MABO2_PAENI
ID MABO2_PAENI Reviewed; 421 AA.
AC Q8GAJ0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=4-methylaminobutanoate oxidase (methylamine-forming);
DE EC=1.5.3.21;
DE AltName: Full=Gamma-N-methylaminobutyrate oxidase 2;
GN Name=mao; ORFNames=ORF56;
OS Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans).
OG Plasmid pAO1.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=29320;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511; PLASMID=pAO1;
RX PubMed=12618462; DOI=10.1128/jb.185.6.1976-1986.2003;
RA Igloi G.L., Brandsch R.;
RT "Sequence of the 165-kilobase catabolic plasmid pAO1 from Arthrobacter
RT nicotinovorans and identification of a pAO1-dependent nicotine uptake
RT system.";
RL J. Bacteriol. 185:1976-1986(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, PATHWAY, AND INDUCTION.
RC STRAIN=ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511; PLASMID=pAO1;
RX PubMed=16689938; DOI=10.1111/j.1742-4658.2006.05173.x;
RA Chiribau C.B., Mihasan M., Ganas P., Igloi G.L., Artenie V., Brandsch R.;
RT "Final steps in the catabolism of nicotine.";
RL FEBS J. 273:1528-1536(2006).
CC -!- FUNCTION: Catalyzes the removal of methylamine from 4-
CC methylaminobutanoate with the formation of succinate semialdehyde. Is
CC involved in the catabolism of 4-methylaminobutanoate produced from
CC nicotine. Has a very weak monoamine oxidase activity with 4-
CC aminobutanoate. Cannot use spermidine, spermine, sarcosine,
CC dimethylglycine, glycine, choline, betaine, alpha-methylamino
CC isobutyrate, methylamine propionitrile and methylamino propylamine as
CC substrate. {ECO:0000269|PubMed:16689938}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(methylamino)butanoate + H2O + O2 = H2O2 + methylamine +
CC succinate semialdehyde; Xref=Rhea:RHEA:33915, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57706,
CC ChEBI:CHEBI:59338, ChEBI:CHEBI:66882; EC=1.5.3.21;
CC Evidence={ECO:0000269|PubMed:16689938};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16689938};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for 4-methylaminobutanoate {ECO:0000269|PubMed:16689938};
CC KM=6.66 mM for 4-aminobutanoate {ECO:0000269|PubMed:16689938};
CC Note=kcat is 1230 sec(-1) with 4-methylaminobutanoate as substrate.
CC kcat is 878 sec(-1) with 4-aminobutanoate as substrate.;
CC pH dependence:
CC Optimum pH is 9.8. {ECO:0000269|PubMed:16689938};
CC -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC {ECO:0000269|PubMed:16689938}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16689938}.
CC -!- INDUCTION: Is transcribed only in the presence of nicotine.
CC {ECO:0000269|PubMed:16689938}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AJ507836; CAD47914.1; -; Genomic_DNA.
DR RefSeq; WP_016359425.1; NC_021229.1.
DR RefSeq; YP_007988740.1; NC_021229.1.
DR PDB; 7RT0; X-ray; 1.80 A; A=1-421.
DR PDBsum; 7RT0; -.
DR AlphaFoldDB; Q8GAJ0; -.
DR SMR; Q8GAJ0; -.
DR KEGG; ag:CAD47914; -.
DR BioCyc; MetaCyc:MON-17144; -.
DR UniPathway; UPA00106; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019608; P:nicotine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 2.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; Oxidoreductase; Plasmid.
FT CHAIN 1..421
FT /note="4-methylaminobutanoate oxidase (methylamine-
FT forming)"
FT /id="PRO_0000424218"
FT BINDING 31
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 26..37
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:7RT0"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:7RT0"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 294..302
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:7RT0"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:7RT0"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:7RT0"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:7RT0"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:7RT0"
FT HELIX 389..410
FT /evidence="ECO:0007829|PDB:7RT0"
SQ SEQUENCE 421 AA; 44431 MW; 1DC4C705858C6723 CRC64;
MGRIGILGAG LAGLAAATKL AEAGENVTVF EARNRPGGRV WSETLDTPKG SYVIERGAEF
VLDGYTSMRR LLSQFGLSLV DTGMSYYVRE PGDTTGITCD DIIRTGREAL ELASGSGLQG
TAEELLAKLP DEPELVDALR ARIEISTAVS ASEVTARSLQ HIASFEPKPS WRVAGGNQRL
PDAMAAALGS AVRYGETVRA VENISDGGVL VTTDTDTSVF DTVVVALPLA VIRDSQLNLP
TTEARDAALK HVLQGHAAKL HLPLETQPAT SAVMSVEGRY WTWTATDESG AVAPVLNAFM
GSPSAITRAN LKQRPAEWVA KARALRTDLA IPQDAAALTT VWSEDQLAGG AYAAHAPGVT
AAGTALLEKP VGDVFWAGEY SEPEFVGLME GAIRSGERAA GRVMQRLETK SGNSDSERSK
A
