|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02617 |
PLN02617 |
imidazole glycerol phosphate synthase hisHF |
33-568 |
0e+00 |
|
imidazole glycerol phosphate synthase hisHF
Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 1130.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 33 ASGDASTVTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREYIRRDRP 112
Cdd:PLN02617 2 SNSADSEVTLLDYGAGNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQNDRP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 113 FLGICLGLQLLFDSSEENGPISGLGVIPGVVRRFDSSKGLIVPHIGWNALEITKDTQLLKGAEGHHVYFVHSYHALPSDE 192
Cdd:PLN02617 82 FLGICLGLQLLFESSEENGPVEGLGVIPGVVGRFDSSNGLRVPHIGWNALQITKDSELLDGVGGRHVYFVHSYRATPSDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 193 NKEWISSVCNYGESFISSISMGNIQAVQFHPEKSGATGLSILKNFLSPNTSGSKVPSRRKASN-LAKRVIACLDVRSNDS 271
Cdd:PLN02617 162 NKDWVLATCNYGGEFIASVRKGNVHAVQFHPEKSGATGLSILRRFLEPKSSATQKPTEGKASKsLAKRVIACLDVRSNDK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 272 GDLVVTKGDQYDVRDHSSSKEVRNLGKPVDLASQYYIDGADEVSFLNITGFRDFPLGDLPMLEVLRCASEKVFVPLTVGG 351
Cdd:PLN02617 242 GDLVVTKGDQYDVREHSEGREVRNLGKPVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEVLRRASENVFVPLTVGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 352 GIRDFTDANGRYYSSLEVASEYFRSGADKISIGSDAVFAAEAYLQTGVKTGKSSLEQISRVYGNQAVVVSIDPRRVYVKN 431
Cdd:PLN02617 322 GIRDFTDANGRYYSSLEVASEYFRSGADKISIGSDAVYAAEEYIASGVKTGKTSIEQISRVYGNQAVVVSIDPRRVYVKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 432 PEEVQFKTVKVSNKGPLGEEYAWYQCTVSGGRDSRPIGAYELAKAVEELGAGEILLNCIDCDGQGCGFDIDLVKMVSDAV 511
Cdd:PLN02617 402 PSDVPFKTVKVTNPGPNGEEYAWYQCTVKGGREGRPIGAYELAKAVEELGAGEILLNCIDCDGQGKGFDIELVKLVSDAV 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 215707215 512 TIPVIASSGAGTVEHFSEVFEKTNASAALAAGIFHRKEVPISAVKEHLVDAGVEVRV 568
Cdd:PLN02617 482 TIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETRI 538
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
40-238 |
7.54e-108 |
|
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: 321.37 E-value: 7.54e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREYIRRDRPFLGICLG 119
Cdd:cd01748 1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 120 LQLLFDSSEENGPISGLGVIPGVVRRFDSSKGLIVPHIGWNALEITKDTQLLKG-AEGHHVYFVHSYHALPSDEnkEWIS 198
Cdd:cd01748 81 MQLLFESSEEGGGTKGLGLIPGKVVRFPASEGLKVPHMGWNQLEITKESPLFKGiPDGSYFYFVHSYYAPPDDP--DYIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 215707215 199 SVCNYGESFISSISMGNIQAVQFHPEKSGATGLSILKNFL 238
Cdd:cd01748 159 ATTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
258-559 |
5.09e-104 |
|
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240082 Cd Length: 243 Bit Score: 313.25 E-value: 5.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 258 KRVIACLDVRsndsgDLVVTKGDQYdvrdhsssKEVRNLGKPVDLASQYYIDGADEVSFLNITGFRDfplGDLPMLEVLR 337
Cdd:cd04731 1 KRIIPCLDVK-----DGRVVKGVNF--------KNLRDAGDPVELAKRYNEQGADELVFLDITASSE---GRETMLDVVE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 338 CASEKVFVPLTVGGGIRdftdangryysSLEVASEYFRSGADKISIGSDAVfaaeaylqtgvkTGKSSLEQISRVYGNQA 417
Cdd:cd04731 65 RVAEEVFIPLTVGGGIR-----------SLEDARRLLRAGADKVSINSAAV------------ENPELIREIAKRFGSQC 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 418 VVVSIDPRRVYVknpeevqfktvkvsnkgplgeeyAWYQCTVSGGRDSRPIGAYELAKAVEELGAGEILLNCIDCDGQGC 497
Cdd:cd04731 122 VVVSIDAKRRGD-----------------------GGYEVYTHGGRKPTGLDAVEWAKEVEELGAGEILLTSMDRDGTKK 178
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215707215 498 GFDIDLVKMVSDAVTIPVIASSGAGTVEHFSEVFEKTNASAALAAGIFHRKEVPISAVKEHL 559
Cdd:cd04731 179 GYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAELKEYL 240
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
39-239 |
2.10e-103 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 310.14 E-value: 2.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 39 TVTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREYIRRDRPFLGICL 118
Cdd:PRK13141 1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 119 GLQLLFDSSEENGPISGLGVIPGVVRRFDSSKGLIVPHIGWNALEITKDTQLLKG-AEGHHVYFVHSYHALPSDEnkEWI 197
Cdd:PRK13141 81 GMQLLFESSEEFGETEGLGLLPGRVRRFPPEEGLKVPHMGWNQLELKKESPLLKGiPDGAYVYFVHSYYADPCDE--EYV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 215707215 198 SSVCNYGESFISSISMGNIQAVQFHPEKSGATGLSILKNFLS 239
Cdd:PRK13141 159 AATTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVE 200
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
256-567 |
8.69e-101 |
|
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439877 Cd Length: 251 Bit Score: 305.02 E-value: 8.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 256 LAKRVIACLDVRSNDsgdlvVTKGDQYdvrdhsssKEVRNLGKPVDLASQYYIDGADEVSFLNITGFRDfplGDLPMLEV 335
Cdd:COG0107 1 LAKRIIPCLDVKDGR-----VVKGVNF--------VNLRDAGDPVELAKRYNEQGADELVFLDITASSE---GRKTMLDV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 336 LRCASEKVFVPLTVGGGIRdftdangryysSLEVASEYFRSGADKISIGSDAVfaaeaylqtgvkTGKSSLEQISRVYGN 415
Cdd:COG0107 65 VRRVAEEVFIPLTVGGGIR-----------SVEDARRLLRAGADKVSINSAAV------------KNPELITEAAERFGS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 416 QAVVVSIDPRRVYVKnpeevqfktvkvsnkgplgeeyaWYQCTVSGGRDSRPIGAYELAKAVEELGAGEILLNCIDCDGQ 495
Cdd:COG0107 122 QCIVVAIDAKRVPDG-----------------------GWEVYTHGGRKPTGLDAVEWAKEAEELGAGEILLTSMDRDGT 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215707215 496 GCGFDIDLVKMVSDAVTIPVIASSGAGTVEHFSEVFEKTNASAALAAGIFHRKEVPISAVKEHLVDAGVEVR 567
Cdd:COG0107 179 KDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAELKAYLAEAGIPVR 250
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
39-235 |
1.47e-100 |
|
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: 302.34 E-value: 1.47e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 39 TVTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREYIRRDRPFLGICL 118
Cdd:COG0118 2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGICL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 119 GLQLLFDSSEENGPISGLGVIPGVVRRFDSSkGLIVPHIGWNALEITKDTQLLKG-AEGHHVYFVHSYHALPSDEnkEWI 197
Cdd:COG0118 82 GMQLLFERSEENGDTEGLGLIPGEVVRFPAS-DLKVPHMGWNTVEIAKDHPLFAGiPDGEYFYFVHSYYVPPDDP--EDV 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 215707215 198 SSVCNYGESFISSISMGNIQAVQFHPEKSGATGLSILK 235
Cdd:COG0118 159 VATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
256-567 |
3.49e-99 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 301.21 E-value: 3.49e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 256 LAKRVIACLDVRsndsgDLVVTKGDQYDvrdhssskEVRNLGKPVDLASQYYIDGADEVSFLNITGFRDfplGDLPMLEV 335
Cdd:TIGR00735 2 LAKRIIPCLDVR-----DGRVVKGVQFL--------NLRDAGDPVELAQRYDEEGADELVFLDITASSE---GRTTMIDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 336 LRCASEKVFVPLTVGGGIRDFTDANgryysslevasEYFRSGADKISIGSDAVFAAEAYlqtgvktgksslEQISRVYGN 415
Cdd:TIGR00735 66 VERTAETVFIPLTVGGGIKSIEDVD-----------KLLRAGADKVSINTAAVKNPELI------------YELADRFGS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 416 QAVVVSIDPRRVYVKnpeevqfktvkvsnkgplgeEYAWYQCTVSGGRDSRPIGAYELAKAVEELGAGEILLNCIDCDGQ 495
Cdd:TIGR00735 123 QCIVVAIDAKRVYVN--------------------SYCWYEVYIYGGRESTGLDAVEWAKEVEKLGAGEILLTSMDKDGT 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215707215 496 GCGFDIDLVKMVSDAVTIPVIASSGAGTVEHFSEVFEKTNASAALAAGIFHRKEVPISAVKEHLVDAGVEVR 567
Cdd:TIGR00735 183 KSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYREITIGEVKEYLAERGIPVR 254
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
40-239 |
2.09e-84 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 260.95 E-value: 2.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREYIRRDRPFLGICLG 119
Cdd:PRK13181 2 IAIIDYGAGNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVEKKQPVLGICLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 120 LQLLFDSSEEnGPISGLGVIPGVVRRFDSSKgLIVPHIGWNALEITKDTQLLKG-AEGHHVYFVHSYHALPSDenKEWIS 198
Cdd:PRK13181 82 MQLLFESSEE-GNVKGLGLIPGDVKRFRSEP-LKVPQMGWNSVKPLKESPLFKGiEEGSYFYFVHSYYVPCED--PEDVL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215707215 199 SVCNYGESFISSISMGNIQAVQFHPEKSGATGLSILKNFLS 239
Cdd:PRK13181 158 ATTEYGVPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFAE 198
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
40-238 |
8.71e-84 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 259.41 E-value: 8.71e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLtrSGMADALREYIRRDRPFLGICLG 119
Cdd:PRK13143 3 IVIIDYGVGNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGVGAFGAAMENL--SPLRDVILEAARSGKPFLGICLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 120 LQLLFDSSEENGPISGLGVIPGVVRRFDssKGLIVPHIGWNALEITKDTQLLKGAEGHHVYFVHSYHALPSDEnkEWISS 199
Cdd:PRK13143 81 MQLLFESSEEGGGVRGLGLFPGRVVRFP--AGVKVPHMGWNTVKVVKDCPLFEGIDGEYVYFVHSYYAYPDDE--DYVVA 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 215707215 200 VCNYGESFISSISMGNIQAVQFHPEKSGATGLSILKNFL 238
Cdd:PRK13143 157 TTDYGIEFPAAVCNDNVFGTQFHPEKSGETGLKILENFV 195
