ID   SARDH_RAT               Reviewed;         919 AA.
AC   Q64380; O88499;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   25-NOV-2008, entry version 56.
DE   RecName: Full=Sarcosine dehydrogenase, mitochondrial;
DE            Short=SarDH;
DE            EC=1.5.99.1;
DE   Flags: Precursor;
GN   Name=Sardh;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 192-207, FAD-BINDING,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley, and Wistar; TISSUE=Liver;
RX   MEDLINE=99053678; PubMed=9839943;
RA   Bergeron F., Otto A., Blache P., Day R., Denoroy L., Brandsch R.,
RA   Bataille D.;
RT   "Molecular cloning and tissue distribution of rat sarcosine
RT   dehydrogenase.";
RL   Eur. J. Biochem. 257:556-561(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 102-115, AND FAD-BINDING.
RC   TISSUE=Liver;
RX   MEDLINE=86033731; PubMed=4055729;
RA   Cook R.J., Misono K.S., Wagner C.;
RT   "The amino acid sequences of the flavin-peptides of dimethylglycine
RT   dehydrogenase and sarcosine dehydrogenase from rat liver
RT   mitochondria.";
RL   J. Biol. Chem. 260:12998-13002(1985).
CC   -!- CATALYTIC ACTIVITY: Sarcosine + acceptor + H(2)O = glycine +
CC       formaldehyde + reduced acceptor.
CC   -!- COFACTOR: Binds 1 FAD covalently per monomer.
CC   -!- PATHWAY: Amine and polyamine degradation; sarcosine degradation;
CC       formaldehyde and glycine from sarcosine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- TISSUE SPECIFICITY: High levels in liver, lung, kidney, thymus and
CC       oviduct, and intermediate levels in the prostate, seminal vesicle,
CC       cardiac muscle and neuro-intermediate pituitary lobe. Also
CC       expressed in pancreas and adrenal gland.
CC   -!- SIMILARITY: Belongs to the gcvT family.
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DR   EMBL; AF067650; AAD03414.1; -; mRNA.
DR   EMBL; U62481; AAB03674.1; -; mRNA.
DR   EMBL; L79910; AAB04667.1; -; mRNA.
DR   RefSeq; NP_446116.1; -.
DR   UniGene; Rn.89832; -.
DR   Ensembl; ENSRNOG00000006916; Rattus norvegicus.
DR   GeneID; 114123; -.
DR   KEGG; rno:114123; -.
DR   RGD; 621125; Sardh.
DR   HOVERGEN; Q64380; -.
DR   NextBio; 618353; -.
DR   ArrayExpress; Q64380; -.
DR   GermOnline; ENSRNOG00000006916; Rattus norvegicus.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IDA:UniProtKB.
DR   GO; GO:0008480; F:sarcosine dehydrogenase activity; IEA:EC.
DR   GO; GO:0042426; P:choline catabolic process; NAS:UniProtKB.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; FAD; Flavoprotein;
KW   Mitochondrion; Oxidoreductase; Phosphoprotein; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    919       Sarcosine dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000010772.
FT   MOD_RES     109    109       Tele-8alpha-FAD histidine (By
FT                                similarity).
FT   MOD_RES     778    778       Phosphotyrosine (By similarity).
FT   MOD_RES     885    885       N6-acetyllysine (By similarity).
FT   CONFLICT     92    102       GGVVLLERERL -> SGVGAAGERAM (in Ref. 1;
FT                                AAB03674/AAB04667).
FT   CONFLICT    114    115       LW -> GR (in Ref. 2; AA sequence).
FT   CONFLICT    154    154       L -> F (in Ref. 1; AAB03674/AAB04667).
SQ   SEQUENCE   919 AA;  101440 MW;  E49E54207BD1DBFB CRC64;
     MASLSRVLRV AATCPRGRSA RNLGLQPLAR EARPTTEKSV PYQCTLKEEA QGASVVPQGP
     SQPLPSTANV VVIGGGSLGC QTLYHLAKLG VGGVVLLERE RLTSGTTWHT AGLLWQLRPS
     DVEVELLAHT RQVVSHDLEE ETGLHTGWIQ NGGLFIASNQ QRLDEYKRLM SLGKAYGIES
     HVLSPAETKD LYPLMNVDDL YGTLYVPRDG TMDPAGTCTT LTRAAVARGA QVIENCAVTG
     IRVRTDDFGV RRVTAVETQH GSIQTPCVVN CAGVWASSVG RMAGVKVPLV AMHHAYVVTE
     RIEGIQNMPN VRDHDASVYL RLQGDALSVG GYEANPIFWD EVSDKFAFGL FDLDWDVFTQ
     HIEGAINRVP VLEKTGIKST VCGPESFTPD HKPLMGEAPE LRGFFLGCGF NSAGMMLGGG
     CGQELAHWIV HGRPEKDMYS YDIRRFHHSL TDHPRWIRER SHESYAKNYS VVFPHDEPLA
     GRNMRRDPLH EELLGQGCVF QERQGWERPG WFNPQETAQV LDYDYYGAYG HQAHKDYAYS
     RLLGDEYTFD FPPHHCVIQK ECLACRTAAA VFNMSYFGKF YLLGADARKA PDWLFSADVN
     RPPGSTVYTC MLNQRGGTES DLTVSCLAPG AQASPLAPAF EGDGYYLAVG GAVAQHNWSH
     INTVLQDQEF RCQLMDCSED LGMLSIQGPA SRDILQDVLD ADLSNEAFPF STHQLVRAAG
     HLVRAIRLSF VGELGWELHV PQASCLPVYR AVMAAGAKHG LVNAGYRAID SLSIEKGYRH
     WHADLRSDDS PLEAGLAFTC KLKTSVPFLG REALEKQRAT GLRRRLVCLT VEEEVPMFGL
     EAIWRNGQVV GHVRRADFGF TVNKTIAYGY IRDPSGGPVS LDFVKNGDYA LERMGVTYAA
     QVHLKSPFDP DNKRVKGIY
//