STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
RB1874Probable 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; PMID: 10360571 best DB hits: BLAST: pir:F72425; 2-amino-4-hydroxy-6- hydroxymethyldihydropteridine; E=7e-12 ddbj:BAB03814.1; (AP001507); E=2e-09 swissprot:P29251; FAS_PNECA FOLIC ACID SYNTHESIS PROTEIN; E=3e-08 COG: TM0041; COG0801 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase; E=7e-13 YNL256w_2; COG0801; E=9e-05 NMB0745; COG0801 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase; E=1e-04 PFAM: PF01288; 7,8-dihydro-6-hydroxymethylpterin-py; E=2.4e-24. (327 aa)    
Predicted Functional Partners:
folP
Dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
 
 
 0.996
folE
GTP cyclohydrolase I; PMID: 1551827 PMID: 95352066 best DB hits: BLAST: swissprot:P19465; GCH1_BACSU GTP CYCLOHYDROLASE I (GTP-CH-I); E=1e-59 ddbj:BAB05365.1; (AP001512) GTP cyclohydrolase I [Bacillus; E=1e-57 swissprot:O06273; GCH1_MYCTU GTP CYCLOHYDROLASE I (GTP-CH-I); E=4e-53 COG: BS_mtrA; COG0302 GTP cyclohydrolase I; E=1e-60 PFAM: PF01227; GTP cyclohydrolase I; E=2.3e-110.
 
  
 0.962
RB5963
Hypothetical protein.
  
  
 0.921
RB1696
Conserved hypothetical protein-putative dihydropteroate synthase; PMID: 8688087 best DB hits: BLAST: swissprot:Q57571; Y107_METJA HYPOTHETICAL PROTEIN MJ0107 -----; E=5e-21 gb:AAB89833.1; (AE001006) dihydropteroate synthase [Archaeoglobus; E=1e-20 pir:H69099; conserved hypothetical protein MTH1741 -; E=1e-16 COG: MJ0107; COG0294 Dihydropteroate synthase; E=5e-22.
  
  
 0.852
folC
PMID: 10360571 best DB hits: BLAST: pir:D72411; folylpolyglutamate synthasedihydrofolate synthase -; E=4e-40 ddbj:BAB06756.1; (AP001517) folyl-polyglutamate synthetase; E=8e-39 swissprot:Q05865; FOLC_BACSU FOLYLPOLYGLUTAMATE SYNTHASE; E=8e-38 COG: TM0166; COG0285 Folylpolyglutamate synthase; E=4e-41 PFAM: PF01225; Mur ligase family, catalytic dom; E=1.6e-13 PF02875; Mur ligase family, glutamate lig; E=0.00031.
 
  
 0.720
ribD
PMID: 9068650 best DB hits: BLAST: pir:T50546; riboflavin bifunctional biosynthesis protein ribG; E=2e-56 swissprot:P50853; RIBD_ACTPL RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBD; E=2e-56 ddbj:BAB05273.1; (AP001512) riboflavin specific; E=9e-52 COG: ribD_1; COG0117 Pyrimidine deaminase; E=1e-28 BH1554_2; COG1985 Pyrimidine reductase, riboflavin biosynthesis; E=6e-21 CPn0871_1; COG0117 Pyrimidine deaminase; E=1e-20 PFAM: PF00383; Cytidine and deoxycytidylate de; E=1.5e-31 PF01872; RibD C-terminal domain; E=4e-33.
 
  
 0.621
RB5134
Xanthosine triphosphate pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
  
  
 0.607
papS
Poly A polymerase; PMID: 10192388 best DB hits: BLAST: pir:E72028; poly A polymerase - Chlamydophila pneumoniae (strains; E=9e-41 pir:B81744; poly(A) polymerase family protein TC0077 [imported] -; E=3e-40 pir:A71481; probable poly A polymerase - Chlamydia trachomatis; E=5e-40 COG: CPn0845; COG0617 tRNA nucleotidyltransferase/poly(A) polymerase; E=9e-42 PFAM: PF01743; Poly A polymerase family; E=2.6e-50; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
  
    0.545
pabB
Para-aminobenzoate synthase component I; PMID: 3057324 best DB hits: BLAST: gb:AAG61067.1; AF322013_186 (AF322013) ID893 [Bradyrhizobium; E=7e-72 swissprot:P12679; PABB_KLEAE PARA-AMINOBENZOATE SYNTHASE COMPONENT; E=4e-59 gb:AAG56801.1; AE005404_4 (AE005404) p-aminobenzoate synthetase,; E=2e-57 COG: pabB; COG0147 Anthranilate/para-aminobenzoate synthases component I; E=4e-58 VC1303; COG0147 Anthranilate/para-aminobenzoate synthases component; E=4e-57 VNG0384G; COG0147 Anthranilate/para-aminobenzoate synthases; E=1e-45 PFAM: PF00425; chorismate binding enzyme; E=2.4e-103.
 
  
 0.512
RB1878
Hypothetical protein.
       0.510
Your Current Organism:
Rhodopirellula baltica
NCBI taxonomy Id: 243090
Other names: Pirellula sp. 1, R. baltica SH 1, Rhodopirellula baltica SH 1, Rhodopirellula baltica str. SH 1, Rhodopirellula baltica strain SH 1
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