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
37-238 |
7.42e-83 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 257.40 E-value: 7.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 37 ASTVTLLDYGAGNVRSVRNAIRHLGFGIrDV---RSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALRE-YIRRDRP 112
Cdd:PRK13146 1 MMTVAIIDYGSGNLRSAAKALERAGAGA-DVvvtADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEaVLAAGRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 113 FLGICLGLQLLFDSSEENGPISGLGVIPGVVRRFDSSK-GLIVPHIGWNALEITKDTQLLKG-AEGHHVYFVHSYHALPS 190
Cdd:PRK13146 80 FLGICVGMQLLFERGLEHGDTPGLGLIPGEVVRFQPDGpALKVPHMGWNTVDQTRDHPLFAGiPDGARFYFVHSYYAQPA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 215707215 191 DENKewISSVCNYGESFISSISMGNIQAVQFHPEKSGATGLSILKNFL 238
Cdd:PRK13146 160 NPAD--VVAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNFL 205
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
40-239 |
2.59e-75 |
|
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: 237.61 E-value: 2.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREYIRRDRPFLGICLG 119
Cdd:TIGR01855 1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 120 LQLLFDSSEENGPISGLGVIPGVVRRFDSSKgliVPHIGWNALEITKDTQLLKG-AEGHHVYFVHSYHALPSDenkEWIS 198
Cdd:TIGR01855 81 MQLLFERSEEGGGVPGLGLIKGNVVKLEARK---VPHMGWNEVHPVKESPLLNGiDEGAYFYFVHSYYAVCEE---EAVL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215707215 199 SVCNYGESFISSISMGNIQAVQFHPEKSGATGLSILKNFLS 239
Cdd:TIGR01855 155 AYADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLE 195
|
|
| hisH |
PRK13170 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
40-239 |
1.80e-63 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 206.63 E-value: 1.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREYirrDRPFLGICLG 119
Cdd:PRK13170 3 VVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKAC---TQPVLGICLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 120 LQLLFDSSEENGPISGLGVIPGVVRRFDSsKGLIVPHIGWNALEITKDTQLLKG-AEGHHVYFVHSYhALPSDENKewIS 198
Cdd:PRK13170 80 MQLLGERSEESGGVDCLGIIDGPVKKMTD-FGLPLPHMGWNQVTPQAGHPLFQGiEDGSYFYFVHSY-AMPVNEYT--IA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215707215 199 SvCNYGESFISSISMGNIQAVQFHPEKSGATGLSILKNFLS 239
Cdd:PRK13170 156 Q-CNYGEPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLE 195
|
|
| hisH |
PRK13152 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
40-239 |
2.32e-55 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 171876 [Multi-domain] Cd Length: 201 Bit Score: 185.43 E-value: 2.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADAL-REYIRRDRPFLGICL 118
Cdd:PRK13152 2 IALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALkEQVLVQKKPILGICL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 119 GLQLLFDSSEENGPISGLGVIPGVVRRFDSSKGLIVPHIGWNALEITKDTQLLKG-AEGHHVYFVHSYHALPSDenkEWI 197
Cdd:PRK13152 82 GMQLFLERGYEGGVCEGLGFIEGEVVKFEEDLNLKIPHMGWNELEILKQSPLYQGiPEKSDFYFVHSFYVKCKD---EFV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 215707215 198 SSVCNYGESFISSISMGNIQAVQFHPEKSGATGLSILKNFLS 239
Cdd:PRK13152 159 SAKAQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENFAR 200
|
|
| hisH |
CHL00188 |
imidazole glycerol phosphate synthase subunit hisH; Provisional |
40-239 |
3.99e-55 |
|
imidazole glycerol phosphate synthase subunit hisH; Provisional
Pssm-ID: 214389 [Multi-domain] Cd Length: 210 Bit Score: 185.09 E-value: 3.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREYIRRDRPFLGICLG 119
Cdd:CHL00188 4 IGIIDYSMGNLHSVSRAIQQAGQQPCIINSESELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKWIAEGNPFIGICLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 120 LQLLFDSSEEnGPISGLGVIPGVVRRFDSSKGLIVPHIGWNALEITK-DTQLLKGAEGHH------VYFVHSYHALPSDE 192
Cdd:CHL00188 84 LHLLFETSEE-GKEEGLGIYKGQVKRLKHSPVKVIPHMGWNRLECQNsECQNSEWVNWKAwplnpwAYFVHSYGVMPKSQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 215707215 193 NKewISSVCNYG-ESFISSISMGNIQAVQFHPEKSGATGLSILKNFLS 239
Cdd:CHL00188 163 AC--ATTTTFYGkQQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREFMK 208
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
259-551 |
3.60e-52 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 178.06 E-value: 3.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 259 RVIACLDVRSndsGDLVV-TKGDQydvrdhssSKEVRNLGKPVDLASQYYIDGADEVSFLNITGFRDfplGDLPMLEVLR 337
