|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02617 |
PLN02617 |
imidazole glycerol phosphate synthase hisHF |
2-549 |
0e+00 |
|
imidazole glycerol phosphate synthase hisHF
Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 744.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 2 PVVHVIDVESGNLQSLTNAIEHLGYEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMG 81
Cdd:PLN02617 7 SEVTLLDYGAGNVRSVRNAIRHLGFTIKDVQTPED--ILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQNDRPFLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 82 ICVGLQALFAGSVESPKSTGLNYIDFKLSRFDDSEK-PVPEIGWNSCIPSEN--LFFGLDPyKRYYFVHSFAAILNSEkk 158
Cdd:PLN02617 85 ICLGLQLLFESSEENGPVEGLGVIPGVVGRFDSSNGlRVPHIGWNALQITKDseLLDGVGG-RHVYFVHSYRATPSDE-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 159 knleNDGWKIAKAKYGsEEFIAAVNKNNIFATQFHPEKSGKAGLNVIENFLKqqsppiPNYSAEEKEllMNDYSNYGLTR 238
Cdd:PLN02617 162 ----NKDWVLATCNYG-GEFIASVRKGNVHAVQFHPEKSGATGLSILRRFLE------PKSSATQKP--TEGKASKSLAK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 239 RIIACLDVRTNDQGDLVVTKGDQYDVREKSDGKGVRNLGKPVQLAQKYYQQGADEVTFLNITSFRDCPLKDTPMLEVLKQ 318
Cdd:PLN02617 229 RVIACLDVRSNDKGDLVVTKGDQYDVREHSEGREVRNLGKPVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEVLRR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 319 AAKTVFVPLTVGGGIKDIVDVDGTKIPALEVASLYFRSGADKVSIGTDAVYAAEKYYELGNRgDGTSPIETISKAYGAQA 398
Cdd:PLN02617 309 ASENVFVPLTVGGGIRDFTDANGRYYSSLEVASEYFRSGADKISIGSDAVYAAEEYIASGVK-TGKTSIEQISRVYGNQA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 399 VVISVDPKRVYVNSQADTKNKVFETEYPGPNGEKYCWYQCTIKGGRESRDLGVWELTRACEALGAGEILLNCIDKDGSNS 478
Cdd:PLN02617 388 VVVSIDPRRVYVKDPSDVPFKTVKVTNPGPNGEEYAWYQCTVKGGREGRPIGAYELAKAVEELGAGEILLNCIDCDGQGK 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365721 479 GYDLELIEHVKDAVKIPVIASSGAGVPEHFEEAFLKTRADACLGAGMFHRGEFTVNDVKEYLLEHGLKVRM 549
Cdd:PLN02617 468 GFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETRI 538
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
235-548 |
1.28e-133 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 388.65 E-value: 1.28e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 235 GLTRRIIACLDVRtndqgDLVVTKGDQYDVreksdgkgVRNLGKPVQLAQKYYQQGADEVTFLNITSFRDcplKDTPMLE 314
Cdd:TIGR00735 1 MLAKRIIPCLDVR-----DGRVVKGVQFLN--------LRDAGDPVELAQRYDEEGADELVFLDITASSE---GRTTMID 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 315 VLKQAAKTVFVPLTVGGGIKDIVDVDgtkipalevasLYFRSGADKVSIGTDAVYAAEKYYELGNRgdgtspietiskaY 394
Cdd:TIGR00735 65 VVERTAETVFIPLTVGGGIKSIEDVD-----------KLLRAGADKVSINTAAVKNPELIYELADR-------------F 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 395 GAQAVVISVDPKRVYVNSqadtknkvfeteypgpngekYCWYQCTIKGGRESRDLGVWELTRACEALGAGEILLNCIDKD 474
Cdd:TIGR00735 121 GSQCIVVAIDAKRVYVNS--------------------YCWYEVYIYGGRESTGLDAVEWAKEVEKLGAGEILLTSMDKD 180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365721 475 GSNSGYDLELIEHVKDAVKIPVIASSGAGVPEHFEEAFLKTRADACLGAGMFHRGEFTVNDVKEYLLEHGLKVR 548
Cdd:TIGR00735 181 GTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYREITIGEVKEYLAERGIPVR 254
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
238-543 |
3.45e-108 |
|
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: 323.26 E-value: 3.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 238 RRIIACLDVRtndqgDLVVTKGDQYdvreksdgKGVRNLGKPVQLAQKYYQQGADEVTFLNITSfrdCPLKDTPMLEVLK 317
Cdd:cd04731 1 KRIIPCLDVK-----DGRVVKGVNF--------KNLRDAGDPVELAKRYNEQGADELVFLDITA---SSEGRETMLDVVE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 318 QAAKTVFVPLTVGGGIKDivdvdgtkipaLEVASLYFRSGADKVSIGTDAVyaaekyyelgnrgDGTSPIETISKAYGAQ 397
Cdd:cd04731 65 RVAEEVFIPLTVGGGIRS-----------LEDARRLLRAGADKVSINSAAV-------------ENPELIREIAKRFGSQ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 398 AVVISVDPKRVYVnsqadtknkvfeteypgpngekyCWYQCTIKGGRESRDLGVWELTRACEALGAGEILLNCIDKDGSN 477
Cdd:cd04731 121 CVVVSIDAKRRGD-----------------------GGYEVYTHGGRKPTGLDAVEWAKEVEELGAGEILLTSMDRDGTK 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365721 478 SGYDLELIEHVKDAVKIPVIASSGAGVPEHFEEAFLKTRADACLGAGMFHRGEFTVNDVKEYLLEH 543
Cdd:cd04731 178 KGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAELKEYLAER 243
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
236-549 |
4.10e-104 |
|
