ALKB_PSEOL
ID ALKB_PSEOL Reviewed; 401 AA.
AC P12691;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 oleovorans.
OG Plasmid OCT.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas;
OC Pseudomonas oleovorans/pseudoalcaligenes group.
OX NCBI_TaxID=301;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC STRAIN=GPo1;
RX PubMed=2647718; DOI=10.1016/s0021-9258(18)83564-5;
RA Kok M., Oldenhuis R., van der Linden M.P.G., Raathes P., Kingma J.,
RA van Lelyveld P.H., Witholt B.;
RT "The Pseudomonas oleovorans alkane hydroxylase gene. Sequence and
RT expression.";
RL J. Biol. Chem. 264:5435-5441(1989).
RN [2]
RP FUNCTION, AND COFACTOR.
RX PubMed=921275; DOI=10.1016/0003-9861(77)90388-5;
RA Ruettinger R.T., Griffith G.R., Coon M.J.;
RT "Characterization of the omega-hydroxylase of Pseudomonas oleovorans as a
RT nonheme iron protein.";
RL Arch. Biochem. Biophys. 183:528-537(1977).
RN [3]
RP TOPOLOGY.
RX PubMed=1315749; DOI=10.1016/s0021-9258(19)50407-0;
RA van Beilen J.B., Penniga D., Witholt B.;
RT "Topology of the membrane-bound alkane hydroxylase of Pseudomonas
RT oleovorans.";
RL J. Biol. Chem. 267:9194-9201(1992).
RN [4]
RP COFACTOR.
RX PubMed=9096332; DOI=10.1073/pnas.94.7.2981;
RA Shanklin J., Achim C., Schmidt H., Fox B.G., Muenck E.;
RT "Mossbauer studies of alkane omega-hydroxylase: evidence for a diiron
RT cluster in an integral-membrane enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2981-2986(1997).
RN [5]
RP INDUCTION.
RX PubMed=10692156; DOI=10.1046/j.1365-2958.2000.01751.x;
RA Canosa I., Sanchez-Romero J.M., Yuste L., Rojo F.;
RT "A positive feedback mechanism controls expression of AlkS, the
RT transcriptional regulator of the Pseudomonas oleovorans alkane degradation
RT pathway.";
RL Mol. Microbiol. 35:791-799(2000).
RN [6]
RP MUTAGENESIS OF HIS-138; HIS-142; HIS-163; HIS-168; HIS-172; HIS-173;
RP ASP-181; HIS-308; HIS-312; HIS-315; HIS-316 AND HIS-318.
RX PubMed=12804773; DOI=10.1016/s0014-5793(03)00529-5;
RA Shanklin J., Whittle E.;
RT "Evidence linking the Pseudomonas oleovorans alkane omega-hydroxylase, an
RT integral membrane diiron enzyme, and the fatty acid desaturase family.";
RL FEBS Lett. 545:188-192(2003).
CC -!- FUNCTION: Catalyzes the hydroxylation of n-alkanes and fatty acids in
CC the presence of a NADH-rubredoxin reductase and rubredoxin.
CC {ECO:0000269|PubMed:921275}.
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;
CC Evidence={ECO:0000269|PubMed:9096332, ECO:0000269|PubMed:921275};
CC Note=Binds 2 Fe(3+) ions per subunit. {ECO:0000269|PubMed:9096332,
CC ECO:0000269|PubMed:921275};
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:10692156}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. AlkB
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ245436; CAB54050.1; -; Genomic_DNA.
DR PIR; A32849; A31266.
DR AlphaFoldDB; P12691; -.
DR BioCyc; MetaCyc:MON-3842; -.
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; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
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; Direct protein sequencing; Iron;
KW Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Plasmid;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..401
FT /note="Alkane 1-monooxygenase"
FT /id="PRO_0000185434"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1315749"
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 40..41
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1315749"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 63..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1315749"
FT TRANSMEM 89..111
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 112..113
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1315749"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 135..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1315749"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 250
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1315749"
FT TRANSMEM 251..270
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 271..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1315749"
FT BINDING 138
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 168
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 312
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 315
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 316
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MUTAGEN 138
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12804773"
FT MUTAGEN 142
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12804773"
FT MUTAGEN 163
FT /note="H->A: 54% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:12804773"
FT MUTAGEN 168
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12804773"
FT MUTAGEN 172
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12804773"
FT MUTAGEN 173
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12804773"
FT MUTAGEN 181
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12804773"
FT MUTAGEN 308
FT /note="H->A: 33% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:12804773"
FT MUTAGEN 312
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12804773"
FT MUTAGEN 315
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12804773"
FT MUTAGEN 316
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12804773"
FT MUTAGEN 318
FT /note="H->A: 28% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:12804773"
SQ SEQUENCE 401 AA; 45806 MW; F32896458039D11B CRC64;
MLEKHRVLDS APEYVDKKKY LWILSTLWPA TPMIGIWLAN ETGWGIFYGL VLLVWYGALP
LLDAMFGEDF NNPPEEVVPK LEKERYYRVL TYLTVPMHYA ALIVSAWWVG TQPMSWLEIG
ALALSLGIVN GLALNTGHEL GHKKETFDRW MAKIVLAVVG YGHFFIEHNK GHHRDVATPM
DPATSRMGES IYKFSIREIP GAFIRAWGLE EQRLSRRGQS VWSFDNEILQ PMIITVILYA
VLLALFGPKM LVFLPIQMAF GWWQLTSANY IEHYGLLRQK MEDGRYEHQK PHHSWNSNHI
VSNLVLFHLQ RHSDHHAHPT RSYQSLRDFP GLPALPTGYP GAFLMAMIPQ WFRSVMDPKV
VDWAGGDLNK IQIDDSMRET YLKKFGTSSA GHSSSTSAVA S
