ID A0A1M5XCI0_9GAMM Unreviewed; 228 AA.
AC A0A1M5XCI0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Succinate dehydrogenase subunit C {ECO:0000313|EMBL:SHH97234.1};
GN ORFNames=SAMN02745129_3416 {ECO:0000313|EMBL:SHH97234.1};
OS Ferrimonas marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Ferrimonadaceae; Ferrimonas.
OX NCBI_TaxID=299255 {ECO:0000313|EMBL:SHH97234.1, ECO:0000313|Proteomes:UP000184268};
RN [1] {ECO:0000313|EMBL:SHH97234.1, ECO:0000313|Proteomes:UP000184268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16917 {ECO:0000313|EMBL:SHH97234.1,
RC ECO:0000313|Proteomes:UP000184268};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC {ECO:0000256|ARBA:ARBA00004050}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
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DR EMBL; FQXG01000005; SHH97234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5XCI0; -.
DR STRING; 299255.SAMN02745129_3416; -.
DR OrthoDB; 9153108at2; -.
DR Proteomes; UP000184268; 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 GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR InterPro; IPR004224; Fum_red_B_TM.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000177; Fumar_rd_cyt_b; 1.
DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000177-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000177-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000177-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184268};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 32
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bD"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000177-1"
FT BINDING 83
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bD"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000177-1"
FT BINDING 133
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bD"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000177-1"
FT BINDING 172
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bD"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000177-1"
SQ SEQUENCE 228 AA; 25552 MW; BA8A64529DB4840D CRC64;
MRKLLEWSRG PARMDILQGA SGAALTLFLF VHLHMEASVL LGPDAFDKVA WFLHAGWADP
AGHGYAGMVM LAVLFITLLL LIHVVAVLRR FPTEYRQMKA LQQHMSIVQH AGTRLWLVQV
LTGVAMMILI PIHLVTMLTQ PHSLGAEPSS YRIVYEGGWL LYGLLLPVSV IHGLAGIARL
WLKWCPYAEP RFQGRRWMRR VAVYLMVLGV VSLLMHVYNG LFVFGGSA
//
