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Database: UniProt
Entry: A0A285LAZ1_9NOCA
LinkDB: A0A285LAZ1_9NOCA
Original site: A0A285LAZ1_9NOCA 
ID   A0A285LAZ1_9NOCA        Unreviewed;       106 AA.
AC   A0A285LAZ1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Ferredoxin {ECO:0000256|ARBA:ARBA00013529, ECO:0000256|RuleBase:RU365098};
GN   ORFNames=SAMN04244553_2328 {ECO:0000313|EMBL:SNY80756.1};
OS   Nocardia amikacinitolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=756689 {ECO:0000313|EMBL:SNY80756.1, ECO:0000313|Proteomes:UP000219565};
RN   [1] {ECO:0000313|EMBL:SNY80756.1, ECO:0000313|Proteomes:UP000219565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45537 {ECO:0000313|EMBL:SNY80756.1,
RC   ECO:0000313|Proteomes:UP000219565};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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};
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DR   EMBL; OBEG01000002; SNY80756.1; -; Genomic_DNA.
DR   RefSeq; WP_011211287.1; NZ_OBEG01000002.1.
DR   AlphaFoldDB; A0A285LAZ1; -.
DR   STRING; 1379680.GCA_001612615_04676; -.
DR   GeneID; 61135350; -.
DR   OrthoDB; 9803397at2; -.
DR   Proteomes; UP000219565; 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:UP000219565};
KW   Transport {ECO:0000256|RuleBase:RU365098}.
FT   DOMAIN          31..60
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   106 AA;  11687 MW;  AA129BA36612AC92 CRC64;
     MPYIIAEPCV DVKDKACIEE CPVDCIYEGG RMLYIHPDEC VDCGACEPVC PVEAIFYEDD
     TPDQWSGYVN ANVDFFDELG SPGGATKVGK VDYDPPFIKE LPPMGE
//
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