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Database: UniProt
Entry: A0A133UTU3_9EURY
LinkDB: A0A133UTU3_9EURY
Original site: A0A133UTU3_9EURY 
ID   A0A133UTU3_9EURY        Unreviewed;       561 AA.
AC   A0A133UTU3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Fumarate reductase {ECO:0000313|EMBL:KXA97615.1};
GN   ORFNames=AKJ38_00720 {ECO:0000313|EMBL:KXA97615.1};
OS   candidate division MSBL1 archaeon SCGC-AAA259I14.
OC   Archaea; Euryarchaeota; candidate division MSBL1.
OX   NCBI_TaxID=1698268 {ECO:0000313|EMBL:KXA97615.1, ECO:0000313|Proteomes:UP000070414};
RN   [1] {ECO:0000313|EMBL:KXA97615.1, ECO:0000313|Proteomes:UP000070414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC-AAA259I14 {ECO:0000313|EMBL:KXA97615.1};
RX   PubMed=26758088; DOI=10.1038/srep19181;
RA   Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA   Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT   "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT   pools of the Red Sea.";
RL   Sci. Rep. 6:19181-19181(2016).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
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:KXA97615.1}.
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DR   EMBL; LHXS01000007; KXA97615.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133UTU3; -.
DR   PATRIC; fig|1698268.3.peg.777; -.
DR   Proteomes; UP000070414; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR   Gene3D; 4.10.80.40; succinate dehydrogenase protein domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR030664; SdhA/FrdA/AprA.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070414}.
FT   DOMAIN          5..381
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          436..561
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   561 AA;  62307 MW;  243ADBC4A70D3D6A CRC64;
     MTSHDVVIVG SGLTGMRAAL SAKEKGADVA IVAKTYPVRA HSVEAQGGIA ASLSRIEKDS
     WEDHMFDTVK GADYLSDQDA AELLAKKAPD AIVELENMGA LFSRKEDGKL NQRAFGGHSN
     IRAVFASDKT GHALEHVLFE QVMKAGVEIY DEWYVTRLIV EDGVCKGIVG YDMQNGEIRV
     IRGKSTIFCT GGYGRVYGIT SNDLQNNGDG ISMAFRAGVP LKDMEFVQFH PTGLYPRGIL
     ITEGARGEGG HLINDEGERF AKKYAPDMME LAPRDILARA IQTEIQEGRG IDGGDYVHLD
     LTHIGEEKIK ERLPLIRELA MDTVGVDPIE EPIPVRPTAH YSMGGIHVDI ECSTPVKGFF
     AAGECSCVSV HGANRLGTNS LLECVVFGKN VGKTAADYAN GTSLPDLSSD EYQEKEKDKM
     SRLMNGESEE TVEKLRKELQ DIMRSNVYIF RNESGLREAL DKIMNIKERF AKVSINDQSK
     VFNTAYTGAL DLEHLIDVAW TITKNALARE ESRGSHYRTD YEERDDENWL KHSLSYLRDG
     EMELDYEPVT ITKFEPKKRE Y
//
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