ID   GCSP_CHICK              Reviewed;        1004 AA.
AC   P15505;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 2.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating), mitochondrial {ECO:0000305};
DE            EC=1.4.4.2 {ECO:0000269|PubMed:1993704, ECO:0000269|PubMed:7440562, ECO:0000269|PubMed:7440563};
DE   AltName: Full=Glycine cleavage system P protein;
DE   AltName: Full=Glycine decarboxylase {ECO:0000303|PubMed:1993704};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring);
DE   Flags: Precursor;
GN   Name=GLDC {ECO:0000250|UniProtKB:P23378};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=White leghorn;
RX   PubMed=1993704; DOI=10.1016/s0021-9258(18)49991-7;
RA   Kume A., Koyata H., Sakakibara T., Ishiguro Y., Kure S., Hiraga K.;
RT   "The glycine cleavage system. Molecular cloning of the chicken and human
RT   glycine decarboxylase cDNAs and some characteristics involved in the
RT   deduced protein structures.";
RL   J. Biol. Chem. 266:3323-3329(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 704-757.
RC   TISSUE=Liver;
RX   PubMed=3426593; DOI=10.1016/0006-291x(87)90413-x;
RA   Fujiwara K., Okamura-Ikeda K., Motokawa Y.;
RT   "Amino acid sequence of the phosphopyridoxyl peptide from P-protein of the
RT   chicken liver glycine cleavage system.";
RL   Biochem. Biophys. Res. Commun. 149:621-627(1987).
RN   [3]
RP   SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP   ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   FUNCTION.
RX   PubMed=7440562; DOI=10.1016/s0021-9258(19)70183-5;
RA   Hiraga K., Kikuchi G.;
RT   "The mitochondrial glycine cleavage system. Purification and properties of
RT   glycine decarboxylase from chicken liver mitochondria.";
RL   J. Biol. Chem. 255:11664-11670(1980).
RN   [4]
RP   SUBUNIT, INTERACTION WITH GCSH, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, ACTIVITY REGULATION, AND FUNCTION.
RX   PubMed=7440563; DOI=10.1016/s0021-9258(19)70184-7;
RA   Hiraga K., Kikuchi G.;
RT   "The mitochondrial glycine cleavage system. Functional association of
RT   glycine decarboxylase and aminomethyl carrier protein.";
RL   J. Biol. Chem. 255:11671-11676(1980).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The P protein (GLDC) binds the alpha-amino group of glycine
CC       through its pyridoxal phosphate cofactor; CO(2) is released and the
CC       remaining methylamine moiety is then transferred to the lipoamide
CC       cofactor of the H protein (GCSH). {ECO:0000269|PubMed:1993704,
CC       ECO:0000269|PubMed:7440562, ECO:0000269|PubMed:7440563}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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; Evidence={ECO:0000269|PubMed:1993704,
CC         ECO:0000269|PubMed:7440562, ECO:0000269|PubMed:7440563};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:7440562};
CC   -!- ACTIVITY REGULATION: Stimulated by lipoic acid. Inhibited in presence
CC       of methylamine. {ECO:0000269|PubMed:7440562,
CC       ECO:0000269|PubMed:7440563}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=20 mM for glycine in presence of GCSH
CC         {ECO:0000269|PubMed:7440563};
CC         KM=27 mM for methylamine in presence of GCSH
CC         {ECO:0000269|PubMed:7440563};
CC         KM=40 mM for glycine {ECO:0000269|PubMed:7440562};
CC         KM=3.5 mM for lipoic acid {ECO:0000269|PubMed:7440562};
CC         KM=63 mM for methylamine {ECO:0000269|PubMed:7440562};
CC   -!- SUBUNIT: Homodimer. Interacts with GCSH. The glycine cleavage system is
CC       composed of four proteins: P (GLDC), T (GCST), L (DLD) and H (GCSH).
CC       {ECO:0000269|PubMed:7440562, ECO:0000269|PubMed:7440563}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7440562}.
CC   -!- TISSUE SPECIFICITY: Liver (at protein level).
CC       {ECO:0000269|PubMed:7440562}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
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DR   EMBL; M64402; AAA49029.1; -; mRNA.
DR   EMBL; D90266; BAA14313.1; -; mRNA.
DR   EMBL; D90240; BAA14287.1; -; Genomic_DNA.
DR   PIR; A39521; A39521.
DR   RefSeq; NP_989653.1; NM_204322.1.
DR   AlphaFoldDB; P15505; -.
DR   SMR; P15505; -.
DR   STRING; 9031.ENSGALP00000037556; -.
DR   PaxDb; 9031-ENSGALP00000037556; -.
DR   GeneID; 374222; -.
DR   KEGG; gga:374222; -.
DR   CTD; 2731; -.
DR   VEuPathDB; HostDB:geneid_374222; -.
DR   eggNOG; KOG2040; Eukaryota.
DR   InParanoid; P15505; -.
DR   PhylomeDB; P15505; -.
DR   BioCyc; MetaCyc:MONOMER-12926; -.
DR   BRENDA; 1.4.1.27; 1306.
DR   BRENDA; 1.4.4.2; 1306.
DR   SABIO-RK; P15505; -.
DR   PRO; PR:P15505; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; ISS:UniProtKB.
DR   GO; GO:0047960; F:glycine dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0070280; F:pyridoxal binding; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0006546; P:glycine catabolic process; IDA:UniProtKB.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR   GO; GO:1903442; P:response to lipoic acid; IDA:UniProtKB.
DR   GO; GO:0036255; P:response to methylamine; IDA:UniProtKB.
DR   CDD; cd00613; GDC-P; 2.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Mitochondrion; Oxidoreductase;
KW   Pyridoxal phosphate; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..1004
FT                   /note="Glycine dehydrogenase (decarboxylating),
FT                   mitochondrial"
FT                   /id="PRO_0000010742"
FT   MOD_RES         738
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:7440562"
SQ   SEQUENCE   1004 AA;  111852 MW;  4446D7C66E0DC4BD CRC64;
     MQSCGRWWGR LAARGAPRHL RPAAGGPRRQ QQRWGGGEAA RCIEQLLPRH DDFCRRHIGP
     REREKREMLS AVGVQSVEEL MDKTIPASIR LRRPLRMDDH VVENEILETL YNIASKNKIW
     RSYIGMGYYN CSVPQPIARN LLENAGWVTQ YTPYQPEVSQ GRLESLLNYQ TMVCDITGMD
     VANASLLDEG TAAAEAMQLC HRQNKRRKFY IDARCHPQTI ANYTGVITEL KLPHEMDFSG
     KDVSGVLFQY PDTEGKVEDF SELIERAHQN GTLACCATDL LALCILKPPG EFGVDVVLGS
     SQRFGVPLCY GGPHAAFFAV KENLVRMMPG RMVGVTRDAN GKEVYRLALQ TREQHIRRDK
     ATSNICTAQA LLANMAAMYG VYHGSDGLKD IARRVHNATL ILAEGLRRAG HKLHHDLFFD
     TLTVTCGCSV KEVLDRAALR KINVRIYSDG RLGVSLDETV NEKDLDDILW IFGCESSAEL
     VAEGMGEETK GILSTPFKRT SKFLTHQVFN SYHSETNIVR YMKRLENKDI SLVHSMIPLG
     SCTMKLNSSA ELAPISWKEF ANIHPFVPLD QAQGYQQLFK DLEKDLCEIT GYDKISFQPN
     SGAQGEYAGL AAIKAYLNAK GERHRSVCLI PRSAHGTNPA SAQMAGMKIQ PIEVDKNGSI
     DISHLKAMVD KHKENLAAIM ITYPSTNGVF EEEIGDVCDL IHKHGGQVYL DGANMNAQVG
     LCRPGDYGSD VSHLNLHKTF CIPHGGGGPG MGPIGVKKHL APYLPTHPVI KIQTDKDACP
     LGTVSAAPWG SSAILPISWV YIKTMGAKGL KHASEIAILN ANYMAKRLEK HYKILFRGVR
     GYVAHEFILD TRPFKKTANI EAVDLAKRLQ DYGFHAPTMS WPVAGTLMIE PTESEDKGEL
     DRFCDAMISI RQEIADIEEG RMDPQVNPLK MSPHTLNCVT SSKWDRPYSR EVAAFPLPFV
     KPESKFWPTI ARIDDIYGDQ HLVCTCPPME AYESPFSEQK RASS
//