GCSP_YEAST
ID GCSP_YEAST Reviewed; 1034 AA.
AC P49095; D6W013;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Glycine dehydrogenase (decarboxylating), mitochondrial;
DE EC=1.4.4.2;
DE AltName: Full=Glycine cleavage system P protein;
DE AltName: Full=Glycine decarboxylase;
DE AltName: Full=Glycine decarboxylase complex subunit P;
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring);
DE Flags: Precursor;
GN Name=GCV2; Synonyms=GSD2; OrderedLocusNames=YMR189W; ORFNames=YM9646.01;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=8830251; DOI=10.1046/j.1365-2958.1996.419947.x;
RA Sinclair D.A., Hong S.-P., Dawes I.W.;
RT "Specific induction by glycine of the gene for the P-subunit of glycine
RT decarboxylase from Saccharomyces cerevisiae.";
RL Mol. Microbiol. 19:611-623(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: The glycine cleavage system (glycine decarboxylase complex)
CC catalyzes the degradation of glycine. The P protein binds the alpha-
CC amino group of glycine through its pyridoxal phosphate cofactor; CO(2)
CC is released and the remaining methylamine moiety is then transferred to
CC the lipoamide cofactor of the H protein.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; Xref=Rhea:RHEA:24304,
CC Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83143; EC=1.4.4.2;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the glycine decarboxylase complex (GDC), which is
CC composed of four proteins: P, T, L and H.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- INDUCTION: By glycine. {ECO:0000269|PubMed:8830251}.
CC -!- MISCELLANEOUS: Present with 12000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
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DR EMBL; U20641; AAB18933.1; -; Genomic_DNA.
DR EMBL; Z47815; CAA87810.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10087.1; -; Genomic_DNA.
DR PIR; S50917; S50917.
DR RefSeq; NP_013914.1; NM_001182695.1.
DR AlphaFoldDB; P49095; -.
DR SMR; P49095; -.
DR BioGRID; 35367; 71.
DR ComplexPortal; CPX-1268; Glycine decarboxylase multienzyme complex.
DR DIP; DIP-6823N; -.
DR IntAct; P49095; 6.
DR MINT; P49095; -.
DR STRING; 4932.YMR189W; -.
DR iPTMnet; P49095; -.
DR MaxQB; P49095; -.
DR PaxDb; P49095; -.
DR PRIDE; P49095; -.
DR EnsemblFungi; YMR189W_mRNA; YMR189W; YMR189W.
DR GeneID; 855227; -.
DR KEGG; sce:YMR189W; -.
DR SGD; S000004801; GCV2.
DR VEuPathDB; FungiDB:YMR189W; -.
DR eggNOG; KOG2040; Eukaryota.
DR GeneTree; ENSGT00390000017970; -.
DR HOGENOM; CLU_004620_3_1_1; -.
DR InParanoid; P49095; -.
DR OMA; CVPMSEY; -.
DR BioCyc; YEAST:YMR189W-MON; -.
DR Reactome; R-SCE-6783984; Glycine degradation.
DR PRO; PR:P49095; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P49095; protein.
DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IDA:SGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006546; P:glycine catabolic process; IC:ComplexPortal.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IMP:SGD.
DR GO; GO:0006730; P:one-carbon metabolic process; IGI:SGD.
DR CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 2.
DR InterPro; IPR003437; GcvP.
DR InterPro; IPR020581; GDC_P.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11773; PTHR11773; 1.
DR Pfam; PF02347; GDC-P; 2.
DR SUPFAM; SSF53383; SSF53383; 2.
DR TIGRFAMs; TIGR00461; gcvP; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Oxidoreductase; Pyridoxal phosphate; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..1034
FT /note="Glycine dehydrogenase (decarboxylating),
FT mitochondrial"
FT /id="PRO_0000010752"
FT MOD_RES 773
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1034 AA; 114451 MW; F4D52642B0BDA041 CRC64;
MLRTRVTALL CRATVRSSTN YVSLARTRSF HSQSILLKTA ATDITSTQYS RIFNPDLKNI
DRPLDTFARR HLGPSPSDVK KMLKTMGYSD LNAFIEELVP PNILKRRPLK LEAPSKGFCE
QEMLQHLEKI ANKNHYKVKN FIGKGYYGTI LPPVIQRNLL ESPEWYTSYT PYQPEISQGR
LEALLNFQTV VSDLTGLPVA NASLLDEGTA AGEAMLLSFN ISRKKKLKYV IDKKLHQQTK
SVLHTRAKPF NIEIIEVDCS DIKKAVDVLK NPDVSGCLVQ YPATDGSILP PDSMKQLSDA
LHSHKSLLSV ASDLMALTLL KPPAHYGADI VLGSSQRFGV PMGYGGPHAA FFAVIDKLNR
KIPGRIVGIS KDRLGKTALR LALQTREQHI KRDKATSNIC TAQALLANVA SSYCVYHGPK
GLQNISRRIF SLTSILANAI ENDSCPHELI NKTWFDTLTI KLGNGISSEQ LLDKALKEFN
INLFAVDTTT ISLALDETTT KADVENLLKV FDIENSSQFL SEDYSNSFPR EFQRTDEILR
NEVFHMHHSE TAMLRYLHRL QSRDLSLANS MIPLGSCTMK LNSTVEMMPI TWPQFSNIHP
FQPSNQVQGY KELITSLEKD LCSITGFDGI SLQPNSGAQG EYTGLRVIRS YLESKGENHR
NVCLIPVSAH GTNPASAAMA GLKVVPVNCL QDGSLDLVDL KNKAEQHSKE LAAVMITYPS
TYGLFEPGIQ HAIDIVHSFG GQVYLDGANM NAQVGLTSPG DLGADVCHLN LHKTFSIPHG
GGGPAGAPIC VKSHLIPHLP KHDVVDMITG IGGSKSIDSV SSAPYGNALV LPISYAYIKM
MGNEGLPFSS VIAMLNSNYM MTRLKDHYKI LFVNEMSTLK HCAHEFIVDL REYKAKGVEA
IDVAKRLQDY GFHAPTLAFP VPGTLMIEPT ESENLEELDR FCDAMISIKE EINALVAGQP
KGQILKNAPH SLEDLITSSN WDTRGYTREE AAYPLPFLRY NKFWPTVARL DDTYGDMNLI
CTCPSVEEIA NETE
