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ETFB_PARDE
ID   ETFB_PARDE              Reviewed;         252 AA.
AC   P38975;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Electron transfer flavoprotein subunit beta;
DE            Short=Beta-ETF;
DE   AltName: Full=Electron transfer flavoprotein small subunit;
DE            Short=ETFSS;
GN   Name=etfB;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-7.
RC   STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX   PubMed=8376381; DOI=10.1016/s0021-9258(20)80716-9;
RA   Bedzyk L.A., Escudero K.W., Gill R.E., Griffin K.J., Frerman F.E.;
RT   "Cloning, sequencing, and expression of the genes encoding subunits of
RT   Paracoccus denitrificans electron transfer flavoprotein.";
RL   J. Biol. Chem. 268:20211-20217(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-23; 33-51; 74-82; 163-183 AND 189-197.
RC   STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX   PubMed=1576992; DOI=10.1111/j.1432-1033.1992.tb16877.x;
RA   Watmough N.J., Kiss J., Frerman F.E.;
RT   "Structural and redox relationships between Paracoccus denitrificans,
RT   porcine and human electron-transferring flavoproteins.";
RL   Eur. J. Biochem. 205:1089-1097(1992).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=10026281; DOI=10.1021/bi9820917;
RA   Roberts D.L., Salazar D., Fulmer J.P., Frerman F.E., Kim J.-J.P.;
RT   "Crystal structure of Paracoccus denitrificans electron transfer
RT   flavoprotein: structural and electrostatic analysis of a conserved flavin
RT   binding domain.";
RL   Biochemistry 38:1977-1989(1999).
CC   -!- FUNCTION: The electron transfer flavoprotein serves as a specific
CC       electron acceptor for other dehydrogenases. It transfers the electrons
CC       to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF
CC       dehydrogenase).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=Binds 1 FAD per dimer.;
CC   -!- COFACTOR:
CC       Name=AMP; Xref=ChEBI:CHEBI:456215;
CC       Note=Binds 1 AMP per subunit.;
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC   -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family. {ECO:0000305}.
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DR   EMBL; L14864; AAA03071.1; -; Unassigned_DNA.
DR   PIR; A48008; A48008.
DR   PDB; 1EFP; X-ray; 2.60 A; B/D=1-252.
DR   PDBsum; 1EFP; -.
DR   AlphaFoldDB; P38975; -.
DR   SMR; P38975; -.
DR   DIP; DIP-6158N; -.
DR   IntAct; P38975; 1.
DR   PRIDE; P38975; -.
DR   EvolutionaryTrace; P38975; -.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   CDD; cd01714; ETF_beta; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR000049; ET-Flavoprotein_bsu_CS.
DR   InterPro; IPR014730; ETF_a/b_N.
DR   InterPro; IPR012255; ETF_b.
DR   InterPro; IPR033948; ETF_beta_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR21294; PTHR21294; 1.
DR   Pfam; PF01012; ETF; 1.
DR   PIRSF; PIRSF000090; Beta-ETF; 1.
DR   SMART; SM00893; ETF; 1.
DR   PROSITE; PS01065; ETF_BETA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport; FAD;
KW   Flavoprotein; Transport.
FT   CHAIN           1..252
FT                   /note="Electron transfer flavoprotein subunit beta"
FT                   /id="PRO_0000167884"
FT   CONFLICT        10
FT                   /note="L -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="G -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="V -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="Q -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   HELIX           37..50
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   TURN            51..53
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   STRAND          56..65
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   HELIX           69..78
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   STRAND          81..87
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   HELIX           98..112
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   STRAND          115..121
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   HELIX           131..139
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   STRAND          142..152
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   STRAND          154..163
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   STRAND          166..180
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   HELIX           192..198
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   STRAND          203..207
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   HELIX           208..211
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   STRAND          218..225
FT                   /evidence="ECO:0007829|PDB:1EFP"
FT   HELIX           239..243
FT                   /evidence="ECO:0007829|PDB:1EFP"
SQ   SEQUENCE   252 AA;  26673 MW;  00C43128BEA1EDED CRC64;
     MKVLVPVKRL IDYNVKARVK SDGSGVDLAN VKMSMNPFDE IAVEEAIRLK EKGQAEEIIA
     VSIGVKQAAE TLRTALAMGA DRAILVVAAD DVQQDIEPLA VAKILAAVAR AEGTELIIAG
     KQAIDNDMNA TGQMLAAILG WAQATFASKV EIEGAKAKVT REVDGGLQTI AVSLPAVVTA
     DLRLNEPRYA SLPNIMKAKK KPLDEKTAAD YGVDVAPRLE VVSVREPEGR KAGIKVGSVD
     ELVGKLKEAG VI
 
 
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