| NZ_LR699016.1|WP_099432168.1|1358231_1358822_-|YihA-family-ribosome-biogenesis-GTP-binding-protein |
gnl|CDD|234770 |
PRK00454, engB, GTP-binding protein YsxC; Reviewed.
|
4.11896e-85 |
| NZ_LR699016.1|WP_099432172.1|1362751_1364803_-|formate-C-acetyltransferase |
gnl|CDD|153087 |
cd01678, PFL1, Pyruvate formate lyase 1. Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate in which two cysteines and one glycine form radicals that are required for catalysis. PFL has a ten-stranded alpha/beta barrel domain that is structurally similar to those of all three ribonucleotide reductase (RNR) classes as well as benzylsuccinate synthase and B12-independent glycerol dehydratase.
|
0 |
| NZ_LR699016.1|WP_099432167.1|1355370_1356888_+|threonine-synthase |
gnl|CDD|236418 |
PRK09225, PRK09225, threonine synthase; Validated.
|
0 |
| NZ_LR699016.1|WP_089572344.1|1350724_1351414_-|response-regulator-transcription-factor |
gnl|CDD|223816 |
COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].
|
1.85892e-69 |
| NZ_LR699016.1|WP_099432177.1|1372673_1373705_+|3-deoxy-7-phosphoheptulonate-synthase |
gnl|CDD|236435 |
PRK09261, PRK09261, phospho-2-dehydro-3-deoxyheptonate aldolase; Validated.
|
2.19488e-151 |
| NZ_LR699016.1|WP_099432171.1|1361123_1361978_-|DegV-family-EDD-domain-containing-protein |
gnl|CDD|273257 |
TIGR00762, DegV, EDD domain protein, DegV family. This family of proteins is related to DegV of Bacillus subtilis and includes paralogous sets in several species (B. subtilis, Deinococcus radiodurans, Mycoplasma pneumoniae) that are closer in percent identity to each than to most homologs from other species. This suggests both recent paralogy and diversity of function. DegV itself is encoded immediately downstream of DegU, a transcriptional regulator of degradation, but is itself uncharacterized. Crystallography suggested a lipid-binding site, while comparison of the crystal structure to dihydroxyacetone kinase and to a mannose transporter EIIA domain suggests a conserved domain, EDD, with phosphotransferase activity. [Unknown function, General].
|
1.12265e-48 |
| NZ_LR699016.1|WP_006234874.1|1357091_1357973_+|homoserine-kinase |
gnl|CDD|234920 |
PRK01212, PRK01212, homoserine kinase; Provisional.
|
3.31433e-103 |
| NZ_LR699016.1|WP_099432173.1|1365274_1366309_-|2-keto-3-deoxygluconate-permease |
gnl|CDD|377137 |
pfam03812, KdgT, 2-keto-3-deoxygluconate permease.
|
3.34753e-95 |
| NZ_LR699016.1|WP_099432174.1|1367435_1367885_+|winged-helix-DNA-binding-protein |
gnl|CDD|197670 |
smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.
|
2.19213e-12 |
| NZ_LR699016.1|WP_006234857.1|1366396_1367146_-|SDR-family-oxidoreductase |
gnl|CDD|235546 |
PRK05653, fabG, 3-oxoacyl-ACP reductase FabG.
|
3.64606e-73 |
| NZ_LR699016.1|WP_099432176.1|1370247_1372104_+|ABC-transporter-ATP-binding-protein |
gnl|CDD|224055 |
COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].
|
0 |
| NZ_LR699016.1|WP_099432165.1|1351642_1352224_-|methylated-DNA--[protein]-cysteine-S-methyltransferase |
gnl|CDD|223427 |
COG0350, Ada, Methylated DNA-protein cysteine methyltransferase [DNA replication, recombination, and repair].
|
3.97131e-52 |
| NZ_LR699016.1|WP_089572342.1|1348507_1349182_-|TIGR00266-family-protein |
gnl|CDD|376704 |
pfam01987, AIM24, Mitochondrial biogenesis AIM24. In eukaryotes, this domain is involved in mitochondrial biogenesis. Its function in prokaryotes in unknown.
|
2.65141e-81 |
| NZ_LR699016.1|WP_055252439.1|1362414_1362666_-|autonomous-glycyl-radical-cofactor-GrcA |
gnl|CDD|153087 |
cd01678, PFL1, Pyruvate formate lyase 1. Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate in which two cysteines and one glycine form radicals that are required for catalysis. PFL has a ten-stranded alpha/beta barrel domain that is structurally similar to those of all three ribonucleotide reductase (RNR) classes as well as benzylsuccinate synthase and B12-independent glycerol dehydratase.
|
3.6397e-42 |
| NZ_LR699016.1|WP_089572346.1|1352677_1353703_-|aspartate-semialdehyde-dehydrogenase |
gnl|CDD|237845 |
PRK14874, PRK14874, aspartate-semialdehyde dehydrogenase; Provisional.
|
1.7882e-175 |
| NZ_LR699016.1|WP_099432169.1|1358860_1359601_-|5'-methylthioadenosine/S-adenosylhomocysteine-nucleosidase |
gnl|CDD|350159 |
cd09008, MTAN, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases. This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs): bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.
|
7.48663e-61 |
| NZ_LR699016.1|WP_099432175.1|1367881_1370248_+|ABC-transporter-ATP-binding-protein |
gnl|CDD|224055 |
COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].
|
1.1045e-136 |
| NZ_LR699016.1|WP_099432166.1|1353877_1355266_-|aspartate-kinase |
gnl|CDD|236364 |
PRK09034, PRK09034, aspartate kinase; Reviewed.
|
0 |
| NZ_LR699016.1|WP_099432170.1|1360117_1360936_-|pyruvate-formate-lyase-activating-protein |
gnl|CDD|131546 |
TIGR02493, PFLA, pyruvate formate-lyase 1-activating enzyme. An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair].
|
7.71502e-102 |
| NZ_LR699016.1|WP_099432164.1|1349348_1350728_-|two-component-sensor-histidine-kinase |
gnl|CDD|273593 |
TIGR01386, Probable_sensor_protein_PcoS, heavy metal sensor kinase. Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.
|
1.26157e-36 |
