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Conserved domains on  [gi|18405507|ref|NP_566824|]
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carbamoyl phosphate synthetase A [Arabidopsis thaliana]

Protein Classification

carbamoyl-phosphate synthase small subunit( domain architecture ID 11477131)

small subunit of carbamoyl phosphate synthetase (CPS) which plays a key role in both arginine and pyrimidine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 1-416 0e+00

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


:

Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 873.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507    1 MAMATRTLGFVLPTSLSSQPSFDRRGGgFRVSVIRCSTSPLTFPTSGVVEKPWTSYNARLVLEDGSIWPAKSFGAPGTRI 80
Cdd:PLN02771   1 EAMATRPLGFVLPTSLSSQPSFDRRGG-VRVSVIRCSSSPLTSDGAGVVERPWKTSDARLVLEDGSVWKAKSFGARGTQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   81 AELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIRNLSISTSNWRCTKTLADYLTERDI 160
Cdd:PLN02771  80 GEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  161 MGVYDLDTRAITRRLREDGSLIGVLSTEQSKTDDELLQMSRSWDIVGIDLISDVSCKSPYEWVDKTNAEWDFNTNSRDGK 240
Cdd:PLN02771 160 MGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKMSRSWDIVGIDLISGVSCKSPYEWVDKTNPEWDFNTNSRDGE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  241 SYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMG 320
Cdd:PLN02771 240 SYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  321 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQ 400
Cdd:PLN02771 320 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQ 399

                        410
                 ....*....|....*.
gi 18405507  401 YHPEASPGPHDSDNAF 416
Cdd:PLN02771 400 YHPEASPGPHDSDNAF 415
 
Name Accession Description Interval E-value
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 1-416 0e+00

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 873.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507    1 MAMATRTLGFVLPTSLSSQPSFDRRGGgFRVSVIRCSTSPLTFPTSGVVEKPWTSYNARLVLEDGSIWPAKSFGAPGTRI 80
Cdd:PLN02771   1 EAMATRPLGFVLPTSLSSQPSFDRRGG-VRVSVIRCSSSPLTSDGAGVVERPWKTSDARLVLEDGSVWKAKSFGARGTQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   81 AELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIRNLSISTSNWRCTKTLADYLTERDI 160
Cdd:PLN02771  80 GEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  161 MGVYDLDTRAITRRLREDGSLIGVLSTEQSKTDDELLQMSRSWDIVGIDLISDVSCKSPYEWVDKTNAEWDFNTNSRDGK 240
Cdd:PLN02771 160 MGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKMSRSWDIVGIDLISGVSCKSPYEWVDKTNPEWDFNTNSRDGE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  241 SYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMG 320
Cdd:PLN02771 240 SYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  321 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQ 400
Cdd:PLN02771 320 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQ 399

                        410
                 ....*....|....*.
gi 18405507  401 YHPEASPGPHDSDNAF 416
Cdd:PLN02771 400 YHPEASPGPHDSDNAF 415
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 54-424 0e+00

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: 615.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  54 TSYNARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGL 133
Cdd:COG0505   1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 134 VIRNLSISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVLSTEqSKTDDELLQMSRSW-DIVGIDLIS 212
Cdd:COG0505  81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTG-DLDIEELLEKARAApGMEGLDLVK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 213 DVSCKSPYEWvdktnaewdfntNSRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGP 292
Cdd:COG0505 160 EVSTKEPYEW------------TEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGP 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 293 GDPSAVPYAVETVKELLGK-VPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLP 371
Cdd:COG0505 228 GDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLP 307

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 18405507 372 G-GVEVTHVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMK 424
Cdd:COG0505 308 AtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 58-425 0e+00

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: 608.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507    58 ARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIRN 137
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   138 LSISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVLSTEQSKTDDELLQMSRSWDIVGIDLISDVSCK 217
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   218 SPYEWVDktnaewdfntnsRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSA 297
Cdd:TIGR01368 161 EPYTWGQ------------RGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   298 VPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGG-VEV 376
Cdd:TIGR01368 229 VEPAIETIRKLLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGdLEV 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 18405507   377 THVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMKR 425
Cdd:TIGR01368 309 THVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 244-420 5.29e-113

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: 328.69  E-value: 5.29e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 244 VIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGK-VPVYGICMGHQ 322
Cdd:cd01744   1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 323 LLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQYH 402
Cdd:cd01744  81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                       170
                ....*....|....*...
gi 18405507 403 PEASPGPHDSDNAFREFI 420
Cdd:cd01744 161 PEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 60-185 2.91e-71

