GCSH_FLATR
ID GCSH_FLATR Reviewed; 165 AA.
AC P46485; Q39733;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Glycine cleavage system H protein, mitochondrial;
DE AltName: Full=Lipoyl-bearing H protein;
DE Flags: Precursor;
GN Name=GDCSH; Synonyms=GCDH, GCSH;
OS Flaveria trinervia (Clustered yellowtops) (Oedera trinervia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Tageteae; Flaveria.
OX NCBI_TaxID=4227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Leaf;
RX PubMed=7550380; DOI=10.1046/j.1365-313x.1995.08030435.x;
RA Kopriva S., Cossu R., Bauwe H.;
RT "Alternative splicing results in two different transcripts for H-protein of
RT the glycine cleavage system in the C4 species Flaveria trinervia.";
RL Plant J. 8:435-441(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=8552027; DOI=10.1007/bf00290242;
RA Kopriva S., Bauwe H.;
RT "H-protein of glycine decarboxylase is encoded by multigene families in
RT Flaveria pringlei and F. cronquistii (Asteraceae).";
RL Mol. Gen. Genet. 249:111-116(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-143 (ISOFORM 1), AND ALTERNATIVE SPLICING.
RA Kopriva S., Chu C.C., Bauwe H.;
RT "Molecular phylogeny of Flaveria as deduced from the analysis of H-protein
RT nucleotide sequences.";
RL Plant Cell Environ. 19:1028-1036(1996).
RN [4]
RP ALTERNATIVE SPLICING.
RC TISSUE=Leaf;
RX PubMed=8771790; DOI=10.1046/j.1365-313x.1996.10020369.x;
RA Kopriva S., Chu C.-C., Bauwe H.;
RT "H-protein of the glycine cleavage system in Flaveria: alternative splicing
RT of the pre-mRNA occurs exclusively in advanced C4 species of the genus.";
RL Plant J. 10:369-373(1996).
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; Evidence={ECO:0000250};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC -!- SUBUNIT: The glycine cleavage system is composed of four components
CC that only loosely associate: the P protein (EC 1.4.4.2), the T protein
CC (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H
CC protein.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=This alternative splicing is restricted to C4 species of
CC Flaveria. {ECO:0000269|PubMed:7550380, ECO:0000269|PubMed:8771790,
CC ECO:0000269|Ref.3};
CC Name=1;
CC IsoId=P46485-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P46485-2; Sequence=VSP_040391;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and leaves.
CC {ECO:0000269|PubMed:7550380}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform in stems and leaves.
CC -!- MISCELLANEOUS: [Isoform 2]: Major isoform in roots. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000305}.
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DR EMBL; Z37523; CAA85760.1; -; mRNA.
DR EMBL; Z48797; CAA88734.1; -; Genomic_DNA.
DR EMBL; Z70303; CAA94316.1; -; mRNA.
DR PIR; S49232; S49232.
DR PIR; S57665; S57665.
DR AlphaFoldDB; P46485; -.
DR SMR; P46485; -.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; Lipoyl; Mitochondrion; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 32..165
FT /note="Glycine cleavage system H protein, mitochondrial"
FT /id="PRO_0000010735"
FT DOMAIN 55..137
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 96
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT VAR_SEQ 34..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7550380"
FT /id="VSP_040391"
SQ SEQUENCE 165 AA; 17674 MW; 0BB544B371856BAB CRC64;
MALRIWASST AKALRLSSAS RPHFSPLFRC FSSAAVLDGL KYANSHEWVK HEGSVATIGI
TDHAQDHLGE VVFVELPEVG GSVTKATGFG AVESVKATSD VNSPISGEIV EVNSKLTKTP
GLINKSPYED GWMIKVKPSN PSELDSLMGP KEYTKFCEEE GAAAH
