RNFD_RHOCA
ID RNFD_RHOCA Reviewed; 358 AA.
AC Q52715; Q52713;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305};
DE AltName: Full=Nitrogen fixation protein RnfD {ECO:0000305};
DE AltName: Full=Rnf electron transport complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305};
GN Name=rnfD {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000303|PubMed:8264535};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND GENE NAME.
RC STRAIN=B10S;
RX PubMed=8264535; DOI=10.1007/bf00279903;
RA Schmehl M., Jahn A., Meyer zu Vilsendorf A., Hennecke S., Masepohl B.,
RA Schuppler M., Marxer M., Oelze J., Klipp W.;
RT "Identification of a new class of nitrogen fixation genes in Rhodobacter
RT capsulatus: a putative membrane complex involved in electron transport to
RT nitrogenase.";
RL Mol. Gen. Genet. 241:602-615(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=9492268; DOI=10.1046/j.1432-1327.1998.2510054.x;
RA Jouanneau Y., Jeong H.-S., Hugo N., Meyer C., Willison J.C.;
RT "Overexpression in Escherichia coli of the rnf genes from Rhodobacter
RT capsulatus -- characterization of two membrane-bound iron-sulfur
RT proteins.";
RL Eur. J. Biochem. 251:54-64(1998).
CC -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC transfer with translocation of ions across the membrane (By
CC similarity). Required for nitrogen fixation. Involved in electron
CC transfer to nitrogenase (PubMed:8264535). {ECO:0000255|HAMAP-
CC Rule:MF_00462, ECO:0000269|PubMed:8264535}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00462};
CC -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00462,
CC ECO:0000305|PubMed:9492268}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00462}.
CC -!- INDUCTION: Expression is reduced under iron-limiting conditions.
CC {ECO:0000269|PubMed:9492268}.
CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|HAMAP-
CC Rule:MF_00462}.
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DR EMBL; X72888; CAA51398.1; -; Genomic_DNA.
DR EMBL; Y11913; CAA72664.1; -; Genomic_DNA.
DR PIR; S39892; S39892.
DR AlphaFoldDB; Q52715; -.
DR SMR; Q52715; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-UniRule.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR HAMAP; MF_00462; RsxD_RnfD; 1.
DR InterPro; IPR004338; NqrB/RnfD.
DR InterPro; IPR011303; RnfD.
DR PANTHER; PTHR30578; PTHR30578; 1.
DR Pfam; PF03116; NQR2_RnfD_RnfE; 1.
DR TIGRFAMs; TIGR01946; rnfD; 1.
PE 1: Evidence at protein level;
KW Electron transport; Flavoprotein; FMN; Membrane; Nitrogen fixation;
KW Phosphoprotein; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..358
FT /note="Ion-translocating oxidoreductase complex subunit D"
FT /id="PRO_0000074460"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 68..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT CONFLICT 27
FT /note="L -> V (in Ref. 1; CAA51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="D -> H (in Ref. 1; CAA51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="A -> P (in Ref. 1; CAA51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..157
FT /note="GPSFLHGL -> A (in Ref. 1; CAA51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 161..191
FT /note="FLGSQEFDAVSSASTLSHIKSQISAGATMGE -> LFGSHVPAQLAHQEQIS
FT RATWQ (in Ref. 1; CAA51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 195..225
FT /note="TLADLESRLLGFVPGSLGETSTVLLALGGLL -> SWRIWKAVFWASCPAAW
FT RDLDRASGTGRGFW (in Ref. 1; CAA51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 239..240
FT /note="AV -> GL (in Ref. 1; CAA51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 245..251
FT /note="VTLSAIC -> SRCRRSV (in Ref. 1; CAA51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="R -> P (in Ref. 1; CAA51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 314..358
FT /note="GRGLCGALDELGHAPDRNLHPAADLRTVPHRQAACAAKPAKGAQK -> AWP
FT LRCS (in Ref. 1; CAA51398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 37817 MW; 2E441CE2DE7AE041 CRC64;
MHMPVAGPHT HTLFTVSRTM LTVVAALTPA TLFGLWEFGW PAIFLFLTTV VSAWVFEVAC
LKIADKPIRP FATDGSAILS GWLVAMTLPP YAPWWVGVIG SFIAIVIAKH LFGGLGQNLF
NPAMVARAML VVALPVQMTT WIAPVGLLEG PSFLHGLSIT FLGSQEFDAV SSASTLSHIK
SQISAGATMG EILPTLADLE SRLLGFVPGS LGETSTVLLA LGGLLLLVTR IITPTIPLAV
LGTLVTLSAI CSFLAPDRFA PPILHLTSGS TMLCAFFIAT DYVTSPVTTA GKWVYGIGIG
TLVFVIPLRR LPRGRGLCGA LDELGHAPDR NLHPAADLRT VPHRQAACAA KPAKGAQK
