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Database: UniProt
Entry: A0A1X6ZHV1_9RHOB
LinkDB: A0A1X6ZHV1_9RHOB
Original site: A0A1X6ZHV1_9RHOB 
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
//
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