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   02-SEP-2026, entry version 134.
DE   RecName: Full=Rubredoxin;
DE            Short=Rd;
OS   Clostridium pasteurianum.
OC   Bacteria; Bacillati; Bacillota; 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_CP013019.1.
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   PDB; 7SUS; X-ray; 2.70 A; A=1-54.
DR   AlphaFoldDB; P00268; -.
DR   BMRB; P00268; -.
DR   MDRepo; P00268; -.
DR   PCDDB; P00268; -.
DR   SMR; P00268; -.
DR   GeneID; 93075893; -.
DR   OrthoDB; 9758182at2; -.
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   GO; GO:0043448; P:alkane catabolic process; IEA:TreeGrafter.
DR   CDD; cd00730; rubredoxin; 1.
DR   FunFam; 2.20.28.10:FF:000001; Rubredoxin; 1.
DR   Gene3D; 2.20.28.10; -; 1.
DR   InterPro; IPR024922; Rubredoxin.
DR   InterPro; IPR024934; Rubredoxin-like_dom.
DR   InterPro; IPR024935; Rubredoxin_dom.
DR   InterPro; IPR050526; Rubredoxin_ET.
DR   InterPro; IPR018527; Rubredoxin_Fe_BS.
DR   NCBIfam; NF045768; RubredRD; 1.
DR   PANTHER; PTHR47627; RUBREDOXIN; 1.
DR   PANTHER; PTHR47627:SF1; RUBREDOXIN-1-RELATED; 1.
DR   Pfam; PF00301; Rubredoxin; 1.
DR   PIRSF; PIRSF000071; Rubredoxin; 1.
DR   PRINTS; PR00163; RUBREDOXIN.
DR   SUPFAM; SSF57802; Rubredoxin-like; 1.
DR   PROSITE; PS00202; RUBREDOXIN; 1.
DR   PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
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   PDBsum; 7SUS; -.
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   HELIX           1..3
FT                   /evidence="ECO:0007829|PDB:4XNV"
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"
FT   HELIX           52..54
FT                   /evidence="ECO:0007829|PDB:4MBS"
SQ   SEQUENCE   54 AA;  6048 MW;  81A0826C56A05766 CRC64;
     MKKYTCTVCG YIYNPEDGDP DNGVNPGTDF KDIPDDWVCP LCGVGKDQFE EVEE
//