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: 220.27  E-value: 2.91e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507    60 LVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIRNLS 139
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 18405507   140 ISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVL 185
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 57-185 1.15e-69

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: 216.47  E-value: 1.15e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507     57 NARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIR 136
Cdd:smart01097   2 KAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVVR 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 18405507    137 NLSISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVL 185
Cdd:smart01097  82 ELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
 
Name Accession Description Interval E-value
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 1-416 0e+00

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 873.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507    1 MAMATRTLGFVLPTSLSSQPSFDRRGGgFRVSVIRCSTSPLTFPTSGVVEKPWTSYNARLVLEDGSIWPAKSFGAPGTRI 80
Cdd:PLN02771   1 EAMATRPLGFVLPTSLSSQPSFDRRGG-VRVSVIRCSSSPLTSDGAGVVERPWKTSDARLVLEDGSVWKAKSFGARGTQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   81 AELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIRNLSISTSNWRCTKTLADYLTERDI 160
Cdd:PLN02771  80 GEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  161 MGVYDLDTRAITRRLREDGSLIGVLSTEQSKTDDELLQMSRSWDIVGIDLISDVSCKSPYEWVDKTNAEWDFNTNSRDGK 240
Cdd:PLN02771 160 MGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKMSRSWDIVGIDLISGVSCKSPYEWVDKTNPEWDFNTNSRDGE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  241 SYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMG 320
Cdd:PLN02771 240 SYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  321 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQ 400
Cdd:PLN02771 320 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQ 399

                        410
                 ....*....|....*.
gi 18405507  401 YHPEASPGPHDSDNAF 416
Cdd:PLN02771 400 YHPEASPGPHDSDNAF 415
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 54-424 0e+00

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: 615.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  54 TSYNARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGL 133
Cdd:COG0505   1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 134 VIRNLSISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVLSTEqSKTDDELLQMSRSW-DIVGIDLIS 212
Cdd:COG0505  81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTG-DLDIEELLEKARAApGMEGLDLVK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 213 DVSCKSPYEWvdktnaewdfntNSRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGP 292
Cdd:COG0505 160 EVSTKEPYEW------------TEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGP 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 293 GDPSAVPYAVETVKELLGK-VPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLP 371
Cdd:COG0505 228 GDPAALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLP 307

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 18405507 372 G-GVEVTHVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMK 424
Cdd:COG0505 308 AtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 58-425 0e+00

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: 608.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507    58 ARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIRN 137
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   138 LSISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVLSTEQSKTDDELLQMSRSWDIVGIDLISDVSCK 217
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   218 SPYEWVDktnaewdfntnsRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSA 297
Cdd:TIGR01368 161 EPYTWGQ------------RGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   298 VPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGG-VEV 376
Cdd:TIGR01368 229 VEPAIETIRKLLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGdLEV 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 18405507   377 THVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMKR 425
Cdd:TIGR01368 309 THVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
57-423 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 598.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   57 NARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIR 136
Cdd:PRK12564   4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIVR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  137 NLSISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVLSTEqSKTDDELLQMSRSW-DIVGIDLISDVS 215
Cdd:PRK12564  84 ELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATE-DFDAEELLEKARAFpGLLGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  216 CKSPYEWvdktnaewdfnTNSRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDP 295
Cdd:PRK12564 163 TKEPYPW-----------PGPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDP 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  296 SAVPYAVETVKELLG-KVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGV 374
Cdd:PRK12564 232 AALDYAIEMIRELLEkKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANL 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 18405507  375 EVTHVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELM 423
Cdd:PRK12564 312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 57-424 9.27e-147

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 421.61  E-value: 9.27e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   57 NARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIR 136
Cdd:PRK12838   2 KAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIVY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  137 NLSISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVLSTeqskTDDELLQMSRSWDIVGIDLISDVSC 216
Cdd:PRK12838  82 ELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITT----TDDAHAFDQIKALVLPKNVVAQVST 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  217 KSPYewvdktnaewdfntnSRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPS 296
Cdd:PRK12838 158 KEPY---------------TYGNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPK 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  297 AVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPG-GVE 375
Cdd:PRK12838 223 ELQPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGtPLS 302

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 18405507  376 VTHVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMK 424
Cdd:PRK12838 303 VRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMME 351
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 58-430 2.12e-143

