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Database: UniProt
Entry: S2ZE51_9ACTN
LinkDB: S2ZE51_9ACTN
Original site: S2ZE51_9ACTN 
ID   S2ZE51_9ACTN            Unreviewed;       812 AA.
AC   S2ZE51;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Dimethylglycine oxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1211_03903 {ECO:0000313|EMBL:EPD62269.1};
OS   Streptomyces sp. HGB0020.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1078086 {ECO:0000313|EMBL:EPD62269.1, ECO:0000313|Proteomes:UP000014410};
RN   [1] {ECO:0000313|EMBL:EPD62269.1, ECO:0000313|Proteomes:UP000014410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGB0020 {ECO:0000313|EMBL:EPD62269.1,
RC   ECO:0000313|Proteomes:UP000014410};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Streptomyces sp. HGB0020.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPD62269.1}.
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DR   EMBL; AGER01000015; EPD62269.1; -; Genomic_DNA.
DR   RefSeq; WP_016433856.1; NZ_KE150427.1.
DR   AlphaFoldDB; S2ZE51; -.
DR   STRING; 1078086.HMPREF1211_03903; -.
DR   PATRIC; fig|1078086.3.peg.3950; -.
DR   HOGENOM; CLU_007884_11_2_11; -.
DR   OrthoDB; 2055370at2; -.
DR   Proteomes; UP000014410; 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:UP000014410}.
FT   DOMAIN          5..367
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          374..426
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          429..702
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          725..804
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   812 AA;  89120 MW;  7D9A3C9A464763FE CRC64;
     MAGPRVVIIG AGVVGAALAD EVSARGWTDV TVVDQGPLPA TGGSSSHAPG LVFQTNSSKT
     MTELARYTVE KFCSLDVDGK PCFLQVGGLE VATSPERLAE LRRRHGWITA WGIEARLLTP
     DECVEQHPLV DRDRVLGGLH VPTDGLAKAV LAVEAQIRRA TERGVRFLAR HEVLDIRQDD
     GRVTGVVTDQ GELDADIVVC CAGIWGPRIA RMAGMNLPLT PLGHQLAWTG PVPALAGQKE
     EAVRPILRHQ DADLYYRDRF DGLGIGYYGH RPMPTTADEI LSFDEAAEMP SVLKFTEEDF
     EPAWAETRSL LPATQEAKIE EGINGLFSFT TDNFPLLGES PDVKGFWVAE AVWVTHSAGV
     GRAMAEWLVD GHCSSFDLHE CDVNRFEPHQ LSPEYVLARD CQNFVEVYDI LHPLQPSGDP
     RPIRTSPFHP RQQEHGAFFL EANGWERPQW YEANAHLVEG RSIPTPNDWA ARYWSPIVGA
     EAQVTRETVA LYDMTALKRL EVTGPGAAAF LEGLVTGKVA KSVGSVTYTL LLDRDGGIRS
     DITVARLARD RFQVGANGNL DLDWFTRHLP ADGTVQVRDI TPGTCCIGLW GPLARKVLQP
     LTDDDFSNDG LKYFRGKQAY IGSVPVTALR LSYVGELGWE LYTTADQGLK LWDTLWEAAR
     PLGGIIAGRG AFNSLRLEKG YRSFGADMTY EHDPYEAGVG FAVKLDKGDF VGKPALQRRK
     ADVRRKLTCL TIDDPRSVVM GKEPVYDGER AVGYVTSAAY GYTIGKGIAY AWLPVEVAVP
     GARVRIGYFD QRVEAVVAEE PLFDPSMSRL RG
//
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