Cdd:pfam00977 1 RIIPAIDLKD---GRVVRlVKGDY--------FQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKE---GRPVNLDVVE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 338 CASEKVFVPLTVGGGIRDftdangryyssLEVASEYFRSGADKISIGSDAVfaaeaylqtgvkTGKSSLEQISRVYGNQA 417
Cdd:pfam00977 67 EIAEEVFIPVQVGGGIRS-----------LEDVERLLSAGADRVIIGTAAV------------KNPELIKEAAEKFGSQC 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 418 VVVSIDPRRVYVKnpeevqfktvkvsnkgplgeeyawyqctVSGGRDSRPIGAYELAKAVEELGAGEILLNCIDCDGQGC 497
Cdd:pfam00977 124 IVVAIDARRGKVA----------------------------INGWREDTGIDAVEWAKELEELGAGEILLTDIDRDGTLS 175
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 215707215 498 GFDIDLVKMVSDAVTIPVIASSGAGTVEHFSEVFEkTNASAALAAGIFHRKEVP 551
Cdd:pfam00977 176 GPDLELTRELAEAVNIPVIASGGVGSLEDLKELFT-EGVDGVIAGSALYEGEIT 228
|
|
| hisH |
PRK13142 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
40-238 |
1.95e-46 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 171871 [Multi-domain] Cd Length: 192 Bit Score: 161.53 E-value: 1.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREyiRRDRPFLGICLG 119
Cdd:PRK13142 2 IVIVDYGLGNISNVKRAIEHLGYEVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAK--NTDKKMIGICLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 120 LQLLFDSSEEnGPISGLGVIPGVVRRFDSSKGliVPHIGWNALEiTKDTQLLkgaegHHVYFVHSYHAlpsdENKEWISS 199
Cdd:PRK13142 80 MQLMYEHSDE-GDASGLGFIPGNISRIQTEYP--VPHLGWNNLV-SKHPMLN-----QDVYFVHSYQA----PMSENVIA 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 215707215 200 VCNYGESFISSISMGNIQAVQFHPEKSGATGLSILKNFL 238
Cdd:PRK13142 147 YAQYGADIPAIVQFNNYIGIQFHPEKSGTYGLQILRQAI 185
|
|
| hisH |
PRK14004 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
40-238 |
2.62e-43 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 172505 [Multi-domain] Cd Length: 210 Bit Score: 153.52 E-value: 2.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREYIRRDRPFLGICLG 119
Cdd:PRK14004 2 IAILDYGMGNIHSCLKAVSLYTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIDKHVESGKPLFGICIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 120 LQLLFDSSEENG------PISGLGVIPGVVRRFDsSKGLIVPHIGWNALEITK--DTQLLKG-AEGHHVYFVHSYHalPS 190
Cdd:PRK14004 82 FQILFESSEETNqgtkkeQIEGLGYIKGKIKKFE-GKDFKVPHIGWNRLQIRRkdKSKLLKGiGDQSFFYFIHSYR--PT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 215707215 191 DENKEWISSVCN-YGESFISSISMGNIQAVQFHPEKSGATGLSILKNFL 238
Cdd:PRK14004 159 GAEGNAITGLCDyYQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENFI 207
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
259-557 |
2.85e-29 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240074 [Multi-domain] Cd Length: 233 Bit Score: 115.83 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 259 RVIACLDVRsndsgDLVVTKGDQYDVRDHSSSKE-VRNLGKPVDLASQYYIDGADEVSFLNITGFRdfplGDLPMLEVLR 337
Cdd:cd04723 1 RIIPVIDLK-----DGVVVHGVGGDRDNYRPITSnLCSTSDPLDVARAYKELGFRGLYIADLDAIM----GRGDNDEAIR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 338 CASEKVFVPLTVGGGIRDFtdangryysslEVASEYFRSGADKISIGSDAVFAaeaylqtgvktgkSSLEQISRVYGNQA 417
Cdd:cd04723 72 ELAAAWPLGLWVDGGIRSL-----------ENAQEWLKRGASRVIVGTETLPS-------------DDDEDRLAALGEQR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 418 VVVSIDPRRVYVknpeevqfktvkvsnkgplgeeyawyqctvsgGRDSRPIGAYELAKAVEELgAGEILLNCIDCDGQGC 497
Cdd:cd04723 128 LVLSLDFRGGQL--------------------------------LKPTDFIGPEELLRRLAKW-PEELIVLDIDRVGSGQ 174
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 498 GFDIDLVKMVSDAVTIPVIASSGAGTVEHFSEVFEKtNASAALAAGIFHRKEVPISAVKE 557
Cdd:cd04723 175 GPDLELLERLAARADIPVIAAGGVRSVEDLELLKKL-GASGALVASALHDGGLTLEDVVR 233
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
42-238 |
4.71e-26 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 105.01 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 42 LLDYGAGNVRSVRNAIRHLGFGIRDVRSPEDILAAD------RLVFPGVGAFGsamdvlTRSGMADALREYIRRDRPFLG 115
Cdd:pfam00117 2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILeenpdgIILSGGPGSPG------AAGGAIEAIREARELKIPILG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 116 ICLGLQLLFDSseengpiSGLGVIpgvvrrfdssKGLIVPHIGWNALEITKDTQLLKG-AEGHHVYFVHSYHALPSDENK 194
Cdd:pfam00117 76 ICLGHQLLALA-------FGGKVV----------KAKKFGHHGKNSPVGDDGCGLFYGlPNVFIVRRYHSYAVDPDTLPD 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 215707215 195 EW-ISSVCNYGESFISSISMGN-IQAVQFHPEK-SGATGLSILKNFL 238
Cdd:pfam00117 139 GLeVTATSENDGTIMGIRHKKLpIFGVQFHPESiLTPHGPEILFNFF 185
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
291-525 |
1.19e-18 |
|
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.
