FER6_RHOCA
ID FER6_RHOCA Reviewed; 107 AA.
AC P80306; Q9R767;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ferredoxin-6;
DE AltName: Full=Ferredoxin VI {ECO:0000303|PubMed:8026503};
DE Short=FdVI {ECO:0000303|PubMed:8026503};
GN Name=fdxE {ECO:0000303|PubMed:9150228};
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, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=9150228; DOI=10.1128/jb.179.10.3304-3309.1997;
RA Armengaud J., Meyer C., Jouanneau Y.;
RT "A [2Fe-2S] ferredoxin (FdVI) is essential for growth of the photosynthetic
RT bacterium Rhodobacter capsulatus.";
RL J. Bacteriol. 179:3304-3309(1997).
RN [2]
RP PROTEIN SEQUENCE OF 2-107, COFACTOR, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=8026503; DOI=10.1111/j.1432-1033.1994.tb18942.x;
RA Naud I., Vincon M., Garin J., Gaillard J., Forest E., Jouanneau Y.;
RT "Purification of a sixth ferredoxin from Rhodobacter capsulatus. Primary
RT structure and biochemical properties.";
RL Eur. J. Biochem. 222:933-939(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP (2FE-2S), AND COFACTOR.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=11173487; DOI=10.1107/s0907444900017832;
RA Armengaud J., Sainz G., Jouanneau Y., Sieker L.C.;
RT "Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S]
RT ferredoxin (FdVI) from Rhodobacter capsulatus.";
RL Acta Crystallogr. D 57:301-303(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP (2FE-2S), AND COFACTOR.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=16402206; DOI=10.1007/s00775-005-0069-2;
RA Sainz G., Jakoncic J., Sieker L.C., Stojanoff V., Sanishvili N., Asso M.,
RA Bertrand P., Armengaud J., Jouanneau Y.;
RT "Structure of a [2Fe-2S] ferredoxin from Rhodobacter capsulatus likely
RT involved in Fe-S cluster biogenesis and conformational changes observed
RT upon reduction.";
RL J. Biol. Inorg. Chem. 11:235-246(2006).
CC -!- FUNCTION: Ferredoxins are small electron carrier proteins that
CC participate in various redox reactions. FdVI is an essential protein
CC required for growth of R.capsulatus. May be involved in Fe-S cluster
CC assembly. {ECO:0000269|PubMed:9150228, ECO:0000303|PubMed:16402206}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:11173487, ECO:0000269|PubMed:16402206,
CC ECO:0000269|PubMed:8026503};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:11173487,
CC ECO:0000269|PubMed:16402206, ECO:0000269|PubMed:8026503};
CC -!- INDUCTION: Seems to be constitutively expressed. Is expressed at a
CC similar level under N-limited and N-sufficient conditions.
CC {ECO:0000269|PubMed:9150228}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene is lethal.
CC {ECO:0000269|PubMed:9150228}.
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; Y11304; CAA72162.1; -; Genomic_DNA.
DR PIR; S45612; S45612.
DR RefSeq; WP_013068113.1; NZ_VIBE01000001.1.
DR PDB; 1E9M; X-ray; 2.07 A; A=2-107.
DR PDB; 1UWM; X-ray; 2.00 A; A=2-107.
DR PDBsum; 1E9M; -.
DR PDBsum; 1UWM; -.
DR AlphaFoldDB; P80306; -.
DR SMR; P80306; -.
DR GeneID; 31491235; -.
DR OMA; SACGGVC; -.
DR EvolutionaryTrace; P80306; -.
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:0140647; P:P450-containing electron transport chain; IEA:InterPro.
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; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00814; ADX; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8026503"
FT CHAIN 2..107
FT /note="Ferredoxin-6"
FT /id="PRO_0000201180"
FT DOMAIN 2..106
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:11173487,
FT ECO:0000269|PubMed:16402206"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:11173487,
FT ECO:0000269|PubMed:16402206"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:11173487,
FT ECO:0000269|PubMed:16402206"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:11173487,
FT ECO:0000269|PubMed:16402206"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1UWM"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1UWM"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:1UWM"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1UWM"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1UWM"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1UWM"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1UWM"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:1UWM"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1UWM"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1UWM"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1UWM"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1UWM"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1UWM"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1UWM"
SQ SEQUENCE 107 AA; 11533 MW; 64239FF7451D8D1B CRC64;
MAKIIFIEHN GTRHEVEAKP GLTVMEAARD NGVPGIDADC GGACACSTCH AYVDPAWVDK
LPKALPTETD MIDFAYEPNP ATSRLTCQIK VTSLLDGLVV HLPEKQI