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 414.19  E-value: 2.12e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   58 ARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIRN 137
Cdd:CHL00197   7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGIIAKN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  138 LSISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVLSTEQSKTDDELLQMSRSWDIVGIDLISDVSCK 217
Cdd:CHL00197  87 ICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRAKIKESPHMPSSDLIPRVTTS 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  218 SPYEWVDKTNAEWDFNTNSRDGKSY--KVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDP 295
Cdd:CHL00197 167 SYYEWDEKSHPSFYLADNKRPHSSYqlKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGDP 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  296 SAVPYAVETVKELLG-KVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRtgQVEISAQNHNYAVDPASL-PGG 373
Cdd:CHL00197 247 SAIHYGIKTVKKLLKyNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSGLNQ--QVEITSQNHGFAVNLESLaKNK 324

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18405507  374 VEVTHVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMKRSKQSS 430
Cdd:CHL00197 325 FYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSSK 381
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 244-420 5.29e-113

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: 328.69  E-value: 5.29e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 244 VIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGK-VPVYGICMGHQ 322
Cdd:cd01744   1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 323 LLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQYH 402
Cdd:cd01744  81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                       170
                ....*....|....*...
gi 18405507 403 PEASPGPHDSDNAFREFI 420
Cdd:cd01744 161 PEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 60-185 2.91e-71

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: 220.27  E-value: 2.91e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507    60 LVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIRNLS 139
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 18405507   140 ISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVL 185
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 57-185 1.15e-69

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: 216.47  E-value: 1.15e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507     57 NARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIR 136
Cdd:smart01097   2 KAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVVR 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 18405507    137 NLSISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVL 185
Cdd:smart01097  82 ELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
GATase pfam00117
Glutamine amidotransferase class-I;
248-422 1.25e-67

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 213.25  E-value: 1.25e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   248 DFG--IKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLG-KVPVYGICMGHQLL 324
Cdd:pfam00117   4 DNGdsFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLGHQLL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   325 GQALGGKTFKMK-FGHHGGNHPVRNNR------TGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVM 397
Cdd:pfam00117  84 ALAFGGKVVKAKkFGHHGKNSPVGDDGcglfygLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLPIF 163

                         170       180
                  ....*....|....*....|....*
gi 18405507   398 SLQYHPEASPGPHDSDNAFREFIEL 422
Cdd:pfam00117 164 GVQFHPESILTPHGPEILFNFFIKA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 254-404 6.90e-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: 114.17  E-value: 6.90e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 254 NILRRLSSYGCQITVVPSTFPAAEALK-MNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKT 332
Cdd:cd01743  13 NLVQYLRELGAEVVVVRNDEITLEELElLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGHQAIAEAFGGKV 92

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18405507 333 FKMKFGHHGGNHPVRNNRTG------QVEISAQNHNYAVDPASLPGGVEVTHVNlNDGSCAGLSFPEMNVMSLQYHPE 404
Cdd:cd01743  93 VRAPEPMHGKTSEIHHDGSGlfkglpQPFTVGRYHSLVVDPDPLPDLLEVTAST-EDGVIMALRHRDLPIYGVQFHPE 169
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 254-404 1.94e-24

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 99.43  E-value: 1.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  254 NILRRLSSYGCQITVVPSTFPA-AEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKT 332
Cdd:PRK05670  14 NLVQYLGELGAEVVVYRNDEITlEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCLGHQAIGEAFGGKV 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18405507  333 FKMKFGHHGGNHPVRNNRTG-------QVEIsAQNHNYAVDPASLPGGVEVTHVnLNDGSCAGLSFPEMNVMSLQYHPE 404
Cdd:PRK05670  94 VRAKEIMHGKTSPIEHDGSGifaglpnPFTV-TRYHSLVVDRESLPDCLEVTAW-TDDGEIMGVRHKELPIYGVQFHPE 170
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 254-404 1.04e-22

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: 1.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 254 NILRRLSSYGCQITVVPST-FPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKT 332
Cdd:COG0512  13 NLVQYLGELGAEVVVVRNDeITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGHQAIGEAFGGKV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 333 FKMKFGHHGGNHPVRNNRTG---------QVeisAQNHNYAVDPASLPGGVEVTHVNlNDGSCAGLSFPEMNVMSLQYHP 403
Cdd:COG0512  93 VRAPEPMHGKTSPITHDGSGlfaglpnpfTA---TRYHSLVVDRETLPDELEVTAWT-EDGEIMGIRHRELPIEGVQFHP 168


