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   25-MAY-2022, entry version 88.
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   PRIDE; 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   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   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