Pssm-ID: 240083 Cd Length: 234 Bit Score: 85.22 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 291 KEVRNLGKPVDLASQYYIDGADEVSFLNITGFRDfplGDLPMLEVLRCASEKVFVPLTVGGGIRdftdangryysSLEVA 370
Cdd:cd04732 23 KKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKG---GEPVNLELIEEIVKAVGIPVQVGGGIR-----------SLEDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 371 SEYFRSGADKISIGSDAVfaaeaylqtgvkTGKSSLEQISRVYGNQAVVVSIDPRRVYVKnpeevqfktvkvsnkgplge 450
Cdd:cd04732 89 ERLLDLGVSRVIIGTAAV------------KNPELVKELLKEYGGERIVVGLDAKDGKVA-------------------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215707215 451 eyawyqctVSGGRDSRPIGAYELAKAVEELGAGEILLNCIDCDGQGCGFDIDLVKMVSDAVTIPVIASSGAGTVE 525
Cdd:cd04732 137 --------TKGWLETSEVSLEELAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLD 203
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
299-525 |
5.81e-18 |
|
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]
Pssm-ID: 272850 [Multi-domain] Cd Length: 230 Bit Score: 83.02 E-value: 5.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 299 PVDLASQYYIDGADEVSFLNITGFRDfplGDLPMLEVLRCASEKVFVPLTVGGGIRdftdangryysSLEVASEYFRSGA 378
Cdd:TIGR00007 30 PVEAAKKWEEEGAERIHVVDLDGAKE---GGPVNLPVIKKIVRETGVPVQVGGGIR-----------SLEDVEKLLDLGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 379 DKISIGSDAVfaaeaylqtgvkTGKSSLEQISRVYGNQAVVVSIDPRRVYVKnpeevqfktvkvsnkgplgeeyawyqct 458
Cdd:TIGR00007 96 DRVIIGTAAV------------ENPDLVKELLKEYGPERIVVSLDARGGEVA---------------------------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215707215 459 VSGGRDSRPIGAYELAKAVEELGAGEILLNCIDCDGQGCGFDIDLVKMVSDAVTIPVIASSGAGTVE 525
Cdd:TIGR00007 136 VKGWLEKSEVSLEELAKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSID 202
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
291-556 |
1.06e-15 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 76.87 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 291 KEVRNLGKPVDLASQYYIDGADEVSFLNITGFRDfplGDLPMLEVLRCASEKVFVPLTVGGGIRDFTDAngryyssleva 370
Cdd:PRK13585 26 TETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFE---GERKNAEAIEKIIEAVGVPVQLGGGIRSAEDA----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 371 SEYFRSGADKISIGSDAVFAAEaylqtgvktgksSLEQISRVYGNQAVVVSIDPrrvyvknpeevqfKTVKVSNKGplge 450
Cdd:PRK13585 92 ASLLDLGVDRVILGTAAVENPE------------IVRELSEEFGSERVMVSLDA-------------KDGEVVIKG---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 451 eyaWyqcTVSGGRDsrPIgayELAKAVEELGAGEILLNCIDCDGQGCGFDIDLVKMVSDAVTIPVIASSGAGTVEHFsEV 530
Cdd:PRK13585 143 ---W---TEKTGYT--PV---EAAKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDL-RA 210
|
250 260 270
....*....|....*....|....*....|.
gi 215707215 531 FEKTNASA-----ALAAGIFHRKEVpISAVK 556
Cdd:PRK13585 211 LKEAGAAGvvvgsALYKGKFTLEEA-IEAVK 240
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
333-526 |
1.53e-15 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439876 Cd Length: 236 Bit Score: 76.23 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 333 LEVLRCASEKVFVPLTVGGGIRdftdangryysSLEVASEYFRSGADKISIGSDAVFAAEAylqtgvktgkssLEQISRV 412
Cdd:COG0106 62 LELIEEIAKATGLPVQVGGGIR-----------SLEDIERLLDAGASRVILGTAAVKDPEL------------VKEALEE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 413 YGNQaVVVSIDprrvyVKNPeevqfktvKVSNKGplgeeyaWYQCTvsggrdsrPIGAYELAKAVEELGAGEILLNCIDC 492
Cdd:COG0106 119 FPER-IVVGLD-----ARDG--------KVATDG-------WQETS--------GVDLEELAKRFEDAGVAAILYTDISR 169
|
170 180 190
....*....|....*....|....*....|....
