ID Q42442_FLAPR Unreviewed; 162 AA.
AC Q42442;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 13-SEP-2023, entry version 108.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
GN Name=gdcsH {ECO:0000313|EMBL:CAB16912.1};
OS Flaveria pringlei.
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=4226 {ECO:0000313|EMBL:CAA81074.1};
RN [1] {ECO:0000313|EMBL:CAA81074.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:CAA81074.1};
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 [2] {ECO:0000313|EMBL:CAA81074.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:CAA81074.1};
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 [3] {ECO:0000313|EMBL:CAB16912.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:CAB16912.1};
RX PubMed=9449852;
RA Chu C., Bauwe H.;
RT "The gdcsHA gene encoding H-protein of the glycine cleavage system from
RT Flaveria pringlei.";
RL Plant Physiol. 116:445-445(1998).
CC -!- FUNCTION: The H protein shuttles the methylamine group of glycine from
CC the P protein to the T protein. {ECO:0000256|RuleBase:RU364055}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU364055};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000256|RuleBase:RU364055};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|RuleBase:RU364055}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU364055}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|ARBA:ARBA00009249,
CC ECO:0000256|RuleBase:RU364055}.
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DR EMBL; Z25855; CAA81074.1; -; mRNA.
DR EMBL; Z99763; CAB16912.1; -; Genomic_DNA.
DR PIR; S60195; S60195.
DR PIR; S60199; S60199.
DR AlphaFoldDB; Q42442; -.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|PIRSR:PIRSR617453-50};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU364055}; Transferase {ECO:0000313|EMBL:CAB16912.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU364055}.
FT DOMAIN 53..135
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 94
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 162 AA; 17384 MW; E2B44AA66CE3B86A CRC64;
MALRMWASST ANALRLSSAT RPHFSPLSRC FSSVLDGLKY ANSHEWVKHE GSVATIGITD
HAQDHLGEVV FVDLPETGGS VTKATGFGAV ESVKATSDVN SPISGEIVEV NSKLSETPGL
INSSPYEDGW MIKVKPSNPS ELDSLMGAKE YTKFCEEEDA AH
//
