ID A0A091B3I2_9GAMM Unreviewed; 120 AA.
AC A0A091B3I2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Succinate dehydrogenase cytochrome b556 subunit {ECO:0000256|ARBA:ARBA00020076};
GN ORFNames=N787_02355 {ECO:0000313|EMBL:KFN47163.1};
OS Arenimonas metalli CF5-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1384056 {ECO:0000313|EMBL:KFN47163.1, ECO:0000313|Proteomes:UP000029393};
RN [1] {ECO:0000313|EMBL:KFN47163.1, ECO:0000313|Proteomes:UP000029393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF5-1 {ECO:0000313|EMBL:KFN47163.1,
RC ECO:0000313|Proteomes:UP000029393};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas metalli.";
RL Submitted (SEP-2013) 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|PIRSR:PIRSR000178-1};
CC Note=The heme is bound between the two transmembrane subunits.
CC {ECO:0000256|PIRSR:PIRSR000178-1};
CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC flavoprotein, an iron-sulfur protein, plus two membrane-anchoring
CC proteins, SdhC and SdhD. The complex can form homotrimers.
CC {ECO:0000256|ARBA:ARBA00025912}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome b560 family.
CC {ECO:0000256|ARBA:ARBA00007244}.
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:KFN47163.1}.
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DR EMBL; AVCK01000012; KFN47163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091B3I2; -.
DR STRING; 1384056.N787_02355; -.
DR PATRIC; fig|1384056.3.peg.1084; -.
DR eggNOG; COG2009; Bacteria.
DR Proteomes; UP000029393; Unassembled WGS sequence.
DR GO; GO:0045281; C:succinate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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 CDD; cd03499; SQR_TypeC_SdhC; 1.
DR Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR018495; Succ_DH_cyt_bsu_CS.
DR InterPro; IPR014314; Succ_DH_cytb556.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR NCBIfam; TIGR02970; succ_dehyd_cytB; 1.
DR PANTHER; PTHR10978; SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT; 1.
DR PANTHER; PTHR10978:SF5; SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT, MITOCHONDRIAL; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000178; SDH_cyt_b560; 1.
DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
DR PROSITE; PS01001; SDH_CYT_2; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000178-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000178-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000178-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029393};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 72
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with second transmembrane
FT subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000178-1"
SQ SEQUENCE 120 AA; 12792 MW; 69C40064DFEA6524 CRC64;
MIGPYYRPQL TSMMSIAHRA TGVILALGSL VLAAWLVAAS ENAMIYDGFR GLLASLPGKV
ALFAFSASLV YHFLNGIRHL FWDAGHGFSI PKAYASGYAV LALSVVITAV LWWCGLGGMA
//
