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Database: UniProt
Entry: M3WFY0_FELCA
LinkDB: M3WFY0_FELCA
Original site: M3WFY0_FELCA 
ID   M3WFY0_FELCA            Unreviewed;       864 AA.
AC   M3WFY0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 3.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|Ensembl:ENSFCAP00000011024.5};
GN   Name=DMGDH {ECO:0000313|Ensembl:ENSFCAP00000011024.5,
GN   ECO:0000313|VGNC:VGNC:61526};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000011024.5, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000011024.5, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011024.5,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000011024.5, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011024.5,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000011024.5}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011024.5};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; AANG04001174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M3WFY0; -.
DR   STRING; 9685.ENSFCAP00000011024; -.
DR   PaxDb; 9685-ENSFCAP00000011024; -.
DR   Ensembl; ENSFCAT00000011885.6; ENSFCAP00000011024.5; ENSFCAG00000011882.6.
DR   VGNC; VGNC:61526; DMGDH.
DR   eggNOG; KOG2844; Eukaryota.
DR   GeneTree; ENSGT00940000158176; -.
DR   HOGENOM; CLU_007884_11_1_1; -.
DR   InParanoid; M3WFY0; -.
DR   OMA; NGWERPN; -.
DR   Proteomes; UP000011712; Chromosome A1.
DR   Bgee; ENSFCAG00000011882; Expressed in liver and 9 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0047865; F:dimethylglycine dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0042426; P:choline catabolic process; IEA:Ensembl.
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   Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT   DOMAIN          50..412
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          415..468
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          477..742
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          768..846
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
FT   REGION          16..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   864 AA;  96556 MW;  BDF6A62E3C1D4DF3 CRC64;
     MLRPGAQRGL LLSSLRLQGS PGRPRSACGR QGEENTPLSA ETRWKDRAET VIIGGGCIGV
     SLAYHLAKAG MKDVVLLEKS ELTAGSTWHA AGLTTYFHPG INLKKIHYAS IKLYEKLEEE
     TGQVVGFHQP GSIRIATTPV RVDEFKYQMT RTGWHATEQY IIEPEKIQEM FPLLNMNKIL
     AGLYNPGDGH IDPYSLTMAL AAGARKYGAL LKYPAPVTSL IPRSDGTWDV ETPQGSMRAN
     RIVNAAGFWA REVGKMVGLE HPLIPVQHQY VVTSTIPEVK ALERELPVLR DLEGSYYLRQ
     ERDGLLFGPY ESQEKMKVQD SWVTNGVPPG FGKELFESDL DRIMEHVEAA MEMVPVLKKA
     DIINIVNGPI TYSPDILPMV GPHQGVRNYW VAIGFGYGII HAGGVGKYLS DWILHGEPPF
     DLIELDPNRY GKWTTTQYTE AKARESYGFN NIVGYPKEER FAGRPTQRVS GLYKILESKC
     SMGFHAGWEQ PHWFYKPGQD TRYRPSFRRT NWFEPVGSEY KQVMQSVGVI DLSPFGKFNI
     KGQDSVRLLD HLFANVIPKV GFTNISHMLT PKGRVYAELT VSHQTPGEFL LITGSGSELH
     DLRWIEEEAV NGGYDVEIKN ITDELGVLGI AGPHARKVLQ KLTSEDLSDD VFKFLQTKSL
     MVSNIPVTAI RISYTGELGW ELYHRREDSV ALYDIIMNAG QEEGIDNFGT YAMNALRLEK
     AFRAWGSEMN CDTNPLEAGL DYFIKLNKPA DFIGKQALKQ IKAKGLKRRL VCLTLATDDV
     DPEGNESIWY DGKVVGNTTS GSYSYSVQKS LAFAYVPVEL SKVGQQVEVE LLGTNYPATV
     IQEPLVLTEP ARNRLRKKNG KDTI
//
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