FDXN_RHOCA
ID FDXN_RHOCA Reviewed; 65 AA.
AC P0CY90; P16021;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Ferredoxin-1;
DE AltName: Full=Ferredoxin I;
DE Short=FdI;
GN Name=fdxN;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=2681157; DOI=10.1128/jb.171.11.6218-6226.1989;
RA Schatt E., Jouanneau Y., Vignais P.M.;
RT "Molecular cloning and sequence analysis of the structural gene of
RT ferredoxin I from the photosynthetic bacterium Rhodobacter capsulatus.";
RL J. Bacteriol. 171:6218-6226(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=1847145; DOI=10.1016/s0021-9258(18)49987-5;
RA Grabau C., Schatt E., Jouanneau Y., Vignais P.M.;
RT "A new [2Fe-2S] ferredoxin from Rhodobacter capsulatus. Coexpression with a
RT 2[4Fe-4S] ferredoxin in Escherichia coli.";
RL J. Biol. Chem. 266:3294-3299(1991).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. This ferredoxin probably
CC participates in nitrogen fixation.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000305};
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DR EMBL; M31073; AAA26111.1; -; Genomic_DNA.
DR EMBL; X72888; CAA51404.1; -; Genomic_DNA.
DR EMBL; M59855; AAA26110.1; -; Genomic_DNA.
DR PIR; A33498; FERF1C.
DR RefSeq; WP_013068980.1; NZ_VIBE01000016.1.
DR AlphaFoldDB; P0CY90; -.
DR SMR; P0CY90; -.
DR GeneID; 31492064; -.
DR OMA; CGDCKPV; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF00037; Fer4; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..65
FT /note="Ferredoxin-1"
FT /id="PRO_0000159170"
FT DOMAIN 2..30
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 10
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 65 AA; 6864 MW; 2DF359B3BC3E481E CRC64;
MAMKIDPELC TSCGDCEPVC PTNAIAPKKG VYVINADTCT ECEGEHDLPQ CVNACMTDNC
INPAA