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DHSD_NATPH
ID   DHSD_NATPH              Reviewed;         130 AA.
AC   P72109;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit;
GN   Name=sdhD; Synonyms=sdhC;
OS   Natronomonas pharaonis (Natronobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=2257;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SP-1 / 28;
RA   Mattar S., Souquet M., Henrich H.J., Engelhard M.;
RT   "The first fully resolved primary structure of an archaeal succinate-
RT   dehydrogenase from Natronobacterium pharaonis.";
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=The heme is bound between the two transmembrane subunits.
CC       {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; Y07709; CAA68979.1; -; Genomic_DNA.
DR   PIR; T44959; T44959.
DR   RefSeq; WP_011323842.1; NC_007426.1.
DR   AlphaFoldDB; P72109; -.
DR   SMR; P72109; -.
DR   GeneID; 3703197; -.
DR   OMA; AGMWAWI; -.
DR   UniPathway; UPA00223; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.1300.10; -; 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   PANTHER; PTHR41910; PTHR41910; 1.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   SUPFAM; SSF81343; SSF81343; 1.
DR   TIGRFAMs; TIGR02970; succ_dehyd_cytB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Transmembrane; Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT   CHAIN           1..130
FT                   /note="Succinate dehydrogenase hydrophobic membrane anchor
FT                   subunit"
FT                   /id="PRO_0000158681"
FT   TOPO_DOM        1..25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..71
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..103
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         84
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:0000250"
SQ   SEQUENCE   130 AA;  14309 MW;  42361990C9B978B5 CRC64;
     MSQSYDRGLV EDFGRWQEFS AGMWAWIFHK FTGWVLIGYL FTHVAVLSTA TVDAATYTQT
     LQGLESLLVV RFLEVGLLAV AVFHILNGIR LLFVDLGVGL EAQDKAFYAA LIVTAAITVA
     SIPTFLMGAF
 
 
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