ID A0A1S6IPU6_9LACT Unreviewed; 129 AA.
AC A0A1S6IPU6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272,
GN ECO:0000313|EMBL:AQS53566.1};
GN ORFNames=BW727_101199 {ECO:0000313|EMBL:AQS53566.1};
OS Jeotgalibaca dankookensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Jeotgalibaca.
OX NCBI_TaxID=708126 {ECO:0000313|EMBL:AQS53566.1, ECO:0000313|Proteomes:UP000188993};
RN [1] {ECO:0000313|EMBL:AQS53566.1, ECO:0000313|Proteomes:UP000188993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EX-07 {ECO:0000313|EMBL:AQS53566.1,
RC ECO:0000313|Proteomes:UP000188993};
RX PubMed=24554638; DOI=10.1099/ijs.0.057059-0;
RA Lee D.G., Trujillo M.E., Kang H., Ahn T.Y.;
RT "Jeotgalibaca dankookensis gen. nov., sp. nov., a member of the family
RT Carnobacteriaceae, isolated from seujeot (Korean traditional food).";
RL Int. J. Syst. Evol. Microbiol. 64:1729-1735(2014).
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; CP019728; AQS53566.1; -; Genomic_DNA.
DR RefSeq; WP_062472257.1; NZ_CP019728.1.
DR AlphaFoldDB; A0A1S6IPU6; -.
DR STRING; 708126.BW727_101199; -.
DR KEGG; jda:BW727_101199; -.
DR OrthoDB; 9796712at2; -.
DR Proteomes; UP000188993; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|HAMAP-Rule:MF_00272};
KW Reference proteome {ECO:0000313|Proteomes:UP000188993}.
FT DOMAIN 22..104
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 63
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 129 AA; 14474 MW; C137C1E0FBEA40D0 CRC64;
MTEKKRYYTE EHEWVEIIEG NTARVGITEH AQEQLGDIVF VDYTSDLQEV AVGDDIVTVE
SVKSVSDVYA PVSGTVTKQN EQLADAPETV NVSAMDQGWM IEMEISDPSE LKHLMDEEAY
QAFLAEEEA
//
