GCSH_PEA
ID GCSH_PEA Reviewed; 165 AA.
AC P16048;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glycine cleavage system H protein, mitochondrial;
DE Flags: Precursor;
GN Name=GDCSH; Synonyms=GCDH;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1688555; DOI=10.1016/s0021-9258(19)40127-0;
RA Kim Y., Oliver D.J.;
RT "Molecular cloning, transcriptional characterization, and sequencing of
RT cDNA encoding the H-protein of the mitochondrial glycine decarboxylase
RT complex in peas.";
RL J. Biol. Chem. 265:848-853(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND LIPOYLATION AT LYS-97.
RC TISSUE=Leaf;
RX PubMed=2363710; DOI=10.1042/bj2680783;
RA Macherel D., Lebrun M., Gagnon J., Neuburger M., Douce R.;
RT "cDNA cloning, primary structure and gene expression for H-protein, a
RT component of the glycine-cleavage system (glycine decarboxylase) of pea
RT (Pisum sativum) leaf mitochondria.";
RL Biochem. J. 268:783-789(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1530594; DOI=10.1042/bj2860627;
RA Macherel D., Bourguignon J., Douce R.;
RT "Cloning of the gene (gdcH) encoding H-protein, a component of the glycine
RT decarboxylase complex of pea (Pisum sativum L.).";
RL Biochem. J. 286:627-630(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-165.
RX PubMed=8197146; DOI=10.1073/pnas.91.11.4850;
RA Pares S., Cohen-Addad C., Sieker L., Neuburger M., Douce R.;
RT "X-ray structure determination at 2.6-A resolution of a lipoate-containing
RT protein: the H-protein of the glycine decarboxylase complex from pea
RT leaves.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4850-4853(1994).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The H protein shuttles the methylamine group of glycine from
CC the P protein to the T protein.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Note=Binds 1 lipoyl cofactor covalently.;
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000305}.
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DR EMBL; J05164; AAA33668.1; -; mRNA.
DR EMBL; X53656; CAA37704.1; -; mRNA.
DR EMBL; X64726; CAA45978.1; -; Genomic_DNA.
DR PIR; S29122; GCPMH.
DR PDB; 1DXM; X-ray; 2.60 A; A/B=35-165.
DR PDB; 1HPC; X-ray; 2.00 A; A/B=35-165.
DR PDB; 1HTP; X-ray; 2.20 A; A=35-165.
DR PDBsum; 1DXM; -.
DR PDBsum; 1HPC; -.
DR PDBsum; 1HTP; -.
DR AlphaFoldDB; P16048; -.
DR BMRB; P16048; -.
DR SMR; P16048; -.
DR IntAct; P16048; 1.
DR PRIDE; P16048; -.
DR EnsemblPlants; Psat2g173640.1; Psat2g173640.1.cds; Psat2g173640.
DR Gramene; Psat2g173640.1; Psat2g173640.1.cds; Psat2g173640.
DR BRENDA; 1.4.1.27; 4872.
DR SABIO-RK; P16048; -.
DR EvolutionaryTrace; P16048; -.
DR GO; GO:0005960; C:glycine cleavage complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:InterPro.
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 3D-structure; Lipoyl; Mitochondrion; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT CHAIN 35..165
FT /note="Glycine cleavage system H protein, mitochondrial"
FT /id="PRO_0000010738"
FT DOMAIN 56..138
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 97
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000269|PubMed:2363710"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1HPC"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1HPC"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:1HPC"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1HPC"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:1HPC"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:1HPC"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1HPC"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1HPC"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:1HPC"
FT TURN 128..132
FT /evidence="ECO:0007829|PDB:1HPC"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1HPC"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:1HPC"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:1HPC"
SQ SEQUENCE 165 AA; 17688 MW; 095CBA89F4B565A7 CRC64;
MALRMWASST ANALKLSSSS RLHLSPTFSI SRCFSNVLDG LKYAPSHEWV KHEGSVATIG
ITDHAQDHLG EVVFVELPEP GVSVTKGKGF GAVESVKATS DVNSPISGEV IEVNTGLTGK
PGLINSSPYE DGWMIKIKPT SPDELESLLG AKEYTKFCEE EDAAH
