ORF_ID | e_value | Gene_name | EC_number | CAZy | COGs | Description |
---|---|---|---|---|---|---|
KPLABODI_00001 | 9.1e-261 | pckA | 4.1.1.49 | H | Phosphoenolpyruvate carboxykinase | |
KPLABODI_00002 | 6.3e-51 | pckA | 4.1.1.49 | H | Phosphoenolpyruvate carboxykinase | |
KPLABODI_00003 | 6.4e-265 | frdC | 1.3.5.4 | C | FAD binding domain | |
KPLABODI_00004 | 3.4e-113 | metI | P | ABC transporter permease | ||
KPLABODI_00005 | 5.3e-187 | metN | P | Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system | ||
KPLABODI_00006 | 3.2e-121 | metQ2 | P | Belongs to the nlpA lipoprotein family | ||
KPLABODI_00007 | 0.0 | aha1 | P | E1-E2 ATPase | ||
KPLABODI_00008 | 1.9e-38 | aha1 | P | E1-E2 ATPase | ||
KPLABODI_00009 | 9e-89 | folA | 1.5.1.3 | H | Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis | |
KPLABODI_00010 | 1.8e-189 | thyA | 2.1.1.45 | F | Catalyzes the reductive methylation of 2'-deoxyuridine- 5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis | |
KPLABODI_00011 | 2.9e-122 | 1.1.1.28 | CH | D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain | ||
KPLABODI_00012 | 5.4e-65 | |||||
KPLABODI_00013 | 0.0 | E | ABC transporter, substratebinding protein | |||
KPLABODI_00015 | 2.8e-125 | pnb | C | nitroreductase | ||
KPLABODI_00017 | 3.3e-191 | I | Protein of unknown function (DUF2974) | |||
KPLABODI_00018 | 4.4e-44 | S | Protein of unknown function (DUF2974) | |||
KPLABODI_00019 | 1.8e-107 | engB | D | Necessary for normal cell division and for the maintenance of normal septation | ||
KPLABODI_00020 | 3.8e-232 | clpX | O | ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP | ||
KPLABODI_00021 | 1.1e-194 | tig | D | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase | ||
KPLABODI_00022 | 2.8e-224 | tuf | J | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis | ||
KPLABODI_00023 | 4.5e-149 | |||||
KPLABODI_00024 | 0.0 | rnjB | J | An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and or decay | ||
KPLABODI_00025 | 6e-42 | rpsO | J | Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome | ||
KPLABODI_00026 | 1.6e-33 | rpsT | J | Binds directly to 16S ribosomal RNA | ||
KPLABODI_00027 | 1.6e-180 | holA | 2.7.7.7 | L | DNA polymerase III delta subunit | |
KPLABODI_00028 | 0.0 | comEC | S | Competence protein ComEC | ||
KPLABODI_00029 | 6.4e-70 | comEA | L | Competence protein ComEA | ||
KPLABODI_00030 | 2.3e-190 | ylbL | T | Belongs to the peptidase S16 family | ||
KPLABODI_00031 | 9.8e-83 | coaD | 2.7.7.3 | H | Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate | |
KPLABODI_00032 | 1.6e-97 | rsmD | 2.1.1.171 | L | RNA methyltransferase, RsmD family | |
KPLABODI_00033 | 1.1e-53 | ylbG | S | UPF0298 protein | ||
KPLABODI_00034 | 7.1e-212 | ftsW | D | Belongs to the SEDS family | ||
KPLABODI_00035 | 0.0 | typA | T | GTP-binding protein TypA | ||
KPLABODI_00036 | 4.7e-102 | def | 3.5.1.31, 3.5.1.88 | J | Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions | |
KPLABODI_00037 | 2.7e-35 | ykzG | S | Belongs to the UPF0356 family | ||
KPLABODI_00038 | 0.0 | rnjA | J | An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and or decay | ||
KPLABODI_00039 | 5.1e-251 | merA | 1.16.1.1, 1.8.1.7 | C | Pyridine nucleotide-disulfide oxidoreductase | |
KPLABODI_00040 | 0.0 | recD2 | 3.1.11.5 | L | DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity | |
KPLABODI_00041 | 1e-103 | S | Repeat protein | |||
KPLABODI_00042 | 2e-123 | pgm6 | 5.4.2.11, 5.4.2.12 | G | Phosphoglycerate mutase family | |
KPLABODI_00043 | 2.1e-221 | mnmA | 2.8.1.13 | J | Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34 | |
KPLABODI_00044 | 3.2e-56 | XK27_04120 | S | Putative amino acid metabolism | ||
KPLABODI_00045 | 2.8e-213 | iscS | 2.8.1.7 | E | Aminotransferase class V | |
KPLABODI_00046 | 3.1e-127 | mtnN | 3.2.2.9 | E | Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S- adenosylhomocysteine (SAH AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively | |
KPLABODI_00047 | 5.4e-19 | |||||
KPLABODI_00048 | 1.1e-101 | nudF | 3.6.1.13 | L | ADP-ribose pyrophosphatase | |
KPLABODI_00049 | 1.5e-32 | cspA | K | 'Cold-shock' DNA-binding domain | ||
KPLABODI_00050 | 0.0 | ileS | 6.1.1.5 | J | amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) | |
KPLABODI_00051 | 8.5e-145 | ylmH | S | S4 domain protein | ||
KPLABODI_00052 | 7.6e-46 | yggT | S | YGGT family | ||
KPLABODI_00053 | 1.1e-64 | sepF | D | Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA | ||
KPLABODI_00054 | 8.6e-206 | ftsZ | D | Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity | ||
