GCSP_CHICK
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 03-AUG-2022, entry version 131.
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=(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; 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; P15505; -.
DR PRIDE; P15505; -.
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:MON-12926; -.
DR BRENDA; 1.4.1.27; 1306.
DR BRENDA; 1.4.4.2; 1306.
DR PRO; PR:P15505; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
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:0006546; P:glycine catabolic process; IDA:UniProtKB.
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; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
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; PF01212; Beta_elim_lyase; 1.
DR Pfam; PF02347; GDC-P; 1.
DR SUPFAM; SSF53383; SSF53383; 2.
DR TIGRFAMs; TIGR00461; gcvP; 1.
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
