sync_2339 protein (Synechococcus sp. CC9311)

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Score

sync_2339

Alpha/beta hydrolase family protein. (241 aa)

Predicted Functional Partners:

bioF

0.979

sync_0156

0.906

sync_0258

0.900

ndhH

0.889

ndhJ

0.868

ndhK

0.847

ndhA

0.836

ndhC

0.827

bioD

0.820

sync_2340

0.800

Your Current Organism:

Synechococcus sp. CC9311

NCBI taxonomy Id: 64471
Other names: S. sp. CC9311

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
bioD	bioF	sync_2341	sync_2338	Dethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring.	8-amino-7-oxononanoate synthase; Identified by match to protein family HMM PF00155; match to protein family HMM PF00202; match to protein family HMM TIGR00858.	0.974
bioD	sync_0156	sync_2341	sync_0156	Dethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring.	Polyketide synthase, putative; Identified by match to protein family HMM PF00106; match to protein family HMM PF00107; match to protein family HMM PF00109; match to protein family HMM PF00550; match to protein family HMM PF01073; match to protein family HMM PF01370; match to protein family HMM PF02801; match to protein family HMM PF07993; match to protein family HMM TIGR01746.	0.892
bioD	sync_2339	sync_2341	sync_2339	Dethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring.	Alpha/beta hydrolase family protein.	0.820
bioD	sync_2340	sync_2341	sync_2340	Dethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring.	SAM dependent methyltransferase.	0.873
bioF	bioD	sync_2338	sync_2341	8-amino-7-oxononanoate synthase; Identified by match to protein family HMM PF00155; match to protein family HMM PF00202; match to protein family HMM TIGR00858.	Dethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring.	0.974
bioF	sync_0156	sync_2338	sync_0156	8-amino-7-oxononanoate synthase; Identified by match to protein family HMM PF00155; match to protein family HMM PF00202; match to protein family HMM TIGR00858.	Polyketide synthase, putative; Identified by match to protein family HMM PF00106; match to protein family HMM PF00107; match to protein family HMM PF00109; match to protein family HMM PF00550; match to protein family HMM PF01073; match to protein family HMM PF01370; match to protein family HMM PF02801; match to protein family HMM PF07993; match to protein family HMM TIGR01746.	0.807
bioF	sync_2339	sync_2338	sync_2339	8-amino-7-oxononanoate synthase; Identified by match to protein family HMM PF00155; match to protein family HMM PF00202; match to protein family HMM TIGR00858.	Alpha/beta hydrolase family protein.	0.979
bioF	sync_2340	sync_2338	sync_2340	8-amino-7-oxononanoate synthase; Identified by match to protein family HMM PF00155; match to protein family HMM PF00202; match to protein family HMM TIGR00858.	SAM dependent methyltransferase.	0.856
ndhA	ndhC	sync_2625	sync_0242	NADH dehydrogenase I chain 1 (or H); 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.	NADH dehydrogenase I chain 3 (or A); 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.	0.999
ndhA	ndhH	sync_2625	sync_2648	NADH dehydrogenase I chain 1 (or H); 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.	NADH dehydrogenase I chain 7 (or D); 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.	0.999
ndhA	ndhJ	sync_2625	sync_0244	NADH dehydrogenase I chain 1 (or H); 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.	NADH dehydrogenase I chain J; 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.	0.999
ndhA	ndhK	sync_2625	sync_0243	NADH dehydrogenase I chain 1 (or H); 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.	NADH dehydrogenase I chain B or NdhK; 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.	0.999
ndhA	sync_0156	sync_2625	sync_0156	NADH dehydrogenase I chain 1 (or H); 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.	Polyketide synthase, putative; Identified by match to protein family HMM PF00106; match to protein family HMM PF00107; match to protein family HMM PF00109; match to protein family HMM PF00550; match to protein family HMM PF01073; match to protein family HMM PF01370; match to protein family HMM PF02801; match to protein family HMM PF07993; match to protein family HMM TIGR01746.	0.998
ndhA	sync_2339	sync_2625	sync_2339	NADH dehydrogenase I chain 1 (or H); 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.	Alpha/beta hydrolase family protein.	0.836
ndhC	ndhA	sync_0242	sync_2625	NADH dehydrogenase I chain 3 (or A); 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.	NADH dehydrogenase I chain 1 (or H); 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.	0.999
ndhC	ndhH	sync_0242	sync_2648	NADH dehydrogenase I chain 3 (or A); 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.	NADH dehydrogenase I chain 7 (or D); 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.	0.999
ndhC	ndhJ	sync_0242	sync_0244	NADH dehydrogenase I chain 3 (or A); 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.	NADH dehydrogenase I chain J; 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.	0.999
ndhC	ndhK	sync_0242	sync_0243	NADH dehydrogenase I chain 3 (or A); 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.	NADH dehydrogenase I chain B or NdhK; 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.	0.999
ndhC	sync_0156	sync_0242	sync_0156	NADH dehydrogenase I chain 3 (or A); 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.	Polyketide synthase, putative; Identified by match to protein family HMM PF00106; match to protein family HMM PF00107; match to protein family HMM PF00109; match to protein family HMM PF00550; match to protein family HMM PF01073; match to protein family HMM PF01370; match to protein family HMM PF02801; match to protein family HMM PF07993; match to protein family HMM TIGR01746.	0.999
ndhC	sync_2339	sync_0242	sync_2339	NADH dehydrogenase I chain 3 (or A); 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.	Alpha/beta hydrolase family protein.	0.827