ID A0A1C6LG29_9NEIS Unreviewed; 128 AA.
AC A0A1C6LG29;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=PSELUDRAFT_0125 {ECO:0000313|EMBL:SCK05514.1};
OS Vogesella sp. LIG4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Vogesella.
OX NCBI_TaxID=1192162 {ECO:0000313|EMBL:SCK05514.1, ECO:0000313|Proteomes:UP000198213};
RN [1] {ECO:0000313|EMBL:SCK05514.1, ECO:0000313|Proteomes:UP000198213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LIG4 {ECO:0000313|Proteomes:UP000198213};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; LT607802; SCK05514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6LG29; -.
DR OrthoDB; 9796712at2; -.
DR Proteomes; UP000198213; Chromosome i.
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: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|HAMAP-Rule:MF_00272};
KW Reference proteome {ECO:0000313|Proteomes:UP000198213}.
FT DOMAIN 24..106
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 65
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 128 AA; 13430 MW; A90F7D2D3324D399 CRC64;
MSNIPAELKY VSSHEWLRLE ADGTVSIGIT EHAQELLGDI VFVELPAVGS QLGEGEQAGV
VESVKAASDI YAPIAGEVLE VNSDLEAAPD LANSDPYGAA WFFKIKPANA ADLDRLMDAA
AYAAEIGA
//