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Database: UniProt
Entry: A0A2U1THS1_9MICO
LinkDB: A0A2U1THS1_9MICO
Original site: A0A2U1THS1_9MICO 
ID   A0A2U1THS1_9MICO        Unreviewed;       107 AA.
AC   A0A2U1THS1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Ferredoxin {ECO:0000256|ARBA:ARBA00013529, ECO:0000256|RuleBase:RU365098};
GN   ORFNames=DF223_03635 {ECO:0000313|EMBL:PWC08428.1};
OS   Mycetocola zhujimingii.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Mycetocola.
OX   NCBI_TaxID=2079792 {ECO:0000313|EMBL:PWC08428.1, ECO:0000313|Proteomes:UP000244962};
RN   [1] {ECO:0000313|Proteomes:UP000244962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=622 {ECO:0000313|Proteomes:UP000244962};
RA   Liu S., Wang Z., Li J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWC08428.1}.
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DR   EMBL; QEFB01000001; PWC08428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1THS1; -.
DR   KEGG; myl:C3E77_09815; -.
DR   Proteomes; UP000244962; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244962};
KW   Transport {ECO:0000256|RuleBase:RU365098}.
FT   DOMAIN          31..60
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   107 AA;  11751 MW;  3EE18025426C2F71 CRC64;
     MTYVIALPCV DVKDRACIDE CPVDCIYEGE RSLYIHPDEC VDCGACEPVC PVEAIYYEDD
     LPEEWADYYK ANVEFFTEVG SPGGAAKVGV IKYDHPVISA LPPQAGV
//
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