| CP028360.1|AXN02481.1|73107_73704_+|ATP-phosphoribosyltransferase |
gnl|CDD|272888 |
TIGR00070, hisG, ATP phosphoribosyltransferase. Members of this family from B. subtilis, Aquifex aeolicus, and Synechocystis PCC6803 (and related taxa) lack the C-terminal third of the sequence. The sole homolog from Archaeoglobus fulgidus lacks the N-terminal 50 residues (as reported) and is otherwise atypical of the rest of the family. This model excludes the C-terminal extension. [Amino acid biosynthesis, Histidine family].
|
4.02163e-29 |
| CP028360.1|AXN02489.1|78814_79105_+|hypothetical-protein |
gnl|CDD|212141 |
cd11534, NTP-PPase_HisIE_like, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Escherichia coli phosphoribosyl-ATP pyrophosphohydrolase (HisIE or PRATP-PH) and its homologs. This family includes Escherichia coli phosphoribosyl-ATP pyrophosphohydrolase, HisIE, and its homologs from all three kingdoms of life. E. coli HisIE is encoded by the hisIE gene, which is formed by hisE gene fused to hisl. HisIE is a bifunctional enzyme responsible for the second and third steps of the histidine-biosynthesis pathway. Its N-terminal and C-terminal domains have phosphoribosyl-AMP cyclohydrolase (HisI) and phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) activity, respectively. This family corresponds to the C-terminal domain of HisIE and includes many hisE gene encoding proteins, all of which show significant sequence similarity to Mycobacterium tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH). These proteins may be responsible for only the second step in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate.
|
1.69133e-11 |
| CP028360.1|AXN02490.1|79258_80104_+|Ornithine-carbamoyltransferase |
gnl|CDD|234835 |
PRK00779, PRK00779, ornithine carbamoyltransferase; Provisional.
|
2.83308e-82 |
| CP028360.1|AXN02484.1|75960_76524_+|Imidazoleglycerol-phosphate-dehydratase |
gnl|CDD|153419 |
cd07914, IGPD, Imidazoleglycerol-phosphate dehydratase. Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2.1.19) catalyzes the dehydration of imidazole glycerol phosphate to imidazole acetol phosphate, the sixth step of histidine biosynthesis in plants and microorganisms where the histidine is synthesized de novo. There is an internal repeat in the protein domain that is related by pseudo-dyad symmetry, perhaps as a result of an ancient gene duplication. The apo-form of IGPD exists as a catalytically inactive trimer which, in the presence of specific divalent metal cations such as manganese (Mn2+), cobalt (Co2+), cadmium (Cd2+), nickel (Ni2+), iron (Fe2+) and zinc (Zn2+), assembles to form a biologically active high molecular weight metalloenzyme; a 24-mer with 4-3-2 symmetry. Each 24-mer has 24 active sites, and contains around 1.5 metal ions per monomer, each monomer contributing residues to three separate active sites. IGPD enzymes are monofunctional in fungi, plants, archaea and some eubacteria while they are encoded as bifunctional enzymes in other eubacteria, such that the enzyme is fused to histidinol-phosphate phosphatase, the penultimate enzyme of the histidine biosynthesis pathway. The histidine biosynthesis pathway is a potential target for development of herbicides, and IGPD is a target for the triazole phosphonate herbicides.
|
6.23231e-65 |
| CP028360.1|AXN02483.1|74924_75974_+|Histidinol-phosphate-aminotransferase |
gnl|CDD|273467 |
TIGR01141, Histidinol-phosphate_aminotransferase, histidinol-phosphate aminotransferase. Alternate names: histidinol-phosphate transaminase; imidazole acetol-phosphate transaminase Histidinol-phosphate aminotransferase is a pyridoxal-phosphate dependent enzyme. [Amino acid biosynthesis, Histidine family].
|
1.64816e-54 |
| CP028360.1|AXN02492.1|81665_82553_-|Phenylalanyl-tRNA-synthetase-alpha-chain |
gnl|CDD|238277 |
cd00496, PheRS_alpha_core, Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH ribose of the appropriate tRNA, PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. PheRS is an alpha-2/ beta-2 tetramer.
|
2.3583e-61 |
| CP028360.1|AXN02495.1|83044_83470_-|Translation-initiation-factor-IF-3 |
gnl|CDD|376372 |
pfam00707, IF3_C, Translation initiation factor IF-3, C-terminal domain.
|
8.80195e-12 |
| CP028360.1|AXN02500.1|86383_87058_-|30S-ribosomal-subunit-protein-S2 |
gnl|CDD|100106 |
cd01425, RPS2, Ribosomal protein S2 (RPS2), involved in formation of the translation initiation complex, where it might contact the messenger RNA and several components of the ribosome. It has been shown that in Escherichia coli RPS2 is essential for the binding of ribosomal protein S1 to the 30s ribosomal subunit. In humans, most likely in all vertebrates, and perhaps in all metazoans, the protein also functions as the 67 kDa laminin receptor (LAMR1 or 67LR), which is formed from a 37 kDa precursor, and is overexpressed in many tumors. 67LR is a cell surface receptor which interacts with a variety of ligands, laminin-1 and others. It is assumed that the ligand interactions are mediated via the conserved C-terminus, which becomes extracellular as the protein undergoes conformational changes which are not well understood. Specifically, a conserved palindromic motif, LMWWML, may participate in the interactions. 67LR plays essential roles in the adhesion of cells to the basement membrane and subsequent signalling events, and has been linked to several diseases. Some evidence also suggests that the precursor of 67LR, 37LRP is also present in the nucleus in animals, where it appears associated with histones.
|
9.55238e-07 |
| CP028360.1|AXN02485.1|76511_77147_+|Imidazole-glycerol-phosphate-synthase-amidotransferase-subunit |
gnl|CDD|153219 |
cd01748, GATase1_IGP_Synthase, 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.
|
8.08224e-51 |
| CP028360.1|AXN02482.1|73690_74938_+|Histidinol-dehydrogenase |
gnl|CDD|376389 |
pfam00815, Histidinol_dh, Histidinol dehydrogenase.
|
3.86576e-139 |
| CP028360.1|AXN02493.1|82527_82887_-|LSU-ribosomal-protein-L20p |
gnl|CDD|179959 |
PRK05185, rplT, 50S ribosomal protein L20; Provisional.
|
2.56258e-36 |
| CP028360.1|AXN02488.1|78519_78840_+|Phosphoribosyl-AMP-cyclohydrolase |
gnl|CDD|223217 |
COG0139, HisI, Phosphoribosyl-AMP cyclohydrolase [Amino acid transport and metabolism].
|
1.01426e-33 |
| CP028360.1|AXN02496.1|83550_84549_-|Chorismate-synthase |
gnl|CDD|376510 |
pfam01264, Chorismate_synt, Chorismate synthase.
|
1.11442e-151 |
| CP028360.1|AXN02501.1|87068_88178_+|N-succinyl-L,L-diaminopimelate-aminotransferase-alternative |
gnl|CDD|274637 |
TIGR03538, DapC_gpp, succinyldiaminopimelate transaminase. This family of succinyldiaminopimelate transaminases (DapC) includes the experimentally characterized enzyme from Bordatella pertussis. The majority of genes in this family are proximal to genes encoding components of the lysine biosynthesis via diaminopimelate pathway (GenProp0125).
|
1.30485e-65 |
| CP028360.1|AXN02487.1|77779_78523_+|Imidazole-glycerol-phosphate-synthase-cyclase-subunit |
gnl|CDD|240082 |
cd04731, HisF, 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.
|
4.11664e-95 |
| CP028360.1|AXN02486.1|77112_77790_+|Phosphoribosylformimino-5-aminoimidazole-carboxamide-ribotide-isomerase |
gnl|CDD|240083 |
cd04732, HisA, 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.
|
5.87222e-44 |
