NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|817522520|ref|WP_046578476|]
View 

glutamine amidotransferase [Burkholderia gladioli]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 73)

type 1 glutamine amidotransferase (GATase1) family protein

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-243 2.72e-85

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.


The actual alignment was detected with superfamily member PRK09065:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 237  Bit Score: 253.35  E-value: 2.72e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   3 KPILIVITGETFASISAAHGDFADWIEAGLAASPLPglaIERFDARGAAALPDADDYAGIVLTGSHAMVTAREPWSERLG 82
Cdd:PRK09065   2 KPLLIIQTGTPPPSIRARYGDFPHWIRVALGLAEQP---VVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRLDWSERTA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  83 HWLADCAARGVtPMLGICYGHQLLAQALGGEVDDRRDRRfEIGTVSIGQRAEAAGDPLFAALPARFDAQVVHYQSVHRLP 162
Cdd:PRK09065  79 DWLRQAAAAGM-PLLGICYGHQLLAHALGGEVGYNPAGR-ESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520 163 PGARLLAASDTDPCQAFRHGQACWGVQFHPEFPLPAIEQYLAILRAQPGAHGADALPPQVRLASTPEAFALLARFARLCL 242
Cdd:PRK09065 157 PGAVVLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRARADCLRREGLDARTLLREVSEAPWARKLLRRFVRLAR 236


                 .
gi 817522520 243 T 243
Cdd:PRK09065 237 R 237
 
Name Accession Description Interval E-value
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 3-243 2.72e-85

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 253.35  E-value: 2.72e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   3 KPILIVITGETFASISAAHGDFADWIEAGLAASPLPglaIERFDARGAAALPDADDYAGIVLTGSHAMVTAREPWSERLG 82
Cdd:PRK09065   2 KPLLIIQTGTPPPSIRARYGDFPHWIRVALGLAEQP---VVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRLDWSERTA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  83 HWLADCAARGVtPMLGICYGHQLLAQALGGEVDDRRDRRfEIGTVSIGQRAEAAGDPLFAALPARFDAQVVHYQSVHRLP 162
Cdd:PRK09065  79 DWLRQAAAAGM-PLLGICYGHQLLAHALGGEVGYNPAGR-ESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520 163 PGARLLAASDTDPCQAFRHGQACWGVQFHPEFPLPAIEQYLAILRAQPGAHGADALPPQVRLASTPEAFALLARFARLCL 242
Cdd:PRK09065 157 PGAVVLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRARADCLRREGLDARTLLREVSEAPWARKLLRRFVRLAR 236


                 .
gi 817522520 243 T 243
Cdd:PRK09065 237 R 237
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 4-241 3.03e-60

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: 189.39  E-value: 3.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   4 PILIVITGETfasisaaHGDFADWIEAGLAAsplPGLAIERFDARGAAALP---DADDYAGIVLTGSHAMVTAREPWSER 80
Cdd:COG0518    1 KILILDHDPF-------GGQYPGLIARRLRE---AGIELDVLRVYAGEILPydpDLEDPDGLILSGGPMSVYDEDPWLED 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  81 LGHWLADCAARGVtPMLGICYGHQLLAQALGGEVddRRDRRFEIGTVSIGQRAEaagDPLFAALPARFDAQVVHYQSVHR 160
Cdd:COG0518   71 EPALIREAFELGK-PVLGICYGAQLLAHALGGKV--EPGPGREIGWAPVELTEA---DPLFAGLPDEFTVWMSHGDTVTE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520 161 LPPGARLLAASDTDPCQAFRHGQACWGVQFHPEFPLPAIEQYLAILRAQPGAHGADALPPQVRLASTPEAFALLARFARL 240
Cdd:COG0518  145 LPEGAEVLASSDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADELAAEELLAEASLHDPELREAGRRLLRNFLRE 224


                 .
gi 817522520 241 C 241
Cdd:COG0518  225 I 225
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 4-193 7.73e-54

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: 171.66  E-value: 7.73e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   4 PILIVITGETFAsisaaHGDFADWIEAGLAAsplpGLAIERFDARGAAALPDADDYAGIVLTGSHAMV-TAREPWSERLG 82
Cdd:cd01741    1 RILILQHDTPEG-----PGLFEDLLREAGAE----TIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLKKLK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  83 HWLADCAARGVtPMLGICYGHQLLAQALGGEVDdRRDRRFEIGTVSIGQRAEAAGDPLFAALPARFDAQVVHYQSVHRLP 162
Cdd:cd01741   72 ELIRQALAAGK-PVLGICLGHQLLARALGGKVG-RNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVELP 149

                        170       180       190
                 ....*....|....*....|....*....|.
gi 817522520 163 PGARLLAASDTDPCQAFRHGQACWGVQFHPE 193
Cdd:cd01741  150 PGAVLLASSEACPNQAFRYGDRALGLQFHPE 180
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 60-193 2.29e-27

