ID A0A0U5H1S7_9EURY Unreviewed; 610 AA.
AC A0A0U5H1S7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN Name=sdhA {ECO:0000313|EMBL:CQH57131.1};
GN ORFNames=HHUB_2484 {ECO:0000313|EMBL:CQH57131.1};
OS Halobacterium hubeiense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH57131.1, ECO:0000313|Proteomes:UP000066737};
RN [1] {ECO:0000313|Proteomes:UP000066737}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA Yang C., Oksanen H.M., Bamford D.H.;
RT "The complete genome of a viable archaeum isolated from 123-million-year-
RT old rock salt.";
RL Environ. Microbiol. 18:565-579(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}.
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DR EMBL; LN831302; CQH57131.1; -; Genomic_DNA.
DR RefSeq; WP_059056926.1; NZ_LN831302.1.
DR AlphaFoldDB; A0A0U5H1S7; -.
DR STRING; 1407499.HHUB_2484; -.
DR GeneID; 26659121; -.
DR KEGG; hhb:Hhub_2484; -.
DR OrthoDB; 23539at2157; -.
DR Proteomes; UP000066737; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
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; 2.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CQH57131.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000066737};
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 481..610
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 402..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 610 AA; 66926 MW; 0758BD8E8EC587E1 CRC64;
MYEHDVIVVG GGGAGLRAAI AAHEEGADVA IVTKLHPVRS HTGAAEGGIN AALQDGDSWE
DHAYDTMKGS DYLGDAPAVD TFAQDAPEEV IQLEHWGMPF SREEDGTVSQ RPFGGLSFPR
TTYAGAETGH HMLHTLYEQV VKRGIEVYDE WYVSQVAVTD EDDPNERDCH GVVAWDVQSG
EIAGFRARDG VILATGGLGQ AFDHTTNAVA NTGDGVAIAY RAGVPMEDME MIQFHPTTLP
STGVLISEGV RGEGGILYNS EGERFMFEYG YATNDGELAS RDVVARAELT EVQEGRGVED
EYVYLDMRHL GEERITDRLE NILHLARDFE GVDGLEEPMP VKPGQHYAMG GIEVNEHGET
CIDGLYAAGE CACVSLHGGN RLGGNALPEL LVFGARAGRH AAGADMPEPK IETGPEPDAE
REDLGVPVGE PGAKEAAADG GAVENPASDP KAVVEATAET ERERIETLLE REDGVNHADV
RADLQESMTE NVNVFREEEN LKQALRDIQD ARERYQDVYV ADKSRTFNTD LQHTIETRNL
LDVAEAITMG ALAREEFRGA HWRKEHQERK DDEYLKHTLV SWNDGEPELW YRPVILEGDE
QTYEPKVRSY
//
