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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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ribARiboflavin biosynthesis protein RibA; Catalyzes the conversion of GTP to 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate; Belongs to the GTP cyclohydrolase II family. In the N-terminal section; belongs to the DHBP synthase family. (406 aa)    
Predicted Functional Partners:
ribE
Riboflavin synthase alpha chain; PMID: 9022701 best DB hits: BLAST: embl:CAC17561.1; (AL450443) putative riboflavin synthase; E=1e-44 swissprot:P71680; RISA_MYCTU RIBOFLAVIN SYNTHASE ALPHA CHAIN; E=9e-38 pir:E82098; riboflavin synthase, alpha chain VC2270 [imported] -; E=6e-37 COG: Rv1412; COG0307 Riboflavin synthase alpha chain; E=9e-39 PFAM: PF00677; Lumazine binding domain; E=4.2e-19.
 
 0.999
ribH
6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
 
 
 0.999
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.
 0.999
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.
 
 
 0.947
moaA
Molybdopterin cofactor synthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate.
    
 0.903
rspB
Ribosomal protein S2; PMID: 6806564 PMID: 6272196 PMID: 7023985 PMID: 10094780 best DB hits: BLAST: pir:F75386; ribosomal protein S2 - Deinococcus radiodurans (strain; E=9e-52 swissprot:Q9WZM1; RS2_THEMA 30S RIBOSOMAL PROTEIN S2 -----; E=2e-51 pdb:1FJF; B Chain B, Structure Of The Thermus Thermophilus 30s; E=2e-50 COG: DR1513; COG0052 Ribosomal protein S2; E=8e-53 PFAM: PF00318; Ribosomal protein S2; E=1.2e-82; Belongs to the universal ribosomal protein uS2 family.
   
  
 0.898
ndk
Nucleoside diphosphate kinase (NDK); Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family.
  
 0.872
RB1597
Conserved hypothetical protein; PMID: 8037924 best DB hits: BLAST: swissprot:P30176; YBIA_ECOLI HYPOTHETICAL 18.7 KDA PROTEIN IN; E=3e-34 pir:A75416; conserved hypothetical protein - Deinococcus radiodurans; E=4e-05 pir:B83074; conserved hypothetical protein PA4580 [imported] -; E=1e-04 COG: ybiA; COG3236 Uncharacterized BCR; E=3e-35.
 
    
 0.856
cyaA-2
Adenylate cyclase 1; PMID: 9523018 best DB hits: BLAST: pir:C71320; probable adenylate cyclase - syphilis spirochete -----; E=8e-40 pir:F70563; probable transmembrane protein - Mycobacterium; E=2e-35 embl:CAA18817.1; (AL023093) putative membrane protein; E=4e-35 COG: TP0485; COG2114 Adenylate cyclase, family 3 (some proteins contain; E=8e-41 slr1991_2; COG2114 Adenylate cyclase, family 3 (some proteins; E=9e-14 PA3217; COG2114 Adenylate cyclase, family 3 (some proteins contain; E=4e-12 PFAM: PF00672; HAMP domain; E=8.7e-11 PF00211; Adenylate and Guanylate cyclase; E=7e-26.
    
  0.838
RB2978
Probable MutT-family protein; PMID: 8843436 best DB hits: BLAST: embl:CAC16440.1; (AL450165) putative MutT-family protein; E=2e-05 swissprot:P56380; AP4A_MOUSE BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE; E=5e-05 pir:F75532; MutTnudix family protein - Deinococcus radiodurans; E=3e-04 COG: DR0329; COG0494 NTP pyrophosphohydrolases including oxidative damage; E=3e-05 DR0004; COG0494 NTP pyrophosphohydrolases including oxidative; E=4e-05 DR0550; COG0494 NTP pyrophosphohydrolases including oxidative damage; E=1e-04 PFAM: PF00293; MutT-like domain; E=4.8e-17.
   
 0.830
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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