|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
7-191 |
1.21e-79 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 235.13 E-value: 1.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 7 IDVVDNGGQWTHREWRMLRYLGVDTQIIPNDALCDDLREL-DGLLLSGGAARvgltGKLGNCGE-LLGLDLPILGICAGH 84
Cdd:PRK00758 2 IVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKAFeDGLILSGGPDI----ERAGNCPEyLKELDVPILGICLGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 85 QFMARHYGGDCGEAETPEFGAMEITLNDGGGaLFQETPETQVVWESHNDEVTIVPEDFFITASSPSCQVQAMENTDGNRF 164
Cdd:PRK00758 78 QLIAKAFGGEVGRGEYGEYALVEVEILDEDD-ILKGLPPEIRVWASHADEVKELPDGFEILARSDICEVEAMKHKEKPIY 156
|
170 180
....*....|....*....|....*..
gi 663509034 165 GLQFHPEVNDSEYGAKIMENFVEICRQ 191
Cdd:PRK00758 157 GVQFHPEVAHTEYGEEIFKNFLEICGK 183
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
7-186 |
2.85e-68 |
|
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: 206.23 E-value: 2.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 7 IDVVDNGGQWTHREWRMLRYLGVDTQIIPND--ALCDDLRELDGLLLSGGAARVGLTGKLGNCGELLGLDLPILGICAGH 84
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTtpLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 85 QFMARHYGGDCGEAETPEFGAMEITLNDGGgALFQETPETQVVWESHNDEVTIVPEDFFITASSPSCQVQAMENTDGNRF 164
Cdd:cd01742 81 QLIAKALGGKVERGDKREYGKAEIEIDDSS-PLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIY 159
|
170 180
....*....|....*....|..
gi 663509034 165 GLQFHPEVNDSEYGAKIMENFV 186
Cdd:cd01742 160 GVQFHPEVTHTEKGKEILKNFL 181
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
7-190 |
1.85e-62 |
|
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: 191.76 E-value: 1.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 7 IDVVDNGGQWTHREWRMLRYLGVDTQIIPNDALCDDLRELD--GLLLSGGAARVgltgKLGNC----GELLGLDLPILGI 80
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNpkGIILSGGPSSV----YAENApradEKIFELGVPVLGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 81 CAGHQFMARHYGGDCGEAETPEFGAMEITLnDGGGALFQETPETQVVWESHNDEVTIVPEDFFITASSPSCQVQAMENTD 160
Cdd:TIGR00888 77 CYGMQLMAKQLGGEVGRAEKREYGKAELEI-LDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEE 155
|
170 180 190
....*....|....*....|....*....|.
gi 663509034 161 GNRFGLQFHPEVNDSEYGAKIMENFVE-ICR 190
Cdd:TIGR00888 156 KPIYGVQFHPEVTHTEYGNELLENFVYdVCG 186
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
9-189 |
5.21e-51 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 171.38 E-value: 5.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 9 VVDNGGQWTHREWRMLRYLGVDTQIIPNDALCDDLRELD--GLLLSGGAARVGLTGKLGNCGELLGLDLPILGICAGHQF 86
Cdd:PRK00074 8 ILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNpkGIILSGGPASVYEEGAPRADPEIFELGVPVLGICYGMQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 87 MARHYGGDCGEAETPEFGAMEITLnDGGGALFQETPETQVVWESHNDEVTIVPEDFFITASSPSCQVQAMENTDGNRFGL 166
Cdd:PRK00074 88 MAHQLGGKVERAGKREYGRAELEV-DNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEERKFYGV 166
|
170 180
....*....|....*....|....
gi 663509034 167 QFHPEVNDSEYGAKIMENFV-EIC 189
Cdd:PRK00074 167 QFHPEVTHTPQGKKLLENFVfDIC 190
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
5-189 |
5.27e-46 |
|
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: 150.87 E-value: 5.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 5 LVIDVVDNGGQWTHREWRMLRYLGV--------DTQIIPNDAlcdDLRELDGLLLSGGAARV-----GLTGKLGNCGELL 71
Cdd:COG0518 3 LILDHDPFGGQYPGLIARRLREAGIeldvlrvyAGEILPYDP---DLEDPDGLILSGGPMSVydedpWLEDEPALIREAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 72 GLDLPILGICAGHQFMARHYGGDCGEAETPEFGAMEITLNDGGgALFQETPETQVVWESHNDEVTIVPEDFFITASSPSC 151
Cdd:COG0518 80 ELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEAD-PLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSDNC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663509034 152 QVQAMENTDgNRFGLQFHPEVN------------------------------DSEYGAKIMENFVEIC 189
Cdd:COG0518 159 PNQAFRYGR-RVYGVQFHPEVThtmmeawleeradelaaeellaeaslhdpeLREAGRRLLRNFLREI 225
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
9-189 |
3.18e-37 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 127.35 E-value: 3.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 9 VVDNGGQWTHREWRMLRYLGVDTQIIPNDALCDDLREL--DGLLLSGGAARVG-LTGKLGNCGELLGLDLPILGICAGHQ 85
Cdd:pfam00117 2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEEnpDGIILSGGPGSPGaAGGAIEAIREARELKIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 86 FMARHYGGDCGEAETPEFGAMEITLNDGGGALFQETPETQVVWESHNDEVT--IVPEDFFITA-SSPSCQVQAMENTDGN 162
Cdd:pfam00117 82 LLALAFGGKVVKAKKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDpdTLPDGLEVTAtSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*..
