GCSH_RABIT
ID GCSH_RABIT Reviewed; 173 AA.
AC Q9N121;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Glycine cleavage system H protein, mitochondrial {ECO:0000303|PubMed:11206584};
DE AltName: Full=Lipoic acid-containing protein;
DE Flags: Precursor;
GN Name=GCSH {ECO:0000250|UniProtKB:P23434};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=11206584; DOI=10.1139/o00-081;
RA Choy F., Sharp L., Applegarth D.A.;
RT "Glycine cleavage enzyme complex: rabbit H-protein cDNA sequence analysis
RT and comparison to human, cow, and chicken.";
RL Biochem. Cell Biol. 78:725-730(2000).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The H protein (GCSH) shuttles the methylamine group of glycine
CC from the P protein (GLDC) to the T protein (GCST) (By similarity).
CC {ECO:0000250|UniProtKB:P11183}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000250|UniProtKB:P23434};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000250|UniProtKB:P23434};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P
CC (GLDC), T (GCST), L (DLD) and H (GCSH). Interacts with GLDC (By
CC similarity). {ECO:0000250|UniProtKB:P11183}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P20821}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000305}.
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DR EMBL; AF231451; AAF63472.1; -; mRNA.
DR RefSeq; NP_001076189.1; NM_001082720.1.
DR AlphaFoldDB; Q9N121; -.
DR SMR; Q9N121; -.
DR STRING; 9986.ENSOCUP00000023181; -.
DR GeneID; 100009476; -.
DR KEGG; ocu:100009476; -.
DR CTD; 2653; -.
DR eggNOG; KOG3373; Eukaryota.
DR InParanoid; Q9N121; -.
DR OrthoDB; 1348095at2759; -.
DR SABIO-RK; Q9N121; -.
DR Proteomes; UP000001811; Unplaced.
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 GO; GO:0009249; P:protein lipoylation; ISS:UniProtKB.
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; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 49..173
FT /note="Glycine cleavage system H protein, mitochondrial"
FT /id="PRO_0000010725"
FT DOMAIN 66..148
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 107
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23434,
FT ECO:0000255|PROSITE-ProRule:PRU01066"
SQ SEQUENCE 173 AA; 18811 MW; F624A2EC84E056CA CRC64;
MALRVVRSLR AAACSLFAAS APAAPCSPLP WRLRAGAVRT LRTGPALLSV RKFTEKHEWI
TTENGIGTVG ISNFAQEALG DVVYCSLPEV GTKLKKQDEF GALESVKAAS ELYSPLSGEV
TEINEALAEN PGLVNKSCYE DGWLIKMTLS NPSELDELMS EEAYEKYIKS IEE