                .
gi 18405507 404 E 404
Cdd:COG0512 169 E 169
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
268-420 5.12e-22

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 98.25  E-value: 5.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  268 VVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVR 347
Cdd:PRK14607  30 VRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPID 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18405507  348 NNRTG------QVEISAQNHNYAVDPASLPGGVEVThVNLNDGSCAGLSFPEMNVMSLQYHPEaSPGPHDSDNAFREFI 420
Cdd:PRK14607 110 HNGKGlfrgipNPTVATRYHSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPE-SILTEEGKRILKNFL 186
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 254-405 1.35e-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: 77.52  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   254 NILRRLSSYGCQITVV---PSTFPAAEALKmnPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGG 330
Cdd:TIGR00566  14 NLVQYFCELGAEVVVKrndSLTLQEIEALL--PLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQAFGG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   331 KTFKMKFGHHGGNHPVRNNRTGQVE------ISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQYHPE 404
Cdd:TIGR00566  92 DVVRANTVMHGKTSEIEHNGAGIFRglfnplTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPE 171


                  .
gi 18405507   405 A 405
Cdd:TIGR00566 172 S 172
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
276-405 2.26e-16

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 76.88  E-value: 2.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  276 AEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVE 355
Cdd:PRK08007  37 ADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFR 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18405507  356 ------ISAQNHNYAVDPASLPGGVEVTHVNlNDGSCAGLSFPEMNVMSLQYHPEA 405
Cdd:PRK08007 117 glanplTVTRYHSLVVEPDSLPACFEVTAWS-ETREIMGIRHRQWDLEGVQFHPES 171
PLN02335 PLN02335
anthranilate synthase
 254-405 2.42e-16

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 77.53  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  254 NILRRLSSYGCQITVVPSTFPAAEALK-MNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKT 332
Cdd:PLN02335  33 NLCQYMGELGCHFEVYRNDELTVEELKrKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKI 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  333 FKMKFG-HHGGNHPVRNNRTGQVEI---------SAQNHNYAVDPASLPG-GVEVTHVNlNDGSCAGL---SFPemNVMS 398
Cdd:PLN02335 113 VRSPFGvMHGKSSPVHYDEKGEEGLfsglpnpftAGRYHSLVIEKDTFPSdELEVTAWT-EDGLIMAArhrKYK--HIQG 189


                 ....*..
gi 18405507  399 LQYHPEA 405
Cdd:PLN02335 190 VQFHPES 196
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
280-405 2.34e-15

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 74.13  E-value: 2.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  280 KMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTG------Q 353
Cdd:PRK06774  41 QLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGvfrglnQ 120

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18405507  354 VEISAQNHNYAVDPASLPGGVEVTHVNLNDGS---CAGLSFPEMNVMSLQYHPEA 405
Cdd:PRK06774 121 PLTVTRYHSLVIAADSLPGCFELTAWSERGGEmdeIMGIRHRTLPLEGVQFHPES 175
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
276-430 9.50e-15

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 72.53  E-value: 9.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  276 AEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVE 355
Cdd:PRK07649  37 SDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  356 ------ISAQNHNYAVDPASLPGGVEVThVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDnAFREFIELMKRSKQS 429
Cdd:PRK07649 117 dipnpfTATRYHSLIVKKETLPDCLEVT-SWTEEGEIMAIRHKTLPIEGVQFHPESIMTSHGKE-LLQNFIRKYSPSVTS 194


                 .
gi 18405507  430 S 430
Cdd:PRK07649 195 C 195
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 244-404 9.30e-14

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: 69.10  E-value: 9.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 244 VIAYDFGIK--QNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGP------GDPSAVPYAVETvkellgKVPVY 315
Cdd:cd01742   1 ILILDFGSQytHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPssvyeeDAPRVDPEIFEL------GVPVL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 316 GICMGHQLLGQALGGK---TFKMKFGHHGGNHPVRNNRTGQVEISAQ---NHNYAVDpaSLPGGVEVTHVNLNDGsCAGL 389
Cdd:cd01742  75 GICYGMQLIAKALGGKverGDKREYGKAEIEIDDSSPLFEGLPDEQTvwmSHGDEVV--KLPEGFKVIASSDNCP-VAAI 151

