(data stored in SCRATCH9089 zone)

SWISSPROT: FRDD_PASMU

ID   FRDD_PASMU              Reviewed;         116 AA.
AC   Q9CP59;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 93.
DE   RecName: Full=Fumarate reductase subunit D {ECO:0000255|HAMAP-Rule:MF_00709};
GN   Name=frdD {ECO:0000255|HAMAP-Rule:MF_00709}; OrderedLocusNames=PM0198;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Seems to be involved in the anchoring of the catalytic
CC       components of the fumarate reductase complex to the cytoplasmic
CC       membrane. {ECO:0000255|HAMAP-Rule:MF_00709}.
CC   -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC       flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two hydrophobic
CC       anchor proteins (FrdC and FrdD). {ECO:0000255|HAMAP-Rule:MF_00709}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00709}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00709}.
CC   -!- SIMILARITY: Belongs to the FrdD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00709}.
DR   EMBL; AE004439; AAK02282.1; -; Genomic_DNA.
DR   RefSeq; WP_005720690.1; NC_002663.1.
DR   SMR; Q9CP59; -.
DR   EnsemblBacteria; AAK02282; AAK02282; PM0198.
DR   GeneID; 29387678; -.
DR   KEGG; pmu:PM0198; -.
DR   eggNOG; ENOG4108VP9; Bacteria.
DR   eggNOG; COG3080; LUCA.
DR   HOGENOM; HOG000281495; -.
DR   KO; K00247; -.
DR   OMA; GMWSAIV; -.
DR   BioCyc; PMUL272843:G1FZ8-206-MONOMER; -.
DR   Proteomes; UP000000809; Chromosome.
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:0006106; P:fumarate metabolic process; IEA:InterPro.
DR   CDD; cd00547; QFR_TypeD_subunitD; 1.
DR   Gene3D; 1.20.1300.10; -; 1.
DR   HAMAP; MF_00709; Fumarate_red_D; 1.
DR   InterPro; IPR003418; Fumarate_red_D.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   Pfam; PF02313; Fumarate_red_D; 1.
DR   PIRSF; PIRSF000179; FrdD; 1.
DR   SUPFAM; SSF81343; SSF81343; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CP59.
DR   SWISS-2DPAGE; Q9CP59.
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..116
FT                   /note="Fumarate reductase subunit D"
FT                   /id="PRO_0000196549"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00709"
SQ   SEQUENCE   116 AA;  12947 MW;  B4458E54E5B61913 CRC64;
     MKDTPKRSNE PVVWLLFGAG TTVSAMFYPV LVLILGFLLP FGLIDPKNII ELIGFLHSPL
     GKLLLLVLLI FPMWGAMHRI HHGMHDFKIH IPASGVIFYG LSVLYTVLVC FAVFSL
//

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