ID GCSP_HUMAN Reviewed; 1020 AA. AC P23378; Q2M2F8; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 27-MAR-2024, entry version 200. DE RecName: Full=Glycine dehydrogenase (decarboxylating), mitochondrial {ECO:0000303|PubMed:15489334}; DE EC=1.4.4.2 {ECO:0000269|PubMed:1993704, ECO:0000269|PubMed:1996985, ECO:0000269|PubMed:28244183}; DE AltName: Full=Glycine cleavage system P protein; DE AltName: Full=Glycine decarboxylase {ECO:0000303|PubMed:1993704, ECO:0000303|PubMed:1996985}; DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring); DE Flags: Precursor; GN Name=GLDC {ECO:0000312|HGNC:HGNC:4313}; GN Synonyms=GCSP {ECO:0000312|HGNC:HGNC:4313}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND VARIANT NKH PHE-756 RP DEL. RX PubMed=1996985; DOI=10.1016/0006-291x(91)91545-n; RA Kure S., Narisawa K., Tada K.; RT "Structural and expression analyses of normal and mutant mRNA encoding RT glycine decarboxylase: three-base deletion in mRNA causes nonketotic RT hyperglycinemia."; RL Biochem. Biophys. Res. Commun. 174:1176-1182(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, INVOLVEMENT IN NKH, RP VARIANTS NKH LYS-146; PRO-173; ALA-267; CYS-362; TRP-373; GLU-376; TRP-461; RP PRO-548; TYR-580; ARG-581; ASP-624; ASP-763; GLU-768; TRP-790; HIS-866; RP GLY-905; THR-933 AND ARG-994, AND CHARACTERIZATION OF VARIANTS NKH LYS-146; RP PRO-173; ALA-267; CYS-362; TRP-373; GLU-376; TRP-461; PRO-548; TYR-580; RP ARG-581; ASP-624; ASP-763; GLU-768; TRP-790; HIS-866; GLY-905; THR-933 AND RP ARG-994. RX PubMed=28244183; DOI=10.1002/humu.23208; RA Bravo-Alonso I., Navarrete R., Arribas-Carreira L., Perona A., Abia D., RA Couce M.L., Garcia-Cazorla A., Morais A., Domingo R., Ramos M.A., RA Swanson M.A., Van Hove J.L., Ugarte M., Perez B., Perez-Cerda C., RA Rodriguez-Pombo P.; RT "Nonketotic Hyperglycinemia: functional assessment of missense variants in RT GLDC to understand phenotypes of the disease."; RL Hum. Mutat. 38:678-691(2017). RN [11] RP VARIANT NKH ILE-564. RX PubMed=1634607; DOI=10.1172/jci115831; RA Kure S., Takayanagi M., Narisawa K., Tada K., Leisti J.; RT "Identification of a common mutation in Finnish patients with nonketotic RT hyperglycinemia."; RL J. Clin. Invest. 90:160-164(1992). RN [12] RP VARIANT NKH SER-515. RX PubMed=11286506; DOI=10.1006/mgme.2001.3158; RA Toone J.R., Applegarth D.A., Coulter-Mackie M.B., James E.R.; RT "Recurrent mutations in P- and T-proteins of the glycine cleavage complex RT and a novel T-protein mutation (N145I): a strategy for the molecular RT investigation of patients with nonketotic hyperglycinemia (NKH)."; RL Mol. Genet. Metab. 72:322-325(2001). RN [13] RP VARIANT NKH PRO-283, AND VARIANT THR-329. RX PubMed=11592811; DOI=10.1006/mgme.2001.3224; RA Applegarth D.A., Toone J.R.; RT "Nonketotic hyperglycinemia (glycine encephalopathy): laboratory RT diagnosis."; RL Mol. Genet. Metab. 74:139-146(2001). RN [14] RP VARIANT NKH CYS-839. RX PubMed=28737873; DOI=10.5546/aap.2017.eng.e225; RA Liu S., Wang Z., Liang J., Chen N., Ouyang H., Zeng W., Chen L., Xie X., RA Jiang J.; RT "Two novel mutations in the glycine decarboxylase gene in a boy with RT classic nonketotic hyperglycinemia: case report."; RL Arch. Argent. Pediatr. 115:E225-E229(2017). 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:1996985, ECO:0000269|PubMed:28244183}. 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:1996985, ECO:0000269|PubMed:28244183}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250|UniProtKB:P15505}; CC -!- ACTIVITY REGULATION: Stimulated by lipoic acid. Inhibited in presence CC of methylamine (By similarity). {ECO:0000250|UniProtKB:P15505}. CC -!- SUBUNIT: Homodimer (By similarity). Interacts with GCSH (By CC similarity). The glycine cleavage system is composed of four proteins: CC P (GLDC), T (GCST), L (DLD) and H (GCSH). CC {ECO:0000250|UniProtKB:P15505}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:28244183}. CC -!