gi 663509034 163 RFGLQFHPEVNDSEYGAKIMENFVEIC 189
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
4-190 |
3.80e-30 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 115.55 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 4 PLVIdVVDNGGQWTHREWRMLRYLGVDTQIIPNDAlcdDLRELDGL-----LLSGGAARVGLTGK-------LGNCGELl 71
Cdd:PLN02347 11 DVVL-ILDYGSQYTHLITRRVRELGVYSLLLSGTA---SLDRIASLnprvvILSGGPHSVHVEGAptvpegfFDYCRER- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 72 glDLPILGICAGHQFMARHYGGDCGEAETPEFGAMEITLNdGGGALFQETPE--TQVVWESHNDEVTIVPEDFFITASSP 149
Cdd:PLN02347 86 --GVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVV-CGSQLFGDLPSgeTQTVWMSHGDEAVKLPEGFEVVAKSV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663509034 150 SCQVQAMENTDGNRFGLQFHPEVNDSEYGAKIMENFV-EICR 190
Cdd:PLN02347 163 QGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFLfDVCG 204
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
23-191 |
1.40e-25 |
|
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: 97.42 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 23 MLRYLGVDTQIIPNDAL-CDDLREL--DGLLLSGG------AarvgltgklGNCGEL---LGLDLPILGICAGHQFMARH 90
Cdd:COG0512 17 YLGELGAEVVVVRNDEItLEEIEALapDGIVLSPGpgtpeeA---------GISLEViraFAGKIPILGVCLGHQAIGEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 91 YGGDCGEAETPEFG-AMEITLNDGGgaLFQETPETQVVWESHN---DEVTIvPEDFFITASSPSCQVQAMENTDGNRFGL 166
Cdd:COG0512 88 FGGKVVRAPEPMHGkTSPITHDGSG--LFAGLPNPFTATRYHSlvvDRETL-PDELEVTAWTEDGEIMGIRHRELPIEGV 164
|
170 180
....*....|....*....|....*
gi 663509034 167 QFHPEVNDSEYGAKIMENFVEICRQ 191
Cdd:COG0512 165 QFHPESILTEHGHQLLANFLELAGE 189
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
34-186 |
1.53e-24 |
|
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: 94.62 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 34 IPNDALCDDLRELDGLLLSGGAARVG------LTGKLGNCGELLGLDLPILGICAGHQFMARHYGGDCGEAETP-EFGAM 106
Cdd:cd01741 35 VYAGELLPDLDDYDGLVILGGPMSVDeddypwLKKLKELIRQALAAGKPVLGICLGHQLLARALGGKVGRNPKGwEIGWF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 107 EITLNDGGGA--LFQETPETQVVWESHNDEVTIVPEDFFITASSPSCQVQAMEnTDGNRFGLQFHPEvndseygAKIMEN 184
Cdd:cd01741 115 PVTLTEAGKAdpLFAGLPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFR-YGDRALGLQFHPE-------ERLLRN 186
|
..
gi 663509034 185 FV 186
Cdd:cd01741 187 FL 188
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
24-190 |
1.89e-23 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 91.73 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 24 LRYLGVDTQIIPNDAL-CDDLREL--DGLLLSGGAarvGLTGKLGNCGEL---LGLDLPILGICAGHQFMARHYGGDCGE 97
Cdd:PRK05670 19 LGELGAEVVVYRNDEItLEEIEALnpDAIVLSPGP---GTPAEAGISLELireFAGKVPILGVCLGHQAIGEAFGGKVVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 98 AETPEFG-AMEITLNDGGgaLFQETPETQVVWESHNDEV--TIVPEDFFITASSPSCQVQAMENTDGNRFGLQFHPEVND 174
Cdd:PRK05670 96 AKEIMHGkTSPIEHDGSG--IFAGLPNPFTVTRYHSLVVdrESLPDCLEVTAWTDDGEIMGVRHKELPIYGVQFHPESIL 173
|
170
....*....|....*.
gi 663509034 175 SEYGAKIMENFVEICR 190
Cdd:PRK05670 174 TEHGHKLLENFLELAR 189
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
23-186 |
2.65e-23 |
|
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: 91.44 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 23 MLRYLGVDTQIIPNDALCDDLREL---DGLLLSGGAARVGLTGKLGNCGELLGLDLPILGICAGHQFMARHYGGDCGEAE 99
Cdd:cd01743 17 YLRELGAEVVVVRNDEITLEELELlnpDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGHQAIAEAFGGKVVRAP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 100 TPEFG-AMEITLNDGGgaLFQETPETQVVWESHN---DEVTIvPEDFFITASSPSCQVQAMENTDGNRFGLQFHPEVNDS 175
Cdd:cd01743 97 EPMHGkTSEIHHDGSG--LFKGLPQPFTVGRYHSlvvDPDPL-PDLLEVTASTEDGVIMALRHRDLPIYGVQFHPESILT 173
|
170
....*....|.
