STRINGSTRING
ilvD ilvD ilvE ilvE panD panD acpS acpS dfp dfp coaD coaD ilvC ilvC ilvH ilvH ilvI ilvI coaX coaX panB panB panC panC coaE coaE
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
ilvDDihydroxy-acid dehydratase; Original (2000) note: Cj0013, ilvD, probable dihydroxy-acid dehydratase, len: 558 aa; highly similar to e.g. ILVD_ECOLI dihydroxy-acid dehydratase (EC 4.2.1.9) (605 aa), fasta scores; opt: 1091 z-score: 2191.4 E(): 0,46.9% identity in 597 aa overlap. 32.0% identity to HP1100 (6-phosphogluconate dehydratase). Contains PS00886 and PS00887 Dihydroxy-acid and 6-phosphogluconate dehydratases signatures 1 and 2, and Pfam match to entry PF00920 ILVD_EDD, Dehydratase family, score 784.10, E-value 5.5e-232; Updated (2006) note: Characterised within Escherichia coli w [...] (558 aa)
ilvEBranched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (304 aa)
panDAspartate 1-decarboxylase precursor; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. (126 aa)
acpSHolo-[acyl-carrier protein] synthase; Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein; Belongs to the P-Pant transferase superfamily. AcpS family. (115 aa)
dfpPhosphopantothenoylcysteine 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. (384 aa)
coaDPhosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. (158 aa)
ilvCKetol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. (340 aa)
ilvHOriginal (2000) note: Cj0575, ilvH, probable acetolactate synthase small subunit, len 145 aa; similar to many e.g. ILVH_ECOLI acetolactate synthase isozyme III small subunit (EC 4.1.3.18) (163 aa), fasta scores; opt: 341 z-score: 523.3 E(): 7.5e-22, 40.0% identity in 155 aa overlap. No Hp match; Updated (2006) note: Pfam domain PF01842 ACT domain identified within CDS. Further support given to product function. Characterised within Escherichia coli with acceptable identity score. Putative not added to product function. EC number updated. Functional classification -Amino acid biosynthes [...] (154 aa)
ilvIOriginal (2000) note: Cj0574, ilvI, probable acetolactate synthase large subunit, len: 566 aa; highly similar to many e.g.ILVI_ECOLI acetolactate synthase isozyme III large subunit (EC 4.1.3.18) (574 aa), fasta scores; opt: 1713 z-score: 2101.4 E(): 0, 46.5% identity in 572 aa overlap (also 43.4% identity to ILVB_ECOLI, and 42.0% identity to ILVG_ECOLI). No Hp match. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes, score 769.00, E-value 6.9e-238; Updated (2006) note: Characterised within Escherichia coli with acceptable identity score. Putative not adde [...] (566 aa)
coaXPutative transcriptional activator; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis; Belongs to the type III pantothenate kinase family. (209 aa)
panB3-methyl-2-oxobutanoate hydroxymethyltransferase; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate; Belongs to the PanB family. (274 aa)
panCPantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. (282 aa)
coaEPutative dephospho-CoA kinase; Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A; Belongs to the CoaE family. (201 aa)
Your Current Organism:
Campylobacter jejuni NCTC 11168
NCBI taxonomy Id: 192222
Other names: C. jejuni subsp. jejuni NCTC 11168 = ATCC 700819, Campylobacter jejuni subsp. jejuni ATCC 700819, Campylobacter jejuni subsp. jejuni ATCC 700819 = NCTC 11168, Campylobacter jejuni subsp. jejuni NCTC 11168, Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
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