gi 215707215 493 DGQGCGFDIDLVKMVSDAVTIPVIASSGAGTVEH 526
Cdd:COG0106 170 DGTLQGPNLELYRELAAATGIPVIASGGVSSLDD 203
|
|
| GATase1_CobQ |
cd01750 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
40-140 |
2.89e-10 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.
Pssm-ID: 153221 [Multi-domain] Cd Length: 194 Bit Score: 59.95 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYG-AGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREYIRRDRPFLGICL 118
Cdd:cd01750 1 IAVIRYPdISNFTDLDPLAREPGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYARAGGPVLGICG 80
|
90 100
....*....|....*....|....*...
gi 215707215 119 GLQLLFDS------SEENGPISGLGVIP 140
Cdd:cd01750 81 GYQMLGKYivdpegVEGPGEIEGLGLLD 108
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
40-124 |
3.39e-10 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 57.61 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYGAGN---VRSVRNAIRHLGFGIR-------DVRSPEDILAADRLVFPGVgaFGSAMDVLTRSGMADALREYIRR 109
Cdd:cd01653 1 VAVLLFPGFEeleLASPLDALREAGAEVDvvspdggPVESDVDLDDYDGLILPGG--PGTPDDLARDEALLALLREAAAA 78
|
90
....*....|....*
gi 215707215 110 DRPFLGICLGLQLLF 124
Cdd:cd01653 79 GKPILGICLGAQLLV 93
|
|
| PRK13525 |
PRK13525 |
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; |
48-145 |
1.53e-09 |
|
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
Pssm-ID: 237411 [Multi-domain] Cd Length: 189 Bit Score: 57.48 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 48 GNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGvgafG--SAMDVLTRS-GMADALREYIRRDRPFLGICLGLQLLf 124
Cdd:PRK13525 11 GAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPG----GesTTMGKLLRDfGLLEPLREFIASGLPVFGTCAGMILL- 85
|
90 100
....*....|....*....|..
gi 215707215 125 dSSE-ENGPISGLGVIPGVVRR 145
Cdd:PRK13525 86 -AKEiEGYEQEHLGLLDITVRR 106
|
|
| GATase1_PB |
cd01749 |
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ... |
56-145 |
1.87e-09 |
|
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: 57.15 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 56 AIRHLGFGIRDVRSPEDILAADRLVFPGvGAFGSAMDVLTRSGMADALREYIRRDRPFLGICLGLQLLFDSSEENGPISG 135
Cdd:cd01749 16 ALERLGVEVIEVRTPEDLEGIDGLIIPG-GESTTIGKLLRRTGLLDPLREFIRAGKPVFGTCAGLILLAKEVEDQGGQPL 94
|
90
....*....|
gi 215707215 136 LGVIPGVVRR 145
Cdd:cd01749 95 LGLLDITVRR 104
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
40-123 |
1.95e-09 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 54.90 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 40 VTLLDYGAGN---VRSVRNAIRHLGFGIR-------DVRSPEDILAADRLVFPGVgaFGSAMDVLTRSGMADALREYIRR 109
Cdd:cd03128 1 VAVLLFGGSEeleLASPLDALREAGAEVDvvspdggPVESDVDLDDYDGLILPGG--PGTPDDLAWDEALLALLREAAAA 78
|
90
....*....|....
gi 215707215 110 DRPFLGICLGLQLL 123
Cdd:cd03128 79 GKPVLGICLGAQLL 92
|
|
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
345-526 |
1.26e-08 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 55.84 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 345 VPLTVGGGIRDftdangryyssLEVASEYFRSGADKISIGSDAVfaaeaylqtgvkTGKSSLEQISRVYGNQaVVVSIDp 424
Cdd:PRK00748 75 IPVQVGGGIRS-----------LETVEALLDAGVSRVIIGTAAV------------KNPELVKEACKKFPGK-IVVGLD- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 425 rrvyVKNPeevqfktvKVSNKGplgeeyaWyqCTVSGgrdsrpIGAYELAKAVEELGAGEILLNCIDCDGQGCGFDIDLV 504
Cdd:PRK00748 130 ----ARDG--------KVATDG-------W--LETSG------VTAEDLAKRFEDAGVKAIIYTDISRDGTLSGPNVEAT 182
|
170 180
....*....|....*....|..