                       170
                ....*....|....*
gi 18405507 390 SFPEMNVMSLQYHPE 404
Cdd:cd01742 152 ANEEKKIYGVQFHPE 166
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 254-405 9.82e-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: 9.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 254 NILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYA-VETVKELL-----GKVPVYGICMGHQLLGQA 327
Cdd:cd01741  18 DLLREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEDDYPwLKKLKELIrqalaAGKPVLGICLGHQLLARA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 328 LGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQN----------HNYAVDpaSLPGGVEVthvnL--NDGS-CAGLSFPEm 394
Cdd:cd01741  98 LGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGlpdefpvfhwHGDTVV--ELPPGAVL----LasSEACpNQAFRYGD- 170

                       170
                ....*....|.
gi 18405507 395 NVMSLQYHPEA 405
Cdd:cd01741 171 RALGLQFHPEE 181
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 248-332 2.33e-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: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   248 DFGIK--QNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSA--VPYAVETVKELlgKVPVYGICMGHQL 323
Cdd:TIGR00888   5 DFGSQytQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAenAPRADEKIFEL--GVPVLGICYGMQL 82


                  ....*....
gi 18405507   324 LGQALGGKT 332
Cdd:TIGR00888  83 MAKQLGGEV 91
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
254-405 5.65e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 67.21  E-value: 5.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  254 NILRRLSSYGCQITVVPST---FPAAEALkmNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGG 330
Cdd:PRK08857  14 NLYQYFCELGAQVKVVRNDeidIDGIEAL--NPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  331 KTFKMKFGHHGGNHPVRNNrtGQVEISAQN--------HNYAVDPASLPGGVEVTH-VNLNDGS---CAGLSFPEMNVMS 398
Cdd:PRK08857  92 QVVRARQVMHGKTSPIRHT--GRSVFKGLNnpltvtryHSLVVKNDTLPECFELTAwTELEDGSmdeIMGFQHKTLPIEA 169


                 ....*..
gi 18405507  399 LQYHPEA 405
Cdd:PRK08857 170 VQFHPES 176
trpG CHL00101
anthranilate synthase component 2
 280-405 2.15e-12

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 65.52  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  280 KMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVE---- 355
Cdd:CHL00101  41 NLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQglpn 120

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18405507  356 --ISAQNHNYAVDPASLPGGVEVTHVNlNDG---SCAGLSFPEMNvmSLQYHPEA 405
Cdd:CHL00101 121 pfTATRYHSLIIDPLNLPSPLEITAWT-EDGlimACRHKKYKMLR--GIQFHPES 172
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
275-404 2.16e-12

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 65.84  E-value: 2.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  275 AAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLG-KVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQ 353
Cdd:PRK07765  39 DEAAVAAQFDGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGV 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18405507  354 VE------ISAQNHNYAVDPASLPGGVEVThVNLNDGSCAGLSFPEMNVMSLQYHPE 404
Cdd:PRK07765 119 LAglpdpfTATRYHSLTILPETLPAELEVT-ARTDSGVIMAVRHRELPIHGVQFHPE 174
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 253-407 3.43e-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: 3.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 253 QNILRRLSSYGCQITVV--------PSTFPAAealkmNPDGILFSNGPGDPSAVPYAVETVKELL-----GKVPVYGICM 319
Cdd:COG0518  16 GLIARRLREAGIELDVLrvyageilPYDPDLE-----DPDGLILSGGPMSVYDEDPWLEDEPALIreafeLGKPVLGICY 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 320 GHQLLGQALGGKTFKMKfGHHGGNHPVRnnRTGQVEISA---------QNHNYAVDpaSLPGGVEVTHVNlNDGSCAGLS 390
Cdd:COG0518  91 GAQLLAHALGGKVEPGP-GREIGWAPVE--LTEADPLFAglpdeftvwMSHGDTVT--ELPEGAEVLASS-DNCPNQAFR 164

                       170
                ....*....|....*..
gi 18405507 391 FPEmNVMSLQYHPEASP 407
Cdd:COG0518 165 YGR-RVYGVQFHPEVTH 180
PRK13566 PRK13566
anthranilate synthase component I;
259-404 7.51e-12

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 67.25  E-value: 7.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  259 LSSY----GCQITVVPSTFPAAEALKMNPDGILFSNGPGDPS--AVPyavETVKELLGK-VPVYGICMGHQLLGQALGGK 331
Cdd:PRK13566 542 LANYfrqtGAEVTTVRYGFAEEMLDRVNPDLVVLSPGPGRPSdfDCK---ATIDAALARnLPIFGVCLGLQAIVEAFGGE 618

