAGVQSPVFAGLATDVEPDHPEIPGRKVPIaryhSL-GCVVAPDGMESLGTCSSEIGPvimaaettDGKA 179
                        170
                 ....*....|....*.
gi 145332705 325 MSLQYHPEA--SP-GP 337
Cdd:PRK05637 180 IGLQFHPESvlSPtGP 195
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
181-252 4.55e-09

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: 53.76  E-value: 4.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332705 181 QNILRRLSSYGCQITVVPST--FPAAEALKMNPDGILFSNGPGDPSAV---PYAVETVKELLG-KVPVYGICMGHQLL 252
Cdd:cd01653   15 ASPLDALREAGAEVDVVSPDggPVESDVDLDDYDGLILPGGPGTPDDLardEALLALLREAAAaGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
181-252 4.93e-09

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: 52.97  E-value: 4.93e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332705 181 QNILRRLSSYGCQITVVPST--FPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELL----GKVPVYGICMGHQLL 252
Cdd:cd03128   15 ASPLDALREAGAEVDVVSPDggPVESDVDLDDYDGLILPGGPGTPDDLAWDEALLALLReaaaAGKPVLGICLGAQLL 92
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
182-333 5.12e-09

bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 57.73  E-value: 5.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 182 NILRRLSSYGCQITVVPSTFPAAEALK----MNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALG 257
Cdd:PRK09522  16 NLADQLRSNGHNVVIYRNHIPAQTLIErlatMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 258 GKTFKMKFGHHGGNHPVRNNrtGQVEIS--------AQNHNYAvdPASLPGGVEV-THVNlndGSCAGLSFPEMNVMSLQ 328
Cdd:PRK09522  96 GYVGQAGEILHGKASSIEHD--GQAMFAgltnplpvARYHSLV--GSNIPAGLTInAHFN---GMVMAVRHDADRVCGFQ 168

                 ....*
gi 145332705 329 YHPEA 333
Cdd:PRK09522 169 FHPES 173
PRK06895 PRK06895
anthranilate synthase component II;
214-333 1.41e-06

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 48.19  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 214 ILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHG--------GNHPVRNNRTGQVEIS 285
Cdd:PRK06895  47 ILISPGPDVPRAYPQLFAMLERYHQHKSILGVCLGHQTLCEFFGGELYNLNNVRHGqqrplkvrSNSPLFDGLPEEFNIG 126
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 145332705 286 AQnHNYAVDPASLPGGVEVTHVnLNDGSCAGLSFPEMNVMSLQYHPEA 333
Cdd:PRK06895 127 LY-HSWAVSEENFPTPLEITAV-CDENVVMAMQHKTLPIYGVQFHPES 172
PRK09065 PRK09065
glutamine amidotransferase; Provisional
240-335 3.22e-06

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 47.65  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 240 VPVYGICMGHQLLGQALGGKTfkmkfghhgGNHPV-RNNRTGQVEISAQNHNyavDP--ASLPG--GVEVTH----VNLN 310
Cdd:PRK09065  89 MPLLGICYGHQLLAHALGGEV---------GYNPAgRESGTVTVELHPAAAD---DPlfAGLPAqfPAHLTHlqsvLRLP 156
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145332705 311 DGSCAgLSFPEM----------NVMSLQYHPEASP 335
Cdd:PRK09065 157 PGAVV-LARSAQdphqafrygpHAWGVQFHPEFTA 190
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
196-348 8.00e-06

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: 46.03  E-value: 8.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 196 VVPSTFPAAEALKM--NPDGILFSNGP--------GDPSAVPYAV---------ETVKELL-GKVPVYGICMGHQLLGQA 255
Cdd:cd01745   37 LLPPVDDEEDLEQYleLLDGLLLTGGGdvdpplygEEPHPELGPIdperdafelALLRAALeRGKPILGICRGMQLLNVA 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705 256 LGGKTFkmkfghhggnhpvrnnrtgQVEISAQNHNYAVDPasLPGGVEVTHVNlNDG-----SCAGLSFpemnVMSLQYH 330
Cdd:cd01745  117 LGGTLY-------------------QDIRVNSLHHQAIKR--LADGLRVEARA-PDGvieaiESPDRPF----VLGVQWH 170
                        170
                 ....*....|....*....
gi 145332705 331 PE-ASPGPHDSDNAFREFI 348
Cdd:cd01745  171 PEwLADTDPDSLKLFEAFV 189
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
212-308 3.14e-03

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: 38.39  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332705  212 DGILFSNGPG-DPSAvpYAVET------------------VKELLG-KVPVYGICMGHQLLGQALGGKTF---KMKFGHH 268
Cdd:pfam07722  60 DGLLLTGGPNvDPHF--YGEEPsesggpydpardayelalIRAALArGKPILGICRGFQLLNVALGGTLYqdiQEQPGFT 137
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 145332705  269 GGNHPvrnnrtGQVEISAQNHNYAVDPASL---PGGVEVTHVN 308
Cdd:pfam07722 138 DHREH------CQVAPYAPSHAVNVEPGSLlasLLGSEEFRVN 174
PRK08250 PRK08250
glutamine amidotransferase; Provisional
203-259 5.91e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 37.64  E-value: 5.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145332705 203 AAEALKMNPDGILF---SNGPGDP----SAVPY------------AVETvkellGKVpVYGICMGHQLLGQALGGK 259
Cdd:PRK08250  35 AGEALPENADGFDLlivMGGPQSPrttrEECPYfdskaeqrlinqAIKA-----GKA-VIGVCLGAQLIGEALGAK 104
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure