FER3_RHOCA
ID FER3_RHOCA Reviewed; 101 AA.
AC P20624;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ferredoxin-3;
DE AltName: Full=Ferredoxin III;
DE Short=FdIII;
GN Name=fdxB;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2708314; DOI=10.1128/jb.171.5.2591-2598.1989;
RA Moreno-Vivian C., Hennecke S., Puehler A., Klipp W.;
RT "Open reading frame 5 (ORF5), encoding a ferredoxinlike protein, and nifQ
RT are cotranscribed with nifE, nifN, nifX, and ORF4 in Rhodobacter
RT capsulatus.";
RL J. Bacteriol. 171:2591-2598(1989).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX PubMed=8387524; DOI=10.1016/s0021-9258(18)82245-1;
RA Jouanneau Y., Meyer C., Gaillard J., Forest E., Gagnon J.;
RT "Purification and characterization of a novel dimeric ferredoxin (FdIII)
RT from Rhodobacter capsulatus.";
RL J. Biol. Chem. 268:10636-10644(1993).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 2 [4Fe-4S] clusters.;
CC -!- SUBUNIT: Homodimer.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26146.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M26323; AAA26146.1; ALT_INIT; Genomic_DNA.
DR PIR; B32308; FERF3C.
DR RefSeq; WP_023923722.1; NZ_VIBE01000016.1.
DR AlphaFoldDB; P20624; -.
DR GeneID; 31492055; -.
DR OMA; ICPKKCY; -.
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 InterPro; IPR014283; FdIII_4_nif.
DR Pfam; PF13237; Fer4_10; 1.
DR TIGRFAMs; TIGR02936; fdxN_nitrog; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Nitrogen fixation; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..101
FT /note="Ferredoxin-3"
FT /id="PRO_0000159189"
FT DOMAIN 17..46
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 70..100
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 101 AA; 10819 MW; 2F6339AE450C532F CRC64;
MPTVAYTRGG AEYTPVYLMK IDEQKCIGCG RCFKVCGRDV MSLHGLTEDG QVVAPGTDEW
DEVEDEIVKK VMALTGAENC IGCGACARVC PSECQTHAAL S