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: 313.11 E-value: 4.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 236 LTRRIIACLDVRtndQGDLVvtKGDQYdvreksdgKGVRNLGKPVQLAQKYYQQGADEVTFLNITSFRDcplKDTPMLEV 315
Cdd:COG0107 1 LAKRIIPCLDVK---DGRVV--KGVNF--------VNLRDAGDPVELAKRYNEQGADELVFLDITASSE---GRKTMLDV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 316 LKQAAKTVFVPLTVGGGIKDIVDVDgtkipalevasLYFRSGADKVSIGTDAVyaaekyyelgnrgdgTSP--IETISKA 393
Cdd:COG0107 65 VRRVAEEVFIPLTVGGGIRSVEDAR-----------RLLRAGADKVSINSAAV---------------KNPelITEAAER 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 394 YGAQAVVISVDPKRVyvnsqadtknkvfeteypgPNGekycWYQCTIKGGRESRDLGVWELTRACEALGAGEILLNCIDK 473
Cdd:COG0107 119 FGSQCIVVAIDAKRV-------------------PDG----GWEVYTHGGRKPTGLDAVEWAKEAEELGAGEILLTSMDR 175
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365721 474 DGSNSGYDLELIEHVKDAVKIPVIASSGAGVPEHFEEAFLKTRADACLGAGMFHRGEFTVNDVKEYLLEHGLKVRM 549
Cdd:COG0107 176 DGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAELKAYLAEAGIPVRL 251
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
4-209 |
7.20e-88 |
|
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: 269.37 E-value: 7.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 4 VHVIDVESGNLQSLTNAIEHLGYEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGIC 83
Cdd:cd01748 1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEE--ILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGIC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 84 VGLQALFAGSVESPKSTGLNYIDFKLSRFDDSE-KPVPEIGWNSCIPSEN--LFFGLDPYKRYYFVHSFAAILNSEKkkn 160
Cdd:cd01748 79 LGMQLLFESSEEGGGTKGLGLIPGKVVRFPASEgLKVPHMGWNQLEITKEspLFKGIPDGSYFYFVHSYYAPPDDPD--- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365721 161 lendgWKIAKAKYGsEEFIAAVNKNNIFATQFHPEKSGKAGLNVIENFL 209
Cdd:cd01748 156 -----YILATTDYG-GKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
2-206 |
6.71e-69 |
|
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: 220.29 E-value: 6.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 2 PVVHVIDVESGNLQSLTNAIEHLGYEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMG 81
Cdd:COG0118 1 MMIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDE--IRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 82 ICVGLQALFAGSVESPKSTGLNYIDFKLSRFDDSEKPVPEIGWNSCIPSEN--LFFGLDPYKRYYFVHSFAAIlnsekkk 159
Cdd:COG0118 79 ICLGMQLLFERSEENGDTEGLGLIPGEVVRFPASDLKVPHMGWNTVEIAKDhpLFAGIPDGEYFYFVHSYYVP------- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 398365721 160 nLENDGWKIAKAKYGsEEFIAAVNKNNIFATQFHPEKSGKAGLNVIE 206
Cdd:COG0118 152 -PDDPEDVVATTDYG-VPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
4-210 |
2.98e-67 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 216.27 E-value: 2.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 4 VHVIDVESGNLQSLTNAIEHLGYEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGIC 83
Cdd:PRK13181 2 IAIIDYGAGNLRSVANALKRLGVEAVVSSDPEE--IAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVEKKQPVLGIC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 84 VGLQALFAGSvESPKSTGLNYIDFKLSRFDDSEKPVPEIGWNSCIPSEN--LFFGLDPYKRYYFVHSFAAILNSEKKKnl 161
Cdd:PRK13181 80 LGMQLLFESS-EEGNVKGLGLIPGDVKRFRSEPLKVPQMGWNSVKPLKEspLFKGIEEGSYFYFVHSYYVPCEDPEDV-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365721 162 endgwkIAKAKYGsEEFIAAVNKNNIFATQFHPEKSGKAGLNVIENFLK 210
Cdd:PRK13181 157 ------LATTEYG-VPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFAE 198
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
6-211 |
4.08e-62 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 203.05 E-value: 4.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 6 VIDVESGNLQSLTNAIEHLGYEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGICVG 85
Cdd:PRK13141 4 IIDYGMGNLRSVEKALERLGAEAVITSDPEE--ILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 86 LQALFAGSVESPKSTGLNYIDFKLSRFDDSEK-PVPEIGWNSCIPSEN--LFFGLDPYKRYYFVHSFAAilnsekkkNLE 162
Cdd:PRK13141 82 MQLLFESSEEFGETEGLGLLPGRVRRFPPEEGlKVPHMGWNQLELKKEspLLKGIPDGAYVYFVHSYYA--------DPC 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365721 163 NDGWKIAKAKYGsEEFIAAVNKNNIFATQFHPEKSGKAGLNVIENFLKQ 211
Cdd:PRK13141 154 DEEYVAATTDYG-VEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEM 201
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
6-209 |
9.15e-58 |
|
