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Database: UniProt
Entry: A0A1F8N4T3_9CHLR
LinkDB: A0A1F8N4T3_9CHLR
Original site: A0A1F8N4T3_9CHLR 
ID   A0A1F8N4T3_9CHLR        Unreviewed;       559 AA.
AC   A0A1F8N4T3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=4Fe-4S ferredoxin-type domain-containing protein {ECO:0000259|PROSITE:PS51379};
GN   ORFNames=A2Y73_03370 {ECO:0000313|EMBL:OGO05898.1};
OS   Chloroflexi bacterium RBG_13_56_8.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797632 {ECO:0000313|EMBL:OGO05898.1, ECO:0000313|Proteomes:UP000180162};
RN   [1] {ECO:0000313|EMBL:OGO05898.1, ECO:0000313|Proteomes:UP000180162}
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=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the HdrA family.
CC       {ECO:0000256|ARBA:ARBA00006561}.
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:OGO05898.1}.
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DR   EMBL; MGMZ01000060; OGO05898.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8N4T3; -.
DR   Proteomes; UP000180162; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-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   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR039650; HdrA-like.
DR   PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR   PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          482..511
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          518..547
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   559 AA;  60352 MW;  0C5B1BD2A0F696D0 CRC64;
     MEKPKVGVFV CHCGVEIGAV LNVPELVQYA CTLPYVVFAQ DDARTCTEAG LTNLASTISQ
     HSLNRVVIAS CTPRTHAPLF QDTCKKAGLN PHLFEFVNIR DQCAFVHTGD TDGATKKAKD
     LLRMGVASAA KRTPLDPLRL PVEPTALVLG GGVAGMTAAL SLASRGYQVK LGEREPALGG
     LLKSLHRLYP TGEKASTILE KKLEAIENCT NIEVLTSATV RDIRGVPGRY EVVIEKDGEE
     REFVVGAIIT ATGAQEFVPE GMYSYDGEKV ITQGQLERLL SQDGWLNSST PESIVMIQCV
     GARDDTRPYC SRICCMTAVE NAIEIKKARP SRQVYVLYRD MLTQGNKYEG LYGEARNRGV
     AFVQFDPESP PQVLPGEVVV EDKLLGQPLH IDADLVVLST PLVSQPDAAD LAQSLGVMVD
     EYGFLHEPHL KHRPLDTTVD GIFQCGSAHW PCDVGESVLQ AYGAAARASV FLGTDHLEMS
     PIVAKVNVAR CAACGLCEEL CPYHAVSVMV VDQRRGTKAA QVSEVLCKGC GACAAACRSH
     AIDLAGYTNE RVFAMIEAF
//
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