ID A0A1X6WVM6_9MICO Unreviewed; 921 AA.
AC A0A1X6WVM6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative Dimethylglycine oxidase {ECO:0000313|EMBL:SLM88420.1};
GN ORFNames=FM105_00275 {ECO:0000313|EMBL:SLM88420.1};
OS Brevibacterium yomogidense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=946573 {ECO:0000313|EMBL:SLM88420.1, ECO:0000313|Proteomes:UP000196581};
RN [1] {ECO:0000313|EMBL:SLM88420.1, ECO:0000313|Proteomes:UP000196581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B Co 03.10 {ECO:0000313|EMBL:SLM88420.1,
RC ECO:0000313|Proteomes:UP000196581};
RA Peterson S.W.;
RL Submitted (FEB-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; FWFF01000001; SLM88420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6WVM6; -.
DR Proteomes; UP000196581; 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;
FT DOMAIN 34..438
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 442..496
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 499..811
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 834..913
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 97706 MW; 04D8A08D93C95482 CRC64;
MTGTVPRTIA SSAATTLPDR VSARPPGAID PSSRIVIIGA GVVGAALADE LVTRGCTRVT
VLDQGPLPVT GGSSSHAPGF VFQVNGSRVM CGLAQRTLAK LDGLEVDGRR VLDRIGGLEV
ATTEGQLAEL RRRYGYALAW GVPAELIEPA RVAELWPGLD TSQIIGALHT PTDGIVHSKR
AVEHQLARAE EGGAEAIGLT RVVDVETENG RVTGVVVEDA TVPTGGAGAE AAEVPAGGTS
AAVDSTSPSR RTIPADVVVA TGGIWGHLLG ELGGLRLPMH PMEHGYAWTA PVPDLPGTAP
DGSPLGDDQA GRPMIRHQGA GLYMREFGTR IGIGAYEHRP IPLAPEDLTD TAHMLASGQE
PAKRAFTRED FEFCRAEAAR LLPAIADLPL EGEFNGVFSF TPDGGPMLGP SPRLDGFWAA
QAIWVTASAG CAEVLADWML TGDPGVATQE LDAARFDPAL LSDQWIRERA AEAYDEVYDV
SFPHQGTVVT RGLKTSPFHT RIQDAGGYFD EANGWERALW HGENAKLFSD PEFRTRAVKA
FGAAAAATTA LEDPAVPGGV AEGGGDTVPV VVPRRDAWDQ VNWSPIAAAE AWATRNRVAA
YDMTSLTRYR VRGAGATAWL ERLNTNKVGK LPGAVTYSLM LDETGGILSD VTVTSLGGEE
YMIGANGPLD LDRLTRLLPE SGTVVLDDIT TSTCCVGLWG PRARDVLEPI TEGDISHEGL
RYFRAARIRV AGVPVLALRV SYVGELGWEL YTEAAHGLRL WDALMDAGAP HGIVPGGRAA
FSSLRLEKGY RAWGSDMTRE DTPEDAGLGF AVRMEKDGGF IGRDALVRQP SRGRRLAAFG
MRMDAGRPEA GSPVFAGTEV VGWVTSADFG YVTGQVIGLA WVAEERAEPG TPLEIMRFGR
VHGAEVLAEP VYDAGMSRIR R
//