ID A3MVZ1_PYRCJ Unreviewed; 580 AA.
AC A3MVZ1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN OrderedLocusNames=Pcal_1388 {ECO:0000313|EMBL:ABO08808.1};
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359 {ECO:0000313|EMBL:ABO08808.1, ECO:0000313|Proteomes:UP000001431};
RN [1] {ECO:0000313|EMBL:ABO08808.1, ECO:0000313|Proteomes:UP000001431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1
RC {ECO:0000313|Proteomes:UP000001431};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) 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}.
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DR EMBL; CP000561; ABO08808.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MVZ1; -.
DR STRING; 410359.Pcal_1388; -.
DR KEGG; pcl:Pcal_1388; -.
DR eggNOG; arCOG00571; Archaea.
DR HOGENOM; CLU_014312_6_2_2; -.
DR OrthoDB; 23539at2157; -.
DR Proteomes; UP000001431; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 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 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:ABO08808.1}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 7..396
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 455..580
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 580 AA; 63349 MW; AFB0B247C932FFE0 CRC64;
MEVLSCDVVV VGSGLAGLRA AVAAAAASEK LSICVVTKVA GPRSHTISAE GGMAAVVHPE
KTGDTPHLHA YDTVKGGDFL VDQDAAMLLA QEAPSEALFL YKIGVPWNKD SDGTFSLRLF
GGMSKPRTLF VKDKTGFYIL TALYKHAKSF SNIAFYEEHL VTKLVVKHNV FYGVTALDMR
RGEFKFFKAK AGVIATGGGG RMFKLTTMGY LNTGEVYGFA LREGIALKDM EFVQWHPTAL
VPSGILISEA ARAEGAYLVN KYGERFMRRY APQKMELAPR DVIARAIAME CMSGRGFTWR
DGTCYVGLDV RHLDPARVKE RLPLLLELSK TYAGVDPFTE LIPVAPAVHY FMGGIHTDLY
GRVLTVSGEW VRGLWAAGEA AAVSVHGANR LGSNSLAECA VWGRLAGEQA AEYAKGRGEG
EADGAVKALV EREENRVFYK LGRKEVGGTS AAAIRSALQN AMHKGAGIIR EESALAQALS
EVAKLISAFK EVNLHDTGRI YNMELREMVE LDGMLLAAHA VLLGAYFRRE SRGAHYRVDH
PQRDDKTWLK HTLVHKVGEG FGVYYAPVKV DKWPPEVRAY
//
