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Conserved domains on  [gi|4510353|gb|AAD21442|]
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phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase [Arabidopsis thaliana]

Protein Classification

triose-phosphate isomerase; tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like( domain architecture ID 10791361)

triose-phosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate| tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like (DUS1L) catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02446 PLN02446
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 44-302 0e+00

(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase


:

Pssm-ID: 215245  Cd Length: 262  Bit Score: 547.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    44 VQFRPCIDIHKGKVKQIVGSTLRDLK---EDGSVLVTNFESDKSAEEYAKMYKEDGLTGGHVIMLGADPLSQAAAIGALH 120
Cdd:PLN02446   1 VRFRPCIDIHKGKVKQIVGSTLKDSKdgsEDGSELVTNFESDKSAAEFAEMYKRDGLTGGHVIMLGADDASLAAALEALR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   121 AYPGGLQVGGGINSENCMSYIEEGASHVIVTSYVFNNGKIDLERLKDIVSIVGKQRLILDLSCRKKDGRYAIVTDRWQKF 200
Cdd:PLN02446  81 AYPGGLQVGGGVNSENAMSYLDAGASHVIVTSYVFRDGQIDLERLKDLVRLVGKQRLVLDLSCRKKDGRYYVVTDRWQKF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   201 SDVILDEKSLEFLGGFSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKGRVDVTVGSA 280
Cdd:PLN02446 161 SDLAVDEETLEFLAAYCDEFLVHGVDVEGKRLGIDEELVALLGEHSPIPVTYAGGVRSLDDLERVKVAGGGRVDVTVGSA 240

                        250       260
                 ....*....|....*....|..
gi 4510353   281 LDIFGGNLPYKDVVAWHHKQHS 302
Cdd:PLN02446 241 LDIFGGNLPYDDVVAWHKQQKT 262
 
Name Accession Description Interval E-value
PLN02446 PLN02446
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 44-302 0e+00

(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase


Pssm-ID: 215245  Cd Length: 262  Bit Score: 547.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    44 VQFRPCIDIHKGKVKQIVGSTLRDLK---EDGSVLVTNFESDKSAEEYAKMYKEDGLTGGHVIMLGADPLSQAAAIGALH 120
Cdd:PLN02446   1 VRFRPCIDIHKGKVKQIVGSTLKDSKdgsEDGSELVTNFESDKSAAEFAEMYKRDGLTGGHVIMLGADDASLAAALEALR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   121 AYPGGLQVGGGINSENCMSYIEEGASHVIVTSYVFNNGKIDLERLKDIVSIVGKQRLILDLSCRKKDGRYAIVTDRWQKF 200
Cdd:PLN02446  81 AYPGGLQVGGGVNSENAMSYLDAGASHVIVTSYVFRDGQIDLERLKDLVRLVGKQRLVLDLSCRKKDGRYYVVTDRWQKF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   201 SDVILDEKSLEFLGGFSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKGRVDVTVGSA 280
Cdd:PLN02446 161 SDLAVDEETLEFLAAYCDEFLVHGVDVEGKRLGIDEELVALLGEHSPIPVTYAGGVRSLDDLERVKVAGGGRVDVTVGSA 240

                        250       260
                 ....*....|....*....|..
gi 4510353   281 LDIFGGNLPYKDVVAWHHKQHS 302
Cdd:PLN02446 241 LDIFGGNLPYDDVVAWHKQQKT 262
hisA_euk TIGR02129
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, eukaryotic type; This ...
 44-298 3.39e-156

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, eukaryotic type; This enzyme acts in the biosynthesis of histidine and has been characterized in S. cerevisiae and Arabidopsis where it complements the E. coli HisA gene. In eukaryotes the gene is known as HIS6. In bacteria, this gene is found in Fibrobacter succinogenes, presumably due to lateral gene transfer from plants in the rumen gut. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 162719  Cd Length: 253  Bit Score: 436.14  E-value: 3.39e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353     44 VQFRPCIDIHKGKVKQIVGSTLRDlkEDGSVLVTNFESDKSAEEYAKMYKEDGLTGGHVIMLGADplSQAAAIGALHAYP 123
Cdd:TIGR02129   1 TKFRPCIDIHNGKVKQIVGGTLTS--KKGSVLKTNFVSDKPSSYYAKLYKDDGVKGCHVIMLGPN--NDDAAKEALHAYP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    124 GGLQVGGGINSENCMSYIEEGASHVIVTSYVFNNGKIDLERLKDIVSIVGKQRLILDLSCRKK-DGRYAIVTDRWQKFSD 202
Cdd:TIGR02129  77 GGLQVGGGINDTNAQEWLDEGASHVIVTSWLFTKGKFDLKRLKEIVSLVGKDRLIVDLSCRKTqDGRWIVAMNKWQTITD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    203 VILDEKSLEFLGGFSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKGRVDVTVGSALD 282
Cdd:TIGR02129 157 LELNAETLEELSKYCDEFLIHAADVEGLCKGIDEELVSKLGEWSPIPITYAGGAKSIDDLDLVDELSKGKVDLTIGSALD 236

                         250
                  ....*....|....*..
gi 4510353    283 IFGGN-LPYKDVVAWHH 298
Cdd:TIGR02129 237 IFGGNlVKFTDCVAWNK 253
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 45-295 6.22e-74

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: 226.77  E-value: 6.22e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   45 QFRPCIDIHKGKVKQIVGSTLRDLKEdgsvLVTNFESDKSAEEYAKMYKEDGLTGGHVIMLGA---DPLSQAAAIGALHA 121
Cdd:cd04723   1 RIIPVIDLKDGVVVHGVGGDRDNYRP----ITSNLCSTSDPLDVARAYKELGFRGLYIADLDAimgRGDNDEAIRELAAA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353  122 YPGGLQVGGGINS-ENCMSYIEEGASHVIVTSYVFNNgKIDLERLKDIVSivgkQRLILDLSCRKKDGRyaivtdrwqKF 200
Cdd:cd04723  77 WPLGLWVDGGIRSlENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGE----QRLVLSLDFRGGQLL---------KP 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353  201 SDVILDEKSLEFLGGFSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKgrVDVTVGSA 280
Cdd:cd04723 143 TDFIGPEELLRRLAKWPEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKLGA--SGALVASA 220

                       250
                ....*....|....*
gi 4510353  281 LDIFGgnLPYKDVVA 295
Cdd:cd04723 221 LHDGG--LTLEDVVR 233
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 45-296 2.13e-51

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: 169.06  E-value: 2.13e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   45 QFRPCIDIHKGKVKQIVGSTLRDlkedgsvlvtNFESDKSAEEYAKMYKEDGLTGGHVIMLGA----DPlSQAAAIGA-L 119
Cdd:COG0106   1 IIIPAIDLKDGKCVRLVQGDYDQ----------ETVYSDDPVEVAKRWEDAGAEWLHLVDLDGafagKP-VNLELIEEiA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353  120 HAYPGGLQVGGGINS-ENCMSYIEEGASHVIVTSYVFNNGkidlERLKDIVSIVGKqRLILDLSCRkkDGRyaIVTDRWQ 198
Cdd:COG0106  70 KATGLPVQVGGGIRSlEDIERLLDAGASRVILGTAAVKDP----ELVKEALEEFPE-RIVVGLDAR--DGK--VATDGWQ 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353  199 KFSDVILDEKSLEFLGGFSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAgkGRVDVTVG 278
Cdd:COG0106 141 ETSGVDLEELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL--GVEGAIVG 218

                       250
                ....*....|....*...
gi 4510353  279 SALdiFGGNLPYKDVVAW 296
Cdd:COG0106 219 KAL--YEGKIDLEEALAL 234
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 48-281 1.08e-26

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: 104.48  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353     48 PCIDIHKGKVKQIV-GSTLRDLKEDGSVLvtnfesdksaeEYAKMYKEDGLTGGHVIMLGADPLSQAAAIGALHAYPGG- 125
Cdd:pfam00977   4 PAIDLKDGRVVRLVkGDYFQNTVYAGDPV-----------ELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEv 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    126 ---LQVGGGINSENCM-SYIEEGASHVIVTSYVFNNgkidLERLKDIVSIVGKQRLILDLSCRkkDGRyaIVTDRWQKFS 201
Cdd:pfam00977  73 fipVQVGGGIRSLEDVeRLLSAGADRVIIGTAAVKN----PELIKEAAEKFGSQCIVVAIDAR--RGK--VAINGWREDT 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    202 DVILDE--KSLEFLGgfSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKgrVDVTVGS 279
Cdd:pfam00977 145 GIDAVEwaKELEELG--AGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGV--DGVIAGS 220


                  ..
gi 4510353    280 AL 281
Cdd:pfam00977 221 AL 222
 
Name Accession Description Interval E-value
PLN02446 PLN02446
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 44-302 0e+00

(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase


Pssm-ID: 215245  Cd Length: 262  Bit Score: 547.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    44 VQFRPCIDIHKGKVKQIVGSTLRDLK---EDGSVLVTNFESDKSAEEYAKMYKEDGLTGGHVIMLGADPLSQAAAIGALH 120
Cdd:PLN02446   1 VRFRPCIDIHKGKVKQIVGSTLKDSKdgsEDGSELVTNFESDKSAAEFAEMYKRDGLTGGHVIMLGADDASLAAALEALR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   121 AYPGGLQVGGGINSENCMSYIEEGASHVIVTSYVFNNGKIDLERLKDIVSIVGKQRLILDLSCRKKDGRYAIVTDRWQKF 200
Cdd:PLN02446  81 AYPGGLQVGGGVNSENAMSYLDAGASHVIVTSYVFRDGQIDLERLKDLVRLVGKQRLVLDLSCRKKDGRYYVVTDRWQKF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   201 SDVILDEKSLEFLGGFSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKGRVDVTVGSA 280
Cdd:PLN02446 161 SDLAVDEETLEFLAAYCDEFLVHGVDVEGKRLGIDEELVALLGEHSPIPVTYAGGVRSLDDLERVKVAGGGRVDVTVGSA 240

                        250       260
                 ....*....|....*....|..
gi 4510353   281 LDIFGGNLPYKDVVAWHHKQHS 302
Cdd:PLN02446 241 LDIFGGNLPYDDVVAWHKQQKT 262
hisA_euk TIGR02129
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, eukaryotic type; This ...
 44-298 3.39e-156

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, eukaryotic type; This enzyme acts in the biosynthesis of histidine and has been characterized in S. cerevisiae and Arabidopsis where it complements the E. coli HisA gene. In eukaryotes the gene is known as HIS6. In bacteria, this gene is found in Fibrobacter succinogenes, presumably due to lateral gene transfer from plants in the rumen gut. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 162719  Cd Length: 253  Bit Score: 436.14  E-value: 3.39e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353     44 VQFRPCIDIHKGKVKQIVGSTLRDlkEDGSVLVTNFESDKSAEEYAKMYKEDGLTGGHVIMLGADplSQAAAIGALHAYP 123
Cdd:TIGR02129   1 TKFRPCIDIHNGKVKQIVGGTLTS--KKGSVLKTNFVSDKPSSYYAKLYKDDGVKGCHVIMLGPN--NDDAAKEALHAYP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    124 GGLQVGGGINSENCMSYIEEGASHVIVTSYVFNNGKIDLERLKDIVSIVGKQRLILDLSCRKK-DGRYAIVTDRWQKFSD 202
Cdd:TIGR02129  77 GGLQVGGGINDTNAQEWLDEGASHVIVTSWLFTKGKFDLKRLKEIVSLVGKDRLIVDLSCRKTqDGRWIVAMNKWQTITD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    203 VILDEKSLEFLGGFSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKGRVDVTVGSALD 282
Cdd:TIGR02129 157 LELNAETLEELSKYCDEFLIHAADVEGLCKGIDEELVSKLGEWSPIPITYAGGAKSIDDLDLVDELSKGKVDLTIGSALD 236

                         250
                  ....*....|....*..
gi 4510353    283 IFGGN-LPYKDVVAWHH 298
Cdd:TIGR02129 237 IFGGNlVKFTDCVAWNK 253
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 45-295 6.22e-74

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: 226.77  E-value: 6.22e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   45 QFRPCIDIHKGKVKQIVGSTLRDLKEdgsvLVTNFESDKSAEEYAKMYKEDGLTGGHVIMLGA---DPLSQAAAIGALHA 121
Cdd:cd04723   1 RIIPVIDLKDGVVVHGVGGDRDNYRP----ITSNLCSTSDPLDVARAYKELGFRGLYIADLDAimgRGDNDEAIRELAAA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353  122 YPGGLQVGGGINS-ENCMSYIEEGASHVIVTSYVFNNgKIDLERLKDIVSivgkQRLILDLSCRKKDGRyaivtdrwqKF 200
Cdd:cd04723  77 WPLGLWVDGGIRSlENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGE----QRLVLSLDFRGGQLL---------KP 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353  201 SDVILDEKSLEFLGGFSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKgrVDVTVGSA 280
Cdd:cd04723 143 TDFIGPEELLRRLAKWPEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKLGA--SGALVASA 220

                       250
                ....*....|....*
gi 4510353  281 LDIFGgnLPYKDVVA 295
Cdd:cd04723 221 LHDGG--LTLEDVVR 233
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 45-296 2.13e-51

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: 169.06  E-value: 2.13e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   45 QFRPCIDIHKGKVKQIVGSTLRDlkedgsvlvtNFESDKSAEEYAKMYKEDGLTGGHVIMLGA----DPlSQAAAIGA-L 119
Cdd:COG0106   1 IIIPAIDLKDGKCVRLVQGDYDQ----------ETVYSDDPVEVAKRWEDAGAEWLHLVDLDGafagKP-VNLELIEEiA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353  120 HAYPGGLQVGGGINS-ENCMSYIEEGASHVIVTSYVFNNGkidlERLKDIVSIVGKqRLILDLSCRkkDGRyaIVTDRWQ 198
Cdd:COG0106  70 KATGLPVQVGGGIRSlEDIERLLDAGASRVILGTAAVKDP----ELVKEALEEFPE-RIVVGLDAR--DGK--VATDGWQ 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353  199 KFSDVILDEKSLEFLGGFSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAgkGRVDVTVG 278
Cdd:COG0106 141 ETSGVDLEELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL--GVEGAIVG 218

                       250
                ....*....|....*...
gi 4510353  279 SALdiFGGNLPYKDVVAW 296
Cdd:COG0106 219 KAL--YEGKIDLEEALAL 234
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 48-281 1.08e-26

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: 104.48  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353     48 PCIDIHKGKVKQIV-GSTLRDLKEDGSVLvtnfesdksaeEYAKMYKEDGLTGGHVIMLGADPLSQAAAIGALHAYPGG- 125
Cdd:pfam00977   4 PAIDLKDGRVVRLVkGDYFQNTVYAGDPV-----------ELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEv 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    126 ---LQVGGGINSENCM-SYIEEGASHVIVTSYVFNNgkidLERLKDIVSIVGKQRLILDLSCRkkDGRyaIVTDRWQKFS 201
Cdd:pfam00977  73 fipVQVGGGIRSLEDVeRLLSAGADRVIIGTAAVKN----PELIKEAAEKFGSQCIVVAIDAR--RGK--VAINGWREDT 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    202 DVILDE--KSLEFLGgfSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKgrVDVTVGS 279
Cdd:pfam00977 145 GIDAVEwaKELEELG--AGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGV--DGVIAGS 220


