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Database: UniProt
Entry: A0A1Q5MTY2_9ACTN
LinkDB: A0A1Q5MTY2_9ACTN
Original site: A0A1Q5MTY2_9ACTN 
ID   A0A1Q5MTY2_9ACTN        Unreviewed;        64 AA.
AC   A0A1Q5MTY2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU368020};
GN   ORFNames=AMK16_21360 {ECO:0000313|EMBL:OKK17738.1};
OS   Streptomyces sp. CB00455.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703927 {ECO:0000313|EMBL:OKK17738.1, ECO:0000313|Proteomes:UP000185643};
RN   [1] {ECO:0000313|EMBL:OKK17738.1, ECO:0000313|Proteomes:UP000185643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB00455 {ECO:0000313|EMBL:OKK17738.1,
RC   ECO:0000313|Proteomes:UP000185643};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions.
CC       {ECO:0000256|RuleBase:RU368020}.
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|ARBA:ARBA00001927};
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:OKK17738.1}.
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DR   EMBL; LIVQ01000005; OKK17738.1; -; Genomic_DNA.
DR   RefSeq; WP_073918861.1; NZ_LIVQ01000005.1.
DR   AlphaFoldDB; A0A1Q5MTY2; -.
DR   STRING; 1703927.AMK16_21360; -.
DR   OrthoDB; 9803319at2; -.
DR   Proteomes; UP000185643; Unassembled WGS sequence.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.20; -; 1.
DR   InterPro; IPR001080; 3Fe4S_ferredoxin.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   PANTHER; PTHR36923; FERREDOXIN; 1.
DR   PANTHER; PTHR36923:SF3; FERREDOXIN; 1.
DR   Pfam; PF13370; Fer4_13; 1.
DR   PRINTS; PR00352; 3FE4SFRDOXIN.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU368020};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU368020};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU368020};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368020};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185643};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368020}.
FT   DOMAIN          1..29
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   64 AA;  6547 MW;  50EB56BB53427BA4 CRC64;
     MHIDIDTGVC IGAGQCALTA PGVFTQDDDG FSELLPGRED GAGSALVREA ARACPVSAIS
     VREE
//
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