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
//