ID D5APP5_RHOCB Unreviewed; 831 AA.
AC D5APP5;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:ADE86614.1};
DE EC=1.5.8.4 {ECO:0000313|EMBL:ADE86614.1};
GN OrderedLocusNames=RCAP_rcc02885 {ECO:0000313|EMBL:ADE86614.1};
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE86614.1, ECO:0000313|Proteomes:UP000002361};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SB1003;
RA Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N.,
RA Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., Kyrpides N.,
RA Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., Los T., Lykidis A.,
RA Mikhailova N., Reznik G., Vasieva O., Fonstein M., Paces V., Haselkorn R.;
RT "Complete genome sequence of Rhodobacter capsulatus SB1003.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADE86614.1, ECO:0000313|Proteomes:UP000002361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003
RC {ECO:0000313|Proteomes:UP000002361};
RX PubMed=20418398; DOI=10.1128/JB.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CP001312; ADE86614.1; -; Genomic_DNA.
DR RefSeq; WP_013068588.1; NC_014034.1.
DR AlphaFoldDB; D5APP5; -.
DR STRING; 272942.RCAP_rcc02885; -.
DR GeneID; 31491698; -.
DR KEGG; rcp:RCAP_rcc02885; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_11_0_5; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000002361; Chromosome.
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; 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:SF193; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, 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 Oxidoreductase {ECO:0000313|EMBL:ADE86614.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002361}.
FT DOMAIN 14..373
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 376..431
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 433..704
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 728..812
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
FT REGION 812..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 91270 MW; 66AA947CD9A7B50B CRC64;
MPDPAAPDLP AKARVVIIGG GISGCSVAYH LAKLGWTDIV LLERKQLTSG TTWHAAGLIG
QLRASQNMTR LAKYSADLYG RLEAETGLAT GFRRCGSITV ALSAERREEI FRQAALARAF
GVAVDELSPA EVQRLYPHLN IDGVVAGVHL PGDGQADPGN IALALAKGAR MAGARIVEQV
KVTRVTSVAG RVTGVDWDMA GARGHIAADH VVNCGGMWGR DLAAQNGVTL PLHACEHFYI
VTETIPDLAR LPVLRVPDEC AYYKEDAGKI LLGAFEPKAK PWGMNGIPED FCFDQLPEDF
DHFEPILEQA VARMPMLAKA GIHTFFNGPE SFTPDDRYYL GEAPELRGYW VAAGYNSIGI
VSSGGAGMAL AQWMHDGAPP FDLWEVDIRR AQPFQRNRRY LRDRVSETLG LLYADHFPFR
QMASARGIRR SPLHEALKAR GAVFGEVAGW ERANWFAREG QEREYRYSWK RQNWFENQRA
EHMALREGVG LLDMTSFGKI RVEGRDATAF LQRLCANQID VPVGRIVYTQ MLNPRGGIES
DLTVTRLSET AFFLVVPGAT LPRDLAWLRR HLTEERVTIT DVTAAEAVLP IMGPRARDLL
RRVSPDDFSN AAHPFGTARE IEIGMGLARA HRVSYVGELG WELYISTDQA AHVFETLAKA
GAEVGLRLCG LHAMDSCRIE KGYRHFGHDI TDEDHVLEAG LGFAVKPEKG DFLGREAVLR
KRESGLTRRL VQFRLTDPEP LLFHNEPILR DGKIVGQLTS GNYGHALGGA IGLGYVPCRA
GETAAELLSA RYTIDVAGRI FTAEASLTPL YDPKAHRPQA DQVAAAPTPG R
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