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: 191.38 E-value: 9.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 6 VIDVESGNLQSLTNAIEHLGYEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGICVG 85
Cdd:TIGR01855 3 IIDYGVGNLGSVKRALKRVGAEPVVVKDSKE--AELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 86 LQALFAGSVESPKSTGLNYIDFKLSRFDDseKPVPEIGWNSCIP--SENLFFGLDPYKRYYFVHSFAAILNSEkkknlen 163
Cdd:TIGR01855 81 MQLLFERSEEGGGVPGLGLIKGNVVKLEA--RKVPHMGWNEVHPvkESPLLNGIDEGAYFYFVHSYYAVCEEE------- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365721 164 dgWKIAKAKYGsEEFIAAVNKNNIFATQFHPEKSGKAGLNVIENFL 209
Cdd:TIGR01855 152 --AVLAYADYG-EKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFL 194
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
6-210 |
2.37e-54 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 182.37 E-value: 2.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 6 VIDVESGNLQSLTNAIEHLGYEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLfnRGFEKPIREYIESGKPIMGICVG 85
Cdd:PRK13143 5 IIDYGVGNLRSVSKALERAGAEVVITSDPEE--ILDADGIVLPGVGAFGAAMENL--SPLRDVILEAARSGKPFLGICLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 86 LQALFAGSVESPKSTGLNYIDFKLSRFDDSEKpVPEIGWNSCIPSEN--LFFGLDPyKRYYFVHSFAAilnsekkkNLEN 163
Cdd:PRK13143 81 MQLLFESSEEGGGVRGLGLFPGRVVRFPAGVK-VPHMGWNTVKVVKDcpLFEGIDG-EYVYFVHSYYA--------YPDD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 398365721 164 DGWKIAKAKYGSEeFIAAVNKNNIFATQFHPEKSGKAGLNVIENFLK 210
Cdd:PRK13143 151 EDYVVATTDYGIE-FPAAVCNDNVFGTQFHPEKSGETGLKILENFVE 196
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
239-532 |
1.75e-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: 178.44 E-value: 1.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 239 RIIACLDVRtndQGDLVV-TKGDqYDVREKSdgkgvrnLGKPVQLAQKYYQQGADEVTFLNITSFRDCPLKdtpMLEVLK 317
Cdd:pfam00977 1 RIIPAIDLK---DGRVVRlVKGD-YFQNTVY-------AGDPVELAKRYEEEGADELHFVDLDAAKEGRPV---NLDVVE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 318 QAAKTVFVPLTVGGGIKDivdvdgtkipaLEVASLYFRSGADKVSIGTDAVyaaekyyelgnrgdgTSP--IETISKAYG 395
Cdd:pfam00977 67 EIAEEVFIPVQVGGGIRS-----------LEDVERLLSAGADRVIIGTAAV---------------KNPelIKEAAEKFG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 396 AQAVVISVDPKRvyvnsqadtkNKVFeteypgpngekycwyqctIKGGRESRDLGVWELTRACEALGAGEILLNCIDKDG 475
Cdd:pfam00977 121 SQCIVVAIDARR----------GKVA------------------INGWREDTGIDAVEWAKELEELGAGEILLTDIDRDG 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365721 476 SNSGYDLELIEHVKDAVKIPVIASSGAGVPEHFEEAFlKTRADACLGAGMFHRGEFT 532
Cdd:pfam00977 173 TLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELF-TEGVDGVIAGSALYEGEIT 228
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
239-538 |
5.82e-49 |
|
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: 169.37 E-value: 5.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 239 RIIACLDVRtndqgDLVVTKGDQYDVREKSDGK-GVRNLGKPVQLAQKYYQQGADEVTFLNITSFRDcplkDTPMLEVLK 317
Cdd:cd04723 1 RIIPVIDLK-----DGVVVHGVGGDRDNYRPITsNLCSTSDPLDVARAYKELGFRGLYIADLDAIMG----RGDNDEAIR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 318 QAAKTVFVPLTVGGGIKDivdvdgtkipaLEVASLYFRSGADKVSIGTdavyaaekyyELGNRGDGTSPIEtiskAYGAQ 397
Cdd:cd04723 72 ELAAAWPLGLWVDGGIRS-----------LENAQEWLKRGASRVIVGT----------ETLPSDDDEDRLA----ALGEQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 398 AVVISVDPKRVYVNsqadtknkvfeteypgpngekycwyqctikggRESRDLGVWELTRACEALgAGEILLNCIDKDGSN 477
Cdd:cd04723 127 RLVLSLDFRGGQLL--------------------------------KPTDFIGPEELLRRLAKW-PEELIVLDIDRVGSG 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365721 478 SGYDLELIEHVKDAVKIPVIASSGAGVPEHFEEAFLKTrADACLGAGMFHRGEFTVNDVKE 538
Cdd:cd04723 174 QGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKLG-ASGALVASALHDGGLTLEDVVR 233
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
1-210 |
2.57e-47 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 163.80 E-value: 2.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 1 MPVVHVIDVESGNLQSLTNAIEHLG--YEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLFNRGFEKPIRE-YIESGK 77
Cdd:PRK13146 1 MMTVAIIDYGSGNLRSAAKALERAGagADVVVTADPDA--VAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEaVLAAGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 78 PIMGICVGLQALFAGSVESPKSTGLNYIDFKLSRF---DDSEKpVPEIGWNSCIPSEN--LFFGLDPYKRYYFVHSFAAi 152
