ID A0A2K8KN75_9GAMM Unreviewed; 107 AA.
AC A0A2K8KN75;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU364098};
GN ORFNames=REIFOR_00965 {ECO:0000313|EMBL:ATX76132.1};
OS Reinekea forsetii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Reinekea.
OX NCBI_TaxID=1336806 {ECO:0000313|EMBL:ATX76132.1, ECO:0000313|Proteomes:UP000229757};
RN [1] {ECO:0000313|EMBL:ATX76132.1, ECO:0000313|Proteomes:UP000229757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_31_D35 {ECO:0000313|EMBL:ATX76132.1,
RC ECO:0000313|Proteomes:UP000229757};
RX PubMed=28000419;
RA Avci B., Hahnke R.L., Chafee M., Fischer T., Gruber-Vodicka H.,
RA Tegetmeyer H.E., Harder J., Fuchs B.M., Amann R.I., Teeling H.;
RT "Genomic and physiological analyses of 'Reinekea forsetii' reveal a
RT versatile opportunistic lifestyle during spring algae blooms.";
RL Environ. Microbiol. 19:1209-1221(2017).
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011797; ATX76132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8KN75; -.
DR KEGG; rfo:REIFOR_00965; -.
DR OrthoDB; 9803397at2; -.
DR Proteomes; UP000229757; Chromosome.
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:UP000229757};
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"
FT REGION 87..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 107 AA; 11951 MW; 13479C8AE232BFF7 CRC64;
MAFIVLENCI KCKYTDCVEV CPVDCFYEGP NFLVIHPDEC IDCALCEPEC PAEAILSEDE
VPADQIDFIE LNAELAEIWP NITEQKTALP DADAQNGQPG KRAFLER
//