ALKB2_PSEAE
ID ALKB2_PSEAE Reviewed; 377 AA.
AC Q6H941; Q9I3I8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Alkane 1-monooxygenase 2;
DE EC=1.14.15.3 {ECO:0000269|PubMed:14574114};
DE AltName: Full=Alkane hydroxylase;
DE Short=AHs;
DE AltName: Full=Terminal alkane hydroxylase;
GN Name=alkB2; OrderedLocusNames=PA1525;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=19G12, 63741, 892,
RC ATCC 10145 / DSM 50071 / JCM 5962 / LMG 1242 / NBRC 12689 / NCIMB 8295 /
RC NRRL B-771, ATCC15524, ATCC15691, ATCC33356, ATCC33818, CECT119, CHA, DM,
RC G7, HJ2, K9, RR1, SG1, and SG31;
RX PubMed=15205425; DOI=10.1128/jb.186.13.4228-4237.2004;
RA Morales G., Wiehlmann L., Gudowius P., van Delden C., Tummler B.,
RA Martinez J.L., Rojo F.;
RT "Structure of Pseudomonas aeruginosa populations analyzed by single
RT nucleotide polymorphism and pulsed-field gel electrophoresis genotyping.";
RL J. Bacteriol. 186:4228-4237(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP FUNCTION IN ALKANE DEGRADATION.
RX PubMed=14574114; DOI=10.1023/a:1026000622765;
RA Smits T.H., Witholt B., van Beilen J.B.;
RT "Functional characterization of genes involved in alkane oxidation by
RT Pseudomonas aeruginosa.";
RL Antonie Van Leeuwenhoek 84:193-200(2003).
RN [4]
RP INDUCTION, SUBSTRATE SPECIFICITY, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12730186; DOI=10.1128/jb.185.10.3232-3237.2003;
RA Marin M.M., Yuste L., Rojo F.;
RT "Differential expression of the components of the two alkane hydroxylases
RT from Pseudomonas aeruginosa.";
RL J. Bacteriol. 185:3232-3237(2003).
CC -!- FUNCTION: Catalyzes the hydroxylation of n-alkanes in the presence of a
CC NADH-rubredoxin reductase and rubredoxin. It preferably hydroxylases
CC C12-C20 hydrocarbons. {ECO:0000269|PubMed:14574114}.
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:0000269|PubMed:14574114};
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 when cells grow fast during the
CC exponential phase. Expression decreases significantly when cells
CC reached the stationary phase of growth. Repressed by citrate.
CC {ECO:0000269|PubMed:12730186}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. AlkB
CC subfamily. {ECO:0000305}.
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DR EMBL; AE004091; AAG04914.1; -; Genomic_DNA.
DR EMBL; AJ633602; CAG17594.1; -; Genomic_DNA.
DR EMBL; AJ633603; CAG17595.1; -; Genomic_DNA.
DR EMBL; AJ633604; CAG17596.1; -; Genomic_DNA.
DR EMBL; AJ633605; CAG17597.1; -; Genomic_DNA.
DR EMBL; AJ633606; CAG17598.1; -; Genomic_DNA.
DR EMBL; AJ633608; CAG17600.1; -; Genomic_DNA.
DR EMBL; AJ633609; CAG17601.1; -; Genomic_DNA.
DR EMBL; AJ633610; CAG17602.1; -; Genomic_DNA.
DR EMBL; AJ633611; CAG17603.1; -; Genomic_DNA.
DR EMBL; AJ633612; CAG17604.1; -; Genomic_DNA.
DR EMBL; AJ633613; CAG17605.1; -; Genomic_DNA.
DR EMBL; AJ633614; CAG17606.1; -; Genomic_DNA.
DR EMBL; AJ633615; CAG17607.1; -; Genomic_DNA.
DR EMBL; AJ633617; CAG17609.1; -; Genomic_DNA.
DR EMBL; AJ633618; CAG17610.1; -; Genomic_DNA.
DR EMBL; AJ633619; CAG17611.1; -; Genomic_DNA.
DR EMBL; AJ633620; CAG17612.1; -; Genomic_DNA.
DR PIR; B83454; B83454.
DR RefSeq; NP_250216.1; NC_002516.2.
DR RefSeq; WP_003083349.1; NZ_QZGE01000032.1.
DR AlphaFoldDB; Q6H941; -.
DR STRING; 287.DR97_411; -.
DR PaxDb; Q6H941; -.
DR PRIDE; Q6H941; -.
DR EnsemblBacteria; AAG04914; AAG04914; PA1525.
DR GeneID; 879517; -.
DR KEGG; pae:PA1525; -.
DR PATRIC; fig|208964.12.peg.1578; -.
DR PseudoCAP; PA1525; -.
DR HOGENOM; CLU_044462_1_0_6; -.
DR InParanoid; Q6H941; -.
DR OMA; CTYAFIP; -.
DR PhylomeDB; Q6H941; -.
DR BioCyc; PAER208964:G1FZ6-1552-MON; -.
DR UniPathway; UPA00191; -.
DR Proteomes; UP000002438; 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 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..377
FT /note="Alkane 1-monooxygenase 2"
FT /id="PRO_0000392219"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
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 377 AA; 43408 MW; 1F23438DA9F1822E CRC64;
MFASLSSAWM LRLKKYGYWI WLIAVLGIPL SYWWSLGSDY PNAWPWLVIS VVFGLIPILD
AIVGRDPANP EEASEVPEME AQGYYRVLSL ATVPLLLGML VWSGWILAHE TRWDWVGQLG
WILSVGTVMG AIGITVSHEL IHKDPQLEQN AGGLLLAAVC YAGFKVEHVR GHHVHVSTPE
DASSSRYGQS LYSFLPHAYK HNFLNAWRLE AERLKRKGLP ALHWRNELIW WYAISALFLL
GFSLAFGWLG AIFFLGQSVM AFTLLEIVNY VEHYGLHRRR LDNGRYERTT PEHSWNSNFL
LTNLFLFHLQ RHSDHHAYAK RRYQVLRHYD SSPQLPNGYA GMIVLALFPP LWRAVMDPKV
RAYYAGEEYQ LTDTQRI
