ID A0A2Z2HPH3_9EURY Unreviewed; 612 AA. AC A0A2Z2HPH3; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 13-SEP-2023, entry version 16. DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792}; DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792}; GN ORFNames=B1756_02980 {ECO:0000313|EMBL:ARS88822.1}; OS Natrarchaeobaculum aegyptiacum. OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales; OC Natrialbaceae; Natrarchaeobaculum. OX NCBI_TaxID=745377 {ECO:0000313|EMBL:ARS88822.1, ECO:0000313|Proteomes:UP000250088}; RN [1] {ECO:0000313|Proteomes:UP000250088} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JW/NM-HA 15 {ECO:0000313|Proteomes:UP000250088}; RA Zhao B.; RT "Natronthermophilus aegyptiacus gen. nov.,sp. nov., an aerobic, extremely RT halophilic alkalithermophilic archaeon isolated from the athalassohaline RT Wadi An Natrun, Egypt."; RL Submitted (FEB-2017) 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP019893; ARS88822.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2Z2HPH3; -. DR EnsemblBacteria; ARS88822; ARS88822; B1756_02980. DR KEGG; naj:B1756_02980; -. DR OrthoDB; 23539at2157; -. DR Proteomes; UP000250088; Chromosome. 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; 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; 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 Electron transport {ECO:0000256|ARBA:ARBA00022982}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000250088}; 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 483..612 FT /note="Fumarate reductase/succinate dehydrogenase FT flavoprotein-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF02910" FT ACT_SITE 281 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50" SQ SEQUENCE 612 AA; 67147 MW; 08BB1EE9DFAFB1D3 CRC64; MYEHDVIVVG AGGAGLRAAI AAHEAGADTA LVTKLHPVRS HTGAAEGGIN AALQEGDDWE LHAYDTMKGS DYLGDAPAVE TLAQDSPEDT MRLEHWGMPF SREEDGTVSQ RPFGGLSYPR TTFAGAETGH HLLHTMYEQV VKRGIQVYDE WYVMNLAVTD EDDPNDRTCH GVVAYDVQTG QIEGFKANSG VILATGGPGQ AFDHTTNAVS CTGDGHAIAY RAGAPLEDME FIQFHPTSLP STGVLISEGV RGEGGILYNN EGERFMFEYG YANNSGELAS RDVVARAELT EVAEGRGVND EYVHLDMRHL GEERILDRLE NILHLAEDFE GVDGLVEPMP VKPGQHYAMG GIDVDENGQT CINGLYAAGE AACVSVHGGN RLGGNALPEL IVFGKRAGRH AAGEDLGEPQ IQTGYGDDVE DETDADLPVQ PGEAGLETAG GVAADGGVAA DAEGILERTV ERERERVDRL MDRNEGIQHA EIRQKLQKAM TDHVNVFRTE EGIKKALRVI RECREQYQDV YVDDPSRTFN TDLQQTYETR NLIDVAETIA LGALVRNEFR GAHWRQENQE RDDENWLKHT LISWNGGEPR IFYRPVILEG EEKTYEPKER SY //