FER4_RHOCA
ID FER4_RHOCA Reviewed; 95 AA.
AC P0CY92; P16022;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Ferredoxin-4;
DE AltName: Full=Ferredoxin IV;
DE Short=FdIV;
DE AltName: Full=Ferredoxin, plant-type;
GN Name=fdxC; Synonyms=ptfA;
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=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).
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).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. This ferredoxin is required
CC for nitrogen fixation (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; M59855; AAA26109.1; -; Genomic_DNA.
DR EMBL; X72888; CAA51403.1; -; Genomic_DNA.
DR PIR; S08393; FERFNC.
DR RefSeq; WP_013068981.1; NZ_VIBE01000016.1.
DR AlphaFoldDB; P0CY92; -.
DR SMR; P0CY92; -.
DR GeneID; 31492065; -.
DR OMA; VPFACTE; -.
DR GO; GO:0051537; F:2 iron, 2 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 CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Transport.
FT CHAIN 1..95
FT /note="Ferredoxin-4"
FT /id="PRO_0000189389"
FT DOMAIN 2..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 38
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 81
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 95 AA; 10163 MW; 7CD077A779D543F0 CRC64;
MDKATLTFTD VSITVNVPTG TRIIEMSEKV GSGITYGCRE GECGTCMTHI LEGSENLSEP
TALEMRVLEE NLGGKDDRLA CQCRVLGGAV KVRPA
