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Database: UniProt
Entry: A0A1Q4WIQ0_9ACTN
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ID   A0A1Q4WIQ0_9ACTN        Unreviewed;       114 AA.
AC   A0A1Q4WIQ0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Succinate dehydrogenase, cytochrome b556 subunit {ECO:0000313|EMBL:OKI09877.1};
GN   ORFNames=A6A06_04390 {ECO:0000313|EMBL:OKI09877.1};
OS   Streptomyces sp. CB02923.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI09877.1, ECO:0000313|Proteomes:UP000185893};
RN   [1] {ECO:0000313|EMBL:OKI09877.1, ECO:0000313|Proteomes:UP000185893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02923 {ECO:0000313|EMBL:OKI09877.1,
RC   ECO:0000313|Proteomes:UP000185893};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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   -!- 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:OKI09877.1}.
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DR   EMBL; LWKZ01000001; OKI09877.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4WIQ0; -.
DR   STRING; 1718985.A6A06_04390; -.
DR   Proteomes; UP000185893; 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; cd03501; SQR_TypeA_SdhC_like; 1.
DR   Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR   InterPro; IPR039023; SdhC_prok.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   InterPro; IPR014314; Succ_DH_cytb556.
DR   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   NCBIfam; TIGR02970; succ_dehyd_cytB; 1.
DR   PANTHER; PTHR41910; SUCCINATE DEHYDROGENASE 2 MEMBRANE SUBUNIT SDHC; 1.
DR   PANTHER; PTHR41910:SF1; SUCCINATE DEHYDROGENASE 2 MEMBRANE SUBUNIT SDHC; 1.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   PIRSF; PIRSF000178; SDH_cyt_b560; 1.
DR   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 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:UP000185893};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        49..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         61
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   114 AA;  12899 MW;  429CABA15452B625 CRC64;
     MWSWVAHRVT GVLIFFFLFV HVLDTALVRV SPEAYDDVVA TYKTPLVNVM EYGLVAAILF
     HALNGLRVIA VDFWSKGPKY QKQLLWTVVG VWAVLMAGAF YPVLQHTLRT LFGS
//
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