STRINGSTRING
queE queE rlmN rlmN ACL42654.1 ACL42654.1 rimO rimO ACL42783.1 ACL42783.1 cofG cofG moaA moaA leuC leuC ACL43778.1 ACL43778.1 ACL43886.1 ACL43886.1 bioB bioB queG queG ndhI ndhI psaC psaC ACL44406.1 ACL44406.1 ACL44408.1 ACL44408.1 ispH ispH ACL44719.1 ACL44719.1 nifH nifH ACL44861.1 ACL44861.1 ACL45024.1 ACL45024.1 psaB psaB ACL45534.1 ACL45534.1 thiC thiC cofH cofH ACL45713.1 ACL45713.1 ndhK1 ndhK1 ACL45860.1 ACL45860.1 ispG ispG chlB chlB miaB miaB ACL46185.1 ACL46185.1 chlL chlL chlN chlN ACL46365.1 ACL46365.1 ACL46366.1 ACL46366.1 ACL46476.1 ACL46476.1 ACL46494.1 ACL46494.1 ACL46679.1 ACL46679.1 lipA lipA ACL46874.1 ACL46874.1 psaB-2 psaB-2 psaA psaA ndhK2 ndhK2 lipA-2 lipA-2 ACL47083.1 ACL47083.1 ACL47084.1 ACL47084.1 ACL47109.1 ACL47109.1 nadA nadA
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:
queERadical SAM domain protein; 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. (268 aa)
rlmNRadical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family. (367 aa)
ACL42654.1TIGRFAM: phage SPO1 DNA polymerase-related protein; PFAM: Uracil-DNA glycosylase superfamily; KEGG: amr:AM1_4059 DNA polymerase bacteriophage-type, putative. (238 aa)
rimOMiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (450 aa)
ACL42783.1TIGRFAM: RNA methyltransferase, TrmA family; PFAM: deoxyribonuclease/rho motif-related TRAM; (Uracil-5)-methyltransferase; KEGG: npu:Npun_R0877 RNA methyltransferase; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. (457 aa)
cofGRadical SAM domain protein; Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8- hydroxy-5-deazariboflavin (FO) from 5-amino-5-(4-hydroxybenzyl)-6-(D- ribitylimino)-5,6-dihydrouracil. (321 aa)
moaAMolybdenum cofactor biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (329 aa)
leuC3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (468 aa)
ACL43778.1PP-loop domain protein; 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. Belongs to the TtcA family. (274 aa)
ACL43886.1Oxygen-independent coproporphyrinogen III oxidase; 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. (405 aa)
bioBBiotin synthase; 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. (388 aa)
queGIron-sulfur cluster binding protein; 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. (312 aa)
ndhINADH-plastoquinone oxidoreductase, I subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family. (193 aa)
psaCPhotosystem I iron-sulfur protein PsaC; Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized a [...] (81 aa)
ACL44406.1PFAM: Radical SAM domain protein; KEGG: ava:Ava_4632 radical SAM family protein. (267 aa)
ACL44408.1Anaerobic ribonucleoside-triphosphate reductase activating protein; Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine. (208 aa)
ispHHydroxymethylbutenyl pyrophosphate 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. (405 aa)
ACL44719.1TIGRFAM: nitrogenase cofactor biosynthesis protein NifB; PFAM: Dinitrogenase iron-molybdenum cofactor biosynthesis protein; Radical SAM domain protein; KEGG: npu:Npun_R0420 nitrogenase cofactor biosynthesis protein NifB. (495 aa)
nifHNitrogenase iron protein; The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein. (298 aa)
ACL44861.1Ferredoxin thioredoxin reductase beta chain; Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin. (119 aa)
ACL45024.1PFAM: Heme NO binding domain protein; KEGG: ana:alr2278 similar to soluble guanylyl cyclase beta subunit. (189 aa)
psaBPhotosystem I core protein PsaB; PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6; Belongs to the PsaA/PsaB family. (746 aa)
ACL45534.1TIGRFAM: aconitate hydratase 2; PFAM: aconitate hydratase domain protein; Aconitase B, N-terminal; KEGG: amr:AM1_1630 bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Belongs to the aconitase/IPM isomerase family. (869 aa)
thiCThiamine biosynthesis protein ThiC; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Belongs to the ThiC family. (458 aa)
