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Database: UniProt
Entry: U2YQY2_9EURY
LinkDB: U2YQY2_9EURY
Original site: U2YQY2_9EURY 
ID   U2YQY2_9EURY            Unreviewed;       608 AA.
AC   U2YQY2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE            EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN   ORFNames=MBEHAL_0130 {ECO:0000313|EMBL:GAD51370.1};
OS   Halarchaeum acidiphilum MH1-52-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae.
OX   NCBI_TaxID=1261545 {ECO:0000313|EMBL:GAD51370.1, ECO:0000313|Proteomes:UP000016986};
RN   [1] {ECO:0000313|EMBL:GAD51370.1, ECO:0000313|Proteomes:UP000016986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16109 {ECO:0000313|EMBL:GAD51370.1,
RC   ECO:0000313|Proteomes:UP000016986};
RA   Shimane Y., Minegishi H., Nishi S., Echigo A., Shuto A., Konishi M.,
RA   Ito T., Ohkuma M., Ohta Y., Nagano Y., Tsubouchi T., Mori K., Usui K.,
RA   Kamekura M., Usami R., Takaki Y., Hatada Y.;
RT   "Whole genome sequencing of Halarchaeum acidiphilum strain MH1-52-1.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:GAD51370.1}.
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DR   EMBL; BATA01000002; GAD51370.1; -; Genomic_DNA.
DR   RefSeq; WP_021779526.1; NZ_BATA01000002.1.
DR   AlphaFoldDB; U2YQY2; -.
DR   eggNOG; arCOG00571; Archaea.
DR   OrthoDB; 23539at2157; -.
DR   Proteomes; UP000016986; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 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; IPR003952; FRD_SDH_FAD_BS.
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   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   PRINTS; PR00411; PNDRDTASEI.
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.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          5..387
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          479..608
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   COILED          492..519
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        281
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   608 AA;  66366 MW;  A7E94FF73423C917 CRC64;
     MYEHDVIVVG GGGSGLRAAI GAHEAGADVA IVTKLHPVRS HTGAAEGGIN AALREGDDWE
     LHAYDTVKGG DYIVDAPAAE TLAQDAPENV VQLENWGMPF SREEDGRMSQ RPFGGLSFPR
     TTYAGAETGH HLLHTLYEQV VKRGITVYDE WYVTRLAVTD EDDPNDRSCH GVVAWDIQTG
     EIEGFRGRDG VVLATGGDGQ VFDHTTNAVA NTADGVAMAY RAGVPIEDME FVQFHPTTLP
     STGVLISEGT RGEGGILYNG EGERLMYEYG YATNDGELAS RDVVARGELT EINAGRGVDD
     EYVHLDMRHL GEERIVDRLE NILHLAEDFE GVDGLENPMP VKPGHHYEMG GIETNENGET
     CVDGLYAVGE AACVSVHGSN RLGGNALPEL LVFGARAGKH AAGEDLGEPE IPVGKTEGDE
     GIEESDVDFP VEPGALAASS AVVSGDSPEG VVDAALEAET ERIEGLLEKD EGVNHADVRS
     KIQKSMTDNV NVFREEGAIE EALETIREAR EEYEDVSVAD KSRTFNTDLQ HTIETRNVID
     TAELIAMGAL AREEFRGAHW RKEYQERRDD EWLKHTMISW NDGTPELWYR PALLEGENQT
     YEPKERHY
//
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