ID A0A1Y5T6B1_9RHOB Unreviewed; 824 AA.
AC A0A1Y5T6B1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:SLN54743.1};
DE EC=1.5.3.19 {ECO:0000313|EMBL:SLN54743.1};
GN Name=mlr_14 {ECO:0000313|EMBL:SLN54743.1};
GN ORFNames=TRL7639_02907 {ECO:0000313|EMBL:SLN54743.1};
OS Falsiruegeria litorea R37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Falsiruegeria.
OX NCBI_TaxID=1200284 {ECO:0000313|EMBL:SLN54743.1, ECO:0000313|Proteomes:UP000193077};
RN [1] {ECO:0000313|EMBL:SLN54743.1, ECO:0000313|Proteomes:UP000193077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7639 {ECO:0000313|EMBL:SLN54743.1,
RC ECO:0000313|Proteomes:UP000193077};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; FWFO01000002; SLN54743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5T6B1; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000193077; Unassembled WGS sequence.
DR GO; GO:0102317; F:4-methylaminobutyrate oxidase (demethylating) activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 PANTHER; PTHR13847:SF187; DIMETHYLGLYCINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
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; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:SLN54743.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193077}.
FT DOMAIN 28..386
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 389..442
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 445..713
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 738..816
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 824 AA; 91148 MW; 57060B3DA9D57080 CRC64;
MSDQFTQSTL NIHKEEGTGG KPLPSHAKVV VIGGGVVGCS ILFHLAKFGW KDVVLLERDE
LTSGSSWHAA GQIHTISSDP NISRLQSYTI DLYKEIEETS GHSVGLHITG GFYLASNKTW
YDYLKRERSK ARYMGLNQEF ISPAEVAERH PLIDPKHYYA ALWDDQDGDL DPSGATYAFA
KSAKVHGAQY FTHCGVTATR QRPDGSWDVT TPKGVINAEH IVNCGGLWAR EVGHMQGLNL
PVQPMEHHYL ITEKIDAVAK HPTRLPAGID YEANIYFRQE RQGMLLGTYE PKGTPWKVGG
TPWDFGHELL QPDLDRIADR LEMSFERIPA IGEVGIKDMI NGPFTFGPDG NPMIGPVPGM
KNYWCAVGVM AGFCQGGGVG LTMAEWMIDG EPSIDVWAMD VARFGDFATP DWGTVKSTEN
YERRFVMTFP NETLPKGRMQ KTTALYDRLV ARGARMGQGF GLENALWFAD GPEDAHEEPT
FERNRSHEYV AREVQAVREA VGGIEIANFA KHEFKGPGAR SYLDRVLAGY VPKPGRLTLT
PMLTPNGKLY GDLTVACLGE EHFMLFGSGA MQEAHRRWFE KDLPDDVSYA NVSDDWHGIA
LSGPKSRALL QGIMREDISA QTFKFRDLRQ TFVGGVPVIL NRISFSGELG YEIYCKPQYL
LRLAEAIEEA GADLGYRWYG ARALMSMRLE KGWGVWTLDF RPDFDAVESG MDVFINWKKD
FVGKDATLAA RAAGPKQRLV TMTIDVDGID VSNDEAILKD GAAVGYVSSG GYAHHAQRSM
AMGYIAAEHA APGTQLQVEI LGEMYDTEVL GAPIYDANGA NMRA
//