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Database: UniProt
Entry: A0A0L6CT00_9RHOB
LinkDB: A0A0L6CT00_9RHOB
Original site: A0A0L6CT00_9RHOB 
ID   A0A0L6CT00_9RHOB        Unreviewed;       808 AA.
AC   A0A0L6CT00;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:KNX40897.1};
DE            EC=1.5.3.19 {ECO:0000313|EMBL:KNX40897.1};
GN   Name=mlr_5 {ECO:0000313|EMBL:KNX40897.1};
GN   ORFNames=ROTO_25850 {ECO:0000313|EMBL:KNX40897.1};
OS   Roseovarius tolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX40897.1, ECO:0000313|Proteomes:UP000037046};
RN   [1] {ECO:0000313|Proteomes:UP000037046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA   Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT   "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT   Acylated Alanine Methyl Esters (NAMEs).";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNX40897.1}.
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DR   EMBL; LGVV01000037; KNX40897.1; -; Genomic_DNA.
DR   RefSeq; WP_050663444.1; NZ_LGVV01000037.1.
DR   AlphaFoldDB; A0A0L6CT00; -.
DR   STRING; 74031.SAMN04488077_10161; -.
DR   PATRIC; fig|74031.6.peg.2637; -.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000037046; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:KNX40897.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037046}.
FT   DOMAIN          7..364
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          367..421
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          425..692
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          733..800
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   808 AA;  89041 MW;  D5726865474888AA CRC64;
     MKTHAQAVVI GGGVIGCSIL YHLAKLGWSD VVLLERDELT SGSTWHAAAN IHGLHDSANI
     SRLQHYTMNL YNALEEETGQ SCGVFQPGSL YLAQTENRSH QLRLQAAKAK LYGMNFHEIS
     RDEAERLHPL VNFDGIRCIM YEPDGGNVDP SGVTNAYAVG ARQRGAEIHR FTPVMATVPQ
     ADGTWIVETP KGNIHTPWVI NAAGLWGREV AKLAGIELPL QPTEHQYFVT ETIAEIAGMD
     RRLPSVADRD GEYYLRQEGK GLLIGAYERD MRFWAEEGTP LDFAHDLFPD DLERIEDNMM
     RAIDRVPVVG EAGIKRVING PMIWSPDANV ILGPVPELKG YFCCNGIIPG FSQSAGMGWM
     VAEWLVHGEM KYDMFAWDIA RFGLWANDRE FVKAKVKDQY AHRFAIHYPN EERAAGRPLR
     VRPAYEMQKD MGAVFGLNYG WEHPLWFSEV PGTVDTNGFT RQNWWGPVGE EARMLRERAG
     IIDISNFAKY RVKGPGAEEW LNAVFANRMP RAVGRSCLTP LIGVRGGIAG DATVTRLGEE
     EFWVISSGMA ERYHKRFFDA VPLPEGTVFE SLTEAVCGFN VAGPRSREML QRLTNASLST
     EDFAFMRSAK IEIAGVSCVA LRVSFTGDLG WELHCATEDQ ARLYAALIEA GREMGAGPVG
     SRALMSLRIE KGYGSWSREY SPEYWPQEAG LAGLCKMDKD FLNKAALEAV IGEAPRERLV
     LLALEAADVM ASNADATGGE PIFKDGVGVG RVTSGAYGYA VGMSLALGYV KGGAGPGDAV
     EVMVLGQPHR ARILHEPPFD PEGVRLRA
//
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