gi 663509034 176 EYGAKIMENFV 186
Cdd:cd01743 174 EYGLRLLENFL 184
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
7-192 |
1.43e-16 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 76.68 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 7 IDVVDNGGQWTHREWRMLRYLGVDTQII--PNDALCDDLREL--DGLLLSGGAARvglTGKLGNCGEL---LGLDLPILG 79
Cdd:PRK14607 2 IILIDNYDSFTYNIYQYIGELGPEEIEVvrNDEITIEEIEALnpSHIVISPGPGR---PEEAGISVEVirhFSGKVPILG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 80 ICAGHQFMARHYGGDCGEAETPEFGAMEITLNDGGGaLFQETPETQVVWESHN---DEVTIvPEDFFITASSPSCQVQAM 156
Cdd:PRK14607 79 VCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKG-LFRGIPNPTVATRYHSlvvEEASL-PECLEVTAKSDDGEIMGI 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 663509034 157 ENTDGNRFGLQFHPEVNDSEYGAKIMENFVEICRQS 192
Cdd:PRK14607 157 RHKEHPIFGVQFHPESILTEEGKRILKNFLNYQREE 192
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
68-191 |
3.66e-15 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 72.64 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 68 GELLGLDLPILGICAGHQFMARHYGGDCGEAETPEFG-AMEITLNdGGGALFQETPETQVVWESHN--DEVTIVPEDFFI 144
Cdd:PRK13566 592 DAALARNLPIFGVCLGLQAIVEAFGGELGQLAYPMHGkPSRIRVR-GPGRLFSGLPEEFTVGRYHSlfADPETLPDELLV 670
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 663509034 145 TASSPSCQVQAMENTDGNRFGLQFHPE---VNDSEYGAKIMENFVEICRQ 191
Cdd:PRK13566 671 TAETEDGVIMAIEHKTLPVAAVQFHPEsimTLGGDVGLRIIENVVRLLAG 720
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
6-186 |
1.02e-13 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 66.09 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 6 VIDVVDNGGQWThreWRMLRY---LGVDTQIIPNDALCddLRELDGL-----LLSGGAARVGLTG-KLGNCGELLGlDLP 76
Cdd:PRK08007 1 MILLIDNYDSFT---WNLYQYfceLGADVLVKRNDALT--LADIDALkpqkiVISPGPCTPDEAGiSLDVIRHYAG-RLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 77 ILGICAGHQFMARHYGGDCGEAETPEFGAMEITLNDGGGaLFQETPETQVVWESHN---DEVTIvPEDFFITASSPSCQV 153
Cdd:PRK08007 75 ILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEG-VFRGLANPLTVTRYHSlvvEPDSL-PACFEVTAWSETREI 152
|
170 180 190
....*....|....*....|....*....|...
gi 663509034 154 QAMENTDGNRFGLQFHPEVNDSEYGAKIMENFV 186
Cdd:PRK08007 153 MGIRHRQWDLEGVQFHPESILSEQGHQLLANFL 185
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
75-187 |
1.51e-12 |
|
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: 62.88 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 75 LPILGICAGHQFMARHYGGDCGEAETPEFGAM-EITLNDGGGALFQETPETQVVWESHNDEVTIVPEDFFITASSPSCQ- 152
Cdd:TIGR00566 73 LPILGVCLGHQAMGQAFGGDVVRANTVMHGKTsEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIe 152
|
90 100 110
....*....|....*....|....*....|....*
gi 663509034 153 VQAMENTDGNRFGLQFHPEVNDSEYGAKIMENFVE 187
Cdd:TIGR00566 153 IMAIRHRDLPLEGVQFHPESILSEQGHQLLANFLH 187
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
44-182 |
6.10e-12 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 62.29 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 44 RELDGLLLSGGAARVglTGKL-------GNCGELLGLDLPILGICAGHQFMARHYGGDCGeaETP---EFGAMEITLNDG 113
Cdd:PRK09065 53 DDFAGVIITGSWAMV--TDRLdwsertaDWLRQAAAAGMPLLGICYGHQLLAHALGGEVG--YNPagrESGTVTVELHPA 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663509034 114 GG--ALFQETPETQVVWESHNDEVTIVPEDFFITASSPSCQVQAMENTDgNRFGLQFHPevndsEYGAKIM 182
Cdd:PRK09065 129 AAddPLFAGLPAQFPAHLTHLQSVLRLPPGAVVLARSAQDPHQAFRYGP-HAWGVQFHP-----EFTAHIM 193
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
75-194 |
1.07e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 60.97 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 75 LPILGICAGHQFMARHYGGDCGEAETPEFGAMEITLNDGGGaLFQETPETQVVWESHNDEVT--IVPEDFFITASSPSCQ 152
Cdd:PRK07649 73 IPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKT-IFSDIPNPFTATRYHSLIVKkeTLPDCLEVTSWTEEGE 151
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 663509034 153 VQAMENTDGNRFGLQFHPEVNDSEYGAKIMENFVEICRQSRN 194
Cdd:PRK07649 152 IMAIRHKTLPIEGVQFHPESIMTSHGKELLQNFIRKYSPSVT 193
|
|
| PRK07567 |
PRK07567 |
glutamine amidotransferase; Provisional |
69-190 |
1.37e-11 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181035 [Multi-domain] Cd Length: 242 Bit Score: 61.11 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 69 ELLGLDLPILGICAGHQFMARHYGGDCGEAETPEFGAMEITLNDGGGA--LFQETPETQVVWESHNDEVTIVPEDFFITA 146
Cdd:PRK07567 88 EVVARDFPFLGACYGVGTLGHHQGGVVDRTYGEPVGAVTVSLTDAGRAdpLLAGLPDTFTAFVGHKEAVSALPPGAVLLA 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663509034 147 SSPSCQVQAM---ENTdgnrFGLQFHPEVN--------------------------------DSEYGAKIMENFVEICR 190
Cdd:PRK07567 168 TSPTCPVQMFrvgENV----YATQFHPELDadglktridfyrdhgyfapeeadsliararsvDVTAPNRILRNFVERYR 242
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
1-183 |
4.38e-11 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 60.81 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 1 MANPLVIDVVDNggqWTHREWRMLRYLGVDTQI----IPNDALCDDLRELDG--LLLSGGAarvGLTGKLGNCGELLGL- 73
Cdd:PRK09522 1 MADILLLDNIDS---FTYNLADQLRSNGHNVVIyrnhIPAQTLIERLATMSNpvLMLSPGP---GVPSEAGCMPELLTRl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 74 --DLPILGICAGHQFMARHYGGDCGEAETPEFGAMEITLNDgGGALFQETPETQVVWESHNDEVTIVPEDFFITASSpSC 151
Cdd:PRK09522 75 rgKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHD-GQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHF-NG 152
|
170 180 190
....*....|....*....|....*....|..