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: 103.55  E-value: 2.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   60 AGIVLTGSHAMVTAREpwSERLGHWLADCaarGVtPMLGICYGHQLLAQALGGEVdDRRDRRfEIGTVSIgqRAEAAGDp 139
Cdd:TIGR00888  43 KGIILSGGPSSVYAEN--APRADEKIFEL---GV-PVLGICYGMQLMAKQLGGEV-GRAEKR-EYGKAEL--EILDEDD- 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 817522520  140 LFAALPARFDAQVVHYQSVHRLPPGARLLAASDTDPCQAFRHGQACW-GVQFHPE 193
Cdd:TIGR00888 112 LFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIyGVQFHPE 166
GATase pfam00117
Glutamine amidotransferase class-I;
55-194 4.40e-15

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 71.11  E-value: 4.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   55 DADDYAGIVLTGSHAMVTAREpwserlGHWLADCAARGV-TPMLGICYGHQLLAQALGGEVDdrRDRRFEI--GTVSIGQ 131
Cdd:pfam00117  37 LEENPDGIILSGGPGSPGAAG------GAIEAIREARELkIPILGICLGHQLLALAFGGKVV--KAKKFGHhgKNSPVGD 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817522520  132 RaeaaGDPLFAALPARFdaQVVHYQS----VHRLPPGARLLAASDTD-PCQAFRH-GQACWGVQFHPEF 194
Cdd:pfam00117 109 D----GCGLFYGLPNVF--IVRRYHSyavdPDTLPDGLEVTATSENDgTIMGIRHkKLPIFGVQFHPES 171
 
Name Accession Description Interval E-value
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 3-243 2.72e-85

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 253.35  E-value: 2.72e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   3 KPILIVITGETFASISAAHGDFADWIEAGLAASPLPglaIERFDARGAAALPDADDYAGIVLTGSHAMVTAREPWSERLG 82
Cdd:PRK09065   2 KPLLIIQTGTPPPSIRARYGDFPHWIRVALGLAEQP---VVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRLDWSERTA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  83 HWLADCAARGVtPMLGICYGHQLLAQALGGEVDDRRDRRfEIGTVSIGQRAEAAGDPLFAALPARFDAQVVHYQSVHRLP 162
Cdd:PRK09065  79 DWLRQAAAAGM-PLLGICYGHQLLAHALGGEVGYNPAGR-ESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520 163 PGARLLAASDTDPCQAFRHGQACWGVQFHPEFPLPAIEQYLAILRAQPGAHGADALPPQVRLASTPEAFALLARFARLCL 242
Cdd:PRK09065 157 PGAVVLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRARADCLRREGLDARTLLREVSEAPWARKLLRRFVRLAR 236


                 .
gi 817522520 243 T 243
Cdd:PRK09065 237 R 237
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 4-241 3.03e-60

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: 189.39  E-value: 3.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   4 PILIVITGETfasisaaHGDFADWIEAGLAAsplPGLAIERFDARGAAALP---DADDYAGIVLTGSHAMVTAREPWSER 80
Cdd:COG0518    1 KILILDHDPF-------GGQYPGLIARRLRE---AGIELDVLRVYAGEILPydpDLEDPDGLILSGGPMSVYDEDPWLED 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  81 LGHWLADCAARGVtPMLGICYGHQLLAQALGGEVddRRDRRFEIGTVSIGQRAEaagDPLFAALPARFDAQVVHYQSVHR 160
Cdd:COG0518   71 EPALIREAFELGK-PVLGICYGAQLLAHALGGKV--EPGPGREIGWAPVELTEA---DPLFAGLPDEFTVWMSHGDTVTE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520 161 LPPGARLLAASDTDPCQAFRHGQACWGVQFHPEFPLPAIEQYLAILRAQPGAHGADALPPQVRLASTPEAFALLARFARL 240
Cdd:COG0518  145 LPEGAEVLASSDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADELAAEELLAEASLHDPELREAGRRLLRNFLRE 224


                 .
gi 817522520 241 C 241
Cdd:COG0518  225 I 225
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 4-193 7.73e-54

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: 171.66  E-value: 7.73e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   4 PILIVITGETFAsisaaHGDFADWIEAGLAAsplpGLAIERFDARGAAALPDADDYAGIVLTGSHAMV-TAREPWSERLG 82
Cdd:cd01741    1 RILILQHDTPEG-----PGLFEDLLREAGAE----TIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLKKLK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  83 HWLADCAARGVtPMLGICYGHQLLAQALGGEVDdRRDRRFEIGTVSIGQRAEAAGDPLFAALPARFDAQVVHYQSVHRLP 162
Cdd:cd01741   72 ELIRQALAAGK-PVLGICLGHQLLARALGGKVG-RNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVELP 149

                        170       180       190
                 ....*....|....*....|....*....|.
gi 817522520 163 PGARLLAASDTDPCQAFRHGQACWGVQFHPE 193
Cdd:cd01741  150 PGAVLLASSEACPNQAFRYGDRALGLQFHPE 180
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 44-241 6.76e-36

