ID A0A2V0PQ51_9CHLO Unreviewed; 153 AA.
AC A0A2V0PQ51;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
GN ORFNames=Rsub_11737 {ECO:0000313|EMBL:GBF99325.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF99325.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF99325.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF99325.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBF99325.1}.
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DR EMBL; BDRX01000154; GBF99325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0PQ51; -.
DR STRING; 307507.A0A2V0PQ51; -.
DR InParanoid; A0A2V0PQ51; -.
DR Proteomes; UP000247498; Unassembled WGS sequence.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:SF3; GLYCINE CLEAVAGE SYSTEM H PROTEIN, MITOCHONDRIAL; 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 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|PIRSR:PIRSR617453-50};
KW Mitochondrion {ECO:0000256|RuleBase:RU364055};
KW Reference proteome {ECO:0000313|Proteomes:UP000247498};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU364055}.
FT DOMAIN 49..131
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 90
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 153 AA; 16214 MW; FEFBE3747C6A873A CRC64;
MALRALASNA GVQWGVRTQF GAIARAFSSV LPEAKYAASH EWAKVEGSTA TVGISDHAQS
ELGDVVYVEL PEVGATVTKG ETFGVVESVK AASDVYSPLS GKVVEINEAL VAEPAKINQE
PYSGGWMMKI ELSDKGEVAS LMDATAYQKH CEH
//
