ID   RUBR_HELMO              Reviewed;          52 AA.
AC   P56263;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Rubredoxin;
DE            Short=Rd;
OS   Heliobacterium mobile (Heliobacillus mobilis).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliobacterium.
OX   NCBI_TaxID=28064;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, IRON BINDING, AND FORMYLATION AT
RP   MET-1.
RX   PubMed=7726577; DOI=10.1006/abbi.1995.1207;
RA   Lee W.Y., Brune D.C., Lobrutto R., Blankenship R.E.;
RT   "Isolation, characterization, and primary structure of rubredoxin from the
RT   photosynthetic bacterium, Heliobacillus mobilis.";
RL   Arch. Biochem. Biophys. 318:80-88(1995).
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250};
CC   -!- PTM: Observed in four forms, with and without iron, and with and
CC       without formylation at Met-1. {ECO:0000269|PubMed:7726577}.
CC   -!- MASS SPECTROMETRY: Mass=5623.6; Method=MALDI; Note=Without formylation
CC       at Met-1, and without iron.; Evidence={ECO:0000269|PubMed:7726577};
CC   -!- MASS SPECTROMETRY: Mass=5651.4; Method=MALDI; Note=With formylation at
CC       Met-1, and without iron.; Evidence={ECO:0000269|PubMed:7726577};
CC   -!- MASS SPECTROMETRY: Mass=5674.8; Method=MALDI; Note=Without formylation
CC       at Met-1, and with iron.; Evidence={ECO:0000269|PubMed:7726577};
CC   -!- MASS SPECTROMETRY: Mass=5703.6; Method=MALDI; Note=With formylation at
CC       Met-1, and with iron.; Evidence={ECO:0000269|PubMed:7726577};
CC   -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
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DR   PIR; S65620; S65620.
DR   AlphaFoldDB; P56263; -.
DR   SMR; P56263; -.
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   Direct protein sequencing; Electron transport; Formylation; Iron;
KW   Metal-binding; Transport.
FT   CHAIN           1..52
FT                   /note="Rubredoxin"
FT                   /id="PRO_0000135040"
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:0000305"
FT   BINDING         9
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000305"
FT   BINDING         39
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000305"
FT   BINDING         42
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         1
FT                   /note="N-formylmethionine; partial"
FT                   /evidence="ECO:0000269|PubMed:7726577"
SQ   SEQUENCE   52 AA;  5619 MW;  659241131D3124AD CRC64;
     MKKYGCLVCG YVYDPAKGDP DHGIAPGTAF EDLPADWVCP LCGVSKDEFE PL