gi 663509034 152 QVQAMENTDGNRFGLQFHPEVNDSEYGAKIME 183
Cdd:PRK09522 153 MVMAVRHDADRVCGFQFHPESILTTQGARLLE 184
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
7-189 |
4.43e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 59.29 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 7 IDVVDNGGQWTHREWRMLRYLGVDTQIIPND-----ALCDDLRELDGLLLSGGAarvGLTGKLGNCGELL----GLDLPI 77
Cdd:PRK07765 3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDdprlaDEAAVAAQFDGVLLSPGP---GTPERAGASIDMVracaAAGTPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 78 LGICAGHQFMARHYGGDCGEAetPEF--GAMEITLNDGGGaLFQETPE--TQVVWESHNDEVTIVPEDFFITASSPSCQV 153
Cdd:PRK07765 80 LGVCLGHQAIGVAFGATVDRA--PELlhGKTSSVHHTGVG-VLAGLPDpfTATRYHSLTILPETLPAELEVTARTDSGVI 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 663509034 154 QAMENTDGNRFGLQFHPEVNDSEYGAKIMENFVEIC 189
Cdd:PRK07765 157 MAVRHRELPIHGVQFHPESVLTEGGHRMLANWLTVC 192
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
22-186 |
4.26e-10 |
|
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: 55.97 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 22 RMLRYLGVDTQIIPNDALCDDLREL--DGLLLSGG---AARVGLTgkLGNCGELLGLDLPILGICAGHQFMARHYGGD-- 94
Cdd:cd01744 14 RELLKRGCEVTVVPYNTDAEEILKLdpDGIFLSNGpgdPALLDEA--IKTVRKLLGKKIPIFGICLGHQLLALALGAKty 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 95 ------------CGEAETpefGAMEITlndgggalfqetpetqvvweSHN-----DEVTiVPEDFFITASSPSCQ-VQAM 156
Cdd:cd01744 92 kmkfghrgsnhpVKDLIT---GRVYIT--------------------SQNhgyavDPDS-LPGGLEVTHVNLNDGtVEGI 147
|
170 180 190
....*....|....*....|....*....|....
gi 663509034 157 ENTDGNRFGLQFHPEVN----DSEYgakIMENFV 186
Cdd:cd01744 148 RHKDLPVFSVQFHPEASpgphDTEY---LFDEFL 178
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
33-186 |
6.15e-10 |
|
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: 56.04 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 33 IIPND----ALCDDLRELDGLLLSGGA----ARVGLTgKLGNCGEL---------------LGLDLPILGICAGHQFMAR 89
Cdd:cd01745 37 LLPPVddeeDLEQYLELLDGLLLTGGGdvdpPLYGEE-PHPELGPIdperdafelallraaLERGKPILGICRGMQLLNV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 90 HYGGDcgeaetpefgameitlndgggaLFQETpetQVVweS-HNDEVTIVPEDFFITASSPSCQVQAMENTDGNR-FGLQ 167
Cdd:cd01745 116 ALGGT----------------------LYQDI---RVN--SlHHQAIKRLADGLRVEARAPDGVIEAIESPDRPFvLGVQ 168
|
170 180
....*....|....*....|.
gi 663509034 168 FHPE--VNDSEYGAKIMENFV 186
Cdd:cd01745 169 WHPEwlADTDPDSLKLFEAFV 189
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
7-187 |
8.27e-10 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 55.51 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 7 IDVVDNGGQWTHREWRMLRYLGVDTQIIPNDALcdDLRELD-----GLLLSGGAarvGLTGKLGNCGEL---LGLDLPIL 78
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEI--DLSKIKnlnirHIIISPGP---GHPRDSGISLDVissYAPYIPIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 79 GICAGHQFMARHYGGDCGEAETPEFGAMEITLNDGGGaLFQETPETQVVWESHN---DEVTIvPEDFFITASSPSCQVQA 155
Cdd:CHL00101 77 GVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDD-LFQGLPNPFTATRYHSliiDPLNL-PSPLEITAWTEDGLIMA 154
|
170 180 190
....*....|....*....|....*....|....
gi 663509034 156 MENTDgNRF--GLQFHPEVNDSEYGAKIMENFVE 187
Cdd:CHL00101 155 CRHKK-YKMlrGIQFHPESLLTTHGQQILRNFLS 187
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
65-187 |
6.72e-09 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 53.31 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 65 GNCGELLGLDL---PILGICAGHQFMARHYGGDCgEAETPEFGAME-ITLNDGGG--ALF-----------QETPETQV- 126
Cdd:PRK05637 61 GNMMALIDRTLgqiPLLGICLGFQALLEHHGGKV-EPCGPVHGTTDnMILTDAGVqsPVFaglatdvepdhPEIPGRKVp 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663509034 127 VWESHNDEVTIVPEDFFITASSPSC---QVQAMENTDGNRFGLQFHPEVNDSEYGAKIMENFVE 187
Cdd:PRK05637 140 IARYHSLGCVVAPDGMESLGTCSSEigpVIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVE 203
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
77-188 |
6.90e-09 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 53.20 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 77 ILGICAGHQFMARHYGGDCGEAETPEFGAMEITLNDGGGALFQETPETQVVWESHNDEVT--IVPEDFFITASSPSCQVQ 154
Cdd:PRK06895 75 ILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPLFDGLPEEFNIGLYHSWAVSeeNFPTPLEITAVCDENVVM 154
|
90 100 110
....*....|....*....|....*....|....
