RURE_PSEAE
ID RURE_PSEAE Reviewed; 384 AA.
AC Q9HTK9;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Rubredoxin-NAD(+) reductase;
DE Short=RdxR;
DE EC=1.18.1.1;
GN Name=alkT; OrderedLocusNames=PA5349;
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 FUNCTION, SUBUNIT, AND 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] {ECO:0007744|PDB:2V3A, ECO:0007744|PDB:2V3B}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH RUBREDOXIN AND FAD,
RP AND SUBUNIT.
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:12730186,
CC ECO:0000269|PubMed:14574114}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [rubredoxin] = NADH + 2 oxidized
CC [rubredoxin]; Xref=Rhea:RHEA:18597, Rhea:RHEA-COMP:10302, Rhea:RHEA-
CC COMP:10303, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.18.1.1;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Hydrocarbon metabolism; alkane degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12730186,
CC ECO:0000269|PubMed:17636129}.
CC -!- INTERACTION:
CC Q9HTK9; Q9HTK8: rubA2; NbExp=2; IntAct=EBI-15647858, EBI-15647891;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:12730186}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG08734.1; -; Genomic_DNA.
DR PIR; G82976; G82976.
DR RefSeq; NP_254036.1; NC_002516.2.
DR RefSeq; WP_003114369.1; NZ_QZGE01000020.1.
DR PDB; 2V3A; X-ray; 2.40 A; A=1-384.
DR PDB; 2V3B; X-ray; 2.45 A; A=1-384.
DR PDBsum; 2V3A; -.
DR PDBsum; 2V3B; -.
DR AlphaFoldDB; Q9HTK9; -.
DR SMR; Q9HTK9; -.
DR IntAct; Q9HTK9; 1.
DR STRING; 287.DR97_2720; -.
DR PaxDb; Q9HTK9; -.
DR PRIDE; Q9HTK9; -.
DR DNASU; 879643; -.
DR EnsemblBacteria; AAG08734; AAG08734; PA5349.
DR GeneID; 879643; -.
DR KEGG; pae:PA5349; -.
DR PATRIC; fig|208964.12.peg.5606; -.
DR PseudoCAP; PA5349; -.
DR HOGENOM; CLU_003291_4_4_6; -.
DR InParanoid; Q9HTK9; -.
DR OMA; GIDPGHK; -.
DR PhylomeDB; Q9HTK9; -.
DR BioCyc; PAER208964:G1FZ6-5471-MON; -.
DR BRENDA; 1.18.1.1; 5087.
DR UniPathway; UPA00191; -.
DR EvolutionaryTrace; Q9HTK9; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0015044; F:rubredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015046; F:rubredoxin-NADP+ reductase activity; IDA:UniProtKB.
DR GO; GO:0043448; P:alkane catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR041364; Rbx-bd.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18113; Rbx_binding; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..384
FT /note="Rubredoxin-NAD(+) reductase"
FT /id="PRO_0000392226"
FT BINDING 12..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17636129,
FT ECO:0007744|PDB:2V3A, ECO:0007744|PDB:2V3B"
FT BINDING 36..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17636129,
FT ECO:0007744|PDB:2V3A, ECO:0007744|PDB:2V3B"
FT BINDING 45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17636129,
FT ECO:0007744|PDB:2V3A, ECO:0007744|PDB:2V3B"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17636129,
FT ECO:0007744|PDB:2V3A, ECO:0007744|PDB:2V3B"
FT BINDING 159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17636129,
FT ECO:0007744|PDB:2V3A, ECO:0007744|PDB:2V3B"
FT BINDING 277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17636129,
FT ECO:0007744|PDB:2V3A, ECO:0007744|PDB:2V3B"
FT BINDING 289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17636129,
FT ECO:0007744|PDB:2V3A, ECO:0007744|PDB:2V3B"
FT BINDING 320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17636129,
FT ECO:0007744|PDB:2V3A, ECO:0007744|PDB:2V3B"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:2V3A"
FT TURN 51..55
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2V3A"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 170..181
FT /evidence="ECO:0007829|PDB:2V3A"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:2V3A"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 289..303
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:2V3A"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:2V3A"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:2V3A"
SQ SEQUENCE 384 AA; 40618 MW; C98EA1FC3E15FA8F CRC64;
MSERAPLVII GTGLAGYNLA REWRKLDGET PLLMITADDG RSYSKPMLST GFSKNKDADG
LAMAEPGAMA EQLNARILTH TRVTGIDPGH QRIWIGEEEV RYRDLVLAWG AEPIRVPVEG
DAQDALYPIN DLEDYARFRQ AAAGKRRVLL LGAGLIGCEF ANDLSSGGYQ LDVVAPCEQV
MPGLLHPAAA KAVQAGLEGL GVRFHLGPVL ASLKKAGEGL EAHLSDGEVI PCDLVVSAVG
LRPRTELAFA AGLAVNRGIV VDRSLRTSHA NIYALGDCAE VDGLNLLYVM PLMACARALA
QTLAGNPSQV AYGPMPVTVK TPACPLVVSP PPRGMDGQWL VEGSGTDLKV LCRDTAGRVI
GYALTGAAVN EKLALNKELP GLMA
