ALKB1_PSEAE
ID ALKB1_PSEAE Reviewed; 382 AA.
AC Q9I0R2;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Alkane 1-monooxygenase 1;
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=alkB1; OrderedLocusNames=PA2574;
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=XCZ;
RA Shen B., Lu J., Zhang L.;
RT "Identification of genes involved in n-alkane degradation by Pseudomonas
RT aeruginosa XCZ.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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 C16-C24 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 slowly 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU675620; ACD75516.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05962.1; -; Genomic_DNA.
DR PIR; A83325; A83325.
DR RefSeq; NP_251264.1; NC_002516.2.
DR RefSeq; WP_003102475.1; NZ_QZGE01000008.1.
DR AlphaFoldDB; Q9I0R2; -.
DR STRING; 287.DR97_5595; -.
DR PaxDb; Q9I0R2; -.
DR PRIDE; Q9I0R2; -.
DR EnsemblBacteria; AAG05962; AAG05962; PA2574.
DR GeneID; 878705; -.
DR KEGG; pae:PA2574; -.
DR PATRIC; fig|208964.12.peg.2694; -.
DR PseudoCAP; PA2574; -.
DR HOGENOM; CLU_044462_1_0_6; -.
DR InParanoid; Q9I0R2; -.
DR OMA; WHWSNDV; -.
DR PhylomeDB; Q9I0R2; -.
DR BioCyc; PAER208964:G1FZ6-2611-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..382
FT /note="Alkane 1-monooxygenase 1"
FT /id="PRO_0000392218"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
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|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; 43339 MW; 261BA0A90CF7D072 CRC64;
MFENFSPSTM LAIKKYAYWL WLLLALSMPF NYWMAQDSAH PAFWAFSLVI AVFGIGPLLD
MLFGRDPANP DEETQTPQLL GQGYYVLLTL ATVPVLIGTL VWAAGVFVAF QEWGWLGRLG
WILSMGTVMG AVGIVVAHEL IHKDSALEQA AGGILLAAVC YAGFKVEHVR GHHVHVSTPE
DASSARFGQS VYQFLPHAYK YNFLNAWRLE AVRLRKKGLP VFGWQNELIW WYLLSLALLV
GFGWAFGWLG MVFFLGQAFV AVTLLEIINY VEHYGLHRRK GEDGRYERTN HTHSWNSNFV
FTNLVLFHLQ RHSDHHAFAK RPYQVLRHYD DSPQMPSGYA GMVVLALIPP LWRAVMDPKV
RAYYAGEEFQ LTAEQSERPA AS
