ID D1BU41_XYLCX Unreviewed; 711 AA.
AC D1BU41;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN OrderedLocusNames=Xcel_0166 {ECO:0000313|EMBL:ACZ29205.1};
OS Xylanimonas cellulosilytica (strain DSM 15894 / CECT 5975 / LMG 20990 /
OS XIL07).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Xylanimonas.
OX NCBI_TaxID=446471 {ECO:0000313|EMBL:ACZ29205.1, ECO:0000313|Proteomes:UP000002255};
RN [1] {ECO:0000313|Proteomes:UP000002255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC {ECO:0000313|Proteomes:UP000002255};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Foster B., Clum A., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P.,
RA Woyke T., Wu D., Gehrich-Schroeter G., Schneider S., Pukall S.R.,
RA Klenk H.P., Eisen J.A.;
RT "The complete chromosome of Xylanimonas cellulosilytica DSM 15894.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ29205.1, ECO:0000313|Proteomes:UP000002255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC {ECO:0000313|Proteomes:UP000002255};
RX PubMed=21304672; DOI=10.4056/sigs.571102;
RA Foster B., Pukall R., Abt B., Nolan M., Glavina Del Rio T., Chen F.,
RA Lucas S., Tice H., Pitluck S., Cheng J.-F., Chertkov O., Brettin T.,
RA Han C., Detter J.C., Bruce D., Goodwin L., Ivanova N., Mavromatis K.,
RA Pati A., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C.D., Chain P., Rohde M., Goeker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.,
RA Lapidus A.;
RT "Complete genome sequence of Xylanimonas cellulosilytica type strain
RT (XIL07).";
RL Stand. Genomic Sci. 2:1-8(2010).
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 ECO:0000256|PIRSR:PIRSR630664-51};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
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DR EMBL; CP001821; ACZ29205.1; -; Genomic_DNA.
DR RefSeq; WP_012876950.1; NC_013530.1.
DR AlphaFoldDB; D1BU41; -.
DR STRING; 446471.Xcel_0166; -.
DR KEGG; xce:Xcel_0166; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_2_11; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000002255; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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:SF82; FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR Pfam; PF00890; FAD_binding_2; 2.
DR Pfam; PF02910; Succ_DH_flav_C; 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, ECO:0000256|PIRSR:PIRSR630664-51};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR630664-
KW 51}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACZ29205.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002255};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 7..177
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 213..451
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 533..642
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 185..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..675
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 42..57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 260
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 434
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 445
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 450..451
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
SQ SEQUENCE 711 AA; 73730 MW; 296D750B0EA7391B CRC64;
MRVDHADVVV VGGGAAGLSA ALAAVESFAA AGREDAVVAL VSKVYPMRSH TVAAEGGAAG
VVPGGVDTAE QHVADTLAGG AGLGHDDAVR FVVDRAPAEL ARMERLGMPW SRADDGAPAV
RRFGGMTNPR TWFAADKTGF HLLHTLFQTS LREETIRRYD EHIVLDLLLT DPVVEPVETT
TATTPPVVEP VETTPHGGPA PLPVVEPVET TRPRQVRGVV AYDQQRGEPV TLIAPAVVLA
TGGYARAWGT STNAGIVTGD GLSMALRAGL PLRDLEMVQV HPTCLPGSGI LITEAARGEG
GVLLDADGAR YLADYGLGPE TPVGAPVARR MELGPRDKLS QAFWHADRAG RTIPTRDGGV
VHLDLRHLGK AVIDERLPLV AGLARRFAGV DPVTTPIPVR PAAHYTMGGI VTTPQGQVLD
AAGAAVTGLF AAGECASTGL HGANRLGSNS LVETLVVGRA AGTLAAVSGA RTPSPTPGLS
DAPEDGDLRA SDNPGGVGRA SREQARIVEQ ARALAERWLG MRGRGTESPA AIRRELGAVL
DAEVGIFRDA DGLARAAAVL DDLAERYRDV RVADTAAVFN TDWTQALELG AMLDIARGAV
AAAIGRTESR GAHQRLDHPQ TDDVARHSLV TLDANGAITV TWPPAAEPAP AAEPPSVVEP
PPVVEPPPVV EPVETTPRPP AVAAAAPVVE PVETTPAARP ARPARTSEAR P
//