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 127.37  E-value: 6.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  44 RFDARGAAALpDADDYAGIVLTGSHAMVT----AREPWSERLGHWLADCAARGVT---PMLGICYGHQLLAQALGGEVDd 116
Cdd:PRK07567  38 RLDREPLPDL-DLDDYSGVIVGGSPFNVSdpaeSKSPWQRRVEAELSGLLDEVVArdfPFLGACYGVGTLGHHQGGVVD- 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520 117 rrdRRF--EIGTVSIGQRAEAAGDPLFAALPARFDAQVVHYQSVHRLPPGARLLAASDTDPCQAFRHGQACWGVQFHPEF 194
Cdd:PRK07567 116 ---RTYgePVGAVTVSLTDAGRADPLLAGLPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVQMFRVGENVYATQFHPEL 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 817522520 195 PLPAIEQYLAILRaqpgAHG------ADALPPQVRLASTPEAFALLARFARLC 241
Cdd:PRK07567 193 DADGLKTRIDFYR----DHGyfapeeADSLIARARSVDVTAPNRILRNFVERY 241
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 61-193 1.89e-27

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: 103.38  E-value: 1.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  61 GIVLTGSHAMVtaREPWSERLGHWLADCaarGVtPMLGICYGHQLLAQALGGEVdDRRDRRfEIGTVSIGQraeAAGDPL 140
Cdd:cd01742   44 GIILSGGPSSV--YEEDAPRVDPEIFEL---GV-PVLGICYGMQLIAKALGGKV-ERGDKR-EYGKAEIEI---DDSSPL 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 817522520 141 FAALPARFDAQVVHYQSVHRLPPGARLLAASDTDPCQAFRH-GQACWGVQFHPE 193
Cdd:cd01742  113 FEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANeEKKIYGVQFHPE 166
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 60-193 2.29e-27

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: 103.55  E-value: 2.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   60 AGIVLTGSHAMVTAREpwSERLGHWLADCaarGVtPMLGICYGHQLLAQALGGEVdDRRDRRfEIGTVSIgqRAEAAGDp 139
Cdd:TIGR00888  43 KGIILSGGPSSVYAEN--APRADEKIFEL---GV-PVLGICYGMQLMAKQLGGEV-GRAEKR-EYGKAEL--EILDEDD- 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 817522520  140 LFAALPARFDAQVVHYQSVHRLPPGARLLAASDTDPCQAFRHGQACW-GVQFHPE 193
Cdd:TIGR00888 112 LFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIyGVQFHPE 166
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 52-194 1.02e-22

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 92.72  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  52 ALPDA-DDYAGIVLTGSHAMVTAREPWSERLGHWLAdCAARGVTPMLGICYGHQLLAQALGGEVDDRRDRRFEIGTVSIg 130
Cdd:PRK06490  45 PLPDTlEDHAGAVIFGGPMSANDPDDFIRREIDWIS-VPLKENKPFLGICLGAQMLARHLGARVAPHPDGRVEIGYYPL- 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817522520 131 qRAEAAGDPLfaalpARFDAQVVHYqsvHR----LPPGARLLAASDTDPCQAFRHGQACWGVQFHPEF 194
Cdd:PRK06490 123 -RPTEAGRAL-----MHWPEMVYHW---HRegfdLPAGAELLATGDDFPNQAFRYGDNAWGLQFHPEV 181
guaA PRK00074
GMP synthase; Reviewed
 60-193 5.27e-22

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 93.96  E-value: 5.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  60 AGIVLTGSHAMVTarEPWSERLGHWLADCaarGVtPMLGICYGHQLLAQALGGEVdDRRDRRfEIGtvsigqRAE---AA 136
Cdd:PRK00074  48 KGIILSGGPASVY--EEGAPRADPEIFEL---GV-PVLGICYGMQLMAHQLGGKV-ERAGKR-EYG------RAElevDN 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 817522520 137 GDPLFAALPARFDAQVVHYQSVHRLPPGARLLAASDTDPCQAFRHGQACW-GVQFHPE 193
Cdd:PRK00074 114 DSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEERKFyGVQFHPE 171
PRK00758 PRK00758
GMP synthase subunit A; Validated
 95-193 5.22e-20

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 84.13  E-value: 5.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  95 PMLGICYGHQLLAQALGGEVddRRDRRFEIGTVSIGQRAEaagDPLFAALPARFDAQVVHYQSVHRLPPGARLLAASDTD 174
Cdd:PRK00758  69 PILGICLGHQLIAKAFGGEV--GRGEYGEYALVEVEILDE---DDILKGLPPEIRVWASHADEVKELPDGFEILARSDIC 143

                         90       100
                 ....*....|....*....|
gi 817522520 175 PCQAFRHG-QACWGVQFHPE 193
Cdd:PRK00758 144 EVEAMKHKeKPIYGVQFHPE 163
PRK05665 PRK05665
amidotransferase; Provisional
 54-194 6.95e-16

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 74.46  E-value: 6.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  54 PDADDYAGIVLTGSHAMVTAREPWSERLGHWLADCAARGvTPMLGICYGHQLLAQALGGEVDdRRDRRFEIGtvsIGQRA 133
Cdd:PRK05665  53 ADDEKFDAYLVTGSKADSFGTDPWIQTLKTYLLKLYERG-DKLLGVCFGHQLLALLLGGKAE-RASQGWGVG---IHRYQ 127