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  332 TFKMKFGHHGGNHPVRNNRTGQV------EISA-QNHNYAVDPASLPGGVEVTHVNlNDGSCAGLSFPEMNVMSLQYHPE 404
Cdd:PRK13566 619 LGQLAYPMHGKPSRIRVRGPGRLfsglpeEFTVgRYHSLFADPETLPDELLVTAET-EDGVIMAIEHKTLPVAAVQFHPE 697
guaA PRK00074
GMP synthase; Reviewed
 243-331 1.05e-11

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 66.61  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  243 KVIAYDFG--IKQNILRRLSSYG--CQItvVPSTFPAAEALKMNPDGILFSNGPG---DPSAvPYAVETVKELlgKVPVY 315
Cdd:PRK00074   5 KILILDFGsqYTQLIARRVRELGvySEI--VPYDISAEEIRAFNPKGIILSGGPAsvyEEGA-PRADPEIFEL--GVPVL 79

                         90
                 ....*....|....*.
gi 18405507  316 GICMGHQLLGQALGGK 331
Cdd:PRK00074  80 GICYGMQLMAHQLGGK 95
PRK00758 PRK00758
GMP synthase subunit A; Validated
 255-425 1.61e-11

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 62.95  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  255 ILRRLSSYGCQITVVPSTFPAAEaLKMNPDGILFSNGPgDPSAVPYAVETVKELlgKVPVYGICMGHQLLGQALGGKTFK 334
Cdd:PRK00758  15 IHRTLRYLGVDAKIIPNTTPVEE-IKAFEDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICLGHQLIAKAFGGEVGR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  335 mkfGHHGGnhpvrnnrTGQVEISAQNHNyavDP-----------AS-------LPGGVEVThvnLNDGSCA--GLSFPEM 394
Cdd:PRK00758  91 ---GEYGE--------YALVEVEILDED---DIlkglppeirvwAShadevkeLPDGFEIL---ARSDICEveAMKHKEK 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 18405507  395 NVMSLQYHPEASPGPHDSDnAFREFIELMKR 425
Cdd:PRK00758 154 PIYGVQFHPEVAHTEYGEE-IFKNFLEICGK 183
PLN02347 PLN02347
GMP synthetase
 244-410 4.22e-11

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 64.71  E-value: 4.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  244 VIAYDFGIK--QNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGP------GDPSAVPYAVETVKEllGKVPVY 315
Cdd:PLN02347  13 VLILDYGSQytHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYCRE--RGVPVL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  316 GICMGHQLLGQALGGktfKMKFGHHG--GNHPVR---------NNRTGQVEISAQNHNYAVdpASLPGGVEVTHVNLNdG 384
Cdd:PLN02347  91 GICYGMQLIVQKLGG---EVKPGEKQeyGRMEIRvvcgsqlfgDLPSGETQTVWMSHGDEA--VKLPEGFEVVAKSVQ-G 164

                        170       180
                 ....*....|....*....|....*.
gi 18405507  385 SCAGLSFPEMNVMSLQYHPEASPGPH 410
Cdd:PLN02347 165 AVVAIENRERRIYGLQYHPEVTHSPK 190
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 259-409 1.72e-10

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 60.24  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  259 LSSYGCqiTVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGK------- 331
Cdd:PRK05637  23 VAGYKC--TVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLGFQALLEHHGGKvepcgpv 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  332 ---TFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPA----SLpGGVEVTHVNLNDGSCAGLSFP--------EMNV 396
Cdd:PRK05637 101 hgtTDNMILTDAGVQSPVFAGLATDVEPDHPEIPGRKVPIaryhSL-GCVVAPDGMESLGTCSSEIGPvimaaettDGKA 179

