RUBR2_PSEOL
ID RUBR2_PSEOL Reviewed; 173 AA.
AC P00272;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Rubredoxin-2;
DE Short=Rdxs;
DE AltName: Full=Two-iron rubredoxin;
GN Name=alkG;
OS Pseudomonas oleovorans.
OG Plasmid OCT.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas;
OC Pseudomonas oleovorans/pseudoalcaligenes group.
OX NCBI_TaxID=301;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GPo1;
RX PubMed=2647719; DOI=10.1016/s0021-9258(18)83565-7;
RA Kok M., Oldenhuis R., van der Linden M.P.G., Meulenberg C.H.C., Kingma J.,
RA Witholt B.;
RT "The Pseudomonas oleovorans alkBAC operon encodes two structurally related
RT rubredoxins and an aldehyde dehydrogenase.";
RL J. Biol. Chem. 264:5442-5451(1989).
RN [2]
RP PROTEIN SEQUENCE OF 2-173.
RX PubMed=5543946; DOI=10.1016/0006-291x(71)90536-5;
RA Benson A.M., Tomoda K., Chang J., Matsueda G., Lode E.T., Coon M.J.,
RA Yasunobu K.T.;
RT "Evolutionary and phylogenetic relationships of rubredoxin-containing
RT microbes.";
RL Biochem. Biophys. Res. Commun. 42:640-646(1971).
RN [3]
RP FUNCTION, AND COFACTOR.
RX PubMed=4295540; DOI=10.1016/s0021-9258(18)99296-3;
RA Peterson J.A., Coon M.J.;
RT "Enzymatic omega-oxidation. 3. Purification and properties of rubredoxin, a
RT component of the omega-hydroxylation system of Pseudomonas oleovorans.";
RL J. Biol. Chem. 243:329-334(1968).
RN [4]
RP ELECTRON TRANSFER.
RX PubMed=9799514; DOI=10.1021/bi981853v;
RA Lee H.J., Basran J., Scrutton N.S.;
RT "Electron transfer from flavin to iron in the Pseudomonas oleovorans
RT rubredoxin reductase-rubredoxin electron transfer complex.";
RL Biochemistry 37:15513-15522(1998).
RN [5]
RP INDUCTION.
RX PubMed=10692156; DOI=10.1046/j.1365-2958.2000.01751.x;
RA Canosa I., Sanchez-Romero J.M., Yuste L., Rojo F.;
RT "A positive feedback mechanism controls expression of AlkS, the
RT transcriptional regulator of the Pseudomonas oleovorans alkane degradation
RT pathway.";
RL Mol. Microbiol. 35:791-799(2000).
RN [6]
RP FUNCTION.
RX PubMed=11171083; DOI=10.1042/0264-6021:3540089;
RA Perry A., Lian L.-Y., Scrutton N.S.;
RT "Two-iron rubredoxin of Pseudomonas oleovorans: production, stability and
RT characterization of the individual iron-binding domains by optical, CD and
RT NMR spectroscopies.";
RL Biochem. J. 354:89-98(2001).
RN [7]
RP INDUCTION.
RX PubMed=12730186; DOI=10.1128/jb.185.10.3232-3237.2003;
RA Marin M.M., Yuste L., Rojo F.;
RT "Differential expression of the components of the two alkane hydroxylases
RT from Pseudomonas aeruginosa.";
RL J. Bacteriol. 185:3232-3237(2003).
RN [8]
RP STRUCTURE BY NMR OF 87-172 IN COMPLEX WITH IRON.
RX PubMed=15023067; DOI=10.1021/bi035817u;
RA Perry A., Tambyrajah W., Grossmann J.G., Lian L.Y., Scrutton N.S.;
RT "Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans
RT determined by NMR spectroscopy and solution X-ray scattering and
RT interactions with rubredoxin reductase.";
RL Biochemistry 43:3167-3182(2004).
CC -!- FUNCTION: Involved in the hydrocarbon hydroxylating system, which
CC transfers electrons from NADH to rubredoxin reductase and then through
CC rubredoxin to alkane 1 monooxygenase. {ECO:0000269|PubMed:11171083,
CC ECO:0000269|PubMed:4295540}.
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:4295540};
CC Note=Binds 2 Fe(3+) ions per subunit. {ECO:0000269|PubMed:4295540};
CC -!- PATHWAY: Hydrocarbon metabolism; alkane degradation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Induced by AlkS and n-alkanes. {ECO:0000269|PubMed:10692156,
CC ECO:0000269|PubMed:12730186}.
CC -!- MISCELLANEOUS: Unlike other rubredoxins, this rubredoxin is unique in
CC that it contains two binding sites for iron. It is most probably the
CC product of a gene duplication event. The 2Fe form of the rubredoxin is
CC a physiological form but it is less stable than the readily isolated
CC 1Fe form. Both domains can form productive electron transfer complexes
CC with rubredoxin reductase and accept electrons from the enzyme bound
CC FAD.
CC -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
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DR EMBL; AJ245436; CAB54052.1; -; Genomic_DNA.
DR PIR; B32850; RUPSEO.
DR PDB; 1S24; NMR; -; A=87-173.
DR PDBsum; 1S24; -.
DR AlphaFoldDB; P00272; -.
DR SMR; P00272; -.
DR BioCyc; MetaCyc:MON-3844; -.
DR UniPathway; UPA00191; -.
DR EvolutionaryTrace; P00272; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043448; P:alkane catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00730; rubredoxin; 2.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR024935; Rubredoxin_dom.
DR InterPro; IPR018527; Rubredoxin_Fe_BS.
DR Pfam; PF00301; Rubredoxin; 2.
DR PRINTS; PR00163; RUBREDOXIN.
DR PROSITE; PS00202; RUBREDOXIN; 2.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Electron transport;
KW Iron; Metal-binding; Plasmid; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5543946"
FT CHAIN 2..173
FT /note="Rubredoxin-2"
FT /id="PRO_0000135044"
FT DOMAIN 2..53
FT /note="Rubredoxin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT DOMAIN 119..170
FT /note="Rubredoxin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 6
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:15023067"
FT BINDING 9
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:15023067"
FT BINDING 39
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:15023067"
FT BINDING 42
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:15023067"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:15023067"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:15023067"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:15023067"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:15023067"
FT CONFLICT 38..41
FT /note="CCPD -> DCPC (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="E -> EW (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..155
FT /note="DW -> WD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 158..160
FT /note="PDC -> WCBP (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1S24"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:1S24"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1S24"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:1S24"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1S24"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1S24"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1S24"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1S24"
SQ SEQUENCE 173 AA; 18899 MW; 8CA9C654978FDF7D CRC64;
MASYKCPDCN YVYDESAGNV HEGFSPGTPW HLIPEDWCCP DCAVRDKLDF MLIESGVGEK
GVTSTHTSPN LSEVSGTSLT AEAVVAPTSL EKLPSADVKG QDLYKTQPPR SDAQGGKAYL
KWICITCGHI YDEALGDEAE GFTPGTRFED IPDDWCCPDC GATKEDYVLY EEK
