RUBR_CUPNH
ID RUBR_CUPNH Reviewed; 78 AA.
AC P31912;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Rubredoxin;
DE Short=Rd;
GN Name=hoxR; OrderedLocusNames=PHG009;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1383192; DOI=10.1128/jb.174.19.6277-6289.1992;
RA Kortlueke C., Horstmann K., Schwartz E., Rohde M., Binsack R.,
RA Friedrich B.;
RT "A gene complex coding for the membrane-bound hydrogenase of Alcaligenes
RT eutrophus H16.";
RL J. Bacteriol. 174:6277-6289(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
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:0000305};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000305};
CC -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M96433; AAA16469.1; -; Unassigned_DNA.
DR EMBL; AY305378; AAP85765.1; -; Genomic_DNA.
DR PIR; I43255; I43255.
DR RefSeq; WP_011153934.1; NZ_CP039289.1.
DR AlphaFoldDB; P31912; -.
DR SMR; P31912; -.
DR STRING; 381666.PHG009; -.
DR EnsemblBacteria; AAP85765; AAP85765; PHG009.
DR GeneID; 39976746; -.
DR KEGG; reh:PHG009; -.
DR eggNOG; COG1773; Bacteria.
DR HOGENOM; CLU_128747_2_1_4; -.
DR OMA; ECKICWW; -.
DR OrthoDB; 2047418at2; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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; Plasmid; Reference proteome;
KW Transport.
FT CHAIN 1..78
FT /note="Rubredoxin"
FT /id="PRO_0000135022"
FT DOMAIN 23..74
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 28
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 31
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
SQ SEQUENCE 78 AA; 8649 MW; D2D5F381F7A49FDD CRC64;
MNDAGMGRFE GSYLGDRGRL AADARLECKI CWWEYDPEVG DPVWQIAPGT SFSALPAHWR
CPNCDGEAEQ FMVLGPQA