ID   RUBR2_ALCBS             Reviewed;         174 AA.
AC   Q0VKZ2;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Rubredoxin-2;
DE            Short=Rdxs;
GN   Name=alkG; OrderedLocusNames=ABO_2708;
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 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; AM286690; CAL18156.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0VKZ2; -.
DR   SMR; Q0VKZ2; -.
DR   STRING; 393595.ABO_2708; -.
DR   EnsemblBacteria; CAL18156; CAL18156; ABO_2708.
DR   KEGG; abo:ABO_2708; -.
DR   eggNOG; COG1773; Bacteria.
DR   HOGENOM; CLU_1730536_0_0_6; -.
DR   OMA; KWICITC; -.
DR   UniPathway; UPA00191; -.
DR   Proteomes; UP000008871; Chromosome.
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; Reference proteome;
KW   Repeat; Transport.
FT   CHAIN           1..174
FT                   /note="Rubredoxin-2"
FT                   /id="PRO_0000392230"
FT   DOMAIN          1..53
FT                   /note="Rubredoxin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   DOMAIN          121..172
FT                   /note="Rubredoxin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   REGION          56..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         126
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         129
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         159
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         162
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
SQ   SEQUENCE   174 AA;  18665 MW;  1FB478B2773F98D4 CRC64;
     MAKYQCPDCE YIYDEVAGHP HEGFPPGTSW ETIPEEWACP DCAVRDKADF VVIESGSASP
     ASGAATPEVR TATTPPKAEA SPQKSTGAST PSANNKAKAK AKAKPARAKS SKDSTGKETT
     FRKWICITCG HIYDEALGDE TEGFAPGTLF EDIPDDWCCP DCGATKEDYV LHED