ID   GCSP_SOLTU              Reviewed;        1035 AA.
AC   O49954;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
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 dehydrogenase (aminomethyl-transferring);
DE   Flags: Precursor;
GN   Name=GDCSP;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RA   Bauwe H.;
RT   "cDNA encoding P-protein of the glycine cleavage system in Solanum
RT   tuberosum Cv. Desire.";
RL   (er) Plant Gene Register PGR98-005(1998).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The P protein binds the alpha-amino group of glycine through
CC       its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC       methylamine moiety is then transferred to the lipoamide cofactor of the
CC       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   -!- SUBUNIT: Homodimer (By similarity). The glycine cleavage system is
CC       composed of four proteins: P, T, L and H. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
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DR   EMBL; Z99770; CAB16918.1; -; mRNA.
DR   PIR; T07826; T07826.
DR   RefSeq; NP_001305600.1; NM_001318671.1.
DR   AlphaFoldDB; O49954; -.
DR   SMR; O49954; -.
DR   IntAct; O49954; 1.
DR   STRING; 4113.PGSC0003DMT400076966; -.
DR   PRIDE; O49954; -.
DR   GeneID; 102601213; -.
DR   KEGG; sot:102601213; -.
DR   eggNOG; KOG2040; Eukaryota.
DR   InParanoid; O49954; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; O49954; baseline.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd00613; GDC-P; 2.
DR   Gene3D; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   HAMAP; MF_00711; GcvP; 1.
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   2: Evidence at transcript level;
KW   Mitochondrion; Oxidoreductase; Pyridoxal phosphate; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..64
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           65..1035
FT                   /note="Glycine dehydrogenase (decarboxylating),
FT                   mitochondrial"
FT                   /id="PRO_0000010750"
FT   MOD_RES         771
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1035 AA;  112914 MW;  76C8418ED1856AFB CRC64;
     MERARKLANR AILKRLVSQS KQSRSNEIPS SSLYRPSRYV SSLSPYTFQA RNNAKSFNTQ
     QARSISVEAL KPSDTFPRRH NSATPEEQTK MAEFCGFQSL DALIDATVPQ SIRSESMKLP
     KFDSGLTESQ MIEHMQNLAS KNKVFKSYIG MGYYNTYVPP VILRNLLENP AWYTQYTPYQ
     AEISQGRLES LLNYQTMITD LTGLPMSNAS LLDEGTAAAE AMAMCNNILK GKKKTFLIAS
     NCHPQTIDIC KTRADGFDLK VVTVDLKDID YKSGDVCGVL VQYPGTEGEI LDYGEFIKNA
     HAHGVKVVMA SDLLALTMLK PPGELGADIV VGSAQRFGVP MGYGGPHAAF LATSQEYKRM
     MPGRIIGLSV DSTGKPALRM AMQTREQHIR RDKATSNICT AQALLANMAA MYAVYHGPEG
     LKTIGQRVHG LAGTFSAGLK KLGTVEVQDL PFFDTVKVKC SDAKAIADVA NKNDINLRIV
     DNNTITVSFD ETTTLEDVDD LFKVFALGKP VPFTAQSIAQ EVENLIPSGL TRETPFLTHQ
     IFNSYHTEHE LLRYLHKLQS KDLSLCHSMI PLGSCTMKLN ATTEMMPVTW PSFANIHPFA
     PTEQAAGYQE MFDDLGALLC TITGFDSFSL QPNAGAAGEY AGLMVIRAYH MSRGDHHRNV
     CIIPVSAHGT NPASAAMCGM KIVAVGTDAK GNINIEELRK AAEANKDNLA ALMVTYPSTH
     GVYEEGIDEI CKIIHDNGGQ VYMDGANMNA QVGLTSPGFI GADVCHLNLH KTFCIPHGGG
     GPGMGPIGVK KHLAPYLPSH PVVPTGGIPS PDKSEPLGAI SAAPWGSALI LPISYTYIAM
     MGSKGLTDAS KIAILSANYM AKRLEKHYPV LFRGVNGTCA HEFIIDLRGF KNTAGIEPED
     VAKRLIDYGF HGPTMSWPVP GTLMIEPTES ESKAELDRFC DALISIREEI AQIEKGNVDI
     NNNVLKGAPH PPSMLMADAW TKPYSREYAA YPAPWLRSAK FWPTTGRVDN VYGDRNLICT
     LLPVSEMAEE KAATA