ALKB2_ALCBS
ID ALKB2_ALCBS Reviewed; 382 AA.
AC Q0VTH3; Q7WY79;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Alkane 1-monooxygenase 2;
DE EC=1.14.15.3;
DE AltName: Full=Alkane hydroxylase;
DE Short=AHs;
DE AltName: Full=Terminal alkane hydroxylase;
GN Name=alkB2; OrderedLocusNames=ABO_0122;
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].
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 [GENOMIC DNA], AND SUBSTRATE SPECIFICITY.
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).
RN [3]
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 [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=19953301; DOI=10.1007/s10529-009-0177-0;
RA Miri M., Bambai B., Tabandeh F., Sadeghizadeh M., Kamali N.;
RT "Production of a recombinant alkane hydroxylase (AlkB2) from Alcanivorax
RT borkumensis.";
RL Biotechnol. Lett. 32:497-502(2010).
CC -!- FUNCTION: Catalyzes the hydroxylation of n-alkanes in the presence of a
CC NADH-rubredoxin reductase and rubredoxin. It preferably hydroxylases
CC C8-C16 hydrocarbons. {ECO:0000269|PubMed:19953301}.
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 n-alkanes. {ECO:0000269|PubMed:19953301}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. AlkB
CC subfamily. {ECO:0000305}.
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DR EMBL; AB110226; BAC98366.1; -; Genomic_DNA.
DR EMBL; AJ577851; CAE17295.1; -; Genomic_DNA.
DR EMBL; AM286690; CAL15570.1; -; Genomic_DNA.
DR RefSeq; WP_011587420.1; NC_008260.1.
DR AlphaFoldDB; Q0VTH3; -.
DR STRING; 393595.ABO_0122; -.
DR EnsemblBacteria; CAL15570; CAL15570; ABO_0122.
DR KEGG; abo:ABO_0122; -.
DR eggNOG; COG3239; Bacteria.
DR HOGENOM; CLU_044462_1_0_6; -.
DR OMA; CTYAFIP; -.
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 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Iron; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..382
FT /note="Alkane 1-monooxygenase 2"
FT /id="PRO_0000392217"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 138
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 168
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 172
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="2"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 312
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 315
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12691"
FT BINDING 316
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12691"
SQ SEQUENCE 382 AA; 43923 MW; 0ED56F7909DBE722 CRC64;
MFENTNPDVM LKMKKYGYLA FWAIMVPLVP FSAFVGVESG TQDYWAWFMY AFIFGIIPVL
DYLVGKDPTN PSEDVQVPTM SEEVFYRVSA IAMGFVWIAV LFYAGHIFMN NGYGLLGKIG
WIVSIGTVGG IIAINLGHEL IHKDPKVENW MGGLLLSSVT YAGFKVEHVR GHHVHVSTPD
DASSSRYNQS LYNFLPKAFV HNFINAWSLE KKYLERKGKK NISVHNELIW WYSISALFAA
TFGLLWGWQG VVFFLGQSFF AALALEIINY IEHYGLHRRV NDKGRFERVT PAHSWNSNFL
LTNLALFQLQ RHSDHHAYAK RRYQVLRHYE ESPQLPAGYA TMYVLALIPP LWRKVMNPRV
EAYYEGELDQ LFRDGKRVNN IA
