RUBR_PYRFU
ID RUBR_PYRFU Reviewed; 54 AA.
AC P24297; Q9UWP6;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Rubredoxin;
DE Short=Rd;
GN Name=rub; OrderedLocusNames=PF1282;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10514376; DOI=10.1126/science.286.5438.306;
RA Jenney F.E. Jr., Verhagen M.F.J.M., Cui X., Adams M.W.W.;
RT "Anaerobic microbes: oxygen detoxification without superoxide dismutase.";
RL Science 286:306-309(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP PROTEIN SEQUENCE OF 2-54.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=1932012; DOI=10.1021/bi00109a012;
RA Blake P.R., Park J.-B., Bryant F.O., Aono S., Magnuson J.K., Eccleston E.,
RA Howard J.B., Summers M.F., Adams M.W.W.;
RT "Determinants of protein hyperthermostability: purification and amino acid
RT sequence of rubredoxin from the hyperthermophilic archaebacterium
RT Pyrococcus furiosus and secondary structure of the zinc adduct by NMR.";
RL Biochemistry 30:10885-10895(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=1303768; DOI=10.1002/pro.5560011111;
RA Day M.W., Hsu B.T., Joshua-Tor L., Park J.-B., Zhou Z.H., Adams M.W.W.,
RA Rees D.C.;
RT "X-ray crystal structures of the oxidized and reduced forms of the
RT rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus
RT furiosus.";
RL Protein Sci. 1:1494-1507(1992).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=1303769; DOI=10.1002/pro.5560011112;
RA Blake P.R., Park J.-B., Zhou Z.H., Hare D.R., Adams M.W.W., Summers M.F.;
RT "Solution-state structure by NMR of zinc-substituted rubredoxin from the
RT marine hyperthermophilic archaebacterium Pyrococcus furiosus.";
RL Protein Sci. 1:1508-1521(1992).
RN [6]
RP COMPARISON OF NMR STRUCTURE WITH X-RAY STRUCTURE.
RX PubMed=1303770; DOI=10.1002/pro.5560011113;
RA Blake P.R., Day M.W., Hsu B.T., Joshua-Tor L., Park J.-B., Hare D.R.,
RA Adams M.W.W., Rees D.C., Summers M.F.;
RT "Comparison of the X-ray structure of native rubredoxin from Pyrococcus
RT furiosus with the NMR structure of the zinc-substituted protein.";
RL Protein Sci. 1:1522-1525(1992).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
RA Bau R., Rees D.C., Kurtz D.M. Jr., Scott R.A., Huang H., Adams M.W.W.,
RA Eidsness M.K.;
RT "Crystal structure of rubredoxin from Pyrococcus furiosus at 0.95-A
RT resolution, and the structures of N-terminal methionine and
RT formylmethionine variants of Pf Rd. Contributions of N-terminal
RT interactions to thermostability.";
RL J. Biol. Inorg. Chem. 3:484-493(1998).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=10684603; DOI=10.1021/bi992257j;
RA Strop P., Mayo S.L.;
RT "Contribution of surface salt bridges to protein stability.";
RL Biochemistry 39:1251-1255(2000).
CC -!- FUNCTION: Rubredoxin is a small nonheme, iron protein lacking acid-
CC labile sulfide. Its single Fe, chelated to 4 Cys, functions as an
CC electron acceptor and may also stabilize the conformation of the
CC molecule.
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Note=Binds 1 Fe(3+) ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Extremely thermostable, being unaffected after incubation for 24
CC hours at 95 degrees Celsius.;
CC -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
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DR EMBL; AF156097; AAF03228.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81406.1; -; Genomic_DNA.
DR PIR; T44570; RUPF.
DR RefSeq; WP_011012426.1; NC_018092.1.
DR PDB; 1BQ8; X-ray; 1.10 A; A=1-54.
DR PDB; 1BQ9; X-ray; 1.20 A; A=1-54.
DR PDB; 1BRF; X-ray; 0.95 A; A=2-54.
DR PDB; 1CAA; X-ray; 1.80 A; A=2-54.
DR PDB; 1CAD; X-ray; 1.80 A; A=2-54.
DR PDB; 1IU5; X-ray; 1.50 A; A=2-54.
DR PDB; 1IU6; Neutron; 1.60 A; A=2-54.
DR PDB; 1QCV; NMR; -; A=2-54.
DR PDB; 1RWD; NMR; -; A=2-54.
DR PDB; 1VCX; Neutron; 1.50 A; A=2-54.
DR PDB; 1ZRP; NMR; -; A=2-54.
