ID A0A1X6ZHV1_9RHOB Unreviewed; 833 AA.
AC A0A1X6ZHV1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:SLN51896.1};
DE EC=1.5.3.19 {ECO:0000313|EMBL:SLN51896.1};
GN Name=mlr_3 {ECO:0000313|EMBL:SLN51896.1};
GN ORFNames=ROH8110_02868 {ECO:0000313|EMBL:SLN51896.1};
OS Roseovarius halotolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=505353 {ECO:0000313|EMBL:SLN51896.1, ECO:0000313|Proteomes:UP000193207};
RN [1] {ECO:0000313|EMBL:SLN51896.1, ECO:0000313|Proteomes:UP000193207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8110 {ECO:0000313|EMBL:SLN51896.1,
RC ECO:0000313|Proteomes:UP000193207};
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; FWFU01000003; SLN51896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6ZHV1; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000193207; 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:SLN51896.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193207}.
FT DOMAIN 7..381
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 384..437
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 441..721
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 744..823
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 833 AA; 92637 MW; A21582F1A292CD19 CRC64;
MKTHVKALIV GGGAIGTSIA YHLAKFGWDD VVLLERDELT SGSTWHAAGL LPLFNMSYAV
THIHDYSVKF YKTLEEETGL NAGFSVVGNL RMAQSDARMD EYRVYASTAE TVGVPFEWLT
PAQIKERWPL VNCDDLKGAI YHPTDGYINP ADVTMAMARG ARQRGVTIER KWQADAYHWT
GEAWEVTLTK MVEKGGNLVP SEEQIVVTAE HVVTATGNHA QRTARLLGIK TPAIPVEHQF
IVTEPDPALV EYRKAGNPEH PVLRDADAKW YVREERGGWI LGPYELNAPA RFEYGVPDSF
RADLFPLDLE RIEEEYMSMI HRIPSSETVG LKDDFNGPIC YTPDGNPLVG PAPGLRNMWL
AEGFSFGITA AGGTGHYMAQ MMVEGEAEID MASLDPKRFG SWITTEYSAR KNEEAYSHVY
VLHHPDEERE ACRPLRTAPS YDRLKARGAQ FGVVNGFERA NYYGPVGAPA DFDHDARSFR
RGGWWEYAVD EAKAVREGVG LIDASAFTKH TVKGPGATAF LDWFTCNKLP KVGRINLTYA
LTPEGTTRTE YTIVRLGEDS YYLVSAGALT DYDGDYLRKC AEDKAPEFGY IAVEDVTTQW
GVFAIAGPKS RDVLKEVVKD AEPETALSNK RFPWLSQRDI ELGMCPVRAI RVAYTGELGW
ELHHPIEMQN YLFDLLEDAG KKHGMKLVGV RAQNWLRQEK SYRAFGNELG RDATPLEADL
PRFVDQSKDF QGKDAMNALG VRVKCVTLLI DGPEDADPWG AEVLFDGDTR VGRLTSGGYS
VAFGKSIGMG YVSPEKAEVG QKLKVRILGA LWDAEVVEDS PYDPKNEVIR VDG
//