ID A0A1Y5RCK5_9RHOB Unreviewed; 806 AA.
AC A0A1Y5RCK5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:SLN13463.1};
DE EC=1.5.3.19 {ECO:0000313|EMBL:SLN13463.1};
GN Name=mlr_3 {ECO:0000313|EMBL:SLN13463.1};
GN ORFNames=PEL8287_00523 {ECO:0000313|EMBL:SLN13463.1};
OS Roseovarius litorisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN13463.1, ECO:0000313|Proteomes:UP000193827};
RN [1] {ECO:0000313|EMBL:SLN13463.1, ECO:0000313|Proteomes:UP000193827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN13463.1,
RC ECO:0000313|Proteomes:UP000193827};
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; FWFL01000001; SLN13463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5RCK5; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000193827; 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:SLN13463.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193827}.
FT DOMAIN 6..364
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 367..420
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 424..689
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 715..798
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 806 AA; 89608 MW; 11FE7E0DC47E2BA6 CRC64;
MKTTTRVAVI GGGVVGCSVL YHLTKLGWSD VMLIERSELT SGSTWHAAGG FHTLNGDTNM
AALQGYTIKL YKELEEITGM SCGLHHVGGV TLADNQDRFD MLLAERAKHR YMGLDTHIVT
PDEIKKIAPI TNTDGILGAL YDPLDGHLDP SGTTHAYAKA ARMGGASIET HCKVIETNQR
PDGTWDVVTD KGTIHAEHVV NAGGLWAREV GAMAGIYVPL HPMEHQYIVT DDIAEIYERD
EEHPHVMDPA GESYLRQEGR GLCIGFYEQP CKPWAVDGTP WDFGHELLPD NLDKIEDSIE
FAYRRFPVLE AAGVKSVIHG PFTFASDGNP LVGPVPGLRN YWSACGVMAG FSQGGGVGLM
LAQWMIEGEC ERDVTAMDVA RFGDWITPGY TRPKVIENYQ KRFSVAYPNE ELPAARPFRQ
TPMYDVFDKM GAVWGQQYGL EVVNYFAEED EPRYETPSFR RSNAWEATAR EVRAVRESVG
INEVHNFGKY LVTGPNARGW LDRIMAGRIP RPGRVSLTPM LSPKGRLIGD FTVSCLGAEA
FQLTASYGAQ AYHMRWFQMN EAEDVAVENI SDRLNGFQIA GPWAREVLVA CTRDKVGDMK
FMDLRHATIG MVDCLIQRVS YTGDLGYEIY CDPMSQRALW DVLMREGHAY DIQPFGMRAM
MSLRLDRFFG SWLSEFSPDY TPGETRMDRF IRFDKTTDFI GRAAASAERE SGSERKLVAF
EVDALDADAH GYEPIWIDGK VQGFCTSGGY SHHAKKSIAL GLIPRDLAEA AEYSTLTAKI
EILGQMRPAT LISDPLLDPE GDHMRS
//