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Database: UniProt
Entry: R8H4V7_BACCE
LinkDB: R8H4V7_BACCE
Original site: R8H4V7_BACCE 
ID   R8H4V7_BACCE            Unreviewed;       597 AA.
AC   R8H4V7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE            EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN   ORFNames=IIC_05234 {ECO:0000313|EMBL:EOO67826.1};
OS   Bacillus cereus VD021.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1053224 {ECO:0000313|EMBL:EOO67826.1, ECO:0000313|Proteomes:UP000014040};
RN   [1] {ECO:0000313|EMBL:EOO67826.1, ECO:0000313|Proteomes:UP000014040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VD021 {ECO:0000313|EMBL:EOO67826.1,
RC   ECO:0000313|Proteomes:UP000014040};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA   Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA   Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus cereus VD021.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000030};
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:EOO67826.1}.
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DR   EMBL; AHES01000063; EOO67826.1; -; Genomic_DNA.
DR   RefSeq; WP_002143291.1; NZ_KB976283.1.
DR   AlphaFoldDB; R8H4V7; -.
DR   PATRIC; fig|1053224.3.peg.5272; -.
DR   HOGENOM; CLU_014312_7_1_9; -.
DR   Proteomes; UP000014040; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.820; -; 1.
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; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   NCBIfam; TIGR01811; sdhA_Bsu; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF53; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; 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   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          5..391
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          451..578
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   REGION          574..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        284
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   597 AA;  65951 MW;  8E8B5353952AC6F7 CRC64;
     MKGKLIVVGG GLAGLMATIK AAEAGVNVEL FSLVPVKRSH SVCAQGGING AVNTKGEGDS
     PWIHFDDTIY GGDFLANQPP VKAMCDAAPG IIHLMDRMGV MFNRTEEGLL DFRRFGGTQH
     HRTAFAGATT GQQLLYALDE QVRRHEVAGL VTKYEGWDFL RAVVDDEGVC RGIVAQDLQT
     MEIKSFQADA VIMATGGPGI IFGKSTNSII NTGTAASAVY QQGAYYANGE FIQIHPTAIP
     GDDKLRLMSE SARGEGGRVW TYKDGKPWYF LEEKYPAYGN LVPRDIATRE IFDVCVEQKL
     GINGENMVYL DLSHKDPKEL DIKLGGIIEI YEKFTGDDPR KLPMKIFPAV HYSMGGLWVD
     YKQMTSIPGL FAAGECDYSM HGGNRLGANS LLSAIYGGMV AGPNAIEYMK GLSKSSDAVA
     STVYEQNELI ETEKFNNILM LDGNENAYVL HKELGEWMTD NVTVVRENKK LLETDAKIEE
     LMARYKRINI NDTARWSNQG ASFTRQLANM FELARVITIG AYNRNESRGA HYKPEFPNRD
     DANFLKTTMA KFEGEGKAPA FHYEEVDVSL IKPRKRDYSS KHDVAAKGEE KGDKQHV
//
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