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817522520 134 EAAGDPLFAalPARFDAQVV--HYQSVHRLPPGARLLAASDTDPCQAFRHGQACWGVQFHPEF 194
Cdd:PRK05665 128 LAAHAPWMS--PAVTELTLLisHQDQVTALPEGATVIASSDFCPFAAYHIGDQVLCFQGHPEF 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 89-193 2.97e-15

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: 71.41  E-value: 2.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  89 AARGVTPMLGICYGHQLLAQALGGEVdDRRDRRFEIGTVSIGQRaeaaGDPLFAALPARFdaQVVHYQS--VHRLPPGAR 166
Cdd:cd01743   67 ALAGKVPILGVCLGHQAIAEAFGGKV-VRAPEPMHGKTSEIHHD----GSGLFKGLPQPF--TVGRYHSlvVDPDPLPDL 139

                         90       100       110
                 ....*....|....*....|....*....|
gi 817522520 167 LLAASDTDP--CQAFRHGQAC-WGVQFHPE 193
Cdd:cd01743  140 LEVTASTEDgvIMALRHRDLPiYGVQFHPE 169
GATase pfam00117
Glutamine amidotransferase class-I;
55-194 4.40e-15

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 71.11  E-value: 4.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   55 DADDYAGIVLTGSHAMVTAREpwserlGHWLADCAARGV-TPMLGICYGHQLLAQALGGEVDdrRDRRFEI--GTVSIGQ 131
Cdd:pfam00117  37 LEENPDGIILSGGPGSPGAAG------GAIEAIREARELkIPILGICLGHQLLALAFGGKVV--KAKKFGHhgKNSPVGD 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817522520  132 RaeaaGDPLFAALPARFdaQVVHYQS----VHRLPPGARLLAASDTD-PCQAFRH-GQACWGVQFHPEF 194
Cdd:pfam00117 109 D----GCGLFYGLPNVF--IVRRYHSyavdPDTLPDGLEVTATSENDgTIMGIRHkKLPIFGVQFHPES 171
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 89-193 9.15e-15

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 70.07  E-value: 9.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  89 AARGVTPMLGICYGHQLLAQALGGEVDdrrdRRFEI--GTVSigqRAEAAGDPLFAALPARFdaQVVHYQS--VHR--LP 162
Cdd:COG0512   67 AFAGKIPILGVCLGHQAIGEAFGGKVV----RAPEPmhGKTS---PITHDGSGLFAGLPNPF--TATRYHSlvVDRetLP 137

                         90       100       110
                 ....*....|....*....|....*....|..
gi 817522520 163 PGARLLAASDTDPCQAFRHGQA-CWGVQFHPE 193
Cdd:COG0512  138 DELEVTAWTEDGEIMGIRHRELpIEGVQFHPE 169
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 39-239 4.05e-12

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 63.81  E-value: 4.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  39 GLAIERFDARGAAALPDADDYAG--IVLTGS-HAMVTAREPWSERLGHWLAD-CAARGvtPMLGICYGHQLLAQALGGEV 114
Cdd:PRK07053  27 GYRVRYVDVGVDDLETLDALEPDllVVLGGPiGVYDDELYPFLAPEIALLRQrLAAGL--PTLGICLGAQLIARALGARV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520 115 DDRRDRrfEIGTVSIGQRAEAAGDPLfAALPArfDAQVVHYQS-VHRLPPGARLLAASDTDPCQAFRHGQACWGVQFHPE 193
Cdd:PRK07053 105 YPGGQK--EIGWAPLTLTDAGRASPL-RHLGA--GTPVLHWHGdTFDLPEGATLLASTPACRHQAFAWGNHVLALQFHPE 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 817522520 194 FPLPAIEQYLAILRAQPGAHGADalPPQVRlASTPEAFALLARFAR 239
Cdd:PRK07053 180 AREDRFEAWLIGHAGELAAAGID--PRTLR-ADTAQHGPALEAAAR 222
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 89-193 4.53e-12

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 62.84  E-value: 4.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  89 AARGVTPMLGICYGHQLLAQALGGEVddRRDRRFEIGTVSigqRAEAAGDPLFAALPARFdaQVVHYQS--VHR--LPPG 164
Cdd:PRK05670  68 EFAGKVPILGVCLGHQAIGEAFGGKV--VRAKEIMHGKTS---PIEHDGSGIFAGLPNPF--TVTRYHSlvVDResLPDC 140

                         90       100       110
                 ....*....|....*....|....*....|
gi 817522520 165 ARLLAASDTDPCQAFRHGQ-ACWGVQFHPE 193
Cdd:PRK05670 141 LEVTAWTDDGEIMGVRHKElPIYGVQFHPE 170
PLN02347 PLN02347
GMP synthetase
 88-193 4.57e-12

