SARDH_RAT
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 03-AUG-2022, entry version 124.
DE RecName: Full=Sarcosine dehydrogenase, mitochondrial {ECO:0000305};
DE Short=SarDH;
DE EC=1.5.8.3 {ECO:0000305|PubMed:6163778};
DE Flags: Precursor;
GN Name=Sardh {ECO:0000312|RGD:621125};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD03414.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 192-207, FAD-BINDING,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAD03414.1}, and
RC Wistar {ECO:0000269|PubMed:9839943};
RC TISSUE=Liver {ECO:0000269|PubMed:9839943};
RX PubMed=9839943; DOI=10.1046/j.1432-1327.1998.2570556.x;
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] {ECO:0000305}
RP PROTEIN SEQUENCE OF 102-115, AND FAD-BINDING.
RC TISSUE=Liver {ECO:0000269|PubMed:4055729};
RX PubMed=4055729; DOI=10.1016/s0021-9258(17)38827-0;
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 mitochondria.";
RL J. Biol. Chem. 260:12998-13002(1985).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6163778; DOI=10.1016/s0021-9258(19)69572-4;
RA Wittwer A.J., Wagner C.;
RT "Identification of the folate-binding proteins of rat liver mitochondria as
RT dimethylglycine dehydrogenase and sarcosine dehydrogenase. Flavoprotein
RT nature and enzymatic properties of the purified proteins.";
RL J. Biol. Chem. 256:4109-4115(1981).
CC -!- FUNCTION: Catalyzes the last step of the oxidative degradation of
CC choline to glycine. Converts sarcosine into glycine.
CC {ECO:0000305|PubMed:6163778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + H(+) +
CC oxidized [electron-transfer flavoprotein] + sarcosine = (6R)-5,10-
CC methylenetetrahydrofolyl-(gamma-L-Glu)(n) + glycine + reduced
CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:19793, Rhea:RHEA-
CC COMP:10685, Rhea:RHEA-COMP:10686, Rhea:RHEA-COMP:13257, Rhea:RHEA-
CC COMP:14738, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57433,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:136572,
CC ChEBI:CHEBI:141005; EC=1.5.8.3;
CC Evidence={ECO:0000305|PubMed:6163778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19794;
CC Evidence={ECO:0000305|PubMed:6163778};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:4055729, ECO:0000269|PubMed:9839943};
CC Note=Binds 1 FAD covalently per monomer. {ECO:0000269|PubMed:4055729,
CC ECO:0000269|PubMed:9839943};
CC -!- PATHWAY: Amine and polyamine degradation; sarcosine degradation;
CC formaldehyde and glycine from sarcosine: step 1/1.
CC {ECO:0000305|PubMed:6163778}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:9839943}.
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 expressed in
CC pancreas and adrenal gland. {ECO:0000269|PubMed:9839943}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
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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; NM_053664.2.
DR AlphaFoldDB; Q64380; -.
DR SMR; Q64380; -.
DR STRING; 10116.ENSRNOP00000009555; -.
DR iPTMnet; Q64380; -.
DR PhosphoSitePlus; Q64380; -.
DR PaxDb; Q64380; -.
DR PeptideAtlas; Q64380; -.
DR PRIDE; Q64380; -.
DR GeneID; 114123; -.
DR KEGG; rno:114123; -.
DR UCSC; RGD:621125; rat.
DR CTD; 1757; -.
DR RGD; 621125; Sardh.
DR eggNOG; KOG2844; Eukaryota.
DR InParanoid; Q64380; -.
DR OrthoDB; 813396at2759; -.
DR BioCyc; MetaCyc:MON-16116; -.
DR Reactome; R-RNO-6798163; Choline catabolism.
DR UniPathway; UPA00292; UER00398.
DR PRO; PR:Q64380; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0005542; F:folic acid binding; IDA:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008480; F:sarcosine dehydrogenase activity; IDA:RGD.
DR GO; GO:0042426; P:choline catabolic process; TAS:RGD.
DR GO; GO:0006545; P:glycine biosynthetic process; TAS:RGD.
DR GO; GO:1901053; P:sarcosine catabolic process; IBA:GO_Central.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IDA:RGD.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.50.50.60; -; 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 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; SSF101790; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; FAD; Flavoprotein; Mitochondrion;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..919
FT /note="Sarcosine dehydrogenase, mitochondrial"
FT /id="PRO_0000010772"
FT MOD_RES 38
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 109
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT MOD_RES 174
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 174
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 378
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 392
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 535
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 560
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 776
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 778
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL12"
FT MOD_RES 803
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 803
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 885
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 885
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 905
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 905
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT CONFLICT 92..102
FT /note="GGVVLLERERL -> SGVGAAGERAM (in Ref. 1; AAB03674/
FT AAB04667)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..115
FT /note="LW -> GR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="L -> F (in Ref. 1; AAB03674/AAB04667)"
FT /evidence="ECO:0000305"
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