KPLABODI_00055 | 2.2e-241 | ftsA | D | Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring | ||
KPLABODI_00056 | 1.1e-147 | divIB | D | Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex | ||
KPLABODI_00057 | 1.2e-208 | murG | 2.4.1.227, 6.3.2.8 | GT28 | M | Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II) |
KPLABODI_00058 | 5.6e-261 | murD | 6.3.2.9 | M | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) | |
KPLABODI_00059 | 2.7e-177 | mraY | 2.7.8.13 | M | First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan | |
KPLABODI_00060 | 0.0 | ftsI | 3.4.16.4 | M | Penicillin-binding Protein | |
KPLABODI_00061 | 4.8e-55 | ftsL | D | Cell division protein FtsL | ||
KPLABODI_00062 | 1.1e-172 | rsmH | 2.1.1.199 | J | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA | |
KPLABODI_00063 | 4.1e-77 | mraZ | K | Belongs to the MraZ family | ||
KPLABODI_00064 | 5.7e-55 | S | Protein of unknown function (DUF3397) | |||
KPLABODI_00066 | 1.4e-95 | mreD | ||||
KPLABODI_00067 | 1.8e-137 | mreC | M | Involved in formation and maintenance of cell shape | ||
KPLABODI_00068 | 2.6e-175 | mreB | D | cell shape determining protein MreB | ||
KPLABODI_00069 | 2.7e-114 | radC | L | DNA repair protein | ||
KPLABODI_00070 | 6.8e-127 | S | Haloacid dehalogenase-like hydrolase | |||
KPLABODI_00071 | 1.2e-233 | folC | 6.3.2.12, 6.3.2.17 | H | Belongs to the folylpolyglutamate synthase family | |
KPLABODI_00072 | 0.0 | valS | 6.1.1.9 | J | amino acids such as threonine, to avoid such errors, it has a posttransfer editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner | |
KPLABODI_00073 | 7.8e-129 | rsuA | 5.4.99.19, 5.4.99.22 | J | Belongs to the pseudouridine synthase RsuA family | |
KPLABODI_00074 | 3.2e-228 | thiI | 2.8.1.4 | H | Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS | |
KPLABODI_00075 | 1.4e-217 | iscS2 | 2.8.1.7 | E | Aminotransferase class V | |
KPLABODI_00076 | 3.4e-300 | ezrA | D | modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization | ||
KPLABODI_00077 | 1.2e-109 | rpsD | J | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit | ||
KPLABODI_00078 | 3.5e-82 | yueI | S | Protein of unknown function (DUF1694) | ||
KPLABODI_00079 | 3.6e-241 | rarA | L | recombination factor protein RarA | ||
KPLABODI_00080 | 1.3e-42 | |||||
KPLABODI_00081 | 3e-78 | usp6 | T | universal stress protein | ||
KPLABODI_00082 | 2.7e-219 | rodA | D | Belongs to the SEDS family | ||
KPLABODI_00083 | 1.7e-34 | S | Protein of unknown function (DUF2969) | |||
KPLABODI_00084 | 7.4e-48 | yidD | S | Could be involved in insertion of integral membrane proteins into the membrane | ||
KPLABODI_00085 | 6.1e-177 | mbl | D | Cell shape determining protein MreB Mrl | ||
KPLABODI_00086 | 5.1e-32 | ywzB | S | Protein of unknown function (DUF1146) | ||
KPLABODI_00087 | 1.6e-73 | atpC | C | Produces ATP from ADP in the presence of a proton gradient across the membrane | ||
KPLABODI_00088 | 1.3e-247 | atpD | 3.6.3.14 | C | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits | |
KPLABODI_00089 | 2.4e-170 | atpG | C | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex | ||
KPLABODI_00090 | 2.9e-279 | atpA | 3.6.3.14 | C | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit | |
KPLABODI_00091 | 3.9e-93 | atpH | C | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation | ||
KPLABODI_00092 | 4.2e-57 | atpF | C | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0) | ||
KPLABODI_00093 | 3.1e-28 | atpE | C | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation | ||
KPLABODI_00094 | 4.2e-127 | atpB | C | it plays a direct role in the translocation of protons across the membrane | ||
KPLABODI_00095 | 6.8e-113 | upp | 2.4.2.9 | F | Catalyzes the conversion of uracil and 5-phospho-alpha- D-ribose 1-diphosphate (PRPP) to UMP and diphosphate | |
KPLABODI_00096 | 5.4e-189 | ywlC | 2.7.7.87, 3.1.3.48 | J | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine | |
KPLABODI_00097 | 3e-156 | prmB | 2.1.1.297, 2.1.1.298 | J | Methylates the class 1 translation termination release factors RF1 PrfA and RF2 PrfB on the glutamine residue of the universally conserved GGQ motif | |
KPLABODI_00098 | 2.1e-194 | prfA | J | Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA | ||
KPLABODI_00099 | 1.4e-112 | tdk | 2.7.1.21 | F | thymidine kinase | |
KPLABODI_00100 | 7.9e-260 | murD | 3.4.21.10, 6.3.2.13, 6.3.2.9 | M | Mur ligase, middle domain | |
KPLABODI_00101 | 4.3e-34 | |||||
KPLABODI_00102 | 7.6e-191 | ampC | V | Beta-lactamase | ||
KPLABODI_00105 | 9.4e-178 | oppA | E | ABC transporter, substratebinding protein |
eggNOG-mapper v2 (Database: eggNOG v5.0, Jul. 2018 release)