STRINGSTRING
speD speD speE speE AFQ42287.1 AFQ42287.1 AFQ42378.1 AFQ42378.1 AFQ42379.1 AFQ42379.1 metAA metAA AFQ42507.1 AFQ42507.1 AFQ42558.1 AFQ42558.1 AFQ42623.1 AFQ42623.1 AFQ42644.1 AFQ42644.1 AFQ42825.1 AFQ42825.1 serC serC AFQ42918.1 AFQ42918.1 AFQ42943.1 AFQ42943.1 speH speH AFQ43260.1 AFQ43260.1 AFQ43304.1 AFQ43304.1 AFQ43323.1 AFQ43323.1 AFQ43470.1 AFQ43470.1 AFQ43576.1 AFQ43576.1 ahcY ahcY AFQ44093.1 AFQ44093.1 AFQ44685.1 AFQ44685.1 ilvE ilvE AFQ44706.1 AFQ44706.1 AFQ44987.1 AFQ44987.1 AFQ45186.1 AFQ45186.1 AFQ45425.1 AFQ45425.1 AFQ45487.1 AFQ45487.1 asd asd mtaD mtaD mtnA mtnA AFQ45574.1 AFQ45574.1 AFQ45596.1 AFQ45596.1 AFQ45597.1 AFQ45597.1 metK metK AFQ45877.1 AFQ45877.1
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.
Node Color
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
Others
textmining
co-expression
protein homology
Your Input:
speDS-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily. (270 aa)
speESpermidine synthase; Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine; Belongs to the spermidine/spermine synthase family. (284 aa)
AFQ42287.1PFAM: Serine acetyltransferase, N-terminal; Bacterial transferase hexapeptide (three repeats); TIGRFAM: serine O-acetyltransferase. (248 aa)
AFQ42378.1Hypothetical protein; PFAM: Domain of unknown function DUF39. (398 aa)
AFQ42379.1NADH:ubiquinone oxidoreductase chain I-like protein; PFAM: NIL domain. (133 aa)
metAAHomoserine O-succinyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine; Belongs to the MetA family. (307 aa)
AFQ42507.1OAH/OAS sulfhydrylase; PFAM: Cys/Met metabolism PLP-dependent enzyme; TIGRFAM: OAH/OAS sulfhydrylase. (430 aa)
AFQ42558.1Methionine synthase (B12-dependent); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. (1213 aa)
AFQ42623.1Methionine synthase II (cobalamin-independent); PFAM: Cobalamin-independent synthase, Catalytic domain. (379 aa)
AFQ42644.11-aminocyclopropane-1-carboxylate deaminase; PFAM: Pyridoxal-phosphate dependent enzyme. (331 aa)
AFQ42825.1PFAM: Aminotransferase class I and II. (391 aa)
serCPhosphoserine aminotransferase apoenzyme; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. (360 aa)
AFQ42918.1Phosphoglycerate dehydrogenase-like oxidoreductase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain. (387 aa)
AFQ42943.1Cysteine synthase A; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: cysteine synthase A; cysteine synthases; Belongs to the cysteine synthase/cystathionine beta- synthase family. (306 aa)
speHS-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. (125 aa)
AFQ43260.1DNA-methyltransferase Dcm; PFAM: C-5 cytosine-specific DNA methylase; TIGRFAM: DNA-methyltransferase (dcm); Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family. (380 aa)
AFQ43304.1Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. (492 aa)
AFQ43323.1Cytosine deaminase-like metal-dependent hydrolase; PFAM: Amidohydrolase family. (443 aa)
AFQ43470.1PFAM: Aminotransferase class IV; TIGRFAM: branched-chain amino acid aminotransferase, group II. (363 aa)
AFQ43576.1Putative cobalamin binding protein; PFAM: B12 binding domain; TIGRFAM: methyltransferase cognate corrinoid proteins, Methanosarcina family. (212 aa)
ahcYAdenosylhomocysteinase; May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. (419 aa)
AFQ44093.1Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor activities; PFAM: Aminotransferase class I and II. (393 aa)
AFQ44685.1PFAM: Aminotransferase class I and II. (394 aa)
ilvEBranched chain amino acid aminotransferase apoenzyme; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (291 aa)
AFQ44706.1PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. (430 aa)
AFQ44987.1Aspartokinase; PFAM: Amino acid kinase family; TIGRFAM: aspartate kinase; manually curated. (463 aa)
AFQ45186.1Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: cysteine synthases; cysteine synthase B. (299 aa)
AFQ45425.1Cobalamin-dependent methionine synthase I; PFAM: Homocysteine S-methyltransferase. (433 aa)
AFQ45487.1PFAM: Amino acid kinase family; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase; Belongs to the aspartokinase family. (408 aa)
asdAspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family. (328 aa)
mtaDCytosine deaminase-like metal-dependent hydrolase; Catalyzes the deamination of 5-methylthioadenosine and S- adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L- homocysteine, respectively. Is also able to deaminate adenosine. Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family. (434 aa)
mtnAMethylthioribose-1-phosphate isomerase; Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). (345 aa)
AFQ45574.1Methylthioadenosine phosphorylase; Purine nucleoside phosphorylase which is highly specific for 6-oxopurine nucleosides. Cleaves guanosine or inosine to respective bases and sugar-1-phosphate molecules. Involved in purine salvage. (262 aa)
AFQ45596.1L-serine ammonia-lyase; PFAM: Serine dehydratase alpha chain; TIGRFAM: L-serine dehydratase, iron-sulfur-dependent, alpha subunit. (287 aa)
AFQ45597.1L-serine ammonia-lyase; PFAM: ACT domain; Serine dehydratase beta chain; TIGRFAM: L-serine dehydratase, iron-sulfur-dependent, beta subunit. (222 aa)
metKMethionine 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. (397 aa)
AFQ45877.1PFAM: B12 binding domain; TIGRFAM: methyltransferase cognate corrinoid proteins, Methanosarcina family; methylmalonyl-CoA mutase C-terminal domain. (210 aa)
Your Current Organism:
Desulfosporosinus meridiei
NCBI taxonomy Id: 768704
Other names: D. meridiei DSM 13257, Desulfosporosinus meridiei DSM 13257, Desulfosporosinus meridiei str. DSM 13257, Desulfosporosinus meridiei strain DSM 13257, Desulfosporosinus sp. S10
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