gi 663509034 155 AMENTDGNRFGLQFHPEVNDSEYGAKIMENFVEI 188
Cdd:PRK06895 155 AMQHKTLPIYGVQFHPESYISEFGEQILRNWLAI 188
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
24-191 |
8.58e-09 |
|
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: 53.78 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 24 LRYL---GVDTQIIPNDALCDDLREL--DGLLLSGG-----AARVGLTgklgNCGELLGlDLPILGICAGHQFMARHYGG 93
Cdd:TIGR01368 187 LRRLvkrGCEVTVVPYDTDAEEIKKYnpDGIFLSNGpgdpaAVEPAIE----TIRKLLE-KIPIFGICLGHQLLALAFGA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 94 D--------------CGEAETpefGAMEITlndgggalfqetpetqvvweSHN-----DEVTIVPEDFFITASSPSCQ-V 153
Cdd:TIGR01368 262 KtykmkfghrggnhpVKDLIT---GRVEIT--------------------SQNhgyavDPDSLPAGDLEVTHVNLNDGtV 318
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663509034 154 QAMENTDGNRFGLQFHPEV----NDSEYgakIMENFVEICRQ 191
Cdd:TIGR01368 319 EGIRHKDLPVFSVQYHPEAspgpHDTEY---LFDEFIDLMKK 357
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
71-188 |
8.79e-09 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 53.41 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 71 LGLDLPILGICAGHQFMARHYGGDCGEAETPEFGAMEITLNDGG-----GALFQETPetqvVWESHNDEVTIvPEDFFIT 145
Cdd:PRK07053 80 LAAGLPTLGICLGAQLIARALGARVYPGGQKEIGWAPLTLTDAGrasplRHLGAGTP----VLHWHGDTFDL-PEGATLL 154
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 663509034 146 ASSPSCQVQAMENTDgNRFGLQFHPEVNDSEYGAKIMENFVEI 188
Cdd:PRK07053 155 ASTPACRHQAFAWGN-HVLALQFHPEAREDRFEAWLIGHAGEL 196
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
1-188 |
2.30e-08 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 52.11 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 1 MANPLVidVVDNGGQWTHREWRMLRYLGVDTQIIPNDALC-DDLRELD--GLLLSGGAARVGLTG-KLGNCGELlGLDLP 76
Cdd:PLN02335 17 QNGPII--VIDNYDSFTYNLCQYMGELGCHFEVYRNDELTvEELKRKNprGVLISPGPGTPQDSGiSLQTVLEL-GPLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 77 ILGICAGHQFMARHYGGDCGEAetpEFGAME------ITLNDGGGALFQETPETQVVWESHN---DEVTIVPEDFFITAS 147
Cdd:PLN02335 94 LFGVCMGLQCIGEAFGGKIVRS---PFGVMHgksspvHYDEKGEEGLFSGLPNPFTAGRYHSlviEKDTFPSDELEVTAW 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663509034 148 SPSCQVQAMENTDGNRF-GLQFHPEVNDSEYGAKIMENFVEI 188
Cdd:PLN02335 171 TEDGLIMAARHRKYKHIqGVQFHPESIITTEGKTIVRNFIKI 212
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
9-186 |
3.60e-08 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 51.03 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 9 VVDNGGQWTHREWRMLRYLGVDTQIIPNDAL-CDDLRELD--GLLLSGGAARVGLTGKLGNCGELLGLDLPILGICAGHQ 85
Cdd:PRK08857 4 MIDNYDSFTYNLYQYFCELGAQVKVVRNDEIdIDGIEALNptHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 86 FMARHYGGDCGEAETPEFGAMEITLNDGGGaLFQ--ETPETQVVWESHNDEVTIVPEDFFITASSpscqvqamENTDGNR 163
Cdd:PRK08857 84 AIAQVFGGQVVRARQVMHGKTSPIRHTGRS-VFKglNNPLTVTRYHSLVVKNDTLPECFELTAWT--------ELEDGSM 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 663509034 164 -------------FGLQFHPEVNDSEYGAKIMENFV 186
Cdd:PRK08857 155 deimgfqhktlpiEAVQFHPESIKTEQGHQLLANFL 190
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
22-177 |
4.64e-08 |
|
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: 51.95 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 22 RMLRYLGVDTQIIPNDALCDDLREL--DGLLLSGG----AArvgLTGKLGNCGELLGLDLPILGICAGHQFMARHYGGD- 94
Cdd:COG0505 192 RELAERGCRVTVVPATTSAEEILALnpDGVFLSNGpgdpAA---LDYAIETIRELLGKGIPIFGICLGHQLLALALGAKt 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 95 -------------CGEAETpefGAMEITlndgggalfqetpetqvvweSHN-----DEVTIVPEDFFITASSP---ScqV 153
Cdd:COG0505 269 yklkfghrganhpVKDLET---GRVEIT--------------------SQNhgfavDEDSLPATDLEVTHVNLndgT--V 323
|
170 180
....*....|....*....|....*...
gi 663509034 154 QAMENTDGNRFGLQFHPEV----NDSEY 177
Cdd:COG0505 324 EGLRHKDLPAFSVQYHPEAspgpHDSAY 351
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
7-87 |
5.28e-08 |
|
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: 49.13 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 7 IDVVDNGGQWT---HREWRMLRYLGVDTQIIPNDA----LCDDLRELDGLLLSGG----AARVGLTGKLGNCGELLGLDL 75
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGgpveSDVDLDDYDGLILPGGpgtpDDLARDEALLALLREAAAAGK 80
|
90
....*....|..