                        170
                 ....*....|....*.
gi 18405507  397 MSLQYHPEA--SP-GP 409
Cdd:PRK05637 180 IGLQFHPESvlSPtGP 195
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 253-324 5.69e-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: 5.69e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18405507 253 QNILRRLSSYGCQITVVPST--FPAAEALKMNPDGILFSNGPGDPSAV---PYAVETVKELLG-KVPVYGICMGHQLL 324
Cdd:cd01653  15 ASPLDALREAGAEVDVVSPDggPVESDVDLDDYDGLILPGGPGTPDDLardEALLALLREAAAaGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 253-324 6.10e-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: 6.10e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18405507 253 QNILRRLSSYGCQITVVPST--FPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELL----GKVPVYGICMGHQLL 324
Cdd:cd03128  15 ASPLDALREAGAEVDVVSPDggPVESDVDLDDYDGLILPGGPGTPDDLAWDEALLALLReaaaAGKPVLGICLGAQLL 92
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 254-405 7.75e-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: 7.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  254 NILRRLSSYGCQITVVPSTFPAAEALK----MNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALG 329
Cdd:PRK09522  16 NLADQLRSNGHNVVIYRNHIPAQTLIErlatMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  330 GKTFKMKFGHHGGNHPVRNNrtGQVEIS--------AQNHNYAvdPASLPGGVEV-THVNlndGSCAGLSFPEMNVMSLQ 400
Cdd:PRK09522  96 GYVGQAGEILHGKASSIEHD--GQAMFAgltnplpvARYHSLV--GSNIPAGLTInAHFN---GMVMAVRHDADRVCGFQ 168


                 ....*
gi 18405507  401 YHPEA 405
Cdd:PRK09522 169 FHPES 173
PRK06895 PRK06895
anthranilate synthase component II;
286-405 1.46e-06

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 48.58  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  286 ILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHG--------GNHPVRNNRTGQVEIS 357
Cdd:PRK06895  47 ILISPGPDVPRAYPQLFAMLERYHQHKSILGVCLGHQTLCEFFGGELYNLNNVRHGqqrplkvrSNSPLFDGLPEEFNIG 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18405507  358 AQnHNYAVDPASLPGGVEVTHVnLNDGSCAGLSFPEMNVMSLQYHPEA 405
Cdd:PRK06895 127 LY-HSWAVSEENFPTPLEITAV-CDENVVMAMQHKTLPIYGVQFHPES 172
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 312-407 4.26e-06

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 47.65  E-value: 4.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507  312 VPVYGICMGHQLLGQALGGKTfkmkfghhgGNHPV-RNNRTGQVEISAQNHNyavDP--ASLPG--GVEVTH----VNLN 382
Cdd:PRK09065  89 MPLLGICYGHQLLAHALGGEV---------GYNPAgRESGTVTVELHPAAAD---DPlfAGLPAqfPAHLTHlqsvLRLP 156

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 18405507  383 DGSCAgLSFPEM----------NVMSLQYHPEASP 407
Cdd:PRK09065 157 PGAVV-LARSAQdphqafrygpHAWGVQFHPEFTA 190
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 268-420 1.03e-05

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: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 268 VVPSTFPAAEALKM--NPDGILFSNGP--------GDPSAVPYAV---------ETVKELL-GKVPVYGICMGHQLLGQA 327
Cdd:cd01745  37 LLPPVDDEEDLEQYleLLDGLLLTGGGdvdpplygEEPHPELGPIdperdafelALLRAALeRGKPILGICRGMQLLNVA 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507 328 LGGKTFkmkfghhggnhpvrnnrtgQVEISAQNHNYAVDPasLPGGVEVTHVNlNDG-----SCAGLSFpemnVMSLQYH 402
Cdd:cd01745 117 LGGTLY-------------------QDIRVNSLHHQAIKR--LADGLRVEARA-PDGvieaiESPDRPF----VLGVQWH 170

                       170
                ....*....|....*....
gi 18405507 403 PE-ASPGPHDSDNAFREFI 420
Cdd:cd01745 171 PEwLADTDPDSLKLFEAFV 189
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 284-380 4.05e-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: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405507   284 DGILFSNGPG-DPSAvpYAVET------------------VKELLG-KVPVYGICMGHQLLGQALGGKTF---KMKFGHH 340
Cdd:pfam07722  60 DGLLLTGGPNvDPHF--YGEEPsesggpydpardayelalIRAALArGKPILGICRGFQLLNVALGGTLYqdiQEQPGFT 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 18405507   341 GGNHPvrnnrtGQVEISAQNHNYAVDPASL---PGGVEVTHVN 380
Cdd:pfam07722 138 DHREH------CQVAPYAPSHAVNVEPGSLlasLLGSEEFRVN 174
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 275-331 7.64e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 37.64  E-value: 7.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18405507  275 AAEALKMNPDGILF---SNGPGDP----SAVPY------------AVETvkellGKVpVYGICMGHQLLGQALGGK 331
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.
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