ID A0A1F8M0A7_9CHLR Unreviewed; 579 AA.
AC A0A1F8M0A7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Ferredoxin {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2Z70_03095 {ECO:0000313|EMBL:OGN92051.1};
OS Chloroflexi bacterium RBG_13_48_17.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797621 {ECO:0000313|EMBL:OGN92051.1, ECO:0000313|Proteomes:UP000180319};
RN [1] {ECO:0000313|EMBL:OGN92051.1, ECO:0000313|Proteomes:UP000180319}
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=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:OGN92051.1}.
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DR EMBL; MGMO01000012; OGN92051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8M0A7; -.
DR Proteomes; UP000180319; 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; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PRINTS; PR00419; ADXRDTASE.
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; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
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 2..81
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 81..145
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 208..238
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 579 AA; 63133 MW; E8B6A1A23D83A1D9 CRC64;
MDTINLTIDG IEVKTTRGKR ILEAALDAGI YIPNLCALRD IKLPFGACRL CQVQIEGRRG
TITACSEPAA DGMVVHSNTS EVNCLRREIL EIMLARHPHE CLTCWRKERC QPFDICLRNV
SVTERCVTCP KNGYCELQKV ADFIGLVTMP FPYTSKGLPV EMENPFIVRN NNLCILCGRC
IRVDQEVLGF EAIAFNLRGA KTYIGGAFGK SLIESGCTFC GSCVEVCPTG ALMDRGEEWN
QGGEREALSI RCKYNCPTRV DVPRFIRFIR EKKYTEAVAV IRESVPFAAV CSLICEHPCE
AEGACRRGDL DQPVAIRALE RFAVERSGKY EPPEGLKAAP SGKKIAIVGS GPAGLTAAYY
LAKKGGHTVT VFESLSQPGG MMRELIPEYI LPRDILDAEI EGLSKLGVKI KTQSKVVSVD
KLFEKGFDAV LLATGITAEL DKFNGETGRK NGRKGVFGCG NTVTGMISFI ESVAAGRQAA
VSIDRYLGGT GIMSESLAPI IEGVPRVGRI DNFAQRRRQE MPAAKPAKPV GNFSQVELGF
SDELGQEESK RCMSCDLRFA VARMVAGPEG KATKTLARS
//