cofHRadical SAM domain protein; Catalyzes the radical-mediated synthesis of 5-amino-5-(4- hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D- ribitylamino)uracil and L-tyrosine. (381 aa)
ACL45713.1PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; protein of unknown function DUF224 cysteine-rich region domain protein; KEGG: npu:Npun_F0763 hypothetical protein. (445 aa)
ndhK1NADH-quinone oxidoreductase, B subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. (238 aa)
ACL45860.1Hypothetical protein; KEGG: cyt:cce_0556 4Fe-4S ferredoxin. (84 aa)
ispG1-hydroxy-2-methyl-2-(E)-butenyl 4-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. (407 aa)
chlBLight-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. (507 aa)
miaBRNA modification enzyme, MiaB family; 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. (446 aa)
ACL46185.1TIGRFAM: sulfite reductase, ferredoxin dependent; PFAM: nitrite/sulfite reductase hemoprotein beta-component ferrodoxin domain protein; nitrite and sulphite reductase 4Fe-4S region; KEGG: ava:Ava_5043 sulfite reductase subunit beta. (660 aa)
chlLLight-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. (286 aa)
chlNLight-independent protochlorophyllide reductase, N subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. (468 aa)
ACL46365.1NADH dehydrogenase (ubiquinone); PFAM: ferredoxin; 4Fe-4S ferredoxin iron-sulfur binding domain protein; 4Fe-4S ferredoxin, iron-sulphur binding, conserved site; KEGG: syn:sll1223 diaphorase subunit of the bidirectional hydrogenase. (238 aa)
ACL46366.1PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; KEGG: mar:MAE_01090 bidirectional hydrogenase diaphorase subunit. (543 aa)
ACL46476.14Fe-4S ferredoxin iron-sulfur binding domain protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (75 aa)
ACL46494.1TIGRFAM: mutator MutT protein; A/G-specific adenine glycosylase; PFAM: NUDIX hydrolase; HhH-GPD family protein; A/G-specific adenine glycosylase MutY; KEGG: cyt:cce_3596 mutator protein MutT. (386 aa)
ACL46679.1Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin. (1193 aa)
lipALipoic acid synthetase; 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. (307 aa)
ACL46874.1PFAM: molybdopterin oxidoreductase; molydopterin dinucleotide-binding region; molybdopterin oxidoreductase Fe4S4 region; KEGG: npu:Npun_R1526 molybdopterin oxidoreductase NarB; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. (724 aa)
psaB-2Photosystem I core protein PsaB; PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6; Belongs to the PsaA/PsaB family. (742 aa)
psaAPhotosystem I core protein PsaA; PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6. (756 aa)
ndhK2NADH-quinone oxidoreductase, B subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration (By similarity); Belongs to the complex I 20 kDa subunit family. (259 aa)
lipA-2Lipoic acid synthetase; 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. (306 aa)
ACL47083.1Response regulator receiver protein; KEGG: rrs:RoseRS_0942 magnesium-protoporphyrin IX monomethyl ester anaerobic oxidative cyclase; TIGRFAM: magnesium-protoporphyrin IX monomethyl ester anaerobic oxidative cyclase; PFAM: response regulator receiver; cobalamin B12-binding domain protein; Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB. (675 aa)
ACL47084.1KEGG: ava:Ava_4393 coproporphyrinogen III oxidase; TIGRFAM: oxygen-independent coproporphyrinogen III oxidase; PFAM: Radical SAM domain protein; HemN domain protein; SMART: Elongator protein 3/MiaB/NifB; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (465 aa)
ACL47109.1TIGRFAM: ferredoxin III, nif-specific; PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: ava:Ava_4259 4Fe-4S ferredoxin, iron-sulfur binding. (98 aa)
nadAQuinolinate synthetase complex, A subunit; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. (322 aa)
Your Current Organism:
Cyanothece sp. PCC7425
NCBI taxonomy Id: 395961
Other names: C. sp. PCC 7425, Cyanothece sp. ATCC 29141, Cyanothece sp. PCC 7425, Synechococcus sp. PCC 7425
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.