ALMA_ACIAD
ID ALMA_ACIAD Reviewed; 498 AA.
AC Q6F7T9;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable FAD-binding monooxygenase AlmA {ECO:0000305};
DE EC=1.14.13.- {ECO:0000305};
GN Name=almA {ECO:0000250|UniProtKB:A5H9N6};
GN OrderedLocusNames=ACIAD3192 {ECO:0000312|EMBL:CAG69876.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
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 able to catalyze the degradation of n-alkanes with C chain
CC lengths of 32 and 36. Probably allows Acinetobacter baylyi strain ADP1
CC to grow on the long-chain n-alkane dotriacontane (C32H66) as a sole
CC carbon source. {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 -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; CR543861; CAG69876.1; -; Genomic_DNA.
DR RefSeq; WP_004924170.1; NC_005966.1.
DR AlphaFoldDB; Q6F7T9; -.
DR SMR; Q6F7T9; -.
DR STRING; 62977.ACIAD3192; -.
DR EnsemblBacteria; CAG69876; CAG69876; ACIAD3192.
DR GeneID; 45235407; -.
DR KEGG; aci:ACIAD3192; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_032067_2_0_6; -.
DR OMA; ASWTLKC; -.
DR OrthoDB; 324612at2; -.
DR BioCyc; ASP62977:ACIAD_RS14460-MON; -.
DR UniPathway; UPA00191; -.
DR Proteomes; UP000000430; 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: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; IGI: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; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..498
FT /note="Probable FAD-binding monooxygenase AlmA"
FT /id="PRO_0000435700"
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 498 AA; 55896 MW; 68204BAF0927578F CRC64;
MEKHIDILIV GAGISGIGIA AHLSKDAPQR QFEIIERREN IGGTWDLFRY PGIRSDSDMS
TFGFNFKPWQ SPNVLASGSS IKGYLSEVVD EYDLKKKIHF KHRVLAANYD TASKKWYVEI
EDAAQKKQTW IANFIVGCTG YYNYDQGFEP DFPNKDAFKG QFIHPQHWPE NLDYVGKKVV
IIGSGATAIT LVPAMSKGGA EHVTMLQRSP TYIASIPSID FVYDKMRKVL PEDLAYKLTR
ARNIGVQRGI YTLSQKQPKL VRKFLLKSIE MQLKGKVDMK HFTPSYNPWD QRLCVVPDGD
LFKILRSGQA SVETDQIEKF TETGIQLKSG KHLDADIVVS ATGLEIQILG GIKGTIDGQP
LDTSKSMLYQ GVMVSDVPNM AMIIGYINAS WTLKVDVAAD YICRLLNYMD KQGYDEVIPE
GDQTELMEDT VMGSLTSGYI ARAANVMPKQ GKHAPWKVTN NYLADRKALK NARFDDGVLH
FDKKTDTVER KTKPKLVS
