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Database: UniProt
Entry: A0A132C1C3_9RHOB
LinkDB: A0A132C1C3_9RHOB
Original site: A0A132C1C3_9RHOB 
ID   A0A132C1C3_9RHOB        Unreviewed;       805 AA.
AC   A0A132C1C3;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:KUP93927.1};
DE            EC=1.5.3.19 {ECO:0000313|EMBL:KUP93927.1};
GN   Name=mlr_1 {ECO:0000313|EMBL:KUP93927.1};
GN   ORFNames=TRIHO_12480 {ECO:0000313|EMBL:KUP93927.1};
OS   Tritonibacter horizontis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Tritonibacter.
OX   NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP93927.1, ECO:0000313|Proteomes:UP000068382};
RN   [1] {ECO:0000313|EMBL:KUP93927.1, ECO:0000313|Proteomes:UP000068382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O3.65 {ECO:0000313|EMBL:KUP93927.1,
RC   ECO:0000313|Proteomes:UP000068382};
RA   Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT   "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT   Tritonibacter horizontis.";
RL   Submitted (DEC-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:KUP93927.1}.
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DR   EMBL; LPUY01000040; KUP93927.1; -; Genomic_DNA.
DR   RefSeq; WP_068241357.1; NZ_LPUY01000040.1.
DR   AlphaFoldDB; A0A132C1C3; -.
DR   PATRIC; fig|1768241.3.peg.1307; -.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000068382; 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:KUP93927.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068382}.
FT   DOMAIN          6..367
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          370..423
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          427..692
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          718..797
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   805 AA;  88612 MW;  4EA2D7FC518F647A CRC64;
     MKTTTRVAVI GGGVVGCSVL YHLTKLGWSD VMLIERSELT SGSTWHAAGG FHTLNGDTNM
     AALQGYTIKL YKELEAITGM SCGLHHVGGV TLADTQERFD MLKAERAKHR FMGLETEIVS
     PEEIKKIAPV TNIDGIVGGL YDPLDGHLDP SGTTHAYAKA ARMGGATIET HCKVIETNQR
     PDGTWDVVTN KGTIHAEHIV NAGGLWAREV GAMAGIYFPL HPMEHQYIVT DEVPMVAEII
     DGGGEHPHVM DPAGESYLRQ EGRGLCIGFY EQPCRPWAVD GTPWDFGHEL LPDDFDKIEE
     SIEFAYKRFP ALAEAGVKSV IHGPFTFAPD GNPLVGPVPG VRNYWSACAV MAGFSQGGGV
     GLMLAQWMVE GECERDTAAM DVARFGTWIT PGYTRPKVVE NYQKRFSIAY PNEELPAARP
     FRTTPMYDIF DSMGAVWGHQ YGTEIPNYFA AEGEARYETP SFRRSNAFDA TAREVKAVRE
     AVGINEIHNF GKYRVKGAGA RAWLDRIMAG RVPQQGRLSL TPMLSPKGRL IGDFTISCLA
     EDDFQLTASY GAQAYHMRWF LQNRDAGVTI DNVSDQVNGF QIAGPKAREV LQACTRSDIS
     DMRFLDVRRL TVGMVDCLVQ RVSYTGDLGY EIYCDLPSQR ALWTSLWGAG QSHGMKPFGM
     RAMMSLRLDK FFGSWLSEFS PDYTAAETGL DRFISFKKPV DFIGRSAAEA ERVTGVNRKL
     CAFEVSAEDA DVVAYEPIWL DGDVVGFCTS GGYSHYAQKS IALGFLPVDR IADGLEVEIE
     ILGKRHAARL LAEPLFDTDG TRMRG
//
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