ID   A0A1M5BJA8_9RHOB        Unreviewed;       820 AA.
AC   A0A1M5BJA8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:SHF42526.1};
GN   ORFNames=SAMN05444273_1064 {ECO:0000313|EMBL:SHF42526.1};
OS   Litoreibacter ascidiaceicola.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Litoreibacter.
OX   NCBI_TaxID=1486859 {ECO:0000313|EMBL:SHF42526.1, ECO:0000313|Proteomes:UP000184144};
RN   [1] {ECO:0000313|EMBL:SHF42526.1, ECO:0000313|Proteomes:UP000184144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100566 {ECO:0000313|EMBL:SHF42526.1,
RC   ECO:0000313|Proteomes:UP000184144};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; FQUV01000006; SHF42526.1; -; Genomic_DNA.
DR   RefSeq; WP_073144443.1; NZ_FQUV01000006.1.
DR   AlphaFoldDB; A0A1M5BJA8; -.
DR   STRING; 1486859.SAMN05444273_1064; -.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000184144; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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:SF193; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..367
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          370..425
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          427..699
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          726..810
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   820 AA;  89756 MW;  35ADC0F5153B2EA0 CRC64;
     MAKTELPERA QYVIVGGGIV GCSVAYHLAK MGHNDVVLLE QGQLSCGTTW HAAGLVGQLR
     SQPAMTNLIR YSTQLYADLE AETELATGWM QCGSVTVART EDRMTMLMRT AAAARAQGVD
     VDVLTPQQAQ DKWPVMQVDD LKGGIWMPGD GKANPTDLTQ SLAKGARMRG AKVIEGIKVT
     DVLTKDGRVT GVETDQGRIE AEVVVNCAGQ WARSLGKMCG VNVPLHSAEH MYIVTETMKG
     VNPDLPVLRD PDGFIYFKEE TGGLVMGGFE PEAKPWGMDG IPDKFEFSLL PDDWEQFEIL
     LENALIRVPE METTGVRKFY NGPESFTPDN NYLLGEAPEL KNFFVGAGFN SMGIASAGGA
     GRALAEWIVH GEPTSDLFAV DIRRFADFNN NPTWLHDRVK ETLGLHYAMP WPNRELDTAR
     PFRRSALYDR LAAKNAVFGS KMGWERANWF APEGTTPENE YSFGRQNWHD AVAAEHKATR
     EDVAVFDQSS FAKLLVQGCD ACTELNRICA ANIDVAVGGT VYTGLLNTRG GFESDLTVLR
     LKEQEFLLIT GSAQAVRDAD WIGKNFSPDA HVFLTDVTAA WSVLALMGPK SRQVLQQLTK
     TNLSNAAFPF GTVQKIDLGY ATVWANRMTY VGELGWELIV PVEFTVGVYE DLKRAGQDHG
     IIDAGYYALD GLRLEKGFRA WSRELTPDIT PLQAGLSFAV DFDKPSGFIG KDALVAAKAD
     PNHLSKRIIQ LVVEDEMVQL WGGEAVLCDG VEIGEVRSAG YGHTLGAAVA LCEINATEPV
     KADFIKAHSF EVDVAGMRFA AKAHLRTPYD PKSERVRADG
//