ID A0A160FLT3_9BURK Unreviewed; 107 AA.
AC A0A160FLT3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU364098};
GN ORFNames=AYM40_14805 {ECO:0000313|EMBL:ANB73485.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB73485.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB73485.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB73485.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC {ECO:0000256|RuleBase:RU364098}.
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927,
CC ECO:0000256|RuleBase:RU364098};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU364098};
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DR EMBL; CP014578; ANB73485.1; -; Genomic_DNA.
DR RefSeq; WP_020069367.1; NZ_CP014578.1.
DR AlphaFoldDB; A0A160FLT3; -.
DR STRING; 1804984.AYM40_14805; -.
DR KEGG; buz:AYM40_14805; -.
DR Proteomes; UP000076852; Chromosome 1.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR022569; Fd_C.
DR PANTHER; PTHR42859:SF2; FERREDOXIN; 1.
DR PANTHER; PTHR42859; OXIDOREDUCTASE; 1.
DR Pfam; PF11953; DUF3470; 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; 2.
PE 4: Predicted;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|RuleBase:RU364098};
KW 4Fe-4S {ECO:0000256|RuleBase:RU364098};
KW Electron transport {ECO:0000256|RuleBase:RU364098};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364098};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364098};
KW Reference proteome {ECO:0000313|Proteomes:UP000076852};
KW Repeat {ECO:0000256|RuleBase:RU364098};
KW Transport {ECO:0000256|RuleBase:RU364098}.
FT DOMAIN 1..30
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 31..60
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 107 AA; 11881 MW; 1964D7AF9D2151A3 CRC64;
MTHVVTESCI KCRYTDCVDV CPVDCFREGP NFLAIDPDEC IDCAVCVAEC PVNAIYAEED
VPGDQQNFIE LNADLAKNWP SITKTKAPLP EADEFKDVKE KLALLAR
//
