ID   RUBR_MEGGA              Reviewed;          52 AA.
AC   P00270;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   28-JUN-2023, entry version 109.
DE   RecName: Full=Rubredoxin;
DE            Short=Rd;
OS   Megalodesulfovibrio gigas (Desulfovibrio gigas).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Megalodesulfovibrio.
OX   NCBI_TaxID=879;
RN   [1]
RP   PROTEIN SEQUENCE, AND FORMYLATION AT MET-1.
RX   PubMed=938515; DOI=10.1016/0006-291x(76)91092-5;
RA   Bruschi M.;
RT   "The amino acid sequence of rubredoxin from the sulfate reducing bacterium,
RT   Desulfovibrio gigas.";
RL   Biochem. Biophys. Res. Commun. 70:615-621(1976).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX   PubMed=3441010; DOI=10.1016/0022-2836(87)90562-6;
RA   Frey M., Sieker L.C., Payan F., Haser R., Bruschi M., Pepe G., le Gall J.;
RT   "Rubredoxin from Desulfovibrio gigas. A molecular model of the oxidized
RT   form at 1.4-A resolution.";
RL   J. Mol. Biol. 197:525-541(1987).
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   -!- FUNCTION: Electron acceptor for cytoplasmic lactate dehydrogenase.
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC       Note=Binds 1 Fe(3+) ion per subunit.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
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DR   PIR; A00275; RUDVEG.
DR   PDB; 1E8J; NMR; -; A=1-52.
DR   PDB; 1RDG; X-ray; 1.40 A; A=1-52.
DR   PDB; 1SPW; NMR; -; A=1-52.
DR   PDB; 2DSX; X-ray; 0.68 A; A=1-52.
DR   PDBsum; 1E8J; -.
DR   PDBsum; 1RDG; -.
DR   PDBsum; 1SPW; -.
DR   PDBsum; 2DSX; -.
DR   AlphaFoldDB; P00270; -.
DR   SMR; P00270; -.
DR   OMA; MSAYRCP; -.
DR   EvolutionaryTrace; P00270; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Gene3D; 2.20.28.10; -; 1.
DR   InterPro; IPR024922; Rubredoxin.
DR   InterPro; IPR024934; Rubredoxin-like_dom.
DR   InterPro; IPR024935; Rubredoxin_dom.
DR   InterPro; IPR018527; Rubredoxin_Fe_BS.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Electron transport;
KW   Formylation; Iron; Metal-binding; Transport.
FT   CHAIN           1..52
FT                   /note="Rubredoxin"
FT                   /id="PRO_0000135037"
FT   DOMAIN          1..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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT                   ECO:0000269|PubMed:938515"
FT   BINDING         9
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT                   ECO:0000269|PubMed:938515"
FT   BINDING         39
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT                   ECO:0000269|PubMed:938515"
FT   BINDING         42
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT                   ECO:0000269|PubMed:938515"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:3441010,
FT                   ECO:0000269|PubMed:938515"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:2DSX"
FT   TURN            7..9
FT                   /evidence="ECO:0007829|PDB:2DSX"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:2DSX"
FT   HELIX           20..22
FT                   /evidence="ECO:0007829|PDB:2DSX"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:2DSX"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:2DSX"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:2DSX"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:2DSX"
SQ   SEQUENCE   52 AA;  5677 MW;  3E08147A4AC262F7 CRC64;
     MDIYVCTVCG YEYDPAKGDP DSGIKPGTKF EDLPDDWACP VCGASKDAFE KQ
//