ID   GCSH_FLAPU              Reviewed;         152 AA.
AC   P49360;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Glycine cleavage system H protein, mitochondrial;
DE   Flags: Precursor; Fragment;
GN   Name=GDCSH; Synonyms=GCDH, GCSH;
OS   Flaveria pubescens (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=35880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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).
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; Z37530; CAA85768.1; -; mRNA.
DR   PIR; S49251; S49251.
DR   AlphaFoldDB; P49360; -.
DR   SMR; P49360; -.
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..>152
FT                   /note="Glycine cleavage system H protein, mitochondrial"
FT                   /id="PRO_0000010734"
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   NON_TER         152
SQ   SEQUENCE   152 AA;  16196 MW;  778B88A482330DCE CRC64;
     MALRMWASST ANALRLSSAT RPHYSPLSRC FSSVLDGLKY ANSHEWVKHE GSVATVGITD
     HAQDHLGEVV FVDLPEAGGS VTKATGFGAV ESVKATSDVN SPISGEIVEV NSKLSETPGL
     INSSPYEDGW MIKVKPSNPS ELDSLMGAKE YT