gi 215707215 505 KMVSDAVTIPVIASSGAGTVEH 526
Cdd:PRK00748 183 RELAAAVPIPVIASGGVSSLDD 204
|
|
| PRK00784 |
PRK00784 |
cobyric acid synthase; |
58-150 |
2.17e-08 |
|
cobyric acid synthase;
Pssm-ID: 234838 [Multi-domain] Cd Length: 488 Bit Score: 56.63 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 58 RHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLTRSGMADALREYIRRDRPFLGICLGLQLL-------FDSSEEN 130
Cdd:PRK00784 273 AEPGVDVRYVRPGEPLPDADLVILPGSKNTIADLAWLRESGWDEAIRAHARRGGPVLGICGGYQMLgrriadpDGVEGAP 352
|
90 100
....*....|....*....|
gi 215707215 131 GPISGLGVIPgVVRRFDSSK 150
Cdd:PRK00784 353 GSVEGLGLLD-VETVFEPEK 371
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
53-224 |
3.83e-08 |
|
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: 54.18 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 53 VRNAIRHLGFGIRDVR--------SPEDILAADRLVFpgvgaFGSAMDVLTRSGMADALREYIRR----DRPFLGICLGL 120
Cdd:COG0518 18 IARRLREAGIELDVLRvyageilpYDPDLEDPDGLIL-----SGGPMSVYDEDPWLEDEPALIREafelGKPVLGICYGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 121 QLLFDSseengpisgLGvipGVVRRFDsskgliVPHIGWNALEITKDTQLLKG-AEGHHVYFVHSYH--ALPsdENKEWI 197
Cdd:COG0518 93 QLLAHA---------LG---GKVEPGP------GREIGWAPVELTEADPLFAGlPDEFTVWMSHGDTvtELP--EGAEVL 152
|
170 180 190
....*....|....*....|....*....|....
gi 215707215 198 --SSVCN-----YGESFIssismgniqAVQFHPE 224
Cdd:COG0518 153 asSDNCPnqafrYGRRVY---------GVQFHPE 177
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
46-238 |
5.73e-08 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 53.02 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 46 GAGNVRSVRNAIRHLGFGIRDVRSPEDILAADRLVFPGVGAFGSAMDVLT-RSGMADALREYIRR----DRPFLGICLGL 120
Cdd:cd01741 12 GPGLFEDLLREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEdDYPWLKKLKELIRQalaaGKPVLGICLGH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 121 QLLFDSseengpisgLGvipGVVRRfdSSKGlivPHIGWNALEITKDTQLLKGAEGHHVYF-VHSYH-----ALPsdENK 194
Cdd:cd01741 92 QLLARA---------LG---GKVGR--NPKG---WEIGWFPVTLTEAGKADPLFAGLPDEFpVFHWHgdtvvELP--PGA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 215707215 195 EWI--SSVCN-----YGESFIssismgniqAVQFHPEKsgatglSILKNFL 238
Cdd:cd01741 153 VLLasSEACPnqafrYGDRAL---------GLQFHPEE------RLLRNFL 188
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
96-238 |
8.08e-08 |
|
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: 52.54 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 96 RSGMADALREYIRRDRPFLGICLGLQLLFDssEENGPISGLGVIPGvvrrfdsskGLIVPHIGWNALEITKDTQLLKgae 175
Cdd:cd01743 57 DAGISLEIIRALAGKVPILGVCLGHQAIAE--AFGGKVVRAPEPMH---------GKTSEIHHDGSGLFKGLPQPFT--- 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215707215 176 ghhVYFVHSYHALPSDENKEWISSVCNYGEsfissISMG------NIQAVQFHPEkSGAT--GLSILKNFL 238
Cdd:cd01743 123 ---VGRYHSLVVDPDPLPDLLEVTASTEDG-----VIMAlrhrdlPIYGVQFHPE-SILTeyGLRLLENFL 184
|
|
| GATase_3 |
pfam07685 |
CobB/CobQ-like glutamine amidotransferase domain; |
64-144 |
7.24e-07 |
|
CobB/CobQ-like glutamine amidotransferase domain;
Pssm-ID: 429595 [Multi-domain] Cd Length: 189 Bit Score: 49.93 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 64 IRDVRSPEDILA--ADRLVFPGVGAFGSAMDVLTRSGMADALREYIRRDRPFLGICLGLQLLFDS--SEENGPISGLGVI 139
Cdd:pfam07685 29 VRFVPLPDESLGpdADLIILPGGKPTIQDLALLRNSGMDEAIKEAAEDGGPVLGICGGYQMLGETieDPEGVRIEGLGLL 108
|
....*
gi 215707215 140 PGVVR 144
Cdd:pfam07685 109 DIETV 113
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
69-238 |
6.70e-06 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 46.77 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 69 SPEDILA-ADRLVFPGvgafGSAMDVLTRSGmadalrEYIRR-DRPFLGICLGLQLLfdsSEENGpisglgvipGVVRRF 146
Cdd:PRK00758 34 PVEEIKAfEDGLILSG----GPDIERAGNCP------EYLKElDVPILGICLGHQLI---AKAFG---------GEVGRG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 147 DS-SKGLIvphigwnALEITKDTQLLKGaeghhvyfvhsyhaLPsDENKEWIS---SVCNYGESFI----SSI----SMG 214
Cdd:PRK00758 92 EYgEYALV-------EVEILDEDDILKG--------------LP-PEIRVWAShadEVKELPDGFEilarSDIceveAMK 149
|
170 180
....*....|....*....|....*....
