imidazole glycerol phosphate synthase subunit HisF [Rhizobium leguminosarum]
Protein Classification
imidazole glycerol phosphate synthase subunit HisF( domain architecture ID 10785016)
imidazole glycerol phosphate synthase cyclase subunit HisF catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| HisF | COG0107 | Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
3-261 | 6.79e-161 | |||||
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: 446.01 E-value: 6.79e-161
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| Name | Accession | Description | Interval | E-value | |||||
| HisF | COG0107 | Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
3-261 | 6.79e-161 | |||||
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: 446.01 E-value: 6.79e-161
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| HisF | cd04731 | The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
6-255 | 2.87e-137 | |||||
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: 386.05 E-value: 2.87e-137
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| hisF | TIGR00735 | imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
2-260 | 4.74e-118 | |||||
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family] Pssm-ID: 273241 Cd Length: 254 Bit Score: 337.80 E-value: 4.74e-118
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| His_biosynth | pfam00977 | Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
6-244 | 6.03e-103 | |||||
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: 298.62 E-value: 6.03e-103
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| AglZ_HisF2_fam | NF038364 | AglZ/HisF2 family acetamidino modification protein; |
3-240 | 6.88e-94 | |||||
AglZ/HisF2 family acetamidino modification protein; Pssm-ID: 439657 Cd Length: 248 Bit Score: 276.28 E-value: 6.88e-94
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| PRK00748 | PRK00748 | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
7-222 | 1.88e-42 | |||||
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated Pssm-ID: 179108 Cd Length: 233 Bit Score: 144.44 E-value: 1.88e-42
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| Name | Accession | Description | Interval | E-value | ||||||
| HisF | COG0107 | Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
3-261 | 6.79e-161 | ||||||
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: 446.01 E-value: 6.79e-161
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| HisF | cd04731 | The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
6-255 | 2.87e-137 | ||||||
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: 386.05 E-value: 2.87e-137
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| hisF | TIGR00735 | imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
2-260 | 4.74e-118 | ||||||
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family] Pssm-ID: 273241 Cd Length: 254 Bit Score: 337.80 E-value: 4.74e-118
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| His_biosynth | pfam00977 | Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
6-244 | 6.03e-103 | ||||||
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: 298.62 E-value: 6.03e-103
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| WbuZ | TIGR03572 | glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ... |
3-240 | 1.58e-102 | ||||||
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the HisF protein, but generally represents the second HisF homolog in the genome where the other is an authentic HisF observed in the context of a complete histidine biosynthesis operon. The similarity between these WbuZ sequences and true HisFs is such that often the closest match by BLAST of a WbuZ is a HisF. Only by making a multiple sequence alignment is the homology relationship among the WbuZ sequences made apparent. WbuZ genes are invariably observed in the presence of a homolog of the HisH protein (designated WbuY) and a proposed N-acetyl sugar amidotransferase designated in WbuX in E. coli, IfnA in P. aeriginosa and PseA in C. jejuni. Similarly, this trio of genes is invariably found in the context of saccharide biosynthesis loci. It has been shown that the WbuYZ homologs are not essential components of the activity expressed by WbuX, leading to the proposal that these to proteins provide ammonium ions to the amidotransferase when these are in low concentration. WbuY (like HisH) is proposed to act as a glutaminase to release ammonium. In histidine biosynthesis this is also dispensible in the presence of exogenous ammonium ion. HisH and HisF form a complex such that the ammonium ion is passed directly to HisF where it is used in an amidation reaction causing a subsequent cleavage and cyclization. In the case of WbuYZ, the ammonium ion would be passed from WbuY to WbuZ. WbuZ, being non-essential and so similar to HisF that a sugar substrate is unlikely, would function instead as a amoonium channel to the WbuX protein which does the enzymatic work. Pssm-ID: 132611 [Multi-domain] Cd Length: 232 Bit Score: 297.64 E-value: 1.58e-102
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| AglZ_HisF2_fam | NF038364 | AglZ/HisF2 family acetamidino modification protein; |
3-240 | 6.88e-94 | ||||||
AglZ/HisF2 family acetamidino modification protein; Pssm-ID: 439657 Cd Length: 248 Bit Score: 276.28 E-value: 6.88e-94
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| HisA | cd04732 | HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
6-224 | 1.72e-46 | ||||||
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: 154.95 E-value: 1.72e-46
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| HisA | COG0106 | Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
6-222 | 2.45e-46 | ||||||
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: 154.81 E-value: 2.45e-46
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| PRK00748 | PRK00748 | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
7-222 | 1.88e-42 | ||||||
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated Pssm-ID: 179108 Cd Length: 233 Bit Score: 144.44 E-value: 1.88e-42
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| PLN02617 | PLN02617 | imidazole glycerol phosphate synthase hisHF |
2-261 | 5.89e-41 | ||||||
imidazole glycerol phosphate synthase hisHF Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 147.55 E-value: 5.89e-41
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| TIGR00007 | TIGR00007 | phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
7-233 | 1.28e-40 | ||||||
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: 139.64 E-value: 1.28e-40
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| PRK13585 | PRK13585 | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
7-248 | 7.35e-38 | ||||||
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase; Pssm-ID: 184165 Cd Length: 241 Bit Score: 133.11 E-value: 7.35e-38
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| HisA_HisF | cd04723 | Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
6-249 | 4.14e-30 | ||||||
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: 112.36 E-value: 4.14e-30
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| PRK14024 | PRK14024 | phosphoribosyl isomerase A; Provisional |
8-222 | 8.84e-19 | ||||||
phosphoribosyl isomerase A; Provisional Pssm-ID: 237589 Cd Length: 241 Bit Score: 82.70 E-value: 8.84e-19
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| PRK13587 | PRK13587 | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
77-220 | 4.98e-13 | ||||||
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional Pssm-ID: 172156 Cd Length: 234 Bit Score: 66.78 E-value: 4.98e-13
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| PRK04128 | PRK04128 | 1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
4-249 | 6.33e-12 | ||||||
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase; Pssm-ID: 167709 Cd Length: 228 Bit Score: 63.25 E-value: 6.33e-12
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| PRK14114 | PRK14114 | 1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
7-251 | 2.52e-11 | ||||||
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase; Pssm-ID: 172604 Cd Length: 241 Bit Score: 61.95 E-value: 2.52e-11
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| PRK13586 | PRK13586 | 1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
6-221 | 6.25e-08 | ||||||
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase; Pssm-ID: 237439 Cd Length: 232 Bit Score: 52.05 E-value: 6.25e-08
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| OYE_like_FMN_family | cd02803 | Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
130-232 | 2.51e-06 | ||||||
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 47.57 E-value: 2.51e-06
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| DUS_like_FMN | cd02801 | Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
161-235 | 1.22e-04 | ||||||
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present. Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 42.10 E-value: 1.22e-04
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| YrpB | COG2070 | NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
163-222 | 1.63e-04 | ||||||
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only]; Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 42.02 E-value: 1.63e-04
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| NMO | pfam03060 | Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
160-238 | 6.04e-04 | ||||||
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite. Pssm-ID: 367316 [Multi-domain] Cd Length: 331 Bit Score: 40.57 E-value: 6.04e-04
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| OYE_like_4_FMN | cd04735 | Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
53-131 | 6.87e-04 | ||||||
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. Pssm-ID: 240086 [Multi-domain] Cd Length: 353 Bit Score: 40.27 E-value: 6.87e-04
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| PLN02446 | PLN02446 | (5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
78-220 | 1.05e-03 | ||||||
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase Pssm-ID: 215245 Cd Length: 262 Bit Score: 39.69 E-value: 1.05e-03
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| NPD_like | cd04730 | 2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
164-238 | 1.70e-03 | ||||||
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN. Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 38.62 E-value: 1.70e-03
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| OYE_YqiM_FMN | cd02932 | Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
162-235 | 1.92e-03 | ||||||
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs. Pssm-ID: 239242 [Multi-domain] Cd Length: 336 Bit Score: 39.01 E-value: 1.92e-03
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| OYE_like_3_FMN | cd04734 | Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
130-232 | 4.28e-03 | ||||||
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. One member of this subgroup, the Sinorhizobium meliloti stachydrine utilization protein stcD, has been idenified as a putative N-methylproline demethylase. Pssm-ID: 240085 [Multi-domain] Cd Length: 343 Bit Score: 37.98 E-value: 4.28e-03
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