- DISEASE: Non-ketotic hyperglycinemia (NKH) [MIM:605899]: Autosomal CC recessive disease characterized by accumulation of a large amount of CC glycine in body fluid and by severe neurological symptoms. CC {ECO:0000269|PubMed:11286506, ECO:0000269|PubMed:11592811, CC ECO:0000269|PubMed:1634607, ECO:0000269|PubMed:1996985, CC ECO:0000269|PubMed:28244183, ECO:0000269|PubMed:28737873}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M63635; AAA36478.1; -; mRNA. DR EMBL; M64590; AAA36463.1; -; mRNA. DR EMBL; D90239; BAA14286.1; -; mRNA. DR EMBL; AK314156; BAG36841.1; -; mRNA. DR EMBL; AL353718; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL162411; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58740.1; -; Genomic_DNA. DR EMBL; BC111993; AAI11994.1; -; mRNA. DR EMBL; BC111995; AAI11996.1; -; mRNA. DR CCDS; CCDS34987.1; -. DR PIR; JN0124; JN0124. DR RefSeq; NP_000161.2; NM_000170.2. DR PDB; 6I33; X-ray; 2.30 A; A/B=45-1020. DR PDB; 6I34; X-ray; 2.10 A; A/B/C/D=45-1020. DR PDB; 6I35; X-ray; 2.00 A; A/B/C/D=45-1020. DR PDBsum; 6I33; -. DR PDBsum; 6I34; -. DR PDBsum; 6I35; -. DR AlphaFoldDB; P23378; -. DR SASBDB; P23378; -. DR SMR; P23378; -. DR BioGRID; 108993; 307. DR IntAct; P23378; 18. DR MINT; P23378; -. DR STRING; 9606.ENSP00000370737; -. DR DrugBank; DB00145; Glycine. DR DrugBank; DB00114; Pyridoxal phosphate. DR iPTMnet; P23378; -. DR PhosphoSitePlus; P23378; -. DR SwissPalm; P23378; -. DR BioMuta; GLDC; -. DR DMDM; 229462870; -. DR EPD; P23378; -. DR jPOST; P23378; -. DR MassIVE; P23378; -. DR MaxQB; P23378; -. DR PaxDb; 9606-ENSP00000370737; -. DR PeptideAtlas; P23378; -. DR ProteomicsDB; 54084; -. DR Pumba; P23378; -. DR Antibodypedia; 9715; 218 antibodies from 31 providers. DR DNASU; 2731; -. DR Ensembl; ENST00000321612.8; ENSP00000370737.4; ENSG00000178445.10. DR GeneID; 2731; -. DR KEGG; hsa:2731; -. DR MANE-Select; ENST00000321612.8; ENSP00000370737.4; NM_000170.3; NP_000161.2. DR UCSC; uc003zkc.4; human. DR AGR; HGNC:4313; -. DR CTD; 2731; -. DR DisGeNET; 2731; -. DR GeneCards; GLDC; -. DR GeneReviews; GLDC; -. DR HGNC; HGNC:4313; GLDC. DR HPA; ENSG00000178445; Tissue enriched (liver). DR MalaCards; GLDC; -. DR MIM; 238300; gene. DR MIM; 605899; phenotype. DR neXtProt; NX_P23378; -. DR OpenTargets; ENSG00000178445; -. DR Orphanet; 289863; Atypical glycine encephalopathy. DR Orphanet; 289860; Infantile glycine encephalopathy. DR Orphanet; 289857; Neonatal glycine encephalopathy. DR PharmGKB; PA28716; -. DR VEuPathDB; HostDB:ENSG00000178445; -. DR eggNOG; KOG2040; Eukaryota. DR GeneTree; ENSGT00390000017970; -. DR HOGENOM; CLU_004620_3_2_1; -. DR InParanoid; P23378; -. DR OMA; RNLICTC; -. DR OrthoDB; 177349at2759; -. DR PhylomeDB; P23378; -. DR TreeFam; TF300678; -. DR BioCyc; MetaCyc:HS00622-MONOMER; -. DR BRENDA; 1.4.1.27; 2681. DR BRENDA; 1.4.4.2; 2681. DR PathwayCommons; P23378; -. DR Reactome; R-HSA-6783984; Glycine degradation. DR SABIO-RK; P23378; -. DR SignaLink; P23378; -. DR SIGNOR; P23378; -. DR BioGRID-ORCS; 2731; 11 hits in 1153 CRISPR screens. DR ChiTaRS; GLDC; human. DR GeneWiki; Glycine_dehydrogenase_(decarboxylating); -. DR GenomeRNAi; 2731; -. DR Pharos; P23378; Tbio. DR PRO; PR:P23378; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P23378; Protein. DR Bgee; ENSG00000178445; Expressed in right lobe of liver and 151 other cell types or tissues. DR ExpressionAtlas; P23378; baseline and differential. DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB. DR GO; GO:0016594; F:glycine binding; IBA:GO_Central. DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IDA:UniProtKB. DR GO; GO:0016829; F:lyase activity; IEA:InterPro. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0070280; F:pyridoxal binding; ISS:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl. 