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
//