ID A0A1E7DM81_9BACI Unreviewed; 202 AA.
AC A0A1E7DM81;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:OES44190.1};
GN ORFNames=BA724_07820 {ECO:0000313|EMBL:OES44190.1};
OS Domibacillus iocasae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714016 {ECO:0000313|EMBL:OES44190.1, ECO:0000313|Proteomes:UP000095658};
RN [1] {ECO:0000313|EMBL:OES44190.1, ECO:0000313|Proteomes:UP000095658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29979 {ECO:0000313|EMBL:OES44190.1,
RC ECO:0000313|Proteomes:UP000095658};
RA Verma A., Pal Y., Ojha A.K., Krishnamurthi S.;
RT "Domibacillus iocasae genome sequencing.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:OES44190.1}.
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; MAMP01000022; OES44190.1; -; Genomic_DNA.
DR RefSeq; WP_069939234.1; NZ_MAMP01000022.1.
DR AlphaFoldDB; A0A1E7DM81; -.
DR STRING; 1714016.BA724_07820; -.
DR OrthoDB; 9789209at2; -.
DR Proteomes; UP000095658; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd03497; SQR_TypeB_1_TM; 1.
DR Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR InterPro; IPR011138; Cytochrome_b-558.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR016002; Succ_DH_cyt_b558_Firmicute.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR NCBIfam; TIGR02046; sdhC_b558_fam; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000170; Succ_dh_cyt_b558; 1.
DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000170-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000170-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000170-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095658};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 28
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000170-1"
FT BINDING 70
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000170-1"
FT BINDING 113
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000170-1"
FT BINDING 155
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000170-1"
SQ SEQUENCE 202 AA; 23057 MW; 2A680B772C447FE1 CRC64;
MADNREFFYR RLHSLLGVIP VGLFMTQHLV VNHFATKGEE AFNQAAGFMA SLPFVLVLET
FIIFLPLLFH AIYGLYIAFT AKNNVGRYGY FRNWMFVLQR WSGVVTLIFV AWHVWETRVQ
AALGAEVNFQ MMENILGNPF MLVFYIVGVL AAIFHFANGL WSFCVSWGIA VSPRSQQIVT
YATLFVFFAL SIIGLRAIFA FV
//