Cdd:PRK13146 79 PFLGICVGMQLLFERGLEHGDTPGLGLIPGEVVRFqpdGPALK-VPHMGWNTVDQTRDhpLFAGIPDGARFYFVHSYYA- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365721 153 lnsekkkNLENDGWKIAKAKYGsEEFIAAVNKNNIFATQFHPEKSGKAGLNVIENFLK 210
Cdd:PRK13146 157 -------QPANPADVVAWTDYG-GPFTAAVARDNLFATQFHPEKSQDAGLALLRNFLA 206
|
|
| hisH |
PRK13170 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
1-209 |
3.97e-45 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 157.71 E-value: 3.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 1 MPVVhVIDVESGNLQSLTNAIEHLGYEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREyieSGKPIM 80
Cdd:PRK13170 1 MNVV-IIDTGCANLSSVKFAIERLGYEPVVSRDPDV--ILAADKLFLPGVGTAQAAMDQLRERELIDLIKA---CTQPVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 81 GICVGLQALFAGSVESPKSTGLNYIDFKLSRFDDSEKPVPEIGWNSCIPSEN--LFFGLDPYKRYYFVHSFAAILNSekk 158
Cdd:PRK13170 75 GICLGMQLLGERSEESGGVDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQAGhpLFQGIEDGSYFYFVHSYAMPVNE--- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 398365721 159 knlendgWKIAKAKYGsEEFIAAVNKNNIFATQFHPEKSGKAGLNVIENFL 209
Cdd:PRK13170 152 -------YTIAQCNYG-EPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFL 194
|
|
| hisH |
CHL00188 |
imidazole glycerol phosphate synthase subunit hisH; Provisional |
4-211 |
2.21e-43 |
|
imidazole glycerol phosphate synthase subunit hisH; Provisional
Pssm-ID: 214389 [Multi-domain] Cd Length: 210 Bit Score: 153.50 E-value: 2.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 4 VHVIDVESGNLQSLTNAIEHLGYEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGIC 83
Cdd:CHL00188 4 IGIIDYSMGNLHSVSRAIQQAGQQPCIINSESE--LAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKWIAEGNPFIGIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 84 VGLQALFAGSVESPKStGLNYIDFKLSRFDDS-EKPVPEIGWN-------SCIPSE-NLFFGLDPYKRYYFVHSFAAILN 154
Cdd:CHL00188 82 LGLHLLFETSEEGKEE-GLGIYKGQVKRLKHSpVKVIPHMGWNrlecqnsECQNSEwVNWKAWPLNPWAYFVHSYGVMPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365721 155 SEKKKNlendgwkiAKAKYGSEEFIAAVNKNNIFATQFHPEKSGKAGLNVIENFLKQ 211
Cdd:CHL00188 161 SQACAT--------TTTFYGKQQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREFMKK 209
|
|
| hisH |
PRK13152 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
6-210 |
1.53e-39 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 171876 [Multi-domain] Cd Length: 201 Bit Score: 143.06 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 6 VIDVESGNLQSLTNAIEHLGYEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLFNRGFEKPI-REYIESGKPIMGICV 84
Cdd:PRK13152 4 LIDYKAGNLNSVAKAFEKIGAINFIAKNPKD--LQKADKLLLPGVGSFKEAMKNLKELGFIEALkEQVLVQKKPILGICL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 85 GLQALFAGSVESPKSTGLNYIDFKLSRFD-DSEKPVPEIGWNSCIPSEN--LFFGLDPYKRYYFVHSFAAILNsekkknl 161
Cdd:PRK13152 82 GMQLFLERGYEGGVCEGLGFIEGEVVKFEeDLNLKIPHMGWNELEILKQspLYQGIPEKSDFYFVHSFYVKCK------- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365721 162 enDGWKIAKAKYGSEeFIAAVNKNNIFATQFHPEKSGKAGLNVIENFLK 210
Cdd:PRK13152 155 --DEFVSAKAQYGHK-FVASLQKDNIFATQFHPEKSQNLGLKLLENFAR 200
|
|
| AglZ_HisF2_fam |
NF038364 |
AglZ/HisF2 family acetamidino modification protein; |
236-526 |
1.11e-38 |
|
AglZ/HisF2 family acetamidino modification protein;
Pssm-ID: 439657 Cd Length: 248 Bit Score: 141.84 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 236 LTRRIIACLDVRtndQGDLVVTkgdqydVREKsDGKGVrnlGKPVQLAQKYYQQGADEVTFLNITSFRDcplKDTPMLEV 315
Cdd:NF038364 1 LRPRIIPCLLLH---NGGLVKT------VKFK-DPKYV---GDPINAVRIFNEKEVDELIVLDIDATKE---GREPDYEL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 316 LKQAAKTVFVPLTVGGGIKDivdvdgtkipaLEVASLYFRSGADKVSIGTDAVyaaekyyelgnrgdgTSP--IETISKA 393
Cdd:NF038364 65 IEDLASECFMPLCYGGGIKT-----------LEQARRIFSLGVEKVALNSAAL---------------ENPelITEAAEE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 394 YGAQAVVISVDPKRvyvnsqadtknKVFETeypgpngekycwYQCTIKGGRESRDLGVWELTRACEALGAGEILLNCIDK 473
Cdd:NF038364 119 FGSQSVVVSIDVKK-----------NLFGG------------YEVYTHNGTKKTKLDPVEFAKELEALGAGEIVLNSIDR 175
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 398365721 474 DGSNSGYDLELIEHVKDAVKIPVIASSGAGVPEHFEEAFLKTRADAClGAG-MF 526
Cdd:NF038364 176 DGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAV-AAGsLF 228
|
|
| hisH |
PRK14004 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
3-210 |
