STRINGSTRING
HemN_1 HemN_1 FumB FumB bioB bioB KamA KamA nth nth leuC leuC SdaA SdaA sdhB sdhB OOS07450.1 OOS07450.1 RnfB RnfB queG queG miaB miaB MutY MutY ispH ispH queE queE AcnB AcnB rlmN rlmN ispG ispG rlmD rlmD nfuA nfuA OOS05376.1 OOS05376.1 lipA lipA nuoB nuoB NuoF NuoF NuoG NuoG nuoI nuoI rimO rimO CitB CitB FdxA FdxA Sir Sir ttcA ttcA
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:
HemN_1YggW family oxidoreductase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (392 aa)
FumBFumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (508 aa)
bioBBiotin synthase BioB; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family. (346 aa)
KamAEF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. (352 aa)
nthEndonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. (214 aa)
leuC3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (473 aa)
SdaAL-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. (470 aa)
sdhBPart of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (236 aa)
OOS07450.1Phosphoadenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite. (254 aa)
RnfBIron-sulfur protein; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily. (286 aa)
queGtRNA epoxyqueuosine(34) reductase QueG; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr); Belongs to the QueG family. (384 aa)
miaBtRNA (N6-isopentenyl adenosine(37)-C2)-methylthiotransferase MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. (490 aa)
MutYA/G-specific adenine glycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. (388 aa)
ispH4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. Belongs to the IspH family. (313 aa)
queE7-carboxy-7-deazaguanine synthase QueE; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. (240 aa)
AcnBBifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aconitase/IPM isomerase family. (874 aa)
rlmN23S rRNA (adenine(2503)-C(2))-methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. (402 aa)
ispG4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family. (371 aa)
rlmD23S rRNA (uracil(1939)-C(5))-methyltransferase; Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmD subfamily. (494 aa)
nfuAFe/S biogenesis protein NfuA; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. (207 aa)
OOS05376.1Electron transfer flavoprotein-ubiquinone oxidoreductase; Accepts electrons from ETF and reduces ubiquinone. (553 aa)
lipALipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. (354 aa)
nuoBHypothetical protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (223 aa)
NuoFNADH oxidoreductase (quinone) subunit F; Derived by automated computational analysis using gene prediction method: Protein Homology. (478 aa)
NuoGNADH-quinone oxidoreductase subunit G; Catalyzes the transfer of electrons from NADH to quinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (1022 aa)
nuoINADH-quinone oxidoreductase subunit I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (182 aa)
rimORibosomal protein S12 methylthiotransferase; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (500 aa)
CitBFe/S-dependent 2-methylisocitrate dehydratase AcnD; Derived by automated computational analysis using gene prediction method: Protein Homology. (858 aa)
FdxAFerredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (107 aa)
SirSulfite reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (558 aa)
ttcAtRNA 2-thiocytidine(32) synthetase TtcA; Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. (366 aa)
Your Current Organism:
Moraxella cuniculi
NCBI taxonomy Id: 34061
Other names: ATCC 14688, CCUG 2154, DSM 21768, LMG 8382, LMG:8382, M. cuniculi, NCTC 10297, Neisseria cuniculi, strain K 19
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.