MABO1_PAENI
ID MABO1_PAENI Reviewed; 824 AA.
AC Q8GAI3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=4-methylaminobutanoate oxidase (formaldehyde-forming);
DE Short=MABO;
DE EC=1.5.3.19;
DE AltName: Full=Demethylating gamma-N-methylaminobutyrate oxidase;
DE AltName: Full=Gamma-N-methylaminobutyrate oxidase 1;
GN Name=abo; Synonyms=mabO; ORFNames=ORF63;
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, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND MUTAGENESIS OF TRP-66 AND
RP HIS-67.
RC STRAIN=ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511; PLASMID=pAO1;
RX PubMed=15606755; DOI=10.1111/j.1432-1033.2004.04432.x;
RA Chiribau C.B., Sandu C., Fraaije M., Schiltz E., Brandsch R.;
RT "A novel gamma-N-methylaminobutyrate demethylating oxidase involved in
RT catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans
RT pAO1.";
RL Eur. J. Biochem. 271:4677-4684(2004).
RN [3]
RP INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511; PLASMID=pAO1;
RX PubMed=15838033; DOI=10.1128/jb.187.9.3062-3070.2005;
RA Chiribau C.B., Sandu C., Igloi G.L., Brandsch R.;
RT "Characterization of PmfR, the transcriptional activator of the pAO1-borne
RT purU-mabO-folD operon of Arthrobacter nicotinovorans.";
RL J. Bacteriol. 187:3062-3070(2005).
CC -!- FUNCTION: Catalyzes the oxidative demethylation of 4-
CC methylaminobutanoate produced from the pyrrolidine ring of nicotine. To
CC a much lesser extent, can also use sarcosine as substrate, but is not
CC active against dimethylglycine, methylaminopropionitrile,
CC methylaminopropylamine, and alpha-methylaminobutanoate.
CC {ECO:0000269|PubMed:15606755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(methylamino)butanoate + H2O + O2 = 4-aminobutanoate +
CC formaldehyde + H2O2; Xref=Rhea:RHEA:33907, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:59888, ChEBI:CHEBI:66882; EC=1.5.3.19;
CC Evidence={ECO:0000269|PubMed:15606755};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15606755};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000269|PubMed:15606755};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 uM for 4-methylaminobutanoate {ECO:0000269|PubMed:15606755};
CC KM=25 mM for sarcosine {ECO:0000269|PubMed:15606755};
CC Note=kcat is 800 sec(-1) with 4-methylaminobutanoate as substrate.
CC kcat is 4 sec(-1) with sarcosine as substrate.;
CC -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC {ECO:0000269|PubMed:15606755}.
CC -!- INDUCTION: Is transcribed only in the presence of nicotine under the
CC control of the transcriptional activator PmfR. Forms part of an operon
CC with purU, folD, nepA and nepB. {ECO:0000269|PubMed:15838033}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
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DR EMBL; AJ507836; CAD47921.1; -; Genomic_DNA.
DR RefSeq; WP_016359432.1; NC_021229.1.
DR RefSeq; YP_007988747.1; NC_021229.1.
DR AlphaFoldDB; Q8GAI3; -.
DR SMR; Q8GAI3; -.
DR KEGG; ag:CAD47921; -.
DR BioCyc; MetaCyc:MON-17148; -.
DR UniPathway; UPA00106; -.
DR GO; GO:0102317; F:4-methylaminobutyrate oxidase (demethylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019608; P:nicotine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Plasmid.
FT CHAIN 1..824
FT /note="4-methylaminobutanoate oxidase (formaldehyde-
FT forming)"
FT /id="PRO_0000424214"
FT MOD_RES 67
FT /note="Pros-8alpha-FAD histidine"
FT MUTAGEN 66
FT /note="W->F,S: Contains a non-covalently bound FAD. Loss of
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:15606755"
FT MUTAGEN 67
FT /note="H->A: Contains a non-covalently bound FAD. Exhibits
FT about 10% of the wild-type enzyme activity."
FT /evidence="ECO:0000269|PubMed:15606755"
SQ SEQUENCE 824 AA; 89418 MW; 8BB42E2B428385B4 CRC64;
MDRLVDRDIS ASMFTATSHD PLPTHVRTVV VGGGIIGASI AYHLSAAGEN DTLLLESNVL
GSGTSWHAAG LVTGARGTTT MTKLAKYGLD FYSRLEQMSG LDVSFQRCGS LSVARTAGRV
DELLYAKDVA DQQGVRTEWL TEDRYKELWP LATYSGVAGA LLLPDDGHIN PGHATVALAK
LAHSLGTQIR ENVAVHKVLR QGDLVVGVLT DQGIVHCDRV ILACGLWTRD LAATAGVKVP
LYAAEHIHVR SAEIDGAVPE LPVYRDLDNS YYIRHEAGRL LVGAFEPDGL PRPVEEIPSN
GFAEFGPEWE HFAPIRAKAE GVVPALASAG FDRFLNAPES FTPDANFAVG ETSELSNLFV
AAGFNSQGII FAPGIGKELA EWVISGTPGF DSSAVDVQRF SGHQNNRNYL KARTKEGLGR
LYAMHWPNLQ METGRNVRRT PLHARLAELG ACFGEVNGGE RANWYGAPGT SPTYDYSYGR
PNWFDRVAEE HKAAREGVVL FDLSPFAKFE VAGPDALEVC QMAATADIDV ETDKAVYTLF
LNDRAGIELD GTITRLGLDR FLVVTPSFTQ QKTAAYLKRI ARGKAAAVFD CTAALATIGV
MGPKSRELLS RISPEDWSDE AQRYTHGRMV EIADGYAYSL RVSFVGELGY ELYPSADMAV
NVLDALWEAG QDLGLKLAGY HALDSLRSEK GFRHLGHDIG PIDDPYSAGL RFTISMDKPG
GFLGKDALLK LDPTAPDHRT VYVALEDPDP VFVHDETVYC NGLPVGRMTS GSYGHTLGRA
VGIAALEPDA DLSGDFEVQC KGRLYPAKVS RRPFYDPKGE RLRG
