node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AEB07027.1 | ispH | Corgl_0916 | Corgl_0908 | Phosphopantothenoylcysteine decarboxylase; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family. | Hydroxymethylbutenyl pyrophosphate reductase; Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. Belongs to the IspH family. | 0.483 |
AEB07027.1 | metK | Corgl_0916 | Corgl_1080 | Phosphopantothenoylcysteine decarboxylase; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family. | Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | 0.821 |
AEB07027.1 | priA | Corgl_0916 | Corgl_1079 | Phosphopantothenoylcysteine decarboxylase; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family. | Replication restart DNA helicase PriA; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.578 |
AEB07184.1 | def | Corgl_1076 | Corgl_1078 | NusB/RsmB/TIM44; COGs: COG0144 tRNA and rRNA cytosine-C5-methylase; InterPro IPR006027:IPR001678; KEGG: apv:Apar_0866 NusB/RsmB/TIM44; PFAM: NusB/RsmB/TIM44; Fmu (Sun) domain protein; SPTR: Putative uncharacterized protein; IMG reference gene:2503575875; PFAM: NOL1/NOP2/sun family; NusB family; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Peptide deformylase; 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. | 0.855 |
AEB07184.1 | fmt | Corgl_1076 | Corgl_1077 | NusB/RsmB/TIM44; COGs: COG0144 tRNA and rRNA cytosine-C5-methylase; InterPro IPR006027:IPR001678; KEGG: apv:Apar_0866 NusB/RsmB/TIM44; PFAM: NusB/RsmB/TIM44; Fmu (Sun) domain protein; SPTR: Putative uncharacterized protein; IMG reference gene:2503575875; PFAM: NOL1/NOP2/sun family; NusB family; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.927 |
AEB07184.1 | metK | Corgl_1076 | Corgl_1080 | NusB/RsmB/TIM44; COGs: COG0144 tRNA and rRNA cytosine-C5-methylase; InterPro IPR006027:IPR001678; KEGG: apv:Apar_0866 NusB/RsmB/TIM44; PFAM: NusB/RsmB/TIM44; Fmu (Sun) domain protein; SPTR: Putative uncharacterized protein; IMG reference gene:2503575875; PFAM: NOL1/NOP2/sun family; NusB family; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | 0.639 |
AEB07184.1 | pheT | Corgl_1076 | Corgl_1487 | NusB/RsmB/TIM44; COGs: COG0144 tRNA and rRNA cytosine-C5-methylase; InterPro IPR006027:IPR001678; KEGG: apv:Apar_0866 NusB/RsmB/TIM44; PFAM: NusB/RsmB/TIM44; Fmu (Sun) domain protein; SPTR: Putative uncharacterized protein; IMG reference gene:2503575875; PFAM: NOL1/NOP2/sun family; NusB family; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR004532:IPR002547:IPR005121:IPR005146:IPR 005147; KEGG: apv:Apar_1054 phenylalanyl-tRNA synthetase, beta subunit; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: Putative uncharacterized protein; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; IMG reference gene:2503576306; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta su [...] | 0.601 |
AEB07184.1 | priA | Corgl_1076 | Corgl_1079 | NusB/RsmB/TIM44; COGs: COG0144 tRNA and rRNA cytosine-C5-methylase; InterPro IPR006027:IPR001678; KEGG: apv:Apar_0866 NusB/RsmB/TIM44; PFAM: NusB/RsmB/TIM44; Fmu (Sun) domain protein; SPTR: Putative uncharacterized protein; IMG reference gene:2503575875; PFAM: NOL1/NOP2/sun family; NusB family; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Replication restart DNA helicase PriA; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.665 |
AEB07872.1 | AEB07876.1 | Corgl_1777 | Corgl_1781 | Primary replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. Belongs to the helicase family. DnaB subfamily. | Single-strand binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. | 0.786 |
AEB07872.1 | pheT | Corgl_1777 | Corgl_1487 | Primary replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. Belongs to the helicase family. DnaB subfamily. | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR004532:IPR002547:IPR005121:IPR005146:IPR 005147; KEGG: apv:Apar_1054 phenylalanyl-tRNA synthetase, beta subunit; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: Putative uncharacterized protein; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; IMG reference gene:2503576306; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta su [...] | 0.547 |
AEB07872.1 | priA | Corgl_1777 | Corgl_1079 | Primary replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. Belongs to the helicase family. DnaB subfamily. | Replication restart DNA helicase PriA; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.641 |
AEB07876.1 | AEB07872.1 | Corgl_1781 | Corgl_1777 | Single-strand binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. | Primary replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. Belongs to the helicase family. DnaB subfamily. | 0.786 |
AEB07876.1 | pheT | Corgl_1781 | Corgl_1487 | Single-strand binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR004532:IPR002547:IPR005121:IPR005146:IPR 005147; KEGG: apv:Apar_1054 phenylalanyl-tRNA synthetase, beta subunit; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: Putative uncharacterized protein; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; IMG reference gene:2503576306; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta su [...] | 0.463 |
AEB07876.1 | priA | Corgl_1781 | Corgl_1079 | Single-strand binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. | Replication restart DNA helicase PriA; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.811 |
def | AEB07184.1 | Corgl_1078 | Corgl_1076 | Peptide deformylase; 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. | NusB/RsmB/TIM44; COGs: COG0144 tRNA and rRNA cytosine-C5-methylase; InterPro IPR006027:IPR001678; KEGG: apv:Apar_0866 NusB/RsmB/TIM44; PFAM: NusB/RsmB/TIM44; Fmu (Sun) domain protein; SPTR: Putative uncharacterized protein; IMG reference gene:2503575875; PFAM: NOL1/NOP2/sun family; NusB family; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.855 |
def | fmt | Corgl_1078 | Corgl_1077 | Peptide deformylase; 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. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.966 |
def | metK | Corgl_1078 | Corgl_1080 | Peptide deformylase; 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. | Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | 0.623 |
def | priA | Corgl_1078 | Corgl_1079 | Peptide deformylase; 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. | Replication restart DNA helicase PriA; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.615 |
fmt | AEB07184.1 | Corgl_1077 | Corgl_1076 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | NusB/RsmB/TIM44; COGs: COG0144 tRNA and rRNA cytosine-C5-methylase; InterPro IPR006027:IPR001678; KEGG: apv:Apar_0866 NusB/RsmB/TIM44; PFAM: NusB/RsmB/TIM44; Fmu (Sun) domain protein; SPTR: Putative uncharacterized protein; IMG reference gene:2503575875; PFAM: NOL1/NOP2/sun family; NusB family; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.927 |
fmt | def | Corgl_1077 | Corgl_1078 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Peptide deformylase; 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. | 0.966 |