ID GCSH_FLAAN Reviewed; 162 AA.
AC Q39732; O49848;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 13-SEP-2023, entry version 92.
DE RecName: Full=Glycine cleavage system H protein, mitochondrial;
DE Flags: Precursor;
GN Name=GDCSH; Synonyms=GCDH, GCSH;
OS Flaveria anomala (Yellowtops).
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=35877;
RN [1]
RP NUCLEOTIDE SEQUENCE.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RA Chu C.-C., Qu N., Bauwe H.;
RT "The GDCSH gene encoding H-protein of the glycine cleavage system in the
RT C3-C4 intermediate plant Flaveria anomala.";
RL (er) Plant Gene Register PGR98-001(1998).
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; Z37524; CAA85761.1; -; mRNA.
DR EMBL; Z99530; CAB16710.1; -; Genomic_DNA.
DR PIR; S49248; S49248.
DR AlphaFoldDB; Q39732; -.
DR SMR; Q39732; -.
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 Gene3D; 2.40.50.100; -; 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 NCBIfam; TIGR00527; gcvH; 1.
DR PANTHER; PTHR11715; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 1.
DR PANTHER; PTHR11715:SF27; GLYCINE CLEAVAGE SYSTEM H PROTEIN 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 2: Evidence at transcript level;
KW Lipoyl; Mitochondrion; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 32..162
FT /note="Glycine cleavage system H protein, mitochondrial"
FT /id="PRO_0000010731"
FT DOMAIN 53..135
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 94
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 5
FT /note="M -> I (in Ref. 2; CAB16710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 162 AA; 17354 MW; 03F15EE36CF8A2DB CRC64;
MALRMWASST ANALRLSSAT RPHFSPLSRC FSSVLDGLKY ANSHEWVKHE GSVATIGITD
HAQDHLGEVV FVDLPEAGGS VTKATGFGAV ESVKATSDVN SPISGEIVEV NSKLSETPGL
INSSPYEDGW MIKVKPSNPS ELDSLMGAKE YTKFCEEEDA AH
//
