ID A5CEP2_ORITB Unreviewed; 106 AA.
AC A5CEP2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Ferredoxin {ECO:0000256|ARBA:ARBA00013529, ECO:0000256|RuleBase:RU364098};
GN Name=fdxA {ECO:0000313|EMBL:CAM80671.1};
GN OrderedLocusNames=OTBS_1578 {ECO:0000313|EMBL:CAM80671.1};
OS Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=357244 {ECO:0000313|EMBL:CAM80671.1, ECO:0000313|Proteomes:UP000001565};
RN [1] {ECO:0000313|EMBL:CAM80671.1, ECO:0000313|Proteomes:UP000001565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boryong {ECO:0000313|EMBL:CAM80671.1,
RC ECO:0000313|Proteomes:UP000001565};
RX PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT "The Orientia tsutsugamushi genome reveals massive proliferation of
RT conjugative type IV secretion system and host-cell interaction genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
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: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; AM494475; CAM80671.1; -; Genomic_DNA.
DR RefSeq; WP_011944951.1; NC_009488.1.
DR AlphaFoldDB; A5CEP2; -.
DR KEGG; ots:OTBS_1578; -.
DR eggNOG; COG1146; Bacteria.
DR HOGENOM; CLU_139698_0_0_5; -.
DR Proteomes; UP000001565; 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:UP000001565};
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 106 AA; 12110 MW; 16EE5615DBA158F0 CRC64;
MTYVVTDSCV KCKYTDCVEV CPVDCFHEGE MMVVIDPEKC IDCGVCEAEC PVGAIKPEAE
ELIKWIELGQ EFSKKWPQIL HKKAPLPQAD LYKDKTNKFE KYCISK
//