1.55e-33 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 172505 [Multi-domain] Cd Length: 210 Bit Score: 126.94 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 3 VVHVIDVESGNLQSLTNAIEHlgYEVQLVKSPKDFNISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGI 82
Cdd:PRK14004 1 MIAILDYGMGNIHSCLKAVSL--YTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIDKHVESGKPLFGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 83 CVGLQALFAGSVE----SPKST--GLNYIDFKLSRFDDSEKPVPEIGWNSC--IPSEN--LFFGLDPYKRYYFVHSFaai 152
Cdd:PRK14004 79 CIGFQILFESSEEtnqgTKKEQieGLGYIKGKIKKFEGKDFKVPHIGWNRLqiRRKDKskLLKGIGDQSFFYFIHSY--- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365721 153 lnsekkKNLENDGWKI-AKAKYGSEEFIAAVNKNNIFATQFHPEKSGKAGLNVIENFLK 210
Cdd:PRK14004 156 ------RPTGAEGNAItGLCDYYQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENFIE 208
|
|
| hisH |
PRK13142 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
6-210 |
3.69e-31 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 171871 [Multi-domain] Cd Length: 192 Bit Score: 119.54 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 6 VIDVESGNLQSLTNAIEHLGYEVQLVKSPKDfnISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREyiESGKPIMGICVG 85
Cdd:PRK13142 4 IVDYGLGNISNVKRAIEHLGYEVVVSNTSKI--IDQAETIILPGVGHFKDAMSEIKRLNLNAILAK--NTDKKMIGICLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 86 LQALFAGSVESPKStGLNYIDFKLSRFDdSEKPVPEIGWNSCIPSENLFfgldpYKRYYFVHSFAAilnsekkknlENDG 165
Cdd:PRK13142 80 MQLMYEHSDEGDAS-GLGFIPGNISRIQ-TEYPVPHLGWNNLVSKHPML-----NQDVYFVHSYQA----------PMSE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365721 166 WKIAKAKYGSEeFIAAVNKNNIFATQFHPEKSGKAGLNVIENFLK 210
Cdd:PRK13142 143 NVIAYAQYGAD-IPAIVQFNNYIGIQFHPEKSGTYGLQILRQAIQ 186
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
5-211 |
3.32e-29 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 113.87 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 5 HVIDVESGNLQSLTNAIEHLGYEVQLVKSPKDFNIS----GTSRLILPGVGNYGHFvdnlfnRGFEKPIREYIESGKPIM 80
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEIleenPDGIILSGGPGSPGAA------GGAIEAIREARELKIPIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 81 GICVGLQAL---FAGSVEspkstglnyidfklsrfddSEKPVPEIGWNSCI--PSENLFFGLDPYKRYYFVHSFAAIlns 155
Cdd:pfam00117 75 GICLGHQLLalaFGGKVV-------------------KAKKFGHHGKNSPVgdDGCGLFYGLPNVFIVRRYHSYAVD--- 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365721 156 ekkKNLENDGWKIAKAKYGSEEFIAAVNKNN-IFATQFHPEKSGK-AGLNVIENFLKQ 211
Cdd:pfam00117 133 ---PDTLPDGLEVTATSENDGTIMGIRHKKLpIFGVQFHPESILTpHGPEILFNFFIK 187
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
269-501 |
1.34e-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: 84.84 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 269 DGKGVR-----------NLGKPVQLAQKYYQQGAdevTFLNITSFrDCPLKDTPM-LEVLKQAAKTVFVPLTVGGGIKDI 336
Cdd:cd04732 10 DGKCVRlyqgdydkktvYSDDPVEVAKKWEEAGA---KWLHVVDL-DGAKGGEPVnLELIEEIVKAVGIPVQVGGGIRSL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 337 vdvdgtkipalEVASLYFRSGADKVSIGTDAVYAAEKYYElgnrgdgtspietISKAYGAQAVVISVDPKRVYVNsqadt 416
Cdd:cd04732 86 -----------EDIERLLDLGVSRVIIGTAAVKNPELVKE-------------LLKEYGGERIVVGLDAKDGKVA----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 417 knkvfeteypgpngekycwyqctIKGGRESRDLGVWELTRACEALGAGEILLNCIDKDGSNSGYDLELIEHVKDAVKIPV 496
Cdd:cd04732 137 -----------------------TKGWLETSEVSLEELAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPV 193
|
....*
gi 398365721 497 IASSG 501
Cdd:cd04732 194 IASGG 198
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
277-524 |
4.22e-16 |
|
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: 76.86 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 277 GKPVQLAQKYYQQGADEVTFLNITSFRDCPLKDTPmlEVLKQAAKTVFVPLTVGGGIKDIVDVDGTKIPALEVAslyfrs 356
Cdd:cd04722 12 GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDK--EVLKEVAAETDLPLGVQLAINDAAAAVDIAAAAARAA------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 357 GADKVSIGTDAVYAAEkyyelgnrgDGTSPIETISKAYGAQAVVISVDPKRVYVNSQadtknkvfeteypgpngekycwy 436
Cdd:cd04722 84 GADGVEIHGAVGYLAR---------EDLELIRELREAVPDVKVVVKLSPTGELAAAA----------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 437 qctikggresrdlgvweltraCEALGAGEILLNCIDKDGSNSGYD---LELIEHVKDAVKIPVIASSGAGVPEHFEEAfL 513
Cdd:cd04722 132 ---------------------AEEAGVDEVGLGNGGGGGGGRDAVpiaDLLLILAKRGSKVPVIAGGGINDPEDAAEA-L 189
|
250
....*....|.
