ALKB_ACIAD
ID ALKB_ACIAD Reviewed; 408 AA.
AC O31250;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Alkane 1-monooxygenase;
DE EC=1.14.15.3;
DE AltName: Full=Alkane hydroxylase;
DE Short=AHs;
DE AltName: Full=Terminal alkane hydroxylase;
GN Name=alkB; Synonyms=alkM; OrderedLocusNames=ACIAD1411;
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=9546151; DOI=10.1128/aem.64.4.1175-1179.1998;
RA Ratajczak A., Geissdorfer W., Hillen W.;
RT "Alkane hydroxylase from Acinetobacter sp. strain ADP1 is encoded by alkM
RT and belongs to a new family of bacterial integral-membrane hydrocarbon
RT hydroxylases.";
RL Appl. Environ. Microbiol. 64:1175-1179(1998).
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 ALKANE DEGRADATION, SUBSTRATE SPECIFICITY, AND INDUCTION.
RX PubMed=9811637; DOI=10.1128/jb.180.22.5822-5827.1998;
RA Ratajczak A., Geissdorfer W., Hillen W.;
RT "Expression of alkane hydroxylase from Acinetobacter sp. Strain ADP1 is
RT induced by a broad range of n-alkanes and requires the transcriptional
RT activator AlkR.";
RL J. Bacteriol. 180:5822-5827(1998).
CC -!- FUNCTION: Catalyzes the hydroxylation of n-alkanes in the presence of a
CC NADH-rubredoxin reductase and rubredoxin. It preferably hydroxylases
CC long-chain-length alkanes with at least 12 carbon atoms.
CC {ECO:0000269|PubMed:9811637}.
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;
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: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Induced by AlkR and n-alkanes only in stationary phase.
CC Repressed by oxidized alkane derivatives. {ECO:0000269|PubMed:9811637}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. AlkB
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ002316; CAA05333.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG68276.1; -; Genomic_DNA.
DR RefSeq; WP_004925568.1; NC_005966.1.
DR AlphaFoldDB; O31250; -.
DR STRING; 62977.ACIAD1411; -.
DR EnsemblBacteria; CAG68276; CAG68276; ACIAD1411.
DR GeneID; 45233825; -.
DR KEGG; aci:ACIAD1411; -.
DR eggNOG; COG3696; Bacteria.
DR HOGENOM; CLU_044462_1_0_6; -.
DR OMA; WHWSNDV; -.
DR OrthoDB; 1202565at2; -.
DR BioCyc; ASP62977:ACIAD_RS06515-MON; -.
DR UniPathway; UPA00191; -.
DR Proteomes; UP000000430; 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; ISS: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; ISS: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..408
FT /note="Alkane 1-monooxygenase"
FT /id="PRO_0000392215"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 150
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 408 AA; 46759 MW; 8A974794555B1466 CRC64;
MNAPVHVDQN FEEVINAARS MREIDRKRYL WMISPALPVI GIGILAGYQF SPRPIKKIFA
LGGPIVLHII IPVIDTIIGK DASNPTSEEI KQLENDPYYA RLVKSFIPLQ YIANVYACYL
VSRKKTSFID KILLGISMGA INGIAVNTAH ELSHKADRLD HILSHLALVP TGYNHFRIEH
PYGHHKRAAT PEDPASSQMG ETFYEFWPRT VFGSLKSAIE IETHRLKRKG KKFWSKDNEL
LQGWGMSAAF HSSIIAIFGK GTIPYLVTQA FYGISLFEII NYIEHYGLKR QKRADGNYER
TMPEHSWNNN NIVTNLFLYQ LQRHSDHHAY PTRPFQALRH FDEAPELPSG YASMLLPAMI
PPLWFKMMDK RVFEHYKEDL TKANIYPKRR AKILAKFGLT DPNIENGK
