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Database: UniProt
Entry: D8GPY2_CLOLD
LinkDB: D8GPY2_CLOLD
Original site: D8GPY2_CLOLD 
ID   D8GPY2_CLOLD            Unreviewed;       926 AA.
AC   D8GPY2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein-like protein {ECO:0000313|EMBL:ADK16073.1};
GN   OrderedLocusNames=CLJU_c30250 {ECO:0000313|EMBL:ADK16073.1};
OS   Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK16073.1, ECO:0000313|Proteomes:UP000001656};
RN   [1] {ECO:0000313|EMBL:ADK16073.1, ECO:0000313|Proteomes:UP000001656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55383 / DSM 13528 / PETC
RC   {ECO:0000313|Proteomes:UP000001656};
RX   PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA   Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA   Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT   "Clostridium ljungdahlii represents a microbial production platform based
RT   on syngas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP001666; ADK16073.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8GPY2; -.
DR   STRING; 748727.CLJU_c30250; -.
DR   KEGG; clj:CLJU_c30250; -.
DR   PATRIC; fig|748727.19.peg.3758; -.
DR   eggNOG; COG1053; Bacteria.
DR   eggNOG; COG1145; Bacteria.
DR   eggNOG; COG1894; Bacteria.
DR   HOGENOM; CLU_320221_0_0_9; -.
DR   Proteomes; UP000001656; Chromosome.
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:UniProtKB-KW.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR   InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF13187; Fer4_9; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          319..348
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          349..379
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   COILED          794..821
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   926 AA;  101497 MW;  04D9EA376DA3F66B CRC64;
     MLTNNTEALI LAEKIGKEAA LSCLQGMYDY GTSPMKVLDM IKEKPNCKVI VGALNNSDTD
     GMLNILAKTN PAGLAAGLSV LAKASGAEEA LLELRNTDNE AELLASAKTA GVKLRVEVGE
     LVDVRAHKEH IIFNLETLAG IADKITGTAP GIIIAVDEDV PKEVKFGTKL VDFLDTAKVK
     SVMINHHFYR LDVLNNGIIK ENSYGSGVIH IIYENDCIVE KTKKELENLR KQSCGKCTFC
     REGLYQLDVI FDDMIKGRSE KEDLAMVEEL TSAMKFSCNC SLGKCSGEPA ASAITEFKLE
     VEQHIKKRGC PAGQCLAFTN IYVDPRKCKG CGKCLEVCPE DCIEAKKGYI SMIDEFDCTK
     CGICIDECPN NAIVKVNGKT PKLPTKLTRV KGSKNITEED TEKKKRHNLK RHRTKLVIPL
     KKDNNKASEK ISEIKKSKEG TIMKKMETDI IIAAGGPAGL AAAITAGENN LKSILFEKSS
     TTGGAANMGM GPLGIDTKIQ KDNFNNISVA EALDMHMKYT HYRVDEDLVQ TYFNKSAETI
     EWLQDMGVEF AGAFRYFKES AATWHIVKPE NGVIGPRAAS GMAKIMTERA KELGTKILLE
     TPVVSLIKEN GRICGVKAQD SEGNIIEVRA KAVIVATGGF GNNKNMIKSE FGLTIGEDYF
     PFMVPGITGD GLKMMWEAGA MKYGENIEAI YQLPDNLNWF LLDAVLRQPN LLINQLGDRF
     MNEGDMGNTT FTGNAIAMQP GNYAYCIMDE GILKHYKKNG PDIFDIVHPA DAFLAVDGEI
     AKAVEQGYES YFEARTVEEL AKKLNIDAEK LQDTIDEYNE ACETGVDTKF HKKQAYLHPI
     TGKGKYLVGK FYLGAYGTIG GVRINKYCEV LDESFNPIEG LYSAGTDANT IYGDSYNFTL
     PGNSMGFAIN SGRMAGESAA EYIEEV
//
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