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Database: UniProt
Entry: A0A2P8F4D9_9RHOB
LinkDB: A0A2P8F4D9_9RHOB
Original site: A0A2P8F4D9_9RHOB 
ID   A0A2P8F4D9_9RHOB        Unreviewed;       822 AA.
AC   A0A2P8F4D9;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:PSL16587.1};
GN   ORFNames=CLV88_12240 {ECO:0000313|EMBL:PSL16587.1};
OS   Shimia abyssi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1662395 {ECO:0000313|EMBL:PSL16587.1, ECO:0000313|Proteomes:UP000240418};
RN   [1] {ECO:0000313|EMBL:PSL16587.1, ECO:0000313|Proteomes:UP000240418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100673 {ECO:0000313|EMBL:PSL16587.1,
RC   ECO:0000313|Proteomes:UP000240418};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) 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:PSL16587.1}.
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DR   EMBL; PYGJ01000022; PSL16587.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8F4D9; -.
DR   Proteomes; UP000240418; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240418};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..384
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          387..440
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          443..711
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          736..814
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   822 AA;  90964 MW;  5A2DCA98FBFE37A4 CRC64;
     MPEIQKDETS TGKQLPSHAK VVVIGGGVVG CSILFHLAKF GWKDAVLLER DELTSGSSWH
     AAGQIHTISS DPNISRLQSY TIDLYKEIEE TSGHSVGLHI TGGFYAASTK EWYDYLKRER
     SKARYMGLHQ EFISPQELAE RHPLIDPKHY YAALWDDQDG DLDPSGATYA FAKSARVHGA
     QYFTHCGVTD MKQRPDGSWD LTTPKGNINA EHVVNCGGLW AREVGHMSGI HLPVQPMEHH
     YLITDKIPMI ADRMESMGEA GRLPAGIDYE ANIYFRQERH GMLLGTYEPK STPWKVDGTP
     WDFGHELLQP DLDRIADRLE MSFERIPAIG ESGIKDMING PFTFGPDGNP MIGPVPGMKN
     YWVAVGVMAG FCQGGGVGLT MAEWMIDGEP SIDVWAMDVA RFGEFATPDW GTVKSSENYE
     RRFVMTFPNE TLPKGRLQKT TALYDRLIAK GAVMDQGFGL ENAQWFADDA KDAHEVPTFE
     RNRSFDYVKR EVEAVRNAVG GIEIANFAKH EFKGAGARAY LDSILAGYVP KPGRLTLTPM
     LTEKGRLYGD LTVACLAEDH FMLFGSGAMQ EAHRRWFEKD LPADATYENV SDDWHGVALS
     GPMSRELLAR LTRDDVSAEA FKFRDLHQTF VGGVPVILNR ISFSGELGYE IYCKPQYLLR
     LAESIEDAGA DLGYRWYGAR ALMSMRLEKG WGVWTLEFRP DFNAVESGMD AFINWKKDFV
     GKAATEAFRD SGVKQKLVTM TIDVDGIDVS GDEAILKDGE AVGYVSSGGY GHRAGASMAM
     GYVSADNAAP GSQLQVEILG EFYQANVLGA PAYDANGANM RA
//
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