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RHOCA:RNFA

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Species (Taxon ID) Rhodobacter capsulatus (Rhodopseudomonas capsulata). (1061)
Gene Name(s) rnfA (ECO:0000255 with HAMAP-Rule:MF_00459)
Protein Name(s) Electron transport complex subunit RnfA (ECO:0000255 with HAMAP-Rule:MF_00459)

Nitrogen fixation protein RnfA (ECO:0000255 with HAMAP-Rule:MF_00459)

External Links
UniProt P0CZ13
EMBL X72888
Y11913
PIR S39895
HOGENOM HOG000279324
GO GO:0016021
GO:0042717
GO:0022900
GO:0009399
HAMAP MF_00459
InterPro IPR003667
IPR011293
Pfam PF02508
PIRSF PIRSF006102
TIGRFAMs TIGR01943

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0016021

integral to membrane

PMID:9154934[1]

ECO:0000314

C

Figure 1B illustrates the PhoA activity of diazotrophically grown cells split into chromatophore and soluble fractions. The high PhoA activity in chromatophore fragments and low PhoA activity in soluble fragments suggests that RnfA has alternating hydrophobic and hydrophilic regions; thus, RnfA is a transmembrane protein.

complete
CACAO 8538

GO:0070111

organellar chromatophore

PMID:9154934[1]

ECO:0000314

C

Figure 1B illustrates a high amount of alkaline phosphatase activity in the chromatophore fraction of R. capsulatus cells; therefore, a high amount of RnfA activity.

complete
CACAO 8693

part_of

GO:0016021

integral component of membrane

PMID:9154934[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0070111

organellar chromatophore

PMID:9154934[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003667

C

Seeded From UniProt

complete

involved_in

GO:0022900

electron transport chain

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011293

P

Seeded From UniProt

complete

involved_in

GO:0009399

nitrogen fixation

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000062678

P

Seeded From UniProt

complete

involved_in

GO:0022900

electron transport chain

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000062678

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000062678

P

Seeded From UniProt

complete

involved_in

GO:0009399

nitrogen fixation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0535

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0249

P

Seeded From UniProt

complete

part_of

GO:0042717

plasma membrane-derived chromatophore membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0042

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Kumagai, H et al. (1997) Membrane localization, topology, and mutual stabilization of the rnfABC gene products in Rhodobacter capsulatus and implications for a new family of energy-coupling NADH oxidoreductases. Biochemistry 36 5509-21 PubMed GONUTS page