ID A0A1G4WPR1_9MYCO Unreviewed; 818 AA.
AC A0A1G4WPR1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:SCX27081.1};
GN ORFNames=SAMN02799620_04208 {ECO:0000313|EMBL:SCX27081.1};
OS Mycolicibacterium fluoranthenivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=258505 {ECO:0000313|EMBL:SCX27081.1, ECO:0000313|Proteomes:UP000199707};
RN [1] {ECO:0000313|Proteomes:UP000199707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNC267MFSha1.1M11 {ECO:0000313|Proteomes:UP000199707};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FMUB01000009; SCX27081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4WPR1; -.
DR STRING; 1502745.SAMN02799620_04208; -.
DR Proteomes; UP000199707; Unassembled WGS sequence.
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.
PE 3: Inferred from homology;
FT DOMAIN 11..368
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 371..426
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 429..696
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 725..811
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 818 AA; 88544 MW; BB76C0957890D36A CRC64;
MTNKPLPDRA RVVIIGGGVI GTSVAYHLTK LGHTDVVLVE QGQLSCGTTW HAAGLVGQLR
ASESGTRLVQ YSTQLYAELE RETGLSAGYK RCGGVTVART EDRLIQLRRT AANAAAFDME
CEILTPEEAL AHYPVMRVDD LAGAIWLPGD GKANPTDLTL ALAKGARLRG ARVFEHVRVT
GVDLRDGVVT GVRTDRGDIE TEIVVNCAGQ WAKQVGALAG VNVPLHSAEH FYVVSETITG
VHTDMPILRD PDGYTYFKEE VGGLVIGGFE PEAKPWVSPD ALPYPFEFQL LEEDWDHFQI
LMDNAMLRIP ALEETGIKKF YNGPESFTPD NQFILGEAPE CRNFFVAAGF NSVGIASAGG
AGRALAEWIV NGSPTSDLTS VDIRRFAPFN GNTRWLHDRV GEILGLHYEI PWPNRELASA
RPFRRSPVHH LLAAAGANFG SRMGWERANF FAPPGVAPDI EYSWGKQNWL PFSAAEQIAT
RTAVTVFDQT SFSKYLMVGA GAESALQWLC TADIGVDVGR TVYTGMLNDR GTYESDVTVT
RTAADEFLIV SSAATTERDQ DHIRRNLPAG VNAHLVDITS ALAVFGVMGP RSRDLLAVLT
DADLADAAFP FGTSRRISLG YATVRATRLT YVGELGWELY VPAEFAVGVY EDLLAAGQAL
GVVRGGYYAI ESLRLEKGYR AFGRELTPGD GPVEAGQLFT CKLGTDIDFL GRAALEQARA
HGPRRRLVGF AVSSPEPMLW GGELILRDGV VAGQVTSAAW GATTGACVGL AYLRAEDGRV
IDAEWIDGGA YEVNVGGTRY PVTVSRKALY DPTNARIR
//
