ID O87086_STRGR Unreviewed; 57 AA.
AC O87086;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 3.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Ferredoxin {ECO:0000256|ARBA:ARBA00013529, ECO:0000256|RuleBase:RU365098};
DE Flags: Fragment;
OS Streptomyces griseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1911 {ECO:0000313|EMBL:BAA33533.3};
RN [1] {ECO:0000313|EMBL:BAA33533.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HH1 {ECO:0000313|EMBL:BAA33533.3};
RX PubMed=8458843;
RA Ueda K., Miyake K., Horinouchi S., Beppu T.;
RT "A gene cluster involved in aerial mycelium formation in Streptomyces
RT griseus encodes proteins similar to the response regulators of two-
RT component regulatory systems and membrane translocators.";
RL J. Bacteriol. 175:2006-2016(1993).
RN [2] {ECO:0000313|EMBL:BAA33533.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HH1 {ECO:0000313|EMBL:BAA33533.3};
RX PubMed=9748440;
RA Ueda K., Hsheh C.-W., Tosaki T., Shinkawa H., Beppu T., Horinouchi S.;
RT "Characterization of an A-factor-responsive repressor for amfR essential
RT for onset of aerial mycelium formation in Streptomyces griseus.";
RL J. Bacteriol. 180:5085-5093(1998).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC {ECO:0000256|ARBA:ARBA00003532, ECO:0000256|RuleBase:RU365098}.
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|RuleBase:RU365098};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|RuleBase:RU365098};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU365098};
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DR EMBL; AB006206; BAA33533.3; -; Genomic_DNA.
DR AlphaFoldDB; O87086; -.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR000813; 7Fe_ferredoxin.
DR PANTHER; PTHR42859:SF2; FERREDOXIN; 1.
DR PANTHER; PTHR42859; OXIDOREDUCTASE; 1.
DR Pfam; PF00037; Fer4; 1.
DR PRINTS; PR00354; 7FE8SFRDOXIN.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW 3Fe-4S {ECO:0000256|RuleBase:RU365098};
KW 4Fe-4S {ECO:0000256|RuleBase:RU365098};
KW Electron transport {ECO:0000256|RuleBase:RU365098};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365098};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU365098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365098}; Transport {ECO:0000256|RuleBase:RU365098}.
FT DOMAIN 31..57
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT NON_TER 57
FT /evidence="ECO:0000313|EMBL:BAA33533.3"
SQ SEQUENCE 57 AA; 6375 MW; FDFE72FBCD76C170 CRC64;
MTYVIAQPCV DVKDKACIEE CPVDCIYEGQ RSLYIHPDEC VDCGACEPVC PVEAIFY
//
