ID G0HN83_THES4 Unreviewed; 134 AA.
AC G0HN83;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Probable glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN OrderedLocusNames=GQS_09200 {ECO:0000313|EMBL:AEK73734.1};
OS Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK73734.1, ECO:0000313|Proteomes:UP000000874};
RN [1] {ECO:0000313|EMBL:AEK73734.1, ECO:0000313|Proteomes:UP000000874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX PubMed=21914870; DOI=10.1128/JB.05851-11;
RA Wang X., Gao Z., Xu X., Ruan L.;
RT "Complete genome sequence of Thermococcus sp. strain 4557, a
RT hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT area.";
RL J. Bacteriol. 193:5544-5545(2011).
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; CP002920; AEK73734.1; -; Genomic_DNA.
DR RefSeq; WP_014013416.1; NC_015865.1.
DR AlphaFoldDB; G0HN83; -.
DR STRING; 1042877.GQS_09200; -.
DR GeneID; 11016521; -.
DR KEGG; the:GQS_09200; -.
DR PATRIC; fig|1042877.9.peg.1793; -.
DR eggNOG; arCOG01303; Archaea.
DR HOGENOM; CLU_097408_2_0_2; -.
DR OrthoDB; 9810at2157; -.
DR Proteomes; UP000000874; 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; 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}.
FT DOMAIN 29..110
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 70
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 134 AA; 15065 MW; 2D5240160235C994 CRC64;
MIEVGEYRVK EGLYYTKDHE WVQVLEDGTV LVGISDYAQK ELGDLAYVEL PDVGSELSKG
DVLCELESVK AVSEVYAPVS GEVAEVNEEL EDSPELINED PYENWIAKLK PSNLDEELKE
LMDAKAYAEY LESL
//
