ID   RUBR_AZOVI              Reviewed;          72 AA.
AC   P30778;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Rubredoxin;
DE            Short=Rd;
GN   Name=hoxR;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=1581355; DOI=10.1016/0167-4781(92)90111-c;
RA   Chen J.C., Mortenson L.E.;
RT   "Two open reading frames (ORFs) identified near the hydrogenase structural
RT   genes in Azotobacter vinelandii, the first ORF may encode for a polypeptide
RT   similar to rubredoxins.";
RL   Biochim. Biophys. Acta 1131:122-124(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=1624446; DOI=10.1128/jb.174.14.4549-4557.1992;
RA   Menon A., Mortenson L.E., Robson R.L.;
RT   "Nucleotide sequences and genetic analysis of hydrogen oxidation (hox)
RT   genes in Azotobacter vinelandii.";
RL   J. Bacteriol. 174:4549-4557(1992).
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. Could be involved in hydrogenase-linked redox processes.
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
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DR   EMBL; M80522; AAA22130.1; -; Genomic_DNA.
DR   EMBL; X63778; CAA45311.1; -; Genomic_DNA.
DR   EMBL; L23970; AAA19505.1; -; Unassigned_DNA.
DR   PIR; S22223; E44915.
DR   RefSeq; WP_012703493.1; NZ_FPKM01000029.1.
DR   AlphaFoldDB; P30778; -.
DR   SMR; P30778; -.
DR   OMA; ECKICWW; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   CDD; cd00730; rubredoxin; 1.
DR   InterPro; IPR024934; Rubredoxin-like_dom.
DR   InterPro; IPR024935; Rubredoxin_dom.
DR   InterPro; IPR018527; Rubredoxin_Fe_BS.
DR   Pfam; PF00301; Rubredoxin; 1.
DR   PRINTS; PR00163; RUBREDOXIN.
DR   PROSITE; PS00202; RUBREDOXIN; 1.
DR   PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Electron transport; Iron; Metal-binding; Transport.
FT   CHAIN           1..72
FT                   /note="Rubredoxin"
FT                   /id="PRO_0000135023"
FT   DOMAIN          19..72
FT                   /note="Rubredoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         24
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         27
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         57
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         60
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
SQ   SEQUENCE   72 AA;  8086 MW;  1B7E7268C970255B CRC64;
     MSARFEGSYL GDATRLADDA VLECKICWQR YDPAEGDPVW QIPPGTPFAA LPAHWRCPRC
     DGDREQFMVV DG