ID   ALMA_ACISP              Reviewed;         497 AA.
AC   A5H9N6;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Probable FAD-binding monooxygenase AlmA {ECO:0000305};
DE            EC=1.14.13.- {ECO:0000305};
DE   AltName: Full=n-alkane metabolism protein A {ECO:0000303|PubMed:17400787};
GN   Name=almA {ECO:0000303|PubMed:17400787};
OS   Acinetobacter sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=ATCC 55024 / DSM 17874 / 6A2;
RX   PubMed=17400787; DOI=10.1128/aem.00064-07;
RA   Throne-Holst M., Wentzel A., Ellingsen T.E., Kotlar H.K., Zotchev S.B.;
RT   "Identification of novel genes involved in long-chain n-alkane degradation
RT   by Acinetobacter sp. strain DSM 17874.";
RL   Appl. Environ. Microbiol. 73:3327-3332(2007).
CC   -!- FUNCTION: Is involved in the degradation of n-alkanes with C chain
CC       lengths of 32 and longer. Allows Acinetobacter sp. strain DSM 17874 to
CC       grow on long-chain n-alkanes such as dotriacontane (C32H66) or
CC       hexatriacontane (C36H74) as a sole carbon source.
CC       {ECO:0000269|PubMed:17400787}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q47PU3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q47PU3};
CC   -!- PATHWAY: Hydrocarbon metabolism; alkane degradation.
CC       {ECO:0000269|PubMed:17400787}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene can no longer utilize n-
CC       alkanes with C chain lengths of 32 and 36, but can still grow with C24,
CC       C20, C16 alkanes or acetate as a sole carbon source.
CC       {ECO:0000269|PubMed:17400787}.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; EF212873; ABQ18224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5H9N6; -.
DR   SMR; A5H9N6; -.
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:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0043448; P:alkane catabolic process; IMP:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   Pfam; PF00743; FMO-like; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Cell membrane; FAD; Flavoprotein; Membrane; Monooxygenase; NADP;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..497
FT                   /note="Probable FAD-binding monooxygenase AlmA"
FT                   /id="PRO_0000435699"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         36
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         54..56
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         56
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         62
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         104
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         184..190
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         208..209
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         292..293
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT   BINDING         395
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q47PU3"
SQ   SEQUENCE   497 AA;  55913 MW;  3EEC59B321409A4D CRC64;
     MEKQVDVLII GAGISGIGLA VHLSKNCPQR KFEILERRES FGGTWDLFRY PGIRSDSDMS
     TFGFNFKPWA KDKVLASGAE IKGYLSDVIS ENQLKDKIHF GHRVLSANYD STKKKWLVEI
     EDNNKKKQTW SANFVMGCTG YYNYDQGYAP KFPKQEDFKG QFIHPQHWPE NLDYTGKKVV
     IIGSGATAIT LVPSMVKGGA GHVTMLQRSP TYIATIPSID FIYEKTRKFM SEETAYKFTR
     ARNIGMQRGI YALAQKYPKT VRRLLLKGIE LQLKGKVDMK HFTPSYNPWD QRLCVVPDGD
     LFKALREGQA SVETDQIEKF TANGIQLKSG KHLEADIVIS ATGLEIQILG GVQGSIDGKP
     MNTSQHMLYQ GVMVSDVPNM AMIIGYINAS WTLKVDIAAD YICRLINHMD KNGFDEVIAH
     ADPSQRENDT IMGKMSSGYI ARAADVMPKQ GKQAPWKITN NYLADRKELK DAKFNDGVLE
     FHKRGEQTAN RKPKLVS