gi 663509034 76 PILGICAGHQFM 87
Cdd:cd01653 81 PILGICLGAQLL 92
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
22-187 |
5.65e-08 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 51.61 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 22 RMLRYLGVDTQIIPNDALCDDLREL--DGLLLSGG----AArvgLTGKLGNCGELLGLDLPILGICAGHQFMARHYGGD- 94
Cdd:PRK12564 193 RELAERGCRVTVVPATTTAEEILALnpDGVFLSNGpgdpAA---LDYAIEMIRELLEKKIPIFGICLGHQLLALALGAKt 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 95 -------------CGEAETpefGAMEITlndgggalfqetpetqvvweSHN-----DEVTIvPEDFFITASSP---ScqV 153
Cdd:PRK12564 270 ykmkfghrganhpVKDLET---GKVEIT--------------------SQNhgfavDEDSL-PANLEVTHVNLndgT--V 323
|
170 180 190
....*....|....*....|....*....|....*...
gi 663509034 154 QAMENTDGNRFGLQFHPEV----NDSEYgakIMENFVE 187
Cdd:PRK12564 324 EGLRHKDLPAFSVQYHPEAspgpHDSAY---LFDEFVE 358
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
9-190 |
6.90e-08 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 51.77 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 9 VVDNGGQWTHREWRMLRYL-GVDTQIIPNDAL-----CDDLRE---LDGLLLSGGAARVGLTGKLGNCGELL--GLDLPI 77
Cdd:PLN02889 86 LIDNYDSYTYNIYQELSIVnGVPPVVVRNDEWtweevYHYLYEekaFDNIVISPGPGSPTCPADIGICLRLLleCRDIPI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 78 LGICAGHQFMARHYGGDCGEAETPEFGAM-EITLNdgGGALFQETPETQ-------------------------VVWESH 131
Cdd:PLN02889 166 LGVCLGHQALGYVHGARIVHAPEPVHGRLsEIEHN--GCRLFDDIPSGRnsgfkvvryhslvidaeslpkelvpIAWTSS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 132 ND-----------------EVTIVPEDFFIT--------ASSPSCQVQAMEN---------TDGNRFGLQFHPEVNDSEY 177
Cdd:PLN02889 244 SDtlsflesqksglvpdayESQIGQSGSSDPfssklkngTSWPSSHSERMQNgkilmgimhSTRPHYGLQFHPESIATCY 323
|
250
....*....|...
gi 663509034 178 GAKIMENFVEICR 190
Cdd:PLN02889 324 GRQIFKNFREITQ 336
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
7-87 |
9.69e-08 |
|
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: 47.97 E-value: 9.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 7 IDVVDNGGQWT---HREWRMLRYLGVDTQIIPNDA----LCDDLRELDGLLLSGG----AARVGLTGKLGNCGELLGLDL 75
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGgpveSDVDLDDYDGLILPGGpgtpDDLAWDEALLALLREAAAAGK 80
|
90
....*....|..
gi 663509034 76 PILGICAGHQFM 87
Cdd:cd03128 81 PVLGICLGAQLL 92
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
4-194 |
2.45e-07 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 49.80 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 4 PLVIDVVDNGGQWThrewrMLRYL---GVDTQIIPNDALCDDLREL--DGLLLSGGAAR-VGLTGKLGNCGELLGLDLPI 77
Cdd:CHL00197 192 QLKIIVIDFGVKYN-----ILRRLksfGCSITVVPATSPYQDILSYqpDGILLSNGPGDpSAIHYGIKTVKKLLKYNIPI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 78 LGICAGHQFMARhyggdCGEAET--PEFG------------AMEITLNDGGGALFQETPETQVVWESH---NDeVTIVPe 140
Cdd:CHL00197 267 FGICMGHQILSL-----ALEAKTfkLKFGhrglnhpsglnqQVEITSQNHGFAVNLESLAKNKFYITHfnlND-GTVAG- 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 663509034 141 dffiTASSPScqvqamentdgNRFGLQFHPEVN----DSEYgakIMENFVEICRQSRN 194
Cdd:CHL00197 340 ----ISHSPK-----------PYFSVQYHPEASpgphDADY---LFEYFIEIIKHSKS 379
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
46-171 |
2.64e-07 |
|
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: 48.79 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 46 LDGLLLSGGA----ARVG--LTGKLG------NCGEL------LGLDLPILGICAGHQFMARHYGG-------------- 93
Cdd:pfam07722 59 LDGLLLTGGPnvdpHFYGeePSESGGpydparDAYELaliraaLARGKPILGICRGFQLLNVALGGtlyqdiqeqpgftd 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 94 -DCGEAETPEFGAMEITLNdGGGALFQETPETQVVWES-HNDEVTIVPEDFFITASSPSCQVQAMENTDGNRF--GLQFH 169
Cdd:pfam07722 139 hREHCQVAPYAPSHAVNVE-PGSLLASLLGSEEFRVNSlHHQAIDRLAPGLRVEAVAPDGTIEAIESPNAKGFalGVQWH 217
|
..
gi 663509034 170 PE 171
Cdd:pfam07722 218 PE 219
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
23-187 |
3.21e-07 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 49.50 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 23 MLRYL---GVDTQIIPNDALCDDLREL--DGLLLSGGAARVG-LTGKLGNCGELLgLDLPILGICAGHQFMARHYGGDcg 96
Cdd:PRK12838 181 ILRSLskrGCKVTVLPYDTSLEEIKNLnpDGIVLSNGPGDPKeLQPYLPEIKKLI-SSYPILGICLGHQLIALALGAD-- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 97 eAETPEFGameitlNDGGGALFQETpETQVVW-ESHN-----DEVTIVPEDF---FITASSPScqVQAMENTDGNRFGLQ 167
Cdd:PRK12838 258 -TEKLPFG------HRGANHPVIDL-TTGRVWmTSQNhgyvvDEDSLDGTPLsvrFFNVNDGS--IEGLRHKKKPVLSVQ 327
|
170 180
....*....|....*....|....