                  ..
gi 4510353    280 AL 281
Cdd:pfam00977 221 AL 222
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 87-281 8.09e-16

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: 75.21  E-value: 8.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   87 EYAKMYKEDGLTGGHVIML-GA-DPLS-QAAAIGALHAYPGG-LQVGGGINSENCM-SYIEEGASHVIVTSYVFNNGkid 161
Cdd:cd04732  33 EVAKKWEEAGAKWLHVVDLdGAkGGEPvNLELIEEIVKAVGIpVQVGGGIRSLEDIeRLLDLGVSRVIIGTAAVKNP--- 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353  162 lERLKDIVSIVGKQRLILDLSCRkkDGRYAivTDRWQKFSDVILDEKSLEFLGGFSDEFLVHGVDVEGKKLGIDEELVAL 241
Cdd:cd04732 110 -ELVKELLKEYGGERIVVGLDAK--DGKVA--TKGWLETSEVSLEELAKRFEELGVKAIIYTDISRDGTLSGPNFELYKE 184

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4510353  242 LGNYSPIPVTYAGGVTVMDDVERIKDAG-KGrvdVTVGSAL 281
Cdd:cd04732 185 LAAATGIPVIASGGVSSLDDIKALKELGvAG---VIVGKAL 222
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 48-281 1.63e-14

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;


Pssm-ID: 184165  Cd Length: 241  Bit Score: 71.48  E-value: 1.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    48 PCIDIHKGKVKQIVGStlrdlkEDGSVLVtnfeSDKSAEEYAKMYKEDGLTGGHVIML-GA--DPLSQAAAIGA-LHAYP 123
Cdd:PRK13585   7 PAVDMKGGKCVQLVQG------EPGTETV----SYGDPVEVAKRWVDAGAETLHLVDLdGAfeGERKNAEAIEKiIEAVG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   124 GGLQVGGGINS-ENCMSYIEEGASHVIVTSYVFNNGKIdlerLKDIVSIVGKQRLILDLSCrkKDGRyaIVTDRWQKFSD 202
Cdd:PRK13585  77 VPVQLGGGIRSaEDAASLLDLGVDRVILGTAAVENPEI----VRELSEEFGSERVMVSLDA--KDGE--VVIKGWTEKTG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   203 VILDE--KSLEFLGGFSdeFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAG-KGrvdVTVGS 279
Cdd:PRK13585 149 YTPVEaaKRFEELGAGS--ILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRALKEAGaAG---VVVGS 223


                 ..
gi 4510353   280 AL 281
Cdd:PRK13585 224 AL 225
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 48-292 6.63e-14

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: 69.54  E-value: 6.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353     48 PCIDIHKGK-VKQIVGstlrdlkEDGSVLVTNfesdKSAEEYAKMYKEDGLTGGHVIML-GA--------DPLSQAAAIG 117
Cdd:TIGR00007   3 PAIDIKDGKcVRLYQG-------DYDKETVYG----DDPVEAAKKWEEEGAERIHVVDLdGAkeggpvnlPVIKKIVRET 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    118 ALHaypggLQVGGGINS-ENCMSYIEEGASHVIVTSYVFNNgkidLERLKDIVSIVGKQRLILDLSCRkkDGRyaIVTDR 196
Cdd:TIGR00007  72 GVP-----VQVGGGIRSlEDVEKLLDLGVDRVIIGTAAVEN----PDLVKELLKEYGPERIVVSLDAR--GGE--VAVKG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    197 WQKFSDVILDE--KSLEFLGgfSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKGrvD 274
Cdd:TIGR00007 139 WLEKSEVSLEElaKRLEELG--LEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVY--G 214

                         250
                  ....*....|....*...
gi 4510353    275 VTVGSALdiFGGNLPYKD 292
Cdd:TIGR00007 215 VIVGKAL--YEGKITLEE 230
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 126-269 1.65e-06

