RUBR1_PSEPU
ID RUBR1_PSEPU Reviewed; 175 AA.
AC Q9WWW4;
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-1;
DE Short=Rdxs;
GN Name=alkG;
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 2 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}.
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DR EMBL; AJ233397; CAB51049.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9WWW4; -.
DR SMR; Q9WWW4; -.
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; 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 3: Inferred from homology;
KW Cytoplasm; Electron transport; Iron; Metal-binding; Repeat; Transport.
FT CHAIN 1..175
FT /note="Rubredoxin-1"
FT /id="PRO_0000392233"
FT DOMAIN 1..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 BINDING 9
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
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 BINDING 42
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
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 BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
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 BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
SQ SEQUENCE 175 AA; 19313 MW; 8E4B3940DFF8224E CRC64;
MARYQCPDCQ YVYDESKGEE HEGFAPNTPW IVIPEDWCCP DCAVRDKLDF VLIEGSTGEK
NISSNNTLSV SAKVSSSDVN TEISNTTMSA EIALDVATEG QHLNGRKPRV TNLQSGAAFL
KWICITCGHI YDEALGDEVE GFAPGTRFED IPNDWCCPDC GATKEDYVLY QEKLG
