ID   RUBR_ACIAD              Reviewed;          54 AA.
AC   P42453;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Rubredoxin;
DE            Short=Rdxs;
GN   Name=rubA; OrderedLocusNames=ACIAD1066;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7670642; DOI=10.1099/13500872-141-6-1425;
RA   Geissdoerfer W., Frosch C.S., Haspel G., Ehrt S., Hillen W.;
RT   "Two genes encoding proteins with similarities to rubredoxin and rubredoxin
RT   reductase are required for conversion of dodecane to lauric acid in
RT   Acinetobacter calcoaceticus ADP1.";
RL   Microbiology 141:1425-1432(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [3]
RP   FUNCTION IN ALKANE DEGRADATION, AND INDUCTION.
RX   PubMed=10400587; DOI=10.1128/jb.181.14.4292-4298.1999;
RA   Geissdorfer W., Kok R.G., Ratajczak A., Hellingwerf K.J., Hillen W.;
RT   "The genes rubA and rubB for alkane degradation in Acinetobacter sp. strain
RT   ADP1 are in an operon with estB, encoding an esterase, and oxyR.";
RL   J. Bacteriol. 181:4292-4298(1999).
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:10400587}.
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Hydrocarbon metabolism; alkane degradation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:10400587}.
CC   -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
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DR   EMBL; Z46863; CAA86925.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG67954.1; -; Genomic_DNA.
DR   PIR; I39520; I39520.
DR   RefSeq; WP_004921639.1; NC_005966.1.
DR   AlphaFoldDB; P42453; -.
DR   SMR; P42453; -.
DR   STRING; 62977.ACIAD1066; -.
DR   EnsemblBacteria; CAG67954; CAG67954; ACIAD1066.
DR   GeneID; 45233508; -.
DR   KEGG; aci:ACIAD1066; -.
DR   eggNOG; COG1773; Bacteria.
DR   HOGENOM; CLU_128747_1_1_6; -.
DR   OMA; APKDMFE; -.
DR   OrthoDB; 2047418at2; -.
DR   BioCyc; ASP62977:ACIAD_RS04915-MON; -.
DR   UniPathway; UPA00191; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0043448; P:alkane catabolic process; IMP:UniProtKB.
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   Cytoplasm; Electron transport; Iron; Metal-binding; Reference proteome;
KW   Transport.
FT   CHAIN           1..54
FT                   /note="Rubredoxin"
FT                   /id="PRO_0000135021"
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   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   54 AA;  6199 MW;  DB0584245A2626BA CRC64;
     MKKYQCIVCG WIYDEAEGWP QDGIAPGTKW EDIPDDWTCP DCGVSKVDFE MIEV