gi 398365721 514 KTRADACLGAG 524
Cdd:cd04722 190 ALGADGVIVGS 200
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
313-510 |
7.57e-16 |
|
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: 77.00 E-value: 7.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 313 LEVLKQAAKTVFVPLTVGGGIKDIVDVDGtkipalevaslYFRSGADKVSIGTDAVYAAEKyyelgnrgdgtspIETISK 392
Cdd:COG0106 62 LELIEEIAKATGLPVQVGGGIRSLEDIER-----------LLDAGASRVILGTAAVKDPEL-------------VKEALE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 393 AYGAQaVVISVDpkrvyvnsqadTKN-KVfeteypgpngekycwyqcTIKGGRESRDLGVWELTRACEALGAGEILLNCI 471
Cdd:COG0106 118 EFPER-IVVGLD-----------ARDgKV------------------ATDGWQETSGVDLEELAKRFEDAGVAAILYTDI 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 398365721 472 DKDGSNSGYDLELIEHVKDAVKIPVIASSGAGVPEHFEE 510
Cdd:COG0106 168 SRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRA 206
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
270-539 |
1.48e-15 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 76.48 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 270 GKGVRNLGKPVQLAQKYYQQGADEVTFLNITSFRDCPLKDTPMLEVLkqaAKTVFVPLTVGGGIKDIVDvdgtkipALEV 349
Cdd:PRK13585 25 GTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKI---IEAVGVPVQLGGGIRSAED-------AASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 350 ASLyfrsGADKVSIGTDAVyaaeKYYELgnrgdgtspIETISKAYGAQAVVISVDPKrvyvnsqadtKNKVfeteypgpn 429
Cdd:PRK13585 95 LDL----GVDRVILGTAAV----ENPEI---------VRELSEEFGSERVMVSLDAK----------DGEV--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 430 gekycwyqcTIKGGRESRDLGVWELTRACEALGAGEILLNCIDKDGSNSGYDLELIEHVKDAVKIPVIASSGAGVPEHFe 509
Cdd:PRK13585 139 ---------VIKGWTEKTGYTPVEAAKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDL- 208
|
250 260 270
....*....|....*....|....*....|
gi 398365721 510 EAFLKTRADACLGAGMFHRGEFTVNDVKEY 539
Cdd:PRK13585 209 RALKEAGAAGVVVGSALYKGKFTLEEAIEA 238
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
279-503 |
1.32e-13 |
|
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: 70.31 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 279 PVQLAQKYYQQGADEVTFLNITSFRDCPLKDtpmLEVLKQAAKTVFVPLTVGGGIKDivdvdgtkipaLEVASLYFRSGA 358
Cdd:TIGR00007 30 PVEAAKKWEEEGAERIHVVDLDGAKEGGPVN---LPVIKKIVRETGVPVQVGGGIRS-----------LEDVEKLLDLGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 359 DKVSIGTDAVYAAEKYYElgnrgdgtspietISKAYGAQAVVISVDPKrvyvnsqadtKNKVFeteypgpngekycwyqc 438
Cdd:TIGR00007 96 DRVIIGTAAVENPDLVKE-------------LLKEYGPERIVVSLDAR----------GGEVA----------------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365721 439 tIKGGRESRDLGVWELTRACEALGAGEILLNCIDKDGSNSGYDLELIEHVKDAVKIPVIASSGAG 503
Cdd:TIGR00007 136 -VKGWLEKSEVSLEELAKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVS 199
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
3-93 |
2.14e-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: 57.99 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 3 VVHVIDVESGNLQSLTNAIEHLGYEVQLV-----KSPKDFNISGTSRLILPGVGNYGHfvDNLFNRGFEKPIREYIESGK 77
Cdd:cd01653 3 VLLFPGFEELELASPLDALREAGAEVDVVspdggPVESDVDLDDYDGLILPGGPGTPD--DLARDEALLALLREAAAAGK 80
|
90
....*....|....*.
gi 398365721 78 PIMGICVGLQALFAGS 93
Cdd:cd01653 81 PILGICLGAQLLVLGV 96
|
|
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
313-501 |
2.27e-09 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 57.77 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 313 LEVLKQAAKTVFVPLTVGGGIKDIVDVDGtkipalevaslYFRSGADKVSIGTDAVYAAEKYYELgnrgdgtspietiSK 392
Cdd:PRK00748 63 LELIEAIVKAVDIPVQVGGGIRSLETVEA-----------LLDAGVSRVIIGTAAVKNPELVKEA-------------CK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 393 AYGAQaVVISVDPKrvyvnsqadtknkvfeteypgpNGekycwyQCTIKGGRESRDLGVWELTRACEALGAGEILLNCID 472
Cdd:PRK00748 119 KFPGK-IVVGLDAR----------------------DG------KVATDGWLETSGVTAEDLAKRFEDAGVKAIIYTDIS 169
|
170 180
....*....|....*....|....*....
