RUBR_CLOPA
ID RUBR_CLOPA Reviewed; 54 AA.
AC P00268;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Rubredoxin;
DE Short=Rd;
OS Clostridium pasteurianum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1501;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FORMYLATION AT MET-1, AND PARTIAL
RP PROTEIN SEQUENCE.
RX PubMed=1637309; DOI=10.1042/bj2850255;
RA Mathieu I., Meyer J., Moulis J.-M.;
RT "Cloning, sequencing and expression in Escherichia coli of the rubredoxin
RT gene from Clostridium pasteurianum.";
RL Biochem. J. 285:255-262(1992).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE.
RA McCarthy K.F.;
RL Thesis (1972), George Washington University, United States.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RA Watenpaugh K.D., Siecker L.C., Herriott J.R., Jensen L.H.;
RT "Refinement of the model of a protein, rubredoxin at 1.5-A resolution.";
RL Acta Crystallogr. B 29:943-956(1973).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
RX PubMed=7411618; DOI=10.1016/s0022-2836(80)80020-9;
RA Watenpaugh K.D., Siecker L.C., Jensen L.H.;
RT "Crystallographic refinement of rubredoxin at 1.2-A resolution.";
RL J. Mol. Biol. 138:615-633(1980).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=10216292; DOI=10.1107/s0907444999001900;
RA Maher M.J., Xiao Z., Wilce M.C., Guss J.M., Wedd A.G.;
RT "Rubredoxin from Clostridium pasteurianum. Structures of G10A, G43A and
RT G10VG43A mutant proteins. Mutation of conserved glycine 10 to valine causes
RT the 9-10 peptide link to invert.";
RL Acta Crystallogr. D 55:962-968(1999).
RN [6] {ECO:0007744|PDB:6BD4}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RX PubMed=30135577; DOI=10.1038/s41586-018-0447-x;
RA Yang S., Wu Y., Xu T.H., de Waal P.W., He Y., Pu M., Chen Y.,
RA DeBruine Z.J., Zhang B., Zaidi S.A., Popov P., Guo Y., Han G.W., Lu Y.,
RA Suino-Powell K., Dong S., Harikumar K.G., Miller L.J., Katritch V.,
RA Xu H.E., Shui W., Stevens R.C., Melcher K., Zhao S., Xu F.;
RT "Crystal structure of the Frizzled 4 receptor in a ligand-free state.";
RL Nature 560:666-670(2018).
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 -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
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DR EMBL; M60116; AAA23279.1; -; Genomic_DNA.
DR PIR; S29120; RUCLEP.
DR RefSeq; WP_003447684.1; NZ_LFYL01000002.1.
DR PDB; 1B13; X-ray; 1.50 A; A=1-54.
DR PDB; 1B2J; X-ray; 1.60 A; A=1-54.
DR PDB; 1B2O; X-ray; 1.90 A; A/B=1-54.
DR PDB; 1BE7; X-ray; 1.65 A; A=1-54.
DR PDB; 1BFY; NMR; -; A=1-54.
DR PDB; 1C09; X-ray; 1.60 A; A/B/C=1-54.
DR PDB; 1FHH; X-ray; 1.50 A; A=1-54.
DR PDB; 1FHM; X-ray; 1.50 A; A=1-54.
DR PDB; 1IRN; X-ray; 1.20 A; A=1-54.
DR PDB; 1IRO; X-ray; 1.10 A; A=1-54.
DR PDB; 1R0F; X-ray; 1.60 A; A=1-54.
DR PDB; 1R0G; X-ray; 1.60 A; A=1-54.
DR PDB; 1R0H; X-ray; 1.70 A; A=1-54.
DR PDB; 1R0I; X-ray; 1.50 A; A=1-54.
DR PDB; 1R0J; X-ray; 2.00 A; A=1-54.
DR PDB; 1SMM; X-ray; 1.36 A; A=1-54.
DR PDB; 1SMU; X-ray; 1.43 A; A=1-54.
DR PDB; 1SMW; X-ray; 1.38 A; A=1-54.
DR PDB; 1T9O; X-ray; 2.00 A; A/B/C=1-54.
DR PDB; 1T9P; X-ray; 1.50 A; A/B/C=1-54.
DR PDB; 1T9Q; X-ray; 1.80 A; A=1-54.
DR PDB; 2PVE; X-ray; 0.79 A; A/B/C=1-54.
DR PDB; 4MBS; X-ray; 2.71 A; A/B=1-54.
