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RUBR1_ALCBS
ID   RUBR1_ALCBS             Reviewed;          54 AA.
AC   Q0VTA9;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Rubredoxin-1;
DE            Short=Rdxs;
GN   Name=rubA; OrderedLocusNames=ABO_0163;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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+) ion 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; AM286690; CAL15611.1; -; Genomic_DNA.
DR   RefSeq; WP_011587460.1; NC_008260.1.
DR   AlphaFoldDB; Q0VTA9; -.
DR   SMR; Q0VTA9; -.
DR   STRING; 393595.ABO_0163; -.
DR   EnsemblBacteria; CAL15611; CAL15611; ABO_0163.
DR   KEGG; abo:ABO_0163; -.
DR   eggNOG; COG1773; Bacteria.
DR   HOGENOM; CLU_128747_3_3_6; -.
DR   OMA; APKDMFE; -.
DR   OrthoDB; 2047418at2; -.
DR   UniPathway; UPA00191; -.
DR   Proteomes; UP000008871; 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; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Cytoplasm; Electron transport; Iron; Metal-binding; Reference proteome;
KW   Transport.
FT   CHAIN           1..54
FT                   /note="Rubredoxin-1"
FT                   /id="PRO_0000392229"
FT   DOMAIN          1..52
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;  6067 MW;  0043E3DED6CBB24E CRC64;
     MKKWECVVCG FIYDEAEGLP DEGIEPGTAW NNVPEDWVCP DCGVGKDDFE MVEI
 
 
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