ID A0A0C2EEP0_9PSED Unreviewed; 122 AA.
AC A0A0C2EEP0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit {ECO:0000256|ARBA:ARBA00019425, ECO:0000256|PIRNR:PIRNR000169};
GN ORFNames=UCMB321_1675 {ECO:0000313|EMBL:KIH84444.1};
OS Pseudomonas batumici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=226910 {ECO:0000313|EMBL:KIH84444.1, ECO:0000313|Proteomes:UP000031535};
RN [1] {ECO:0000313|EMBL:KIH84444.1, ECO:0000313|Proteomes:UP000031535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCM B-321 {ECO:0000313|EMBL:KIH84444.1,
RC ECO:0000313|Proteomes:UP000031535};
RA Klochko V.V., Zelena L.B., Elena K.A., Reva O.N.;
RT "Complete genome of Pseudomonas batumici UCM B-321 producer of the batumin
RT antibiotic with strong antistaphilococcal and potential anticancer
RT activity.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC {ECO:0000256|ARBA:ARBA00004050, ECO:0000256|PIRNR:PIRNR000169}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR000169-2};
CC Note=The heme is bound between the two transmembrane subunits.
CC {ECO:0000256|PIRSR:PIRSR000169-2};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC {ECO:0000256|ARBA:ARBA00005163, ECO:0000256|PIRNR:PIRNR000169}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|PIRNR:PIRNR000169}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC ECO:0000256|PIRNR:PIRNR000169}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:KIH84444.1}.
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DR EMBL; JXDG01000018; KIH84444.1; -; Genomic_DNA.
DR RefSeq; WP_040065287.1; NZ_JXDG01000018.1.
DR AlphaFoldDB; A0A0C2EEP0; -.
DR STRING; 226910.UCMB321_1675; -.
DR PATRIC; fig|226910.6.peg.1665; -.
DR OrthoDB; 5612767at2; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000031535; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR CDD; cd03494; SQR_TypeC_SdhD; 1.
DR Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR014312; Succ_DH_anchor.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR NCBIfam; TIGR02968; succ_dehyd_anc; 1.
DR PANTHER; PTHR38689; SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR SUBUNIT; 1.
DR PANTHER; PTHR38689:SF1; SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR SUBUNIT; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000169; SDH_D; 1.
DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|PIRNR:PIRNR000169};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR000169};
KW Electron transport {ECO:0000256|PIRNR:PIRNR000169};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000169-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000169-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000169};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000169-2};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR000169};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000169}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 71
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:PIRSR000169-2"
FT BINDING 83
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000256|PIRSR:PIRSR000169-1"
SQ SEQUENCE 122 AA; 13474 MW; DE15740D7EA18495 CRC64;
MVTNVTNLSR SGLYDWMAQR VSAVVLAAYF IFLIGYVIAN PGLGYAQWHG LFAHSGMRIF
SLLALVALGA HAWVGMWTIA TDYLTPMAFG KSATVVRFLF QVVCGVAMFA YFVWGVQILW
GI
//