DR PDB; 4RXN; X-ray; 1.20 A; A=1-54.
DR PDB; 4XNV; X-ray; 2.20 A; A=1-54.
DR PDB; 4XNW; X-ray; 2.70 A; A/C=1-54.
DR PDB; 5RXN; X-ray; 1.20 A; A=1-54.
DR PDB; 5UIW; X-ray; 2.20 A; A=1-54.
DR PDB; 5VBL; X-ray; 2.60 A; B=1-54.
DR PDB; 6AKX; X-ray; 2.80 A; A/B=1-54.
DR PDB; 6AKY; X-ray; 2.80 A; A=1-54.
DR PDB; 6BD4; X-ray; 2.40 A; A=1-54.
DR PDB; 6GPS; X-ray; 3.30 A; A=1-54.
DR PDB; 6GPX; X-ray; 2.70 A; A/B=1-54.
DR PDB; 6IIU; X-ray; 2.50 A; A=1-54.
DR PDB; 6IIV; X-ray; 3.00 A; A=1-54.
DR PDB; 6KNM; X-ray; 3.20 A; B=1-54.
DR PDB; 6LI2; X-ray; 2.80 A; A=2-54.
DR PDB; 6LN2; X-ray; 3.20 A; A=1-54.
DR PDB; 6ME6; X-ray; 2.80 A; A/B=1-53.
DR PDB; 6ME7; X-ray; 3.20 A; A/B=1-53.
DR PDB; 6ME8; X-ray; 3.10 A; A/B=1-53.
DR PDB; 6ME9; X-ray; 3.30 A; A/B=1-53.
DR PDB; 7F1T; X-ray; 2.60 A; A=1-54.
DR PDBsum; 1B13; -.
DR PDBsum; 1B2J; -.
DR PDBsum; 1B2O; -.
DR PDBsum; 1BE7; -.
DR PDBsum; 1BFY; -.
DR PDBsum; 1C09; -.
DR PDBsum; 1FHH; -.
DR PDBsum; 1FHM; -.
DR PDBsum; 1IRN; -.
DR PDBsum; 1IRO; -.
DR PDBsum; 1R0F; -.
DR PDBsum; 1R0G; -.
DR PDBsum; 1R0H; -.
DR PDBsum; 1R0I; -.
DR PDBsum; 1R0J; -.
DR PDBsum; 1SMM; -.
DR PDBsum; 1SMU; -.
DR PDBsum; 1SMW; -.
DR PDBsum; 1T9O; -.
DR PDBsum; 1T9P; -.
DR PDBsum; 1T9Q; -.
DR PDBsum; 2PVE; -.
DR PDBsum; 4MBS; -.
DR PDBsum; 4RXN; -.
DR PDBsum; 4XNV; -.
DR PDBsum; 4XNW; -.
DR PDBsum; 5RXN; -.
DR PDBsum; 5UIW; -.
DR PDBsum; 5VBL; -.
DR PDBsum; 6AKX; -.
DR PDBsum; 6AKY; -.
DR PDBsum; 6BD4; -.
DR PDBsum; 6GPS; -.
DR PDBsum; 6GPX; -.
DR PDBsum; 6IIU; -.
DR PDBsum; 6IIV; -.
DR PDBsum; 6KNM; -.
DR PDBsum; 6LI2; -.
DR PDBsum; 6LN2; -.
DR PDBsum; 6ME6; -.
DR PDBsum; 6ME7; -.
DR PDBsum; 6ME8; -.
DR PDBsum; 6ME9; -.
DR PDBsum; 7F1T; -.
DR AlphaFoldDB; P00268; -.
DR BMRB; P00268; -.
DR PCDDB; P00268; -.
DR SMR; P00268; -.
DR SABIO-RK; P00268; -.
DR EvolutionaryTrace; P00268; -.
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; Formylation;
KW Iron; Metal-binding; Transport.
FT CHAIN 1..54
FT /note="Rubredoxin"
FT /id="PRO_0000135030"
FT DOMAIN 1..54
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:10216292"
FT BINDING 9
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:10216292"
FT BINDING 39
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:10216292"
FT BINDING 42
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:10216292"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:1637309"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2PVE"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:2PVE"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6ME7"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:2PVE"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2PVE"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:2PVE"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2PVE"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2PVE"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2PVE"
SQ SEQUENCE 54 AA; 6048 MW; 81A0826C56A05766 CRC64;
MKKYTCTVCG YIYNPEDGDP DNGVNPGTDF KDIPDDWVCP LCGVGKDQFE EVEE
