ALKB1_ALCBS
ID ALKB1_ALCBS Reviewed; 404 AA.
AC Q0VKZ3; Q76C56;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Alkane 1-monooxygenase 1;
DE EC=1.14.15.3;
DE AltName: Full=Alkane hydroxylase;
DE Short=AHs;
DE AltName: Full=Terminal alkane hydroxylase;
GN Name=alkB1; OrderedLocusNames=ABO_2707;
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 [GENOMIC DNA], AND FUNCTION IN ALKANE DEGRADATION.
RX PubMed=14871203; DOI=10.1046/j.1462-2920.2003.00550.x;
RA Hara A., Baik S.H., Syutsubo K., Misawa N., Smits T.H., van Beilen J.B.,
RA Harayama S.;
RT "Cloning and functional analysis of alkB genes in Alcanivorax borkumensis
RT SK2.";
RL Environ. Microbiol. 6:191-197(2004).
RN [2]
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).
RN [3]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND INDUCTION.
RC STRAIN=AP1;
RX PubMed=14871210; DOI=10.1111/j.1462-2920.2004.00567.x;
RA van Beilen J.B., Marin M.M., Smits T.H., Rothlisberger M., Franchini A.G.,
RA Witholt B., Rojo F.;
RT "Characterization of two alkane hydroxylase genes from the marine
RT hydrocarbonoclastic bacterium Alcanivorax borkumensis.";
RL Environ. Microbiol. 6:264-273(2004).
CC -!- FUNCTION: Catalyzes the hydroxylation of n-alkanes and fatty acids in
CC the presence of a NADH-rubredoxin reductase and rubredoxin. It
CC preferably hydroxylases C5-C12 hydrocarbons.
CC {ECO:0000269|PubMed:14871203, ECO:0000269|PubMed:14871210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + O2 + octane + 2 reduced [rubredoxin] = H2O + octan-1-
CC ol + 2 oxidized [rubredoxin]; Xref=Rhea:RHEA:19341, Rhea:RHEA-
CC COMP:10302, Rhea:RHEA-COMP:10303, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16188,
CC ChEBI:CHEBI:17590, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC EC=1.14.15.3; Evidence={ECO:0000305|PubMed:14871210};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000250|UniProtKB:P12691};
CC Note=Binds 2 Fe(3+) ions per subunit. {ECO:0000250|UniProtKB:P12691};
CC -!- PATHWAY: Hydrocarbon metabolism; alkane degradation.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Induced by AlkS and n-alkanes.
CC {ECO:0000269|PubMed:14871210}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. AlkB
CC subfamily. {ECO:0000305}.
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DR EMBL; AB110225; BAC98365.1; -; Genomic_DNA.
DR EMBL; AM286690; CAL18155.1; -; Genomic_DNA.
DR RefSeq; WP_011589978.1; NC_008260.1.
DR AlphaFoldDB; Q0VKZ3; -.
DR STRING; 393595.ABO_2707; -.
DR EnsemblBacteria; CAL18155; CAL18155; ABO_2707.
DR KEGG; abo:ABO_2707; -.
DR eggNOG; COG3239; Bacteria.
DR HOGENOM; CLU_044462_1_0_6; -.
DR OMA; WHWSNDV; -.
DR OrthoDB; 1202565at2; -.
DR UniPathway; UPA00191; -.
DR Proteomes; UP000008871; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0018685; F:alkane 1-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0052869; F:arachidonic acid omega-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043448; P:alkane catabolic process; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd03512; Alkane-hydroxylase; 1.
DR InterPro; IPR033885; AlkB/XylM.
DR InterPro; IPR005804; FA_desaturase_dom.
DR PANTHER; PTHR38674; PTHR38674; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Iron; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..404
FT /note="Alkane 1-monooxygenase 1"
FT /id="PRO_0000392216"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 143
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 177
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 317
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 320
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 321
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12691"
SQ SEQUENCE 404 AA; 46475 MW; DE255FD5DDE5B5E2 CRC64;
MSENILTEPP RSDADNEGYV DRKRHLWILS VLWPATPIIG LYLVSQTGWS IWYGLVLILW
YGLVPLIDTM LGEDYSNPPE SVVPKLEQDR YYKVLTYLTV PIHYAALIIS AWWVSTQPIG
VFEFLALALS LGIVNGLALN TGHELGHKKE TFDRWMAKLV LAVVGYGHFF IEHNKGHHRD
VATPMDPATS RMGESIYTFS LREIPGAFKR AWGLEEQRLS RCGKSVWSLD NEVLQPMILT
VVLYAALLAF FGPLMLIFLP IQMAFGWWQL TSANYIEHYG LLREKLPNGR YEHQKPHHSW
NSNHVMSNLI LFHLQRHSDH HAHPTRSYQS LRDFSDLPTL PTGYPGMFFV AFFPSWFRSL
MDDRVMEWAH GDINKIQIQP GMREFYEQKF GVKGSESPDT TVAK
