ALKB_PSEPU
ID ALKB_PSEPU Reviewed; 402 AA.
AC Q9WWW6;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 59.
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;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=P1;
RX PubMed=11207749; DOI=10.1046/j.1462-2920.1999.00037.x;
RA Smits T.H.M., Roethlisberger M., Witholt B., Van Beilen J.B.;
RT "Molecular screening for alkane hydroxylase genes in Gram-negative and
RT Gram-positive strains.";
RL Environ. Microbiol. 1:307-317(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=P1;
RX PubMed=11390693; DOI=10.1099/00221287-147-6-1621;
RA Van Beilen J.B., Panke S., Lucchini S., Franchini A.G., Roethlisberger M.,
RA Witholt B.;
RT "Analysis of Pseudomonas putida alkane degradation gene clusters and
RT flanking insertion sequences: evolution and regulation of the alk-genes.";
RL Microbiology 147:1621-1630(2001).
CC -!- FUNCTION: Catalyzes the hydroxylation of n-alkanes in the presence of a
CC NADH-rubredoxin reductase and rubredoxin. {ECO:0000250}.
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:0000250|UniProtKB:O31250};
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 -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. AlkB
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ233397; CAB51047.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9WWW6; -.
DR BRENDA; 1.14.15.3; 5092.
DR UniPathway; UPA00191; -.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Iron; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..402
FT /note="Alkane 1-monooxygenase"
FT /id="PRO_0000392220"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
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"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 402 AA; 46078 MW; E41B6873FA24D29C CRC64;
MNGKSSVLDS APEYVDKKKY FWILSTFWPA TPMIGIWLAN ETGWGIFYGL VLAVWYGVLP
LLDAMFGEDF NNPPEEVVEK LEKERYYRVL TYLTVPMHYA ALIVSAWWVG TQSMSWFEIV
ALALSLGIVN GLALNTGHEL GHKKEAFDRW MAKIVLAVVG YGHFFIEHNK GHHRDVATPM
DPATSRMGEN IYKFSTREIP GAFRRAWGLE EQRLSRRGQS VWSFDNEILQ PMVITVVLYT
LLLAFFGPKM LVFLPIQMAF GWWQLTSANY IEHYGLLREK MADGRYEHQK PHHSWNSNHI
VSNLVLFHLQ RHSDHHAHPT RSYQSLRDFP GLPALPTGYP GAFLMAMIPQ WFRSVMDPKV
VNWANGDLSK IQIEDSMRAE YIKKFTHNVG ADDKRGATAV AS
