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
//