gi 215707215 215 N----IQAVQFHPE-KSGATGLSILKNFL 238
Cdd:PRK00758 150 HkekpIYGVQFHPEvAHTEYGEEIFKNFL 178
|
|
| COG3442 |
COG3442 |
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ... |
45-145 |
5.63e-04 |
|
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only];
Pssm-ID: 442666 [Multi-domain] Cd Length: 241 Bit Score: 41.70 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 45 YG-AGNVRSVRNAIRHLGFGIRDVR-SPEDILAADR--LVFPGVG---AFGSAMDVLTRsgMADALREYIRRDRPFLGIC 117
Cdd:COG3442 15 YGdRGNVLALKRRAEWRGIDVEVVEvNPGDDLPFDDvdIVFIGGGqdrEQEIVADDLLR--IKDALRAAIEDGVPVLAIC 92
|
90 100 110
....*....|....*....|....*....|.
gi 215707215 118 LGLQLL---FDSSEENGpISGLGVIPGVVRR 145
Cdd:COG3442 93 GGYQLLghyYETADGER-IPGLGILDVYTVA 122
|
|
| PRK13527 |
PRK13527 |
glutamine amidotransferase subunit PdxT; Provisional |
52-145 |
9.38e-04 |
|
glutamine amidotransferase subunit PdxT; Provisional
Pssm-ID: 237412 [Multi-domain] Cd Length: 200 Bit Score: 40.64 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 52 SVRNAIRHLGFG--IRDVRSPEDILAADRLVFPGvGAFGSAMDVLTRSGMADALREYIRRDRPFLGICLGLQLLfdSSEE 129
Cdd:PRK13527 18 ALKRALDELGIDgeVVEVRRPGDLPDCDALIIPG-GESTTIGRLMKREGILDEIKEKIEEGLPILGTCAGLILL--AKEV 94
|
90 100
....*....|....*....|..
gi 215707215 130 NGPISG------LGVIPGVVRR 145
Cdd:PRK13527 95 GDDRVTkteqplLGLMDVTVKR 116
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
297-533 |
1.28e-03 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 40.26 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 297 GKPVDLASQYYIDGADEVSFLNITGFRDFPLGDLPmlEVLRCASEKVFVPLTVGGGIRDFTDANGRYYSSLEVAseyfrs 376
Cdd:cd04722 12 GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDK--EVLKEVAAETDLPLGVQLAINDAAAAVDIAAAAARAA------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 377 GADKISIGSDAVFAAEAYLQTgvktgkssLEQISRVYGNQAVVVSIDPRRVYVknpeevqfktvkvsnkgplgeeyawyq 456
Cdd:cd04722 84 GADGVEIHGAVGYLAREDLEL--------IRELREAVPDVKVVVKLSPTGELA--------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 457 ctvsggrdsrpigayelAKAVEELGAGEILLNCIDCDGQGCGFD---IDLVKMVSDAVTIPVIASSGAGTVEHFSEVFEK 533
Cdd:cd04722 129 -----------------AAAAEEAGVDEVGLGNGGGGGGGRDAVpiaDLLLILAKRGSKVPVIAGGGINDPEDAAEALAL 191
|
|
| GATase1_FGAR_AT |
cd01740 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
56-145 |
1.68e-03 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site
Pssm-ID: 153211 [Multi-domain] Cd Length: 238 Bit Score: 40.29 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 56 AIRHLGFGIRDV------RSPEDILAADRLVFPGvGaFgSAMDVLtRSG--------MADALREYIRRDRPFLGICLGLQ 121
Cdd:cd01740 18 AFELAGFEAEDVwhndllAGRKDLDDYDGVVLPG-G-F-SYGDYL-RAGaiaaasplLMEEVKEFAERGGLVLGICNGFQ 93
|
90 100
....*....|....*....|....
gi 215707215 122 LLfdsSEengpisgLGVIPGVVRR 145
Cdd:cd01740 94 IL---VE-------LGLLPGALIR 107
|
|
| PLN02832 |
PLN02832 |
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex |
56-224 |
9.51e-03 |
|
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
Pssm-ID: 215446 [Multi-domain] Cd Length: 248 Bit Score: 38.15 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 56 AIRHLGFGIRDVRSPEDILAADRLVFPGvGAFGSAMDVLTRSGMADALREYIRRDRPFLGICLGLQLLFDSSE---ENGP 132
Cdd:PLN02832 19 ALRRLGVEAVEVRKPEQLEGVSGLIIPG-GESTTMAKLAERHNLFPALREFVKSGKPVWGTCAGLIFLAERAVgqkEGGQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215707215 133 --ISGLGVipGVVRRFDSSKglivphigWNALEITKDTQLLKGAEGHHVYF------------------VHSYHALPSDE 192
Cdd:PLN02832 98 elLGGLDC--TVHRNFFGSQ--------INSFETELPVPELAASEGGPETFravfirapailsvgpgveVLAEYPLPSEK 167
|
170 180 190
....*....|....*....|....*....|..
gi 215707215 193 NKEWISSVCNYGESFISSISMGNIQAVQFHPE 224
Cdd:PLN02832 168 ALYSSSTDAEGRDKVIVAVKQGNLLATAFHPE 199
|
|
| |
