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Database: UniProt
Entry: A0A1M5M786_9RHOB
LinkDB: A0A1M5M786_9RHOB
Original site: A0A1M5M786_9RHOB 
ID   A0A1M5M786_9RHOB        Unreviewed;       801 AA.
AC   A0A1M5M786;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:SHG73122.1};
GN   ORFNames=SAMN05444003_0674 {ECO:0000313|EMBL:SHG73122.1};
OS   Cognatiyoonia sediminum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cognatiyoonia.
OX   NCBI_TaxID=1508389 {ECO:0000313|EMBL:SHG73122.1, ECO:0000313|Proteomes:UP000184074};
RN   [1] {ECO:0000313|EMBL:SHG73122.1, ECO:0000313|Proteomes:UP000184074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28715 {ECO:0000313|EMBL:SHG73122.1,
RC   ECO:0000313|Proteomes:UP000184074};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQXB01000001; SHG73122.1; -; Genomic_DNA.
DR   RefSeq; WP_072899275.1; NZ_FQXB01000001.1.
DR   AlphaFoldDB; A0A1M5M786; -.
DR   STRING; 1508389.SAMN05444003_0674; -.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000184074; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR13847:SF187; DIMETHYLGLYCINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 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.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000184074}.
FT   DOMAIN          510..625
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
SQ   SEQUENCE   801 AA;  88729 MW;  05898B79D39E2399 CRC64;
     MKTSTRVVVI GGGVVGCSVL YHLTKLGWSD VVLLERSELT SGSTWHAAGG FHTLNGDTNM
     AALQGYTIKL YRELEEITGM SCGLHHVGGV TLADNQDRFD MLVAERAKHR YMGLETEIVG
     PDEIKKIAPI TNTKGIIGAL YDPLDGHLDP SGTTHAYAKA ARMGGAEIEL HTKVEKTNQR
     PDGTWDVVTN KGTIHAEHVV NAGGLWAREV AALAGIYTPL HPMEHQYIVT DDVPEIYERD
     TEHPHVMDPA GESYLRQEGR GLCIGFYEQP CKPWAVDGTP WDFGHELLPD NLDKIEASIE
     FAYRRFPILE RSGVKSVIHG PFTFAPDGNP LVGPVPGVRN YWSACGVMAG FSQGGGVGLM
     LAQWMIEGEC ERDVTAMDVA RYGKWITPGY TRPKVTENYQ NRFSVTYPNE ELPAARPHRT
     TPMYDIFSDL GAVWGHQFGL EVANYFAQGD EPTYEAPSFR RSDAFDATAR EVKAVRESVG
     INEIQNFGKF AITGPNARTW LDNIMAGRIP KPGRMTLTPM LSPKGKLLGD FTVSCFAEGN
     FQLTASYGYQ EIHYRWFMQH IEDGVRVRNV SDRRTGFQIA GPKSRDLLAA CTRDATDLKF
     LDVRQMTIGQ VTCTVQQVSY TGDLGFEIYC DPMDQRQLWS VLWAAGQPMG LTAFGMRAMM
     SLRLDRHFGS WLREFSPDYT AAETGMDRFI QWSKNTDFIG RAATESERAT PPDRTAVVFE
     VDADDADVTA YEPVFIDDEV IGFCTSGGYS HHQGKSIAMA LIPREVAKEG LKVKIEILGQ
     LRSASLITSP LFEPKGVVFD G
//
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