GCSH_CHICK
ID GCSH_CHICK Reviewed; 164 AA.
AC P11183;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Glycine cleavage system H protein, mitochondrial {ECO:0000303|PubMed:1993703};
DE AltName: Full=Lipoic acid-containing protein;
DE Flags: Precursor;
GN Name=GCSH {ECO:0000250|UniProtKB:P23434};
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].
RC STRAIN=White leghorn;
RX PubMed=1993703; DOI=10.1016/s0021-9258(18)49990-5;
RA Yamamoto M., Koyata H., Matsui C., Hiraga K.;
RT "The glycine cleavage system. Occurrence of two types of chicken H-protein
RT mRNAs presumably formed by the alternative use of the polyadenylation
RT consensus sequences in a single exon.";
RL J. Biol. Chem. 266:3317-3322(1991).
RN [2]
RP PROTEIN SEQUENCE OF 40-164, LIPOYLATION AT LYS-98, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=3522581; DOI=10.1016/s0021-9258(19)84457-5;
RA Fujiwara K., Okamura-Ikeda K., Motokawa Y.;
RT "Chicken liver H-protein, a component of the glycine cleavage system. Amino
RT acid sequence and identification of the N epsilon-lipoyllysine residue.";
RL J. Biol. Chem. 261:8836-8841(1986).
RN [3]
RP FUNCTION, INTERACTION WITH GLDC, AND SUBCELLULAR LOCATION.
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 H protein (GCSH) shuttles the methylamine group of glycine
CC from the P protein (GLDC) to the T protein (GCST).
CC {ECO:0000269|PubMed:7440563}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000269|PubMed:3522581};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000269|PubMed:3522581};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P
CC (GLDC), T (GCST), L (DLD) and H (GCSH). Interacts with GLDC.
CC {ECO:0000269|PubMed:7440563}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7440563}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000305}.
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DR EMBL; M64401; AAA48812.1; -; mRNA.
DR EMBL; D90270; BAA14314.1; -; Genomic_DNA.
DR PIR; A39520; GCCHH.
DR RefSeq; NP_001004372.1; NM_001004372.1.
DR AlphaFoldDB; P11183; -.
DR SMR; P11183; -.
DR STRING; 9031.ENSGALP00000038340; -.
DR PaxDb; P11183; -.
DR Ensembl; ENSGALT00000068424; ENSGALP00000048390; ENSGALG00000032679.
DR GeneID; 415803; -.
DR KEGG; gga:415803; -.
DR CTD; 2653; -.
DR VEuPathDB; HostDB:geneid_415803; -.
DR eggNOG; KOG3373; Eukaryota.
DR GeneTree; ENSGT00390000011666; -.
DR HOGENOM; CLU_097408_1_1_1; -.
DR InParanoid; P11183; -.
DR OMA; EHEWLSG; -.
DR OrthoDB; 1348095at2759; -.
DR PhylomeDB; P11183; -.
DR BRENDA; 1.4.1.27; 1306.
DR Reactome; R-GGA-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-GGA-6783984; Glycine degradation.
DR PRO; PR:P11183; -.
DR Proteomes; UP000000539; Chromosome 11.
DR Bgee; ENSGALG00000032679; Expressed in liver and 12 other tissues.
DR ExpressionAtlas; P11183; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR GO; GO:0009249; P:protein lipoylation; IDA:UniProtKB.
DR CDD; cd06848; GCS_H; 1.
DR HAMAP; MF_00272; GcvH; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR002930; GCV_H.
DR InterPro; IPR033753; GCV_H/Fam206.
DR InterPro; IPR017453; GCV_H_sub.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR11715; PTHR11715; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR00527; gcvH; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lipoyl; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:3522581"
FT CHAIN 40..164
FT /note="Glycine cleavage system H protein, mitochondrial"
FT /id="PRO_0000010727"
FT DOMAIN 57..139
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 98
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000269|PubMed:3522581"
SQ SEQUENCE 164 AA; 18011 MW; FF8621EFDA78D4B4 CRC64;
MAWLVLRRLG PVLAPRCPRL SLRPQVPAVR RLGTGSLLLS ARKFTDKHEW ISVENGIGTV
GISNFAQEAL GDVVYCSLPE IGTKLNKDDE FGALESVKAA SELYSPLTGE VTDINAALAD
NPGLVNKSCY QDGWLIKMTV EKPAELDELM SEDAYEKYIK SIED