gi 663509034 168 FHPEV----NDSEYgakIMENFVE 187
Cdd:PRK12838 328 FHPEAhpgpHDAEY---IFDEFLE 348
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
22-188 |
6.52e-07 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 47.55 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 22 RMLRYLGVDTqIIPNDAlcDDLRELDGLLLSG-GAA--------RVGLTGKLGncgELLGLDLPILGICAGHQFMARHY- 91
Cdd:PRK13181 17 NALKRLGVEA-VVSSDP--EEIAGADKVILPGvGAFgqamrslrESGLDEALK---EHVEKKQPVLGICLGMQLLFESSe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 92 -GGDCG----EAET----------PEFGAMEITlNDGGGALFQETPETQVVWESH------NDEVTIVPEDFFITasSPS 150
Cdd:PRK13181 91 eGNVKGlgliPGDVkrfrseplkvPQMGWNSVK-PLKESPLFKGIEEGSYFYFVHsyyvpcEDPEDVLATTEYGV--PFC 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 663509034 151 CQVQAmentdGNRFGLQFHPEvNDSEYGAKIMENFVEI 188
Cdd:PRK13181 168 SAVAK-----DNIYAVQFHPE-KSGKAGLKLLKNFAEL 199
|
|
| PRK06490 |
PRK06490 |
glutamine amidotransferase; Provisional |
76-172 |
1.47e-06 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 180590 [Multi-domain] Cd Length: 239 Bit Score: 46.88 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 76 PILGICAGHQFMARHYGGD-CGEAE-TPEFGAMEITLNDGGGALfQETPETqvVWESHNDEVTIvPEDFFITASSPSCQV 153
Cdd:PRK06490 88 PFLGICLGAQMLARHLGARvAPHPDgRVEIGYYPLRPTEAGRAL-MHWPEM--VYHWHREGFDL-PAGAELLATGDDFPN 163
|
90
....*....|....*....
gi 663509034 154 QAMENtDGNRFGLQFHPEV 172
Cdd:PRK06490 164 QAFRY-GDNAWGLQFHPEV 181
|
|
| PRK13525 |
PRK13525 |
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; |
22-190 |
7.92e-06 |
|
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
Pssm-ID: 237411 [Multi-domain] Cd Length: 189 Bit Score: 44.38 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 22 RMLRYLGVDTQIIPNDalcDDLRELDGLLLSGG--------AARVGLTGKLgncGELLGLDLPILGICAGHQFMARHYGG 93
Cdd:PRK13525 18 AALEALGAEAVEVRRP---EDLDEIDGLILPGGesttmgklLRDFGLLEPL---REFIASGLPVFGTCAGMILLAKEIEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 94 DcgeaETPEFGAMEITL--NDGGgalfqetpeTQVvwESHNDEVTI--VPEDF--------FITASSPSCQVQAMENTD- 160
Cdd:PRK13525 92 Y----EQEHLGLLDITVrrNAFG---------RQV--DSFEAELDIkgLGEPFpavfirapYIEEVGPGVEVLATVGGRi 156
|
170 180 190
....*....|....*....|....*....|....*
gi 663509034 161 -----GNRFGLQFHPEVNDseyGAKIMENFVEICR 190
Cdd:PRK13525 157 vavrqGNILATSFHPELTD---DTRVHRYFLEMVK 188
|
|
| PRK13527 |
PRK13527 |
glutamine amidotransferase subunit PdxT; Provisional |
22-174 |
1.16e-05 |
|
glutamine amidotransferase subunit PdxT; Provisional
Pssm-ID: 237412 [Multi-domain] Cd Length: 200 Bit Score: 44.11 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 22 RMLRYLGVDTQIIP-NDAlcDDLRELDGLLLSGG--------AARVGLTGKLGNCGELlglDLPILGICAGHQFMARHYG 92
Cdd:PRK13527 21 RALDELGIDGEVVEvRRP--GDLPDCDALIIPGGesttigrlMKREGILDEIKEKIEE---GLPILGTCAGLILLAKEVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 93 GD-CGEAETPEFGAMEITLNDGGGALFQETPETQVvweshndEVTIVPEDF---FITA-----SSPSCQVQAMEN----- 158
Cdd:PRK13527 96 DDrVTKTEQPLLGLMDVTVKRNAFGRQRDSFEAEI-------DLSGLDGPFhavFIRApaitkVGGDVEVLAKLDdriva 168
|
170
....*....|....*..
gi 663509034 159 -TDGNRFGLQFHPEVND 174
Cdd:PRK13527 169 vEQGNVLATAFHPELTD 185
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
75-188 |
1.35e-05 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 43.70 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 75 LPILGICAGHQFMARHYGGDCGEAETPEFGAMEITLNDGGGaLFQ--ETPETQVVWESHNDEVTIVPEDFFITASSPscQ 152
Cdd:PRK06774 73 LPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQG-VFRglNQPLTVTRYHSLVIAADSLPGCFELTAWSE--R 149
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 663509034 153 VQAMENTDGNRF------GLQFHPEVNDSEYGAKIMENFVEI 188
Cdd:PRK06774 150 GGEMDEIMGIRHrtlpleGVQFHPESILSEQGHQLLDNFLKN 191
|
|
| PRK05665 |
PRK05665 |
amidotransferase; Provisional |
77-171 |
1.72e-05 |
|
amidotransferase; Provisional
Pssm-ID: 168162 [Multi-domain] Cd Length: 240 Bit Score: 44.03 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 77 ILGICAGHQFMARHYGGDCGEAETP-EFGAMEITLNDGGGALFQETPETQVVwESHNDEVTIVPEDFFITASSPSCQVQA 155
Cdd:PRK05665 94 LLGVCFGHQLLALLLGGKAERASQGwGVGIHRYQLAAHAPWMSPAVTELTLL-ISHQDQVTALPEGATVIASSDFCPFAA 172
|
90
....*....|....*.