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; ISS:UniProtKB. DR GO; GO:0036255; P:response to methylamine; ISS: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. DR Genevisible; P23378; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Disease variant; Mitochondrion; Oxidoreductase; KW Pyridoxal phosphate; Reference proteome; Transit peptide. FT TRANSIT 1..35 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 36..1020 FT /note="Glycine dehydrogenase (decarboxylating), FT mitochondrial" FT /id="PRO_0000010740" FT REGION 21..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 447 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91W43" FT MOD_RES 514 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91W43" FT MOD_RES 648 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91W43" FT MOD_RES 664 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91W43" FT MOD_RES 754 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250|UniProtKB:P15505" FT VARIANT 146 FT /note="T -> K (in NKH; loss of glycine catabolic process; FT loss of expression; dbSNP:rs376578742)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078776" FT VARIANT 173 FT /note="L -> P (in NKH; loss of glycine catabolic process; FT decreased abundance)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078777" FT VARIANT 267 FT /note="P -> A (in NKH; decreased glycine catabolic process; FT changed localization to the mitochondria; also expressed FT diffusely throughout the cytosol; decreased abundance; FT dbSNP:rs1554648117)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078778" FT VARIANT 283 FT /note="A -> P (in NKH; dbSNP:rs386833589)" FT /evidence="ECO:0000269|PubMed:11592811" FT /id="VAR_016849" FT VARIANT 329 FT /note="P -> T (in one non-ketotic hyperglycinemia patient; FT dbSNP:rs386833593)" FT /evidence="ECO:0000269|PubMed:11592811" FT /id="VAR_016850" FT VARIANT 362 FT /note="R -> C (in NKH; decreased glycine catabolic process; FT decreased abundance; dbSNP:rs10975674)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078779" FT VARIANT 373 FT /note="R -> W (in NKH; decreased glycine catabolic process; FT decreased abundance; dbSNP:rs150171524)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078780" FT VARIANT 376 FT /note="K -> E (in NKH; decreased glycine catabolic process; FT decreased abundance; dbSNP:rs774093619)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078781" FT VARIANT 461 FT /note="R -> W (in NKH; decreased glycine catabolic process; FT changed localization to the mitochondria; also expressed FT diffusely throughout the cytosol; decreased abundance; FT dbSNP:rs761957837)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078782" FT VARIANT 515 FT /note="R -> S (in NKH; dbSNP:rs121964976)" FT /evidence="ECO:0000269|PubMed:11286506" FT /id="VAR_016851" FT VARIANT 548 FT /note="L -> P (in NKH; decreased GCSP-protein glycine FT exchange activity; no effect on abundance)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078783" FT VARIANT 564 FT /note="S -> I (in NKH; common mutation in Finland; FT dbSNP:rs121964974)" FT /evidence="ECO:0000269|PubMed:1634607" FT /id="VAR_004979" FT VARIANT 580 FT /note="H -> Y (in NKH; loss of glycine catabolic process; FT loss of expression)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078784" FT VARIANT 581 FT /note="P -> R (in NKH; loss of glycine catabolic process; FT decreased abundance; dbSNP:rs772871471)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078785" FT VARIANT 624 FT /note="A -> D (in NKH; loss of GCSP-protein glycine FT exchange activity; no effect on abundance)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078786" FT VARIANT 756 FT /note="Missing (in NKH)" FT /evidence="ECO:0000269|PubMed:1996985" FT /id="VAR_009939" FT VARIANT 763 FT /note="G -> D (in NKH; loss of GCSP-protein glycine FT exchange activity; no effect on abundance; FT