gi 398365721 473 KDGSNSGYDLELIEHVKDAVKIPVIASSG 501
Cdd:PRK00748 170 RDGTLSGPNVEATRELAAAVPIPVIASGG 198
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
3-89 |
5.26e-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: 53.36 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 3 VVHVIDVESGNLQSLTNAIEHLGYEVQLVKSPKD-----FNISGTSRLILPGVGNYGHfvDNLFNRGFEKPIREYIESGK 77
Cdd:cd03128 3 VLLFGGSEELELASPLDALREAGAEVDVVSPDGGpvesdVDLDDYDGLILPGGPGTPD--DLAWDEALLALLREAAAAGK 80
|
90
....*....|..
gi 398365721 78 PIMGICVGLQAL 89
Cdd:cd03128 81 PVLGICLGAQLL 92
|
|
| GATase1_PB |
cd01749 |
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ... |
20-195 |
6.44e-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: 55.61 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 20 AIEHLGYEVQLVKSPKDfnISGTSRLILPGvgnyGH--FVDNLFNR-GFEKPIREYIESGKPIMGICVGLQALFAGSVES 96
Cdd:cd01749 16 ALERLGVEVIEVRTPED--LEGIDGLIIPG----GEstTIGKLLRRtGLLDPLREFIRAGKPVFGTCAGLILLAKEVEDQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 97 PKSTGLNYIDFKLSRfddsekpvpeigwNscipsenlFFGldpykRYyfVHSFAAILnsekkkNLENDGWKIAKA----- 171
Cdd:cd01749 90 GGQPLLGLLDITVRR-------------N--------AFG-----RQ--VDSFEADL------DIPGLGLGPFPAvfira 135
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365721 172 ----KYGS--------EEFIAAVNKNNIFATQFHPE 195
Cdd:cd01749 136 pvieEVGPgvevlaeyDGKIVAVRQGNVLATSFHPE 171
|
|
| PRK13525 |
PRK13525 |
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; |
20-198 |
7.82e-08 |
|
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
Pssm-ID: 237411 [Multi-domain] Cd Length: 189 Bit Score: 52.47 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 20 AIEHLGYEVQLVKSPKDFNisGTSRLILPGvGN---YGHFVDNLfnrGFEKPIREYIESGKPIMGICVGLqALFAGSVES 96
Cdd:PRK13525 19 ALEALGAEAVEVRRPEDLD--EIDGLILPG-GEsttMGKLLRDF---GLLEPLREFIASGLPVFGTCAGM-ILLAKEIEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 97 PKSTGLNYIDFKLSRfddsekpvpeigwNScipsenlfFGldpykRYyfVHSFAAILNSekkKNLEND-------GWKIA 169
Cdd:PRK13525 92 YEQEHLGLLDITVRR-------------NA--------FG-----RQ--VDSFEAELDI---KGLGEPfpavfirAPYIE 140
|
170 180 190
....*....|....*....|....*....|....*
gi 398365721 170 KAKYGSE------EFIAAVNKNNIFATQFHPEKSG 198
Cdd:PRK13525 141 EVGPGVEvlatvgGRIVAVRQGNILATSFHPELTD 175
|
|
| PRK13527 |
PRK13527 |
glutamine amidotransferase subunit PdxT; Provisional |
8-210 |
2.65e-07 |
|
glutamine amidotransferase subunit PdxT; Provisional
Pssm-ID: 237412 [Multi-domain] Cd Length: 200 Bit Score: 51.04 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 8 DVESgNLQSLTNAIEHLG--YEVQLVKSPKDfnISGTSRLILPGvG---NYGHFVDNLfnrGFEKPIREYIESGKPIMGI 82
Cdd:PRK13527 11 DVEE-HIDALKRALDELGidGEVVEVRRPGD--LPDCDALIIPG-GestTIGRLMKRE---GILDEIKEKIEEGLPILGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 83 CVGLqALFAGSVESPKSTG-----LNYIDFKLSR------FDDSEKPVPeigwnscipsenlFFGLDPYKRYYFVHSFAA 151
Cdd:PRK13527 84 CAGL-ILLAKEVGDDRVTKteqplLGLMDVTVKRnafgrqRDSFEAEID-------------LSGLDGPFHAVFIRAPAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365721 152 ILNSEKKKNLendgwkiakAKYgsEEFIAAVNKNNIFATQFHPEKSGKAGLNviENFLK 210
Cdd:PRK13527 150 TKVGGDVEVL---------AKL--DDRIVAVEQGNVLATAFHPELTDDTRIH--EYFLK 195
|
|
| GATase_3 |
pfam07685 |
CobB/CobQ-like glutamine amidotransferase domain; |
45-89 |
1.40e-05 |
|
CobB/CobQ-like glutamine amidotransferase domain;
Pssm-ID: 429595 [Multi-domain] Cd Length: 189 Bit Score: 46.08 E-value: 1.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 398365721 45 LILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGICVGLQAL 89
Cdd:pfam07685 46 IILPGGKPTIQDLALLRNSGMDEAIKEAAEDGGPVLGICGGYQML 90
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
4-195 |
2.05e-05 |
|
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: 46.09 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 4 VHVID---VESGNLQSLTNAIEHLGYEVQLVK------SPKDFNISGTSRLILPGvGNYGHFVDNLFNRGFEKPIREYIE 74