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: 48.23  E-value: 1.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353  126 LQVGGGINS-ENCMSYIEEGASHVIVTSYVFNNGKIdlerLKDIVSIVGKQRLILDLSCRKK-DGRYAIVTDRWQKFSDV 203
Cdd:cd04731  74 LTVGGGIRSlEDARRLLRAGADKVSINSAAVENPEL----IREIAKRFGSQCVVVSIDAKRRgDGGYEVYTHGGRKPTGL 149

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353  204 ILDE--KSLEFLG-GfsdEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDD-VERIKDAG 269
Cdd:cd04731 150 DAVEwaKEVEELGaG---EILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHfVEAFEEGG 216
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 48-269 3.39e-06

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 237439  Cd Length: 232  Bit Score: 47.43  E-value: 3.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    48 PCIDIHKGK-VKQIvgstlRDLKEDGSVLvtnfesdKSAEEYAKMYKEDGLTGGHVIMLGA--------DPLSQAAAIGA 118
Cdd:PRK13586   6 PSIDISLGKaVKRI-----RGVKGTGLIL-------GNPIEIASKLYNEGYTRIHVVDLDAaegvgnneMYIKEISKIGF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   119 lhaypGGLQVGGGINS-ENCMSYIEEGASHVIVTSYVFNNGKIdlerLKDIVSIVGKQRLILdlSCRKKDGRYAIVT--- 194
Cdd:PRK13586  74 -----DWIQVGGGIRDiEKAKRLLSLDVNALVFSTIVFTNFNL----FHDIVREIGSNRVLV--SIDYDNTKRVLIRgwk 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4510353   195 DRWQKFSDVILDEKSLEFLGgfsdeFLVHGVDVEGKKLGIDEELvallGNYS---PIPVTYAGGVTVMDDVERIKDAG 269
Cdd:PRK13586 143 EKSMEVIDGIKKVNELELLG-----IIFTYISNEGTTKGIDYNV----KDYArliRGLKEYAGGVSSDADLEYLKNVG 211
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 89-281 3.59e-06

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated


Pssm-ID: 179108  Cd Length: 233  Bit Score: 46.98  E-value: 3.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353    89 AKMYKEDGLTGGHVIML-GA-DP-LSQAAAIGA-LHAYPGGLQVGGGINSENCMS-YIEEGASHVIV-TSYVFNNgkidl 162
Cdd:PRK00748  36 AKAWEDQGAKWLHLVDLdGAkAGkPVNLELIEAiVKAVDIPVQVGGGIRSLETVEaLLDAGVSRVIIgTAAVKNP----- 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   163 ERLKDIVSIVGKqRLILDLSCRkkDGRYAivTDRWQKFSDVILDEksleflggFSDEFLVHGV------DVE--GKKLGI 234
Cdd:PRK00748 111 ELVKEACKKFPG-KIVVGLDAR--DGKVA--TDGWLETSGVTAED--------LAKRFEDAGVkaiiytDISrdGTLSGP 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 4510353   235 DEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKgrVD-VTVGSAL 281
Cdd:PRK00748 178 NVEATRELAAAVPIPVIASGGVSSLDDIKALKGLGA--VEgVIVGRAL 223
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 126-281 4.81e-04

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 167709  Cd Length: 228  Bit Score: 40.91  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4510353   126 LQVGGGINS-ENCMSYIEEGASHVIVTSYVFnngkiDLERLKDIVSIVGKQRLILDLscrkKDGRyaIVTDRWQKFSDvI 204
Cdd:PRK04128  76 VQVGGGLRTyESIKDAYEIGVENVIIGTKAF-----DLEFLEKVTSEFEGITVSLDV----KGGR--IAVKGWLEESS-I 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4510353   205 LDEKSLEFLGGFSDEFLVHGVDVEGKKLGIdEELVALLGNYSPIpvtYAGGVTVMDDVERIKDAGKGrvDVTVGSAL 281
Cdd:PRK04128 144 KVEDAYEMLKNYVNRFIYTSIERDGTLTGI-EEIERFWGDEEFI---YAGGVSSAEDVKKLAEIGFS--GVIIGKAL 214
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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