RUBR1_DESDA
ID RUBR1_DESDA Reviewed; 45 AA.
AC P04170; B8J2Y8;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Rubredoxin-1;
DE Short=Rd-1;
GN Name=rd1; OrderedLocusNames=Ddes_2011;
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146;
RN [1]
RP PROTEIN SEQUENCE, AND FORMYLATION AT MET-1.
RX PubMed=3709804; DOI=10.1016/0014-5793(86)80588-9;
RA Hormel S., Walsh K.A., Prickril B.C., Titani K., Legall J., Sieker L.C.;
RT "Amino acid sequence of rubredoxin from Desulfovibrio desulfuricans strain
RT 27774.";
RL FEBS Lett. 201:147-150(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=3770211; DOI=10.1016/0014-5793(86)81535-6;
RA Sieker L.C., Stenkamp R.E., Jensen L.H., Prickril B.C., Legall J.;
RT "Structure of rubredoxin from the bacterium Desulfovibrio desulfuricans.";
RL FEBS Lett. 208:73-76(1986).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=2091025; DOI=10.1002/prot.340080409;
RA Stenkamp R.E., Sieker L.C., Jensen L.H.;
RT "The structure of rubredoxin from Desulfovibrio desulfuricans strain 27774
RT at 1.5-A resolution.";
RL Proteins 8:352-364(1990).
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 EMBL; CP001358; ACL49907.1; -; Genomic_DNA.
DR PIR; A00276; RUDVD.
DR RefSeq; WP_012625631.1; NC_011883.1.
DR PDB; 6NW0; X-ray; 1.85 A; A/B=1-45.
DR PDB; 6NW1; X-ray; 1.86 A; A/B=1-45.
DR PDB; 6RXN; X-ray; 1.50 A; A=1-45.
DR PDBsum; 6NW0; -.
DR PDBsum; 6NW1; -.
DR PDBsum; 6RXN; -.
DR AlphaFoldDB; P04170; -.
DR SMR; P04170; -.
DR STRING; 525146.Ddes_2011; -.
DR EnsemblBacteria; ACL49907; ACL49907; Ddes_2011.
DR KEGG; dds:Ddes_2011; -.
DR eggNOG; COG1773; Bacteria.
DR HOGENOM; CLU_128747_4_1_7; -.
DR OrthoDB; 2047418at2; -.
DR EvolutionaryTrace; P04170; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Electron transport;
KW Formylation; Iron; Metal-binding; Transport.
FT CHAIN 1..45
FT /note="Rubredoxin-1"
FT /id="PRO_0000135035"
FT DOMAIN 1..45
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:3709804"
FT BINDING 9
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:3709804"
FT BINDING 32
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:3709804"
FT BINDING 35
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:3709804"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:3709804"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6RXN"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:6RXN"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:6RXN"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:6RXN"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:6RXN"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6RXN"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6RXN"
SQ SEQUENCE 45 AA; 5115 MW; A22AB77FDA1EDC7C CRC64;
MQKYVCNVCG YEYDPAEHDN VPFDQLPDDW CCPVCGVSKD QFSPA