Cdd:COG0518 2 ILILDhdpFGGQYPGLIARRLREAGIELDVLRvyageiLPYDPDLEDPDGLILSG-GPMSVYDEDPWLEDEPALIREAFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 75 SGKPIMGICVGLQAL---FAGSVEspKStglnyidfklsrfddsekPVPEIGW--NSCIPSENLFFGLDPykRYYFVHS- 148
Cdd:COG0518 81 LGKPVLGICYGAQLLahaLGGKVE--PG------------------PGREIGWapVELTEADPLFAGLPD--EFTVWMSh 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365721 149 ----------FAAILNSEkkknlendgwkiakakygSEEFIAAVNKNNIFATQFHPE 195
Cdd:COG0518 139 gdtvtelpegAEVLASSD------------------NCPNQAFRYGRRVYGVQFHPE 177
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
256-501 |
2.59e-04 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 42.90 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 256 VTKGDqYDVREKsdgkgvrnLGKPVQLAQKYYQQgADEVTFLNITSFRDCPLKDTPMLEVLKQAAKTVFVPLTVGGGIKD 335
Cdd:PRK13587 18 LTEGK-YDSEEK--------MSRSAEESIAYYSQ-FECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGIRT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 336 IVDVDGtkipalevaslYFRSGADKVSIGTDAVyaaekyyelgnrgDGTSPIETISKAYgaqavvisvdPKRVYVNSQAD 415
Cdd:PRK13587 88 KSQIMD-----------YFAAGINYCIVGTKGI-------------QDTDWLKEMAHTF----------PGRIYLSVDAY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 416 TKnkvfeteypgpngekycwyQCTIKGGRESRDLGVWELTRACEALGAGEILLNCIDKDGSNSGYDLELIEHVKDAVKIP 495
Cdd:PRK13587 134 GE-------------------DIKVNGWEEDTELNLFSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIP 194
|
....*.
gi 398365721 496 VIASSG 501
Cdd:PRK13587 195 VIASGG 200
|
|
| GATase1_CobQ |
cd01750 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
22-108 |
2.95e-04 |
|
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: 42.23 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 22 EHLGYEVQLVKSPKDFNisGTSRLILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGICVGLQALF-----AGSVES 96
Cdd:cd01750 20 REPGVDVRYVEVPEGLG--DADLIILPGSKDTIQDLAWLRKRGLAEAIKNYARAGGPVLGICGGYQMLGkyivdPEGVEG 97
|
90
....*....|...
gi 398365721 97 PKST-GLNYIDFK 108
Cdd:cd01750 98 PGEIeGLGLLDVE 110
|
|
| PRK13526 |
PRK13526 |
glutamine amidotransferase subunit PdxT; Provisional |
12-111 |
5.73e-04 |
|
glutamine amidotransferase subunit PdxT; Provisional
Pssm-ID: 184113 [Multi-domain] Cd Length: 179 Bit Score: 41.09 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 12 GNLQSLTNAIEHLGYEVQLVKSPKDFNisGTSRLILPGvGNYGHFVdNLFNRG--FEKpIREYIeSGKPIMGICvglqal 89
Cdd:PRK13526 12 GGYQKHADMFKSLGVEVKLVKFNNDFD--SIDRLVIPG-GESTTLL-NLLNKHqiFDK-LYNFC-SSKPVFGTC------ 79
|
90 100
....*....|....*....|...
gi 398365721 90 fAGSVESPKSTG-LNYIDFKLSR 111
Cdd:PRK13526 80 -AGSIILSKGEGyLNLLDLEVQR 101
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
67-198 |
9.00e-04 |
|
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: 40.56 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 67 KPIREYIESGKPIMGICVGLQ--ALFAGSvespkST--------GLNYidfklsrfddsekPVPEIGWNSC-IPSENlff 135
Cdd:cd01744 60 KTVRKLLGKKIPIFGICLGHQllALALGA-----KTykmkfghrGSNH-------------PVKDLITGRVyITSQN--- 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365721 136 gldpykryyfvHSFAAILNSEKKK------NLeNDgwkiakakyGSEEFIAAVNKnNIFATQFHPEKSG 198
Cdd:cd01744 119 -----------HGYAVDPDSLPGGlevthvNL-ND---------GTVEGIRHKDL-PVFSVQFHPEASP 165
|
|
| GATase1_FGAR_AT |
cd01740 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
20-89 |
1.17e-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: 40.68 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365721 20 AIEHLGYEVQLV---------KSPKDFNIsgtsrLILPGVGNYGhfvDNL-------FNRGFEKPIREYIESGKPIMGIC 83
Cdd:cd01740 18 AFELAGFEAEDVwhndllagrKDLDDYDG-----VVLPGGFSYG---DYLragaiaaASPLLMEEVKEFAERGGLVLGIC 89
|
....*.
gi 398365721 84 VGLQAL 89
Cdd:cd01740 90 NGFQIL 95
|
|
| PRK00784 |
PRK00784 |
cobyric acid synthase; |
60-108 |
9.82e-03 |
|
cobyric acid synthase;
Pssm-ID: 234838 [Multi-domain] Cd Length: 488 Bit Score: 38.53 E-value: 9.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365721 60 LFNRGFEKPIREYIESGKPIMGICVGLQALfaGS-------VESPKST--GLNYIDFK 108
Cdd:PRK00784 309 LRESGWDEAIRAHARRGGPVLGICGGYQML--GRriadpdgVEGAPGSveGLGLLDVE 364
|
|
| |
