ID F6EPM4_HOYSD Unreviewed; 815 AA.
AC F6EPM4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Dimethylglycine oxidase {ECO:0000313|EMBL:AEF39457.1};
GN OrderedLocusNames=AS9A_1005 {ECO:0000313|EMBL:AEF39457.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF39457.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF39457.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CP002786; AEF39457.1; -; Genomic_DNA.
DR AlphaFoldDB; F6EPM4; -.
DR STRING; 443218.AS9A_1005; -.
DR KEGG; asd:AS9A_1005; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_11_2_11; -.
DR Proteomes; UP000009235; Chromosome.
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:UP000009235}.
FT DOMAIN 2..367
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 370..425
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 427..705
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 729..807
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 815 AA; 88823 MW; AC6A30A5E47B6934 CRC64;
MIIGAGIVGA NLADELTVRG WDRVTVLDQG PLPLTGGSTS HAPGLVFQTN ASKALTEFAR
YTVEKFKGLD VDGQWCFNQL GGLEVATNPE RLADLHRKQG WAASWGVADA AVLDPKECVK
LHPLVDESQI LGGLYVPTDG LAKASRVVVA LIRRATQRGA EFRGSSKVTG IEHRAGQVTG
VITPHGVIPA DIVVSCGGFW GPAIGEMVGM QVPLLPLAHQ YAKTGQVPEL VGRNSELAEA
SMPILRHQDQ DLYFREHGDR LGIGSYAHRP MPVDLRDLTE SDEISVAAMP SMLPFTEDDF
APSWEASKLL IPSLESTKVE EGFNGVFSFT PDGGPVVGES PEVAGFWIAE AVWVTHSAGV
ARSVAQLLVD GRSEISLHGC DVHRFEEIQT SPDYVSETGQ QNFVEIYDVL HPLQPRTSPR
NLRVSPFHAR QEELGAFFLE SGGWERPHWY EANTRLLDDL PSEWTSPPRD PWAAQFFSPI
AAAEAWRTRT SVAMYDMTPL RRLEVSGPGA LALLTRLTTG KMDKSVGAVT YTLMLDGSGG
IRSDLTVARL SETTFQLGAN GNIDVDYLRR EAPADGSVQI RDVTGGTCCI GVWGPRARDL
VQALSADDFS GETFKYFRSK KVWIAGIPIT AMRLSYVGEL GWELYTSAEY GLRLWDALWG
EGQQYDVIAA GRAAFNSLRI EKGYRAWGSD MTTEHNPYEA GLSFAVNANK QDYVGYDAIQ
RIKQEPLERR LVCVAIDDGQ SVVLGHEPAF IDGTPVGYVT SAAFGHTVGT PLAYVWLPAS
AAPGTNIEIQ YFDRRIAATV VAEPLVDPDM KRIKA
//