ID A0A1H6XNH4_9RHOB Unreviewed; 816 AA.
AC A0A1H6XNH4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:SEJ30638.1};
GN ORFNames=SAMN05444007_104133 {ECO:0000313|EMBL:SEJ30638.1};
OS Cribrihabitans marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cribrihabitans.
OX NCBI_TaxID=1227549 {ECO:0000313|EMBL:SEJ30638.1, ECO:0000313|Proteomes:UP000199379};
RN [1] {ECO:0000313|EMBL:SEJ30638.1, ECO:0000313|Proteomes:UP000199379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29340 {ECO:0000313|EMBL:SEJ30638.1,
RC ECO:0000313|Proteomes:UP000199379};
RA de Groot N.N.;
RL Submitted (OCT-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; FNYD01000004; SEJ30638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6XNH4; -.
DR STRING; 1227549.SAMN05444007_104133; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000199379; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000199379}.
FT DOMAIN 9..378
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 381..435
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 437..702
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 728..802
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 816 AA; 90494 MW; EDB5B503865C179E CRC64;
MADFPNKARV VIIGGGVVGV SSLYHLAKKG WSDCVLLEKN ELTAGSTWHA AGNVPTFSTS
WAIMNMQRYS TDLYSRLADE VDYPMNYHVT GSIRLAHSAE RMQEFQRAAA MGRYLGVDME
ILTPEETKEH YPFLETHDLA GSLYDPNDGD IDPAQLTQAL AKGARDMGAR ILRFTPATGV
TQHDDGTWTV RTDKGDIACD YVVNAAGYYA QRVGEWFKPY GGRTVPMMVM SHQYLLSEEI
PEIEALTKKT GKKLPLLRDV DVSYYLRQEK HGFNLGPYEP DCRAHWADPD DPMPEDFSFQ
LWSDDLDRIE DIVTDAMERV PLLGSAGVSR VINGPIPYAP DGNPLLGPMP GVRNAFEACV
FTFGIAQGGG AGKVLAEWIV DGATEWDMWA CDPRRFTGYT DHDYCVAKGM EVYGHEYAMH
FPWHEWPAGR NKRRSPLHDR LQAAGAVFGA YNGWERANWF AQPGDDTSEA ATQTWDRSGP
WEPRIRAECE AVRDHCGILA ISGFSRLKVE GPGAKDFVDG LTTSRLPAPR RIGLAYFPDH
RGRVATEMSV MVHSDEDVGL ITAATAQWHD REWLWRQAPE GVTISDHSDN VECLLVTGPK
AREILGPLTN HDLFLPWLSV SFEGKVAGID CALIRVSFAG ELGWEVHCAA EDAPAIWDAV
TGAGARPFGM WALNSLRIEK GYRAWKGDLS TDYSLLESGL DRFVRLDKPQ DFPGKTALLA
ERQQGVKKRF ATLIVDAGGA DAPYMSCIWK DGEIVGETTS GAWGYRVGAS IALGMVRSDL
AEPGTELEVE IYGTRHRAVV QPDQPLWDPQ NERLRA
//
