RUBR_PYRAB
ID RUBR_PYRAB Reviewed; 53 AA.
AC Q9V099; G8ZI58;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Rubredoxin;
DE Short=Rd;
GN Name=rub; Synonyms=rd; OrderedLocusNames=PYRAB08920; ORFNames=PAB7224;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP STUDY OF IRON-SULFUR CENTERS.
RX DOI=10.1023/B:HYPE.0000043243.81833.85;
RA Wegner P., Bever M., Schuenemann V., Trautwein A.X., Schmidt C.,
RA Boenisch H., Gnida M., Meyer-Klaucke W.;
RT "Iron-sulfur proteins investigated by EPR-, Moessbauer- and EXAFS-
RT spectroscopy.";
RL Hyperfine Interact. 156:293-298(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (0.69 ANGSTROMS) IN COMPLEX WITH IRON.
RX PubMed=15983423; DOI=10.1107/s090744490501293x;
RA Boenisch H., Schmidt C.L., Bianco P., Ladenstein R.;
RT "Ultrahigh-resolution study on Pyrococcus abyssi rubredoxin. I. 0.69 A X-
RT ray structure of mutant W4L/R5S.";
RL Acta Crystallogr. D 61:990-1004(2005).
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 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Note=Binds 1 Fe(3+) ion per subunit.;
CC -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
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DR EMBL; AJ248285; CAB49806.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70299.1; -; Genomic_DNA.
DR PIR; E75136; E75136.
DR RefSeq; WP_010868015.1; NC_000868.1.
DR PDB; 1YK4; X-ray; 0.69 A; A=2-53.
DR PDB; 1YK5; X-ray; 1.79 A; A/B/C/D=1-53.
DR PDB; 2PYA; X-ray; 0.86 A; A=2-53.
DR PDBsum; 1YK4; -.
DR PDBsum; 1YK5; -.
DR PDBsum; 2PYA; -.
DR AlphaFoldDB; Q9V099; -.
DR SMR; Q9V099; -.
DR STRING; 272844.PAB7224; -.
DR EnsemblBacteria; CAB49806; CAB49806; PAB7224.
DR GeneID; 1496243; -.
DR KEGG; pab:PAB7224; -.
DR PATRIC; fig|272844.11.peg.944; -.
DR eggNOG; arCOG04391; Archaea.
DR HOGENOM; CLU_128747_3_3_2; -.
DR OMA; APKDMFE; -.
DR OrthoDB; 126197at2157; -.
DR PhylomeDB; Q9V099; -.
DR EvolutionaryTrace; Q9V099; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
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 3D-structure; Electron transport; Iron; Metal-binding; Transport.
FT CHAIN 1..53
FT /note="Rubredoxin"
FT /id="PRO_0000135062"
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:15983423"
FT BINDING 9
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:15983423"
FT BINDING 39
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:15983423"
FT BINDING 42
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:15983423"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1YK4"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1YK4"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1YK4"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1YK4"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:1YK4"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1YK4"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1YK4"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1YK4"
SQ SEQUENCE 53 AA; 6041 MW; 46A7BE222A4D19A0 CRC64;
MAKWRCKICG YIYDEDEGDP DNGISPGTKF EDLPDDWVCP LCGAPKSEFE RIE
