RUBR2_PSEAE
ID RUBR2_PSEAE Reviewed; 55 AA.
AC Q9HTK8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Rubredoxin-2;
DE Short=Rdxs;
GN Name=rubA2; Synonyms=alkG2; OrderedLocusNames=PA5350;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION IN ALKANE DEGRADATION.
RX PubMed=14574114; DOI=10.1023/a:1026000622765;
RA Smits T.H., Witholt B., van Beilen J.B.;
RT "Functional characterization of genes involved in alkane oxidation by
RT Pseudomonas aeruginosa.";
RL Antonie Van Leeuwenhoek 84:193-200(2003).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH RUBREDOXIN REDUCTASE
RP AND IRON, AND COFACTOR.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=17636129; DOI=10.1073/pnas.0702919104;
RA Hagelueken G., Wiehlmann L., Adams T.M., Kolmar H., Heinz D.W., Tummler B.,
RA Schubert W.D.;
RT "Crystal structure of the electron transfer complex rubredoxin rubredoxin
RT reductase of Pseudomonas aeruginosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12276-12281(2007).
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:14574114}.
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:17636129};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:17636129};
CC -!- PATHWAY: Hydrocarbon metabolism; alkane degradation.
CC -!- INTERACTION:
CC Q9HTK8; Q9HTK9: alkT; NbExp=2; IntAct=EBI-15647891, EBI-15647858;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:12730186}.
CC -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08735.1; -; Genomic_DNA.
DR PIR; H82976; H82976.
DR RefSeq; NP_254037.1; NC_002516.2.
DR RefSeq; WP_003098329.1; NZ_QZGE01000020.1.
DR PDB; 2V3B; X-ray; 2.45 A; B=1-55.
DR PDBsum; 2V3B; -.
DR AlphaFoldDB; Q9HTK8; -.
DR SMR; Q9HTK8; -.
DR IntAct; Q9HTK8; 1.
DR STRING; 287.DR97_2721; -.
DR PaxDb; Q9HTK8; -.
DR DNASU; 879561; -.
DR EnsemblBacteria; AAG08735; AAG08735; PA5350.
DR GeneID; 879561; -.
DR KEGG; pae:PA5350; -.
DR PATRIC; fig|208964.12.peg.5607; -.
DR PseudoCAP; PA5350; -.
DR HOGENOM; CLU_128747_1_1_6; -.
DR InParanoid; Q9HTK8; -.
DR OMA; MSAYRCP; -.
DR PhylomeDB; Q9HTK8; -.
DR BioCyc; PAER208964:G1FZ6-5472-MON; -.
DR UniPathway; UPA00191; -.
DR EvolutionaryTrace; Q9HTK8; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043448; P:alkane catabolic process; IBA:GO_Central.
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; Cytoplasm; Electron transport; Iron; Metal-binding;
KW Reference proteome; Transport.
FT CHAIN 1..55
FT /note="Rubredoxin-2"
FT /id="PRO_0000392232"
FT DOMAIN 1..54
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:17636129"
FT BINDING 9
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:17636129"
FT BINDING 39
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:17636129"
FT BINDING 42
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT ECO:0000269|PubMed:17636129"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2V3B"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:2V3B"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:2V3B"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:2V3B"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:2V3B"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:2V3B"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2V3B"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2V3B"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2V3B"
SQ SEQUENCE 55 AA; 6174 MW; 9C27F01DAB7E49C6 CRC64;
MRKWQCVVCG FIYDEALGLP EEGIPAGTRW EDIPADWVCP DCGVGKIDFE MIEIA
