ID   RUBR2_PSEPU             Reviewed;         134 AA.
AC   Q9WWW5;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Rubredoxin-2;
DE            Short=Rdxs;
GN   Name=alkF;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P1;
RX   PubMed=11207749; DOI=10.1046/j.1462-2920.1999.00037.x;
RA   Smits T.H.M., Roethlisberger M., Witholt B., Van Beilen J.B.;
RT   "Molecular screening for alkane hydroxylase genes in Gram-negative and
RT   Gram-positive strains.";
RL   Environ. Microbiol. 1:307-317(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P1;
RX   PubMed=11390693; DOI=10.1099/00221287-147-6-1621;
RA   Van Beilen J.B., Panke S., Lucchini S., Franchini A.G., Roethlisberger M.,
RA   Witholt B.;
RT   "Analysis of Pseudomonas putida alkane degradation gene clusters and
RT   flanking insertion sequences: evolution and regulation of the alk-genes.";
RL   Microbiology 147:1621-1630(2001).
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:0000250}.
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(3+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Hydrocarbon metabolism; alkane degradation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AJ233397; CAB51048.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9WWW5; -.
DR   SMR; Q9WWW5; -.
DR   UniPathway; UPA00191; -.
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; 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   Cytoplasm; Electron transport; Iron; Metal-binding; Transport.
FT   CHAIN           1..134
FT                   /note="Rubredoxin-2"
FT                   /id="PRO_0000392234"
FT   DOMAIN          1..53
FT                   /note="Rubredoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   REGION          99..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         6
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         9
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         39
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         42
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
SQ   SEQUENCE   134 AA;  15534 MW;  10730C54EC59DDCD CRC64;
     MAKYQCPDCQ YIYDECKGEP HEGFQPNTNW GEIPEEWACP DCAVRDKIDF KMLADPRCEI
     TQLKQNDPVI KQDNNIIEDT LSEPSILSAE LEFTAEKISI TDERENTPDN KVERRSQSQA
     VRRSSVKKIK NNKR