gi 663509034 156 MENTDgNRFGLQFHPE 171
Cdd:PRK05665 173 YHIGD-QVLCFQGHPE 187
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
160-190 |
1.76e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 43.70 E-value: 1.76e-05
10 20 30
....*....|....*....|....*....|.
gi 663509034 160 DGNRFGLQFHPEvNDSEYGAKIMENFVEICR 190
Cdd:PRK13143 170 NDNVFGTQFHPE-KSGETGLKILENFVELIK 199
|
|
| hisH |
PRK13170 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
23-188 |
2.74e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 42.92 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 23 MLRYLGVDTqIIPNDAlcDDLRELDGLLLSG-GAARVGLTgKLGNCG--ELL-GLDLPILGICAGHQFMAR----HYGGD 94
Cdd:PRK13170 19 AIERLGYEP-VVSRDP--DVILAADKLFLPGvGTAQAAMD-QLREREliDLIkACTQPVLGICLGMQLLGErseeSGGVD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 95 C-----GEAET--------PEFGAMEITLnDGGGALFQETPETQVVWESHN-----DEVTIVPEDFFITASSpscqvqAM 156
Cdd:PRK13170 95 ClgiidGPVKKmtdfglplPHMGWNQVTP-QAGHPLFQGIEDGSYFYFVHSyampvNEYTIAQCNYGEPFSA------AI 167
|
170 180 190
....*....|....*....|....*....|..
gi 663509034 157 ENtdGNRFGLQFHPEvNDSEYGAKIMENFVEI 188
Cdd:PRK13170 168 QK--DNFFGVQFHPE-RSGAAGAQLLKNFLEM 196
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
29-171 |
4.75e-05 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153217 [Multi-domain] Cd Length: 235 Bit Score: 42.54 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 29 VDTQIIPNDALCDDLRELDGLLLSGGAARVGLTGKLGNCGELLGLDLPILGICAGHQFM----ARHYGG----------- 93
Cdd:cd01746 39 IDSEDLEEENAEEALKGADGILVPGGFGIRGVEGKILAIKYARENNIPFLGICLGMQLAviefARNVLGlpdanstefdp 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 94 ----------DCGEAETPEFGAM-----EITLNDggGALFQETPETQVVWESHNDEVTIVPEDF---------FITASSP 149
Cdd:cd01746 119 dtphpvvdlmPEQKGVKDLGGTMrlgayPVILKP--GTLAHKYYGKDEVEERHRHRYEVNPEYVdeleeaglrFSGTDPD 196
|
170 180
....*....|....*....|....
gi 663509034 150 SCQVQAMENTDgNRF--GLQFHPE 171
Cdd:cd01746 197 GGLVEIVELPD-HPFfvGTQFHPE 219
|
|
| GATase1_PB |
cd01749 |
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ... |
22-109 |
9.03e-05 |
|
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.
Pssm-ID: 153220 [Multi-domain] Cd Length: 183 Bit Score: 41.36 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 22 RMLRYLGVDTQIIPNDalcDDLRELDGLLLSGG--------AARVGLTGKLGncgELLGLDLPILGICAGHQFMARHYGG 93
Cdd:cd01749 15 RALERLGVEVIEVRTP---EDLEGIDGLIIPGGesttigklLRRTGLLDPLR---EFIRAGKPVFGTCAGLILLAKEVED 88
|
90
....*....|....*.
gi 663509034 94 DCGEaetPEFGAMEIT 109
Cdd:cd01749 89 QGGQ---PLLGLLDIT 101
|
|
| puuD |
PRK11366 |
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional |
43-190 |
2.06e-04 |
|
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
Pssm-ID: 183101 [Multi-domain] Cd Length: 254 Bit Score: 40.65 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 43 LRELDGLLLSGGAARVG--LTGKLGN------CGELLGLDL---------PILGICAGHQFMARHYGGD-----CGEA-- 98
Cdd:PRK11366 59 LPKLDGIYLPGSPSNVQphLYGENGDepdadpGRDLLSMALinaalerriPIFAICRGLQELVVATGGSlhrklCEQPel 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 99 ----ETPEFG-------AMEITLNDGGgALFQETPETQVVWES--HNDEVTIVPEDFFITASSPSCQVQAMENTDGN-RF 164
Cdd:PRK11366 139 lehrEDPELPveqqyapSHEVQVEEGG-LLSALLPECSNFWVNslHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPfAL 217
|
170 180
....*....|....*....|....*...
gi 663509034 165 GLQFHPEVNDSEYGAK--IMENFVEICR 190
Cdd:PRK11366 218 GVQWHPEWNSSEYALSriLFEGFITACQ 245
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
22-186 |
3.01e-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: 39.79 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 22 RMLRYLGVDTQIIPNDalcDDLRELDGLLLSG-GAARVGLTgKLgncgELLGLD----------LPILGICAGHQFMARH 90
Cdd:cd01748 16 NALERLGAEVIITSDP---EEILSADKLILPGvGAFGDAMA-NL----RERGLIealkeaiasgKPFLGICLGMQLLFES 87
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663509034 91 yggdcGEaetpEFGAMEiTLN--DGGGALFQETPE--------TQVVW-ESHNDEVTIVPEDFFITASSPSCQVQAMENT 159
Cdd:cd01748 88 -----SE----EGGGTK-GLGliPGKVVRFPASEGlkvphmgwNQLEItKESPLFKGIPDGSYFYFVHSYYAPPDDPDYI 157
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170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663509034 160 ---------------DGNRFGLQFHPEvNDSEYGAKIMENFV 186
Cdd:cd01748 158 lattdyggkfpaaveKDNIFGTQFHPE-KSGKAGLKLLKNFL 198
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