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 65.09  E-value: 4.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  88 CAARGVtPMLGICYGHQLLAQALGGEVD--DRRdrrfEIGTVSIgqrAEAAGDPLFAALPARfDAQVV---HYQSVHRLP 162
Cdd:PLN02347  82 CRERGV-PVLGICYGMQLIVQKLGGEVKpgEKQ----EYGRMEI---RVVCGSQLFGDLPSG-ETQTVwmsHGDEAVKLP 152

                         90       100       110
                 ....*....|....*....|....*....|..
gi 817522520 163 PGARLLAASDTDPCQAFRHGQA-CWGVQFHPE 193
Cdd:PLN02347 153 EGFEVVAKSVQGAVVAIENRERrIYGLQYHPE 184
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 52-193 9.47e-10

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: 56.88  E-value: 9.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   52 ALPDADDYA-------GIVLTGS---HAMVTAREPwSERLGHW-----------LADCAARGVtPMLGICYGHQLLAQAL 110
Cdd:pfam07722  45 ILGDPEDAAaildrldGLLLTGGpnvDPHFYGEEP-SESGGPYdpardayelalIRAALARGK-PILGICRGFQLLNVAL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  111 GG-------EVDDRRDRR--FEIGTVSIGQRAEAAGDPLFAALPARFDAQV--VHYQSVHRLPPGARLLAASDTDPCQAF 179
Cdd:pfam07722 123 GGtlyqdiqEQPGFTDHRehCQVAPYAPSHAVNVEPGSLLASLLGSEEFRVnsLHHQAIDRLAPGLRVEAVAPDGTIEAI 202

                         170
                  ....*....|....*..
gi 817522520  180 RHGQA---CWGVQFHPE 193
Cdd:pfam07722 203 ESPNAkgfALGVQWHPE 219
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
92-193 1.08e-09

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 56.35  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  92 GVTPMLGICYGHQLLAQALGGEVddRRDRRFEIGTVSigqRAEAAGDPLFAALPARFDAQVVHYQSVHR--LPPGARLLA 169
Cdd:PRK07649  71 GKIPIFGVCLGHQSIAQVFGGEV--VRAERLMHGKTS---LMHHDGKTIFSDIPNPFTATRYHSLIVKKetLPDCLEVTS 145

                         90       100
                 ....*....|....*....|....*
gi 817522520 170 ASDTDPCQAFRHGQ-ACWGVQFHPE 193
Cdd:PRK07649 146 WTEEGEIMAIRHKTlPIEGVQFHPE 170
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 92-193 1.28e-09

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: 55.95  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   92 GVTPMLGICYGHQLLAQALGGEVddRRDRRFEIGTVS-IGQRAEAAGDPLFAALPArfdaqvVHYQSVH----RLPPGAR 166
Cdd:TIGR00566  71 GKLPILGVCLGHQAMGQAFGGDV--VRANTVMHGKTSeIEHNGAGIFRGLFNPLTA------TRYHSLVvepeTLPTCFP 142

                          90       100
                  ....*....|....*....|....*....
gi 817522520  167 LLAASDTDP-CQAFRHGQACW-GVQFHPE 193
Cdd:TIGR00566 143 VTAWEEENIeIMAIRHRDLPLeGVQFHPE 171
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 55-208 1.63e-09

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 56.33  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  55 DADDYA----GIVLTGSHAMVTAR--EPWSERLGH-----------WLADCAARGVtPMLGICYGHQLLAQALGG----- 112
Cdd:COG2071   42 DLDELLdrldGLVLTGGADVDPALygEEPHPELGPidperdafelaLIRAALERGK-PVLGICRGMQLLNVALGGtlyqd 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520 113 ---EVDDRRDRRFEIGTVSIGQRAEAAGDPLFAALPARFDAQV--VHYQSVHRLPPGARLLAASDTDPCQAFRHGQA--C 185
Cdd:COG2071  121 lpdQVPGALDHRQPAPRYAPRHTVEIEPGSRLARILGEEEIRVnsLHHQAVKRLGPGLRVSARAPDGVIEAIESPGApfV 200

                        170       180
                 ....*....|....*....|...
gi 817522520 186 WGVQFHPEFPLPAIEQYLAILRA 208
Cdd:COG2071  201 LGVQWHPEWLAASDPLSRRLFEA 223
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
88-193 1.37e-08

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 53.51  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  88 CAARGvTPMLGICYGHQLLAQALGGEVddrrDRRFEI--GTVSIgqrAEAAGDPLFAALPARFDAQVVHYQSV--HRLPP 163
Cdd:PRK07765  72 CAAAG-TPLLGVCLGHQAIGVAFGATV----DRAPELlhGKTSS---VHHTGVGVLAGLPDPFTATRYHSLTIlpETLPA 143

                         90       100       110
                 ....*....|....*....|....*....|.
gi 817522520 164 GARLLAASDTDPCQAFRHGQ-ACWGVQFHPE 193
Cdd:PRK07765 144 ELEVTARTDSGVIMAVRHRElPIHGVQFHPE 174
PRK06895 PRK06895
anthranilate synthase component II;
96-193 1.40e-08

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 53.20  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  96 MLGICYGHQLLAQALGGEVddrrdrrFEIGTVSIGQRA---EAAGDPLFAALPARFDAQVVHYQSV--HRLPPGARLLAA 170
Cdd:PRK06895  75 ILGVCLGHQTLCEFFGGEL-------YNLNNVRHGQQRplkVRSNSPLFDGLPEEFNIGLYHSWAVseENFPTPLEITAV 147

                         90       100
                 ....*....|....*....|....
gi 817522520 171 SDTDPCQAFRHGQ-ACWGVQFHPE 193
Cdd:PRK06895 148 CDENVVMAMQHKTlPIYGVQFHPE 171
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 97-200 3.97e-07

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 49.58  E-value: 3.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  97 LGICYGHQLLAQALGGEVDDRRDRrfEIGTVSIGQRAEAAGDPLFAALPArfDAQVVHYqsvHR----LPPGARLLAASD 172
Cdd:PRK08250  88 IGVCLGAQLIGEALGAKYEHSPEK--EIGYFPITLTEAGLKDPLLSHFGS--TLTVGHW---HNdmpgLTDQAKVLATSE 160

                         90       100
                 ....*....|....*....|....*...
gi 817522520 173 TDPCQAFRHGQACWGVQFHPEFPLPAIE 200
Cdd:PRK08250 161 GCPRQIVQYSNLVYGFQCHMEFTVEAVE 188
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 61-208 4.89e-07

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 48.73  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  61 GIVLTGSH----------AMVTAREPWSER----LgHWLADCAARGVtPMLGICYGHQLLAQALGGevddrrdrrfeigt 126
Cdd:cd01745   56 GLLLTGGGdvdpplygeePHPELGPIDPERdafeL-ALLRAALERGK-PILGICRGMQLLNVALGG-------------- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520 127 vSIGQraeaagdplfaalparfDAQV--VHYQSVHRLPPGARLLAASDTDPCQAFRHGQACW--GVQFHPEFPLPAIEQY 202
Cdd:cd01745  120 -TLYQ-----------------DIRVnsLHHQAIKRLADGLRVEARAPDGVIEAIESPDRPFvlGVQWHPEWLADTDPDS 181


                 ....*.
gi 817522520 203 LAILRA 208
Cdd:cd01745  182 LKLFEA 187
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
92-193 1.06e-06

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 47.60  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  92 GVTPMLGICYGHQLLAQALGGEVddRRDRRFEIGTVSIgqrAEAAGDPLFAALPARFdaQVVHYQSV----HRLPPGARL 167
Cdd:PRK08007  71 GRLPILGVCLGHQAMAQAFGGKV--VRAAKVMHGKTSP---ITHNGEGVFRGLANPL--TVTRYHSLvvepDSLPACFEV 143

                         90       100
                 ....*....|....*....|....*....
gi 817522520 168 LAASDTDPCQAFRHGQacW---GVQFHPE 193
Cdd:PRK08007 144 TAWSETREIMGIRHRQ--WdleGVQFHPE 170
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 52-106 3.66e-06

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: 44.90  E-value: 3.66e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 817522520  52 ALPDADDYAGIVLTGSHAMVTAREpWSERLGHWLADCAARGVtPMLGICYGHQLL 106
Cdd:cd01653   40 SDVDLDDYDGLILPGGPGTPDDLA-RDEALLALLREAAAAGK-PILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 52-106 6.14e-06

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: 43.73  E-value: 6.14e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 817522520  52 ALPDADDYAGIVLTGSHAMVTAREpWSERLGHWLADCAARGVtPMLGICYGHQLL 106
Cdd:cd03128   40 SDVDLDDYDGLILPGGPGTPDDLA-WDEALLALLREAAAAGK-PVLGICLGAQLL 92
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
92-193 8.92e-06

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 46.25  E-value: 8.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  92 GVTPMLGICYGHQLLAQALGGEVddRRDRRFEIGTVSigqRAEAAGDPLFAALPARFDAQVVHYQSVHR--LPPGARLLA 169
Cdd:PRK14607  72 GKVPILGVCLGHQAIGYAFGGKI--VHAKRILHGKTS---PIDHNGKGLFRGIPNPTVATRYHSLVVEEasLPECLEVTA 146

                         90       100
                 ....*....|....*....|....*
gi 817522520 170 ASDTDPCQAFRHGQ-ACWGVQFHPE 193
Cdd:PRK14607 147 KSDDGEIMGIRHKEhPIFGVQFHPE 171
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 85-193 1.54e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 44.35  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  85 LADCAARGvTPMLGICYGHQLL---------AQALG---GEVddrrdRRFE---------IGTVSIGQRAEaagDPLFAA 143
Cdd:PRK13141  65 IKEAVASG-KPLLGICLGMQLLfesseefgeTEGLGllpGRV-----RRFPpeeglkvphMGWNQLELKKE---SPLLKG 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 817522520 144 LPARFDAQVVHyqSVHRLPPGARLLAASdTDpcqafrHGQAC---------WGVQFHPE 193
Cdd:PRK13141 136 IPDGAYVYFVH--SYYADPCDEEYVAAT-TD------YGVEFpaavgkdnvFGAQFHPE 185
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 95-193 1.91e-05

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: 44.02  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  95 PMLGICYGHQLLAQALGGE--------------VDDRRDRRFEIGTVSIGqraeaagdplFAalparfdaqvVHYQSvhr 160
Cdd:cd01744   71 PIFGICLGHQLLALALGAKtykmkfghrgsnhpVKDLITGRVYITSQNHG----------YA----------VDPDS--- 127

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 817522520 161 LPPGARLLAASDTD-PCQAFRH-GQACWGVQFHPE 193
Cdd:cd01744  128 LPGGLEVTHVNLNDgTVEGIRHkDLPVFSVQFHPE 162
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 95-113 2.02e-05

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: 45.01  E-value: 2.02e-05
                         10
                 ....*....|....*....
gi 817522520  95 PMLGICYGHQLLAQALGGE 113
Cdd:COG0505  249 PIFGICLGHQLLALALGAK 267
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 92-218 2.27e-05

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: 44.54  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   92 GVTPMLGICYGHQLLAQALGGE--------------VDDRRDRRFEIGTvsigQRAEAAGDPlfAALPARfDAQVVHYQs 157
Cdd:TIGR01368 241 EKIPIFGICLGHQLLALAFGAKtykmkfghrggnhpVKDLITGRVEITS----QNHGYAVDP--DSLPAG-DLEVTHVN- 312

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 817522520  158 vhrlppgarllaASDtDPCQAFRHGQ-ACWGVQFHPEfplpaieqylailrAQPGAHGADAL 218
Cdd:TIGR01368 313 ------------LND-GTVEGIRHKDlPVFSVQYHPE--------------ASPGPHDTEYL 347
PRK13566 PRK13566
anthranilate synthase component I;
88-193 2.38e-05

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 44.91  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  88 CAARGVtPMLGICYGHQLLAQALGGEVddrrdRRFEI---GTVSIGQRAEaaGDPLFAALPARFdaQVVHYQSVH----R 160
Cdd:PRK13566 594 ALARNL-PIFGVCLGLQAIVEAFGGEL-----GQLAYpmhGKPSRIRVRG--PGRLFSGLPEEF--TVGRYHSLFadpeT 663

                         90       100       110
                 ....*....|....*....|....*....|....
gi 817522520 161 LPPGARLLAASDTDPCQAFRHGQA-CWGVQFHPE 193
Cdd:PRK13566 664 LPDELLVTAETEDGVIMAIEHKTLpVAAVQFHPE 697
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 91-204 2.45e-05

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 45.02  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  91 RGVTPMLGICYGHQLLAQALGGEVDdrrdrrfEIGTVSIGQRA--EAAGDPLFAALPARFdaQVVHYQS-VHRLPPGARL 167
Cdd:PRK09522  75 RGKLPIIGICLGHQAIVEAYGGYVG-------QAGEILHGKASsiEHDGQAMFAGLTNPL--PVARYHSlVGSNIPAGLT 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 817522520 168 LAASDTDPCQAFRH--GQACwGVQFHPEFPLPA-----IEQYLA 204
Cdd:PRK09522 146 INAHFNGMVMAVRHdaDRVC-GFQFHPESILTTqgarlLEQTLA 188
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
95-113 5.30e-05

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 43.53  E-value: 5.30e-05
                         10
                 ....*....|....*....
gi 817522520  95 PMLGICYGHQLLAQALGGE 113
Cdd:PRK12564 250 PIFGICLGHQLLALALGAK 268
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 41-193 6.10e-05

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 42.70  E-value: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520   41 AIERFDARGAAAL--PDADDYAGIVLTG----SHAMVTAREpWSERLghwLADCAARGVTPMLGICYGHQLLAQAL--GG 112
Cdd:TIGR01855  17 ALKRVGAEPVVVKdsKEAELADKLILPGvgafGAAMARLRE-NGLDL---FVELVVRLGKPVLGICLGMQLLFERSeeGG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  113 EVD-----DRRDRRFEIGTV-SIG--QRAEAAGDPLFAALPARFDAQVVH-YQSVhrlPPGARLLAASD--TDPCQAFRH 181
Cdd:TIGR01855  93 GVPglgliKGNVVKLEARKVpHMGwnEVHPVKESPLLNGIDEGAYFYFVHsYYAV---CEEEAVLAYADygEKFPAAVQK 169

                         170
                  ....*....|..
gi 817522520  182 GQACwGVQFHPE 193
Cdd:TIGR01855 170 GNIF-GTQFHPE 180
PLN02335 PLN02335
anthranilate synthase
 95-193 6.44e-05

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 42.86  E-value: 6.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  95 PMLGICYGHQLLAQALGGEVdDRRDRRFEIGTVSIGQRAEAAGDPLFAALPARFDAQVVHYQSVHR--LPPGA-RLLAAS 171
Cdd:PLN02335  93 PLFGVCMGLQCIGEAFGGKI-VRSPFGVMHGKSSPVHYDEKGEEGLFSGLPNPFTAGRYHSLVIEKdtFPSDElEVTAWT 171

                         90       100
                 ....*....|....*....|....
gi 817522520 172 DTDPCQAFRHGQACW--GVQFHPE 193
Cdd:PLN02335 172 EDGLIMAARHRKYKHiqGVQFHPE 195
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 41-193 1.09e-04

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 41.71  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  41 AIER--FDARGAAALPDADDYAGIVLTG----SHAMVTARE-PWSErlghWLADCAARGVtPMLGICYGHQLLA------ 107
Cdd:cd01748   17 ALERlgAEVIITSDPEEILSADKLILPGvgafGDAMANLRErGLIE----ALKEAIASGK-PFLGICLGMQLLFesseeg 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520 108 ---QALG---GEVddrrdRRFE---------IGTVSIGQRAEaagDPLFAALPARFDAQVVH-YqsvhRLPPGARLLAAS 171
Cdd:cd01748   92 ggtKGLGlipGKV-----VRFPaseglkvphMGWNQLEITKE---SPLFKGIPDGSYFYFVHsY----YAPPDDPDYILA 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 817522520 172 DTDpcqafrHGQA---------CWGVQFHPE 193
Cdd:cd01748  160 TTD------YGGKfpaavekdnIFGTQFHPE 184
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 55-193 1.70e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 41.31  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  55 DADDYA---GIVLTGSHAMVTAREPWSER-LGHWLADCAARGVTPMLGICYGHQLLA---------QALG---GEV---- 114
Cdd:PRK13146  35 DPDAVAaadRVVLPGVGAFADCMRGLRAVgLGEAVIEAVLAAGRPFLGICVGMQLLFerglehgdtPGLGlipGEVvrfq 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520 115 -DDRRDRRFEIG--TVSIgqraeAAGDPLFAALPARFDAQVVH-YQSVHRLPP--------GARLLAASDTDPcqafrhg 182
Cdd:PRK13146 115 pDGPALKVPHMGwnTVDQ-----TRDHPLFAGIPDGARFYFVHsYYAQPANPAdvvawtdyGGPFTAAVARDN------- 182

                        170
                 ....*....|.
gi 817522520 183 qaCWGVQFHPE 193
Cdd:PRK13146 183 --LFATQFHPE 191
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
92-193 1.83e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 41.02  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  92 GVTPMLGICYGHQLLAQALGGEVddRRDRRFEIGTVSIgqrAEAAGDPLFAALP-----ARFDAQVVHYQSvhrLPPGAR 166
Cdd:PRK08857  71 GKLPILGVCLGHQAIAQVFGGQV--VRARQVMHGKTSP---IRHTGRSVFKGLNnpltvTRYHSLVVKNDT---LPECFE 142

                         90       100       110
                 ....*....|....*....|....*....|...
gi 817522520 167 LLAASDT-----DPCQAFRHGQ-ACWGVQFHPE 193
Cdd:PRK08857 143 LTAWTELedgsmDEIMGFQHKTlPIEAVQFHPE 175
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 85-193 2.48e-04

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 40.79  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  85 LADCAARGVtPMLGICYGHQLLA---------QALG---GEVddrrdRRFE--------IG--TVSIgqraeAAGDPLFA 142
Cdd:COG0118   66 IREAVAGGK-PVLGICLGMQLLFerseengdtEGLGlipGEV-----VRFPasdlkvphMGwnTVEI-----AKDHPLFA 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 817522520 143 ALPARFDAQVVH-YqsvhRLPPGARLLAASDTDpcqafrHGQA---------CWGVQFHPE 193
Cdd:COG0118  135 GIPDGEYFYFVHsY----YVPPDDPEDVVATTD------YGVPftaavergnVFGTQFHPE 185
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 92-145 4.25e-04

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 41.12  E-value: 4.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817522520  92 GVTPMLGICYGHQLLAQALGGE--------------VDDRRDRRFEIGtvsiGQRAEAAGDPlfAALP 145
Cdd:PLN02771 309 GKVPVFGICMGHQLLGQALGGKtfkmkfghhggnhpVRNNRTGRVEIS----AQNHNYAVDP--ASLP 370
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 95-113 8.32e-04

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 39.87  E-value: 8.32e-04
                         10
                 ....*....|....*....
gi 817522520  95 PMLGICYGHQLLAQALGGE 113
Cdd:PRK12838 239 PILGICLGHQLIALALGAD 257
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
92-193 4.76e-03

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 37.15  E-value: 4.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817522520  92 GVTPMLGICYGHQLLAQALGGEVddRRDRRFEIGTVSIGQRAEAAgdpLFAALP-----ARFDAQVVHYQSvhrLPPGAR 166
Cdd:PRK06774  71 DKLPILGVCLGHQALGQAFGARV--VRARQVMHGKTSAICHSGQG---VFRGLNqpltvTRYHSLVIAADS---LPGCFE 142

                         90       100       110
                 ....*....|....*....|....*....|..
gi 817522520 167 LLAASD----TDPCQAFRHGQ-ACWGVQFHPE 193
Cdd:PRK06774 143 LTAWSErggeMDEIMGIRHRTlPLEGVQFHPE 174
 
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