dbSNP:rs1374110692)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078787" FT VARIANT 768 FT /note="G -> E (in NKH; loss of GCSP-protein glycine FT exchange activity; no effect on abundance)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078788" FT VARIANT 790 FT /note="R -> W (in NKH; decreased glycine catabolic process; FT decreased abundance; dbSNP:rs386833556)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078789" FT VARIANT 839 FT /note="Y -> C (in NKH)" FT /evidence="ECO:0000269|PubMed:28737873" FT /id="VAR_079313" FT VARIANT 866 FT /note="D -> H (in NKH; decreased glycine catabolic process; FT decreased abundance)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078790" FT VARIANT 905 FT /note="V -> G (in NKH; decreased GCSP-protein glycine FT exchange activity; no effect on abundance; FT dbSNP:rs188269735)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078791" FT VARIANT 933 FT /note="I -> T (in NKH; decreased glycine catabolic process; FT decreased abundance; dbSNP:rs758029533)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078792" FT VARIANT 994 FT /note="G -> R (in NKH; loss of glycine catabolic process; FT loss of expression; dbSNP:rs1406713104)" FT /evidence="ECO:0000269|PubMed:28244183" FT /id="VAR_078793" FT CONFLICT 396 FT /note="A -> R (in Ref. 2; AAA36463/BAA14286)" FT /evidence="ECO:0000305" FT CONFLICT 441 FT /note="Q -> H (in Ref. 1; AAA36478 and 2; FT AAA36463/BAA14286)" FT /evidence="ECO:0000305" FT CONFLICT 608 FT /note="Y -> H (in Ref. 1; AAA36478)" FT /evidence="ECO:0000305" FT CONFLICT 976 FT /note="V -> M (in Ref. 2; AAA36463/BAA14286)" FT /evidence="ECO:0000305" FT HELIX 52..56 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 64..67 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 72..81 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 87..94 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 113..124 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 145..150 FT /evidence="ECO:0007829|PDB:6I35" FT TURN 151..153 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 170..187 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 199..214 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 227..240 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 243..246 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 259..267 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 277..285 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 289..294 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 305..308 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 311..316 FT /evidence="ECO:0007829|PDB:6I35" FT TURN 318..321 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 325..327 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 332..336 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 338..343 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 349..354 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 359..363 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 366..368 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 370..373 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 386..424 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 428..430 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 432..441 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 446..455 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 468..471 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 478..487 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 494..500 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 508..510 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 523..526 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 531..543 FT /evidence="ECO:0007829|PDB:6I35" FT TURN 548..550 FT /evidence="ECO:0007829|PDB:6I35" FT TURN 556..558 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 565..568 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 569..572 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 574..577 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 585..587 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 589..606 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 609..612 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 618..635 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 643..647 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 653..660 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 664..668 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 674..676 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 678..688 FT /evidence="ECO:0007829|PDB:6I35" FT TURN 689..691 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 692..700 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 710..718 FT /evidence="ECO:0007829|PDB:6I35" FT TURN 719..721 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 723..727 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 728..733 FT /evidence="ECO:0007829|PDB:6I35" FT TURN 734..737 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 740..742 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 746..749 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 752..755 FT /evidence="ECO:0007829|PDB:6I35" FT TURN 761..763 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 770..772 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 774..779 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 784..786 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 791..793 FT /evidence="ECO:0007829|PDB:6I34" FT STRAND 801..803 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 808..810 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 811..844 FT /evidence="ECO:0007829|PDB:6I35" FT TURN 845..847 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 848..850 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 863..866 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 869..874 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 878..887 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 893..896 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 903..905 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 913..934 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 940..943 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 944..947 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 952..956 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 966..970 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 978..980 FT /evidence="ECO:0007829|PDB:6I35" FT STRAND 985..987 FT /evidence="ECO:0007829|PDB:6I35" FT HELIX 991..996 FT /evidence="ECO:0007829|PDB:6I35" SQ SEQUENCE 1020 AA; 112730 MW; 8FAEA7D56BEB17B2 CRC64; MQSCARAWGL RLGRGVGGGR RLAGGSGPCW APRSRDSSSG GGDSAAAGAS RLLERLLPRH DDFARRHIGP GDKDQREMLQ TLGLASIDEL IEKTVPANIR LKRPLKMEDP VCENEILATL HAISSKNQIW RSYIGMGYYN CSVPQTILRN LLENSGWITQ YTPYQPEVSQ GRLESLLNYQ TMVCDITGLD MANASLLDEG TAAAEALQLC YRHNKRRKFL VDPRCHPQTI AVVQTRAKYT GVLTELKLPC EMDFSGKDVS GVLFQYPDTE GKVEDFTELV ERAHQSGSLA CCATDLLALC ILRPPGEFGV DIALGSSQRF GVPLGYGGPH AAFFAVRESL VRMMPGRMVG VTRDATGKEV YRLALQTREQ HIRRDKATSN ICTAQALLAN MAAMFAIYHG SHGLEHIARR VHNATLILSE GLKRAGHQLQ HDLFFDTLKI QCGCSVKEVL GRAAQRQINF RLFEDGTLGI SLDETVNEKD LDDLLWIFGC ESSAELVAES MGEECRGIPG SVFKRTSPFL THQVFNSYHS ETNIVRYMKK LENKDISLVH SMIPLGSCTM KLNSSSELAP ITWKEFANIH PFVPLDQAQG YQQLFRELEK DLCELTGYDQ VCFQPNSGAQ GEYAGLATIR AYLNQKGEGH RTVCLIPKSA HGTNPASAHM AGMKIQPVEV DKYGNIDAVH LKAMVDKHKE NLAAIMITYP STNGVFEENI SDVCDLIHQH GGQVYLDGAN MNAQVGICRP GDFGSDVSHL NLHKTFCIPH GGGGPGMGPI GVKKHLAPFL PNHPVISLKR NEDACPVGTV SAAPWGSSSI LPISWAYIKM MGGKGLKQAT ETAILNANYM AKRLETHYRI LFRGARGYVG HEFILDTRPF KKSANIEAVD VAKRLQDYGF HAPTMSWPVA GTLMVEPTES EDKAELDRFC DAMISIRQEI ADIEEGRIDP RVNPLKMSPH SLTCVTSSHW DRPYSREVAA FPLPFVKPEN KFWPTIARID DIYGDQHLVC TCPPMEVYES PFSEQKRASS //