ID A0A1G9HJ33_9ACTN Unreviewed; 788 AA.
AC A0A1G9HJ33;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:SDL12957.1};
GN ORFNames=SAMN05421874_11667 {ECO:0000313|EMBL:SDL12957.1};
OS Nonomuraea maritima.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=683260 {ECO:0000313|EMBL:SDL12957.1, ECO:0000313|Proteomes:UP000198683};
RN [1] {ECO:0000313|EMBL:SDL12957.1, ECO:0000313|Proteomes:UP000198683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5681 {ECO:0000313|EMBL:SDL12957.1,
RC ECO:0000313|Proteomes:UP000198683};
RA de Groot N.N.;
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; FNFB01000016; SDL12957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9HJ33; -.
DR STRING; 683260.SAMN05421874_11667; -.
DR OrthoDB; 2055370at2; -.
DR Proteomes; UP000198683; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR028896; GCST/YgfZ/DmdA.
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; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 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 Reference proteome {ECO:0000313|Proteomes:UP000198683}.
FT DOMAIN 6..359
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 362..417
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 420..690
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 710..786
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 788 AA; 86148 MW; EBB1C6B8C041EA52 CRC64;
MSDSARIVII GGGVGGTSVA FHLTQLGERD VVLLERDELT SGSTFHSAGL VGQLRADPTL
TRMNQYSVEL YRTLDAGWSE CGGIKLASTP ERMQEIRRQI GWARTFGLPL EEISVAEAVE
LFPLMDPEGV VGAAYLPTDG QIDPSQLCYA LAARAREGGA TIRTRTRVLG ITVAHGRVTG
VRTDQGDIDC EIVVDCGGMF AAEIGRMAGV RVPIVPMSHQ YVITDAFHDH PVLPTLRDPD
LLVYYRQEVR GLVMGGYERT SAPWTAGPDS YDAVPADFNG RLLPEDWPRF EEISENSRIR
VPAMADVGIR KMINGPEAFT PDNEFCLGET EVGGFFVAAG FCAHGIAGAG GIGKVMAEWI
VEGEPGMDVR HMDIRRFDRH YRSPSYTVKR AVENYETYYD IRYPGHERSA GRPLRVSPAY
SWHVAHGAVF GEKAGWERVN HYTAADPDDT GERPRGWAGR SWSPAIGAEH RATRTTAGLF
DESSFAKIEV TGPGAAALLE WVCDNRVARE IGAVTYTQAL NRRGGIECDF TVTRRAQDEF
LVVTGTAFGT HDLGWLRKQA RLTGSTARIT DVTGRYACFA LWGPRARDIL SRLTPDPLDF
PFMSSREITV GDVPVLALRV TFVGEHGWEL YCSSEYGLAL WQALWRAGEP HALAACGYRA
IDSLRLEKGY RVWGADIGPE TTPYEAGLGF CVKSDKEFLG RDALDPEPER RLRCVRLADP
RAVALGNEPV RVDGRVVSRV TSGGYGYTAR ASIAYAYLAA EVAPGAEVEI EVEGAWVPGT
VVKGPVVP
//
