ID A0A1F6RW91_9BACT Unreviewed; 392 AA.
AC A0A1F6RW91;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Ferredoxin {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=A3J76_03820 {ECO:0000313|EMBL:OGI24941.1};
OS Candidatus Moranbacteria bacterium RBG_13_45_13.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1801635 {ECO:0000313|EMBL:OGI24941.1, ECO:0000313|Proteomes:UP000178026};
RN [1] {ECO:0000313|EMBL:OGI24941.1, ECO:0000313|Proteomes:UP000178026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:OGI24941.1}.
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; MFRT01000038; OGI24941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6RW91; -.
DR Proteomes; UP000178026; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.1780; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR PANTHER; PTHR11615:SF6; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11615; NITRATE, FORMATE, IRON DEHYDROGENASE; 1.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53920; Fe-only hydrogenase; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 1..78
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 78..117
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 153..183
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 193..222
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT NON_TER 392
FT /evidence="ECO:0000313|EMBL:OGI24941.1"
SQ SEQUENCE 392 AA; 44445 MW; CC807FE45EB0777C CRC64;
MRIKINGKIY NANEGETILS VCKRNKIRVP TLCAHPDLLP SEGVCRMCLV ETNQAKGLVP
ACAQMACEGL EVFTETEKVN KARKINLELL WADHAGKCVS CKRNGRCELQ DLAQIYDINE
FRFVPRRKEL ESPDELDLLK DNWEHTAFDE KNASISRDSQ YCIECRRCVR ICRDMQTVEA
YGMNYRSSKT NVGTPYEIPL DCIFCGQCSA VCPTAAITEK DDAAEFEKAL ADPKKMVIVQ
TAPSVRFTFS EEFGEKSGTF WEGKLVASLR ELGCDKVFDT VLGADLTIIE EAHELIHRIK
HKGILPMFTS CCPSWVLYVE KYYPEFIPNL SSCKSPQQML APLIKTYWAE REKIDPAQII
SVSIMPCISK KYEAQRKEIN AGKYMDVDIV LT
//