ID A0A0N0N667_9ACTN Unreviewed; 830 AA.
AC A0A0N0N667;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:KPI21488.1};
DE EC=1.5.8.4 {ECO:0000313|EMBL:KPI21488.1};
GN ORFNames=OK074_1093 {ECO:0000313|EMBL:KPI21488.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI21488.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI21488.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI21488.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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:KPI21488.1}.
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DR EMBL; LJCV01000033; KPI21488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0N667; -.
DR PATRIC; fig|1592327.3.peg.877; -.
DR OrthoDB; 2055370at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0047865; F:dimethylglycine dehydrogenase activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:KPI21488.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991}.
FT DOMAIN 21..392
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 395..450
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 452..724
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 744..822
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 830 AA; 90962 MW; 07193936AF4FA437 CRC64;
MSSTPETRPQ GTAETRASSP RVVVIGAGIV GCSLADELTA RGWTDVTVLE QGPLPAPGGS
TSHAPGLVFQ TNPSKTMTEF ARYTVEKFNS LEVDGVSCFN QVGGLELATT PERLADLHRK
AGYAASWGIR GEIVSTARCK QLWPLLDESV VLGGFHTPDD GLARALLASR AQLERATARG
ARFLDRHTVT GIERDGGRVT AVVTDRGTFP ADHVVSAAGF WGPVIGRMAG IDVPLQPLAH
QYAKTRPLPE LADAADGGVP AEATKPILRF QDRDLYFREH NDRLGIGSYA HKPLPVDPFA
LLSYDDARAE NMEMPSSYPF TEEDWAPSWE DCRGLIPALR ESEIETGFNG VFSFTPDGFP
LMGETRELRG FWLAEAVWVT HSAGVARAVA EWMVDGRPTT DVHECELTRF EGAQRSPSYV
TERGCRQFVE VYDVLHPLQP MEQPRPLRVS PFHARQQALG ARFLEGGGWE RPHWYEANAP
LADGIEVPER DAWSARYWSP IAAAEARATR EKVALYDMTP LRRLEVTGPG ALDFLDRMTT
NNLRKKPGAV TYTLLLDETG GVRSDLTVAR LAPDRFQVGA NSPADLDWLL RHAPSDVHIK
DITSGTCCIG VWGPLARALV QPLTRDDFSH EGFGYFRAKE TFLGHVPVTA MRLSYVGELG
WELYTTADLG LRLWDTLWEA GQEHGVVAAG RSAFNSLRLE KGYRSWGTDM TDEHTPFEAG
VGFAVRMDKE FTGRAALTQD PPTRRLTPLL LDDPAANVLG KEPVHVDGVP AGYVTSAAYG
YTLGRCIAYA WLPAGLATGA AVHVEYFGEK IPATVAEEPL FDPKMTRIRC
//
