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paoD paoD paoC paoC paoB paoB paoA paoA preA preA rihB rihB xdhA xdhA xdhB xdhB xdhC xdhC ygeW ygeW ygeX ygeX ygeY ygeY hyuA hyuA yqeB yqeB yqeC yqeC mocA mocA ygfK ygfK ssnA ssnA ygfM ygfM xdhD xdhD guaD guaD
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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:
paoDMolybdenum cofactor insertion chaperone PaoD; Chaperone required for the production of an active PaoABC aldehyde oxidoreductase. Stabilizes the PaoC subunit and is required for the insertion of the molybdenum cofactor into this subunit. Binds molybdenum cofactor. Binds the molybdopterin cytosine dinucleotide (MCD) form of the cofactor after its formation by the molybdenum cofactor cytidylyltransferase MocA. (318 aa)
paoCPaoABC aldehyde oxidoreductase, Moco-containing subunit; Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. It might play a role in the detoxification of aldehydes to avoid cell damage. Belongs to the xanthine dehydrogenase family. (732 aa)
paoBPaoABC aldehyde oxidoreductase, FAD-containing subunit; Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. It might play a role in the detoxification of aldehydes to avoid cell damage. (318 aa)
paoAPaoABC aldehyde oxidoreductase, 2Fe-2S subunit; Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. It might play a role in the detoxification of aldehydes to avoid cell damage. (229 aa)
preADihydropyrimidine dehydrogenase, NADH-dependent, subunit C; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT). (411 aa)
rihBRibonucleoside hydrolase 2; Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. Has a clear preference for cytidine over uridine. Strictly specific for ribonucleosides. Has a low but significant activity for the purine nucleoside xanthosine; Belongs to the IUNH family. RihB subfamily. (313 aa)
xdhAXanthine dehydrogenase, molybdenum binding subunit; Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism). Deletion results in increased adenine sensitivity, suggesting that this protein contributes to the conversion of adenine to guanine nucleotides during purine salvage. (752 aa)
xdhBXanthine dehydrogenase, FAD-binding subunit; Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism). (292 aa)
xdhCXanthine dehydrogenase, Fe-S binding subunit; Iron-sulfur subunit of the xanthine dehydrogenase complex. (159 aa)
ygeWPutative carbamoyltransferase; Putative carbamoyltransferase. No activity can be detected with allantoin or 25 other related compounds, including 20 naturally occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L- ornithine, oxamate, beta-alanine and putrescine. (396 aa)
ygeX2,3-diaminopropionate ammonia lyase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta- Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, [...] (398 aa)
ygeYPutative deacetylase. (403 aa)
hyuAD-stereospecific phenylhydantoinase; Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'- position. Has no activity on dihydropyrimidines. The physiological function is unknown; Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family. (461 aa)
yqeBXdhC-CoxI family protein with NAD(P)-binding Rossman fold; Putative synthases. (541 aa)
yqeCPutative selenium-dependent hydroxylase accessory protein. (256 aa)
mocACTP:molybdopterin cytidylyltransferase; Transfers a CMP moiety from CTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor. Is specific for CTP; other nucleotides such as ATP and GTP cannot be utilized. Is also able to convert MPT to MCD in the absence of molybdate, however, with only one catalytic turnover. (192 aa)
ygfKPutative Fe-S subunit oxidoreductase subunit; Could be an iron-sulfur flavoprotein with NADPH:O(2) oxidoreductase activity. (1032 aa)
ssnAPutative chlorohydrolase/aminohydrolase; Protein involved in cell cycle. (442 aa)
ygfMPutative oxidoreductase. (259 aa)
xdhDPutative hypoxanthine oxidase, molybdopterin-binding/Fe-S binding; Probably has no xanthine dehydrogenase activity; however deletion results in increased adenine sensitivity, suggesting that this protein contributes to the conversion of adenine to guanine nucleotides during purine salvage. (956 aa)
guaDGuanine deaminase; Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia; Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family. (439 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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