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Database: UniProt
Entry: C8W5H7_DESAS
LinkDB: C8W5H7_DESAS
Original site: C8W5H7_DESAS 
ID   C8W5H7_DESAS            Unreviewed;      1005 AA.
AC   C8W5H7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   SubName: Full=4Fe-4S ferredoxin iron-sulfur binding domain protein {ECO:0000313|EMBL:ACV62159.1};
GN   OrderedLocusNames=Dtox_1277 {ECO:0000313|EMBL:ACV62159.1};
OS   Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS   B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV62159.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV62159.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA   Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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}.
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DR   EMBL; CP001720; ACV62159.1; -; Genomic_DNA.
DR   RefSeq; WP_015756874.1; NC_013216.1.
DR   AlphaFoldDB; C8W5H7; -.
DR   STRING; 485916.Dtox_1277; -.
DR   KEGG; dae:Dtox_1277; -.
DR   eggNOG; COG1148; Bacteria.
DR   HOGENOM; CLU_004231_2_0_9; -.
DR   OMA; FVRYSEN; -.
DR   OrthoDB; 135003at2; -.
DR   Proteomes; UP000002217; Chromosome.
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; -; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like 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; PF12831; FAD_oxidored; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF13237; Fer4_10; 1.
DR   Pfam; PF07992; Pyr_redox_2; 2.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN          102..132
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          933..962
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          964..993
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1005 AA;  109360 MW;  19E26C7E0A675E51 CRC64;
     MSTSKPVTGS VLVVGGGIAG IQASLDLAES GFYVYLVEKT PAIGGVMPML DKTFPTNDCS
     MCILSPKLVE CGGHLNVDVM TTSVVQDIKG EPGNFTVTIL KKARFIDPLK CTGCGSCVEV
     CPKKVTDEFD QGLRDRRSIY KPYAQAFPNA FAIDGSSCLK IKKPKACGKC LEVCQAGAID
     HTMQDEIVEI NVGSVILCPG FEKFDAKLLS YYGYGKFAGV VTSLEFERLL SASGPFGGHL
     IRPADEREPK KVAWIQCVGS RNEKEGCGYC SAVCCMYAIK EAVIAKEHAH YPLDTTIFFM
     DMRTYGKDFE KYYNRAKEEH GVKFVRSRIY EVTENEDKNL VIRYSNEDGT ITTDVFDMVV
     LSIGLKPNSD MVELANKVGI ELNKYNFCEA KELTGVETSK EGIYVAGAFS GPRDIPETVI
     EASAAAGACA VQLASARGTL IKTMEYPEEI NVYGEIPRTG VFICHCGINI GGVVNVPSAV
     EYAKTLPGVV YAQESLYVCS QDAQVQIKEK IAEYNLNRVV VASCTPRTHE PLFQKTLHEA
     GLNPYLFEMA NIRDQCSWVH MHEPEKATVK AKDLVKMAVA KAQLLTPLYE QELDMDHGAL
     VIGGGVSGMT NALNLAEQGY KVSIVERTEK LGGIANRITT GFKGEDIKGF VANLASKVNN
     HANIDVYLNS DLADVHGYLG NYLTKLTDGQ EIKHGVTIIA NGGMEYKPTE YLYGENDRVI
     TQLELEEAMV SGDAKVKDAK NFVLINCVGS RDNERPYCSR VCCNKSIKLA LKIKEKNPDA
     NVFVLYRDIR SYGFFEDNYR EARCKGVIFI RYSVDNKPVV EAVGDVIKVT VTDHVLGQPL
     EIEADIICLA AAIVPQKDNG KLSQFFKVPL NADGFFLEAH LKLRPVDFST DGVFMCGLCH
     GPKSTEENVA QAKAAAARAG TALSKENVQA EGKIANINNK KCAGCGVCEL VCPSKAIAVD
     TEKMIAVVNE ALCKGCGACA SSCRCGALNI KGFTNEQIVA MISAL
//
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