DR PDB; 2PVX; X-ray; 1.04 A; A/B/C/D/E/F/G/H=1-54.
DR PDB; 3KYU; X-ray; 1.10 A; A=1-54.
DR PDB; 3KYV; X-ray; 1.10 A; A=1-54.
DR PDB; 3KYW; X-ray; 1.10 A; A=1-54.
DR PDB; 3KYX; Other; 1.68 A; A=1-54.
DR PDB; 3KYY; X-ray; 1.10 A; A=1-54.
DR PDB; 3RYG; Neutron; 1.75 A; A=1-54.
DR PDB; 3RZ6; Neutron; 1.75 A; A=1-54.
DR PDB; 3RZT; Neutron; 1.75 A; A=1-54.
DR PDB; 3SS2; Neutron; 1.75 A; A=1-54.
DR PDB; 4AR3; Neutron; 1.05 A; A=1-54.
DR PDB; 4AR4; Neutron; 1.38 A; A=1-54.
DR PDB; 4AR5; X-ray; 1.00 A; A=1-54.
DR PDB; 4AR6; X-ray; 0.92 A; A=1-54.
DR PDB; 4K9F; Neutron; 1.75 A; A=1-54.
DR PDB; 5AI2; Neutron; 1.75 A; A=1-54.
DR PDB; 5AI3; X-ray; 1.02 A; A=1-54.
DR PDB; 5NW3; X-ray; 0.59 A; A=1-54.
DR PDB; 5OME; X-ray; 0.75 A; A=1-54.
DR PDBsum; 1BQ8; -.
DR PDBsum; 1BQ9; -.
DR PDBsum; 1BRF; -.
DR PDBsum; 1CAA; -.
DR PDBsum; 1CAD; -.
DR PDBsum; 1IU5; -.
DR PDBsum; 1IU6; -.
DR PDBsum; 1QCV; -.
DR PDBsum; 1RWD; -.
DR PDBsum; 1VCX; -.
DR PDBsum; 1ZRP; -.
DR PDBsum; 2PVX; -.
DR PDBsum; 3KYU; -.
DR PDBsum; 3KYV; -.
DR PDBsum; 3KYW; -.
DR PDBsum; 3KYX; -.
DR PDBsum; 3KYY; -.
DR PDBsum; 3RYG; -.
DR PDBsum; 3RZ6; -.
DR PDBsum; 3RZT; -.
DR PDBsum; 3SS2; -.
DR PDBsum; 4AR3; -.
DR PDBsum; 4AR4; -.
DR PDBsum; 4AR5; -.
DR PDBsum; 4AR6; -.
DR PDBsum; 4K9F; -.
DR PDBsum; 5AI2; -.
DR PDBsum; 5AI3; -.
DR PDBsum; 5NW3; -.
DR PDBsum; 5OME; -.
DR AlphaFoldDB; P24297; -.
DR BMRB; P24297; -.
DR SMR; P24297; -.
DR STRING; 186497.PF1282; -.
DR PRIDE; P24297; -.
DR EnsemblBacteria; AAL81406; AAL81406; PF1282.
DR GeneID; 41713086; -.
DR KEGG; pfu:PF1282; -.
DR PATRIC; fig|186497.12.peg.1345; -.
DR eggNOG; arCOG04391; Archaea.
DR HOGENOM; CLU_128747_3_3_2; -.
DR OMA; MSAYRCP; -.
DR OrthoDB; 126197at2157; -.
DR PhylomeDB; P24297; -.
DR EvolutionaryTrace; P24297; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd00730; rubredoxin; 1.
DR InterPro; IPR024922; Rubredoxin.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR024935; Rubredoxin_dom.
DR InterPro; IPR018527; Rubredoxin_Fe_BS.
DR Pfam; PF00301; Rubredoxin; 1.
DR PIRSF; PIRSF000071; Rubredoxin; 1.
DR PRINTS; PR00163; RUBREDOXIN.
DR PROSITE; PS00202; RUBREDOXIN; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Iron;
KW Metal-binding; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1932012"
FT CHAIN 2..54
FT /note="Rubredoxin"
FT /id="PRO_0000135063"
FT DOMAIN 2..52
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 6
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 9
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 39
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 42
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:5NW3"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:5NW3"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:5NW3"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:5NW3"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:5NW3"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:5NW3"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:5NW3"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:5NW3"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:5NW3"
SQ SEQUENCE 54 AA; 6027 MW; 7181BBB4A3E8B1A8 CRC64;
MAKWVCKICG YIYDEDAGDP DNGISPGTKF EELPDDWVCP ICGAPKSEFE KLED
