ID A0A7N5K9M1_AILME Unreviewed; 994 AA.
AC A0A7N5K9M1;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN Name=GLDC {ECO:0000313|Ensembl:ENSAMEP00000037158.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000037158.1, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000037158.1, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000037158.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSAMEP00000037158.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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:0000256|ARBA:ARBA00059804}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein]
CC + glycine + H(+) = N(6)-[(R)-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 Evidence={ECO:0000256|ARBA:ARBA00049026,
CC ECO:0000256|RuleBase:RU364056};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR603437-50, ECO:0000256|RuleBase:RU364056};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|RuleBase:RU364056}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU364056}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|RuleBase:RU364056}.
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DR AlphaFoldDB; A0A7N5K9M1; -.
DR Ensembl; ENSAMET00000039663.1; ENSAMEP00000037158.1; ENSAMEG00000015836.2.
DR GeneTree; ENSGT00390000017970; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:TreeGrafter.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016594; F:glycine binding; IEA:TreeGrafter.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:TreeGrafter.
DR CDD; cd00613; GDC-P; 2.
DR FunFam; 3.90.1150.10:FF:000025; Glycine cleavage system P protein; 1.
DR FunFam; 3.90.1150.10:FF:000153; Glycine dehydrogenase (decarboxylating); 1.
DR FunFam; 3.40.640.10:FF:000007; glycine dehydrogenase (Decarboxylating), mitochondrial; 1.
DR FunFam; 3.40.640.10:FF:000199; Glycine dehydrogenase [decarboxylating], mitochondrial; 1.
DR FunFam; 3.40.640.10:FF:000225; Glycine dehydrogenase [decarboxylating], mitochondrial; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 3.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 3.
DR HAMAP; MF_00711; GcvP; 1.
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 NCBIfam; NF003346; PRK04366.1; 1.
DR PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR Pfam; PF02347; GDC-P; 3.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU364056};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364056};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 65..213
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 215..462
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 499..770
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 803..924
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 27..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 728
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 994 AA; 110021 MW; A5448549B63DF068 CRC64;
MQKCARAWGL RLGCGVGGGR RLVGGTGPLW VPRGRDSSSG GGDSSRAGDS RLLERLLPRH
DDFARRHIGP GDKDQREMLQ ALGLASIDEL IEKTVPASIR LKRPLKMEDP ICENEILTTL
HAISSKNQIW RSYMGMGYYN CSVPQTILRN LLENAGWITQ YTPYQPEVSQ GRLESLLNYQ
TMVCDITGMD VANASLLDEA TAAAEAMQLC HRYNGVLIEL KLPHEMDFSG KDVSGVLFQY
PDTEGKVEDF TDLVERAHQT GSLACCATDL LALCILRPPG EFGVDIALGS SQRFGVPLGY
GGPHAAFFAV RESLVRMMPG RMVGVTRDAT GKEVYRLALQ TREQHIRRDK ATSNICTAQA
LLANMAAMFA IYHGSRGLEH IARRVHNATL ILSEGLKRAG HQLQHDLFFD TLKIQCGCSV
KEVLDRATQR QINFRLFEDG TLGISLDETV NEKDLDDLLW IFGCESSAEL VAEGMGEEQR
GILGTAFKRT SSFLTHQVFN SYHSETNIVR YMKKLENKDI SLVHSMIPLG SCTMKLNSSS
ELAPITWKEF SNIHPFVPLD QAQGYQQLFL ELEKDLCELT GYDRISFQPN SGAQGEYAGL
ATIRAYFDER GEGHRTVCLI PKSAHGTNPA SAHMAGMKIQ PVEVDKYGNI DTAHLKAMVD
KHKENLAAIM ITYPSTNGVF EENIGDVCDL IHQHGGQVYL DGANMNAQVG ICRPGDFGSD
VSHLNLHKTF CIPHGGGGPG MGPIGVKKHL APFLPNHPII SVKPDEDGRP VGTVSAAPWG
SSSILPISWA YIKMMGGKGL KQATEIAILN ANYMAKRLEK HYRVLFRGAR GYVAHEFILD
TRPFKKSANI EAVDVAKRLQ DYGFHAPTMS WPVAGTLMVE PTESEDKAEL DRFCDAMISI
RQEIADIEEG RIDPRVNPLK MSPHSLTCVT SSHWDRPYSR EVAAFPLPFV KPENKFWPTI
ARIDDIYGDQ HLVCTCPPME VYESPFSEQK RASS
//
