ID   A0A1H3F841_9RHOB        Unreviewed;       121 AA.
AC   A0A1H3F841;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN   ORFNames=SAMN05444340_101259 {ECO:0000313|EMBL:SDX87183.1};
OS   Citreimonas salinaria.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Citreimonas.
OX   NCBI_TaxID=321339 {ECO:0000313|EMBL:SDX87183.1, ECO:0000313|Proteomes:UP000199286};
RN   [1] {ECO:0000313|EMBL:SDX87183.1, ECO:0000313|Proteomes:UP000199286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26880 {ECO:0000313|EMBL:SDX87183.1,
RC   ECO:0000313|Proteomes:UP000199286};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_00272}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00272};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000256|HAMAP-
CC       Rule:MF_00272};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000256|HAMAP-Rule:MF_00272}.
CC   -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|ARBA:ARBA00009249,
CC       ECO:0000256|HAMAP-Rule:MF_00272}.
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DR   EMBL; FNPF01000001; SDX87183.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3F841; -.
DR   STRING; 321339.SAMN05444340_101259; -.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000199286; Unassembled WGS sequence.
DR   GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
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:SF41; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 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|HAMAP-Rule:MF_00272};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199286}.
FT   DOMAIN          17..99
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         58
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT                   ECO:0000256|PIRSR:PIRSR617453-50"
SQ   SEQUENCE   121 AA;  13276 MW;  B08D7716DCAD11B0 CRC64;
     MKFTEEHEWL DAGDDNVVTV GITAHAAEQL GDVVFVELPE VGTEVVKDDE IVVIESVKAA
     SDILAPVDGE IVEVNDAIVD EPSKVNEDPE GDAWFFRIKV